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Entry
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- *601860 - 17-BETA-HYDROXYSTEROID DEHYDROGENASE IV; HSD17B4
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- OMIM
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<div id="mimFloatingTocMenu" class="small" role="navigation">
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<p>
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<span class="h4">*601860</span>
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<br />
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<strong>Table of Contents</strong>
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</p>
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<nav>
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<ul id="mimFloatingTocMenuItems" class="nav nav-pills nav-stacked mim-floating-toc-padding">
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<li role="presentation">
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<a href="#title"><strong>Title</strong></a>
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<li role="presentation">
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<a href="#geneMap"><strong>Gene-Phenotype Relationships</strong></a>
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</li>
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<a href="#text"><strong>Text</strong></a>
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<li role="presentation" style="margin-left: 1em">
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<a href="#description">Description</a>
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</li>
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<li role="presentation" style="margin-left: 1em">
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<a href="#cloning">Cloning and Expression</a>
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</li>
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<li role="presentation" style="margin-left: 1em">
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<a href="#geneStructure">Gene Structure</a>
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<li role="presentation" style="margin-left: 1em">
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<a href="#mapping">Mapping</a>
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<li role="presentation" style="margin-left: 1em">
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<a href="#geneFunction">Gene Function</a>
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<li role="presentation" style="margin-left: 1em">
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<a href="#molecularGenetics">Molecular Genetics</a>
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<li role="presentation" style="margin-left: 1em">
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<a href="#animalModel">Animal Model</a>
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<li role="presentation">
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<a href="#allelicVariants"><strong>Allelic Variants</strong></a>
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</li>
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<li role="presentation" style="margin-left: 1em">
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<a href="/allelicVariants/601860">Table View</a>
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</li>
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<li role="presentation">
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<a href="#seeAlso"><strong>See Also</strong></a>
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</li>
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<li role="presentation">
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<a href="#references"><strong>References</strong></a>
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</li>
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<li role="presentation">
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<a href="#contributors"><strong>Contributors</strong></a>
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<li role="presentation">
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<a href="#creationDate"><strong>Creation Date</strong></a>
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</li>
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<li role="presentation">
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<a href="#editHistory"><strong>Edit History</strong></a>
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</li>
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</ul>
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</nav>
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</div>
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</div>
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<div class="col-lg-2 col-lg-push-8 col-md-2 col-md-push-8 col-sm-2 col-sm-push-8 col-xs-12">
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<div id="mimFloatingLinksMenu">
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<div class="panel panel-primary" style="margin-bottom: 0px; border-radius: 4px 4px 0px 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimExternalLinks">
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<h4 class="panel-title">
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<a href="#mimExternalLinksFold" id="mimExternalLinksToggle" class="mimTriangleToggle" role="button" data-toggle="collapse">
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<div style="display: table-row">
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<div id="mimExternalLinksToggleTriangle" class="small" style="color: white; display: table-cell;">▼</div>
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<div style="display: table-cell;">External Links</div>
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</div>
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</a>
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</h4>
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</div>
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</div>
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<div id="mimExternalLinksFold" class="collapse in">
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<div class="panel-group" id="mimExternalLinksAccordion" role="tablist" aria-multiselectable="true">
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimGenome">
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<span class="panel-title">
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<span class="small">
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<a href="#mimGenomeLinksFold" id="mimGenomeLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<span id="mimGenomeLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> Genome
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</a>
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</span>
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</span>
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</div>
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<div id="mimGenomeLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel" aria-labelledby="genome">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.ensembl.org/Homo_sapiens/Location/View?db=core;g=ENSG00000133835;t=ENST00000510025" class="mim-tip-hint" title="Genome databases for vertebrates and other eukaryotic species." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/genome/gdv/browser/gene/?id=3295" class="mim-tip-hint" title="Detailed views of the complete genomes of selected organisms from vertebrates to protozoa." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Genome Viewer', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Genome Viewer</a></div>
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&hgFind=omimGeneAcc&position=601860" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">UCSC Genome Browser</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimDna">
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<span class="panel-title">
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<span class="small">
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<a href="#mimDnaLinksFold" id="mimDnaLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<span id="mimDnaLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> DNA
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</a>
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</span>
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</span>
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</div>
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<div id="mimDnaLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.ensembl.org/Homo_sapiens/Transcript/Sequence_cDNA?db=core;g=ENSG00000133835;t=ENST00000510025" class="mim-tip-hint" title="Transcript-based views for coding and noncoding DNA." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl (MANE Select)</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/nuccore/NM_000414,NM_001199291,NM_001199292,NM_001292027,NM_001292028,NM_001374497,NM_001374498,NM_001374499,NM_001374500,NM_001374501,NM_001374502,NM_001374503,NR_164653,NR_164654" class="mim-tip-hint" title="A collection of genome, gene, and transcript sequence data from several sources, including GenBank, RefSeq." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI RefSeq', 'domain': 'ncbi.nlm.nih'})">NCBI RefSeq</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/nuccore/NM_000414" class="mim-tip-hint" title="A collection of genome, gene, and transcript sequence data from several sources, including GenBank, RefSeq." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI RefSeq (MANE)', 'domain': 'ncbi.nlm.nih'})">NCBI RefSeq (MANE Select)</a></div>
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&hgFind=omimGeneAcc&position=601860" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">UCSC Genome Browser</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimProtein">
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<span class="panel-title">
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<span class="small">
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<a href="#mimProteinLinksFold" id="mimProteinLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<span id="mimProteinLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">►</span> Protein
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</a>
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</span>
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</span>
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</div>
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<div id="mimProteinLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://hprd.org/summary?hprd_id=03514&isoform_id=03514_1&isoform_name=Isoform_1" class="mim-tip-hint" title="The Human Protein Reference Database; manually extracted and visually depicted information on human proteins." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HPRD', 'domain': 'hprd.org'})">HPRD</a></div>
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<div><a href="https://www.proteinatlas.org/search/HSD17B4" class="mim-tip-hint" title="The Human Protein Atlas contains information for a large majority of all human protein-coding genes regarding the expression and localization of the corresponding proteins based on both RNA and protein data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HumanProteinAtlas', 'domain': 'proteinatlas.org'})">Human Protein Atlas</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/protein/1050517,1706396,1869808,4165049,4504505,13111861,119569295,119569296,189065517,193787598,194375349,194375682,194380056,194388790,194389150,308219336,313151210,313482810,635372936,635372938,957949604,957949607,957949610,957949613,1755203671,1755203675,1755203683,1755203691,1755203693,1755203700,1755203702" class="mim-tip-hint" title="NCBI protein data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Protein', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Protein</a></div>
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<div><a href="https://www.uniprot.org/uniprotkb/P51659" class="mim-tip-hint" title="Comprehensive protein sequence and functional information, including supporting data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UniProt', 'domain': 'uniprot.org'})">UniProt</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimGeneInfo">
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<span class="panel-title">
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<span class="small">
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<a href="#mimGeneInfoLinksFold" id="mimGeneInfoLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
|
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<div style="display: table-row">
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<div id="mimGeneInfoLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Gene Info</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimGeneInfoLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="http://biogps.org/#goto=genereport&id=3295" class="mim-tip-hint" title="The Gene Portal Hub; customizable portal of gene and protein function information." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'BioGPS', 'domain': 'biogps.org'})">BioGPS</a></div>
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<div><a href="https://www.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000133835;t=ENST00000510025" class="mim-tip-hint" title="Orthologs, paralogs, regulatory regions, and splice variants." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Ensembl', 'domain': 'ensembl.org'})">Ensembl</a></div>
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<div><a href="https://www.genecards.org/cgi-bin/carddisp.pl?gene=HSD17B4" class="mim-tip-hint" title="The Human Genome Compendium; web-based cards integrating automatically mined information on human genes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GeneCards', 'domain': 'genecards.org'})">GeneCards</a></div>
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<div><a href="http://amigo.geneontology.org/amigo/search/annotation?q=HSD17B4" class="mim-tip-hint" title="Terms, defined using controlled vocabulary, representing gene product properties (biologic process, cellular component, molecular function) across species." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GeneOntology', 'domain': 'amigo.geneontology.org'})">Gene Ontology</a></div>
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<div><a href="https://www.genome.jp/dbget-bin/www_bget?hsa+3295" class="mim-tip-hint" title="Kyoto Encyclopedia of Genes and Genomes; diagrams of signaling pathways." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'KEGG', 'domain': 'genome.jp'})">KEGG</a></div>
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<dd><a href="http://v1.marrvel.org/search/gene/HSD17B4" class="mim-tip-hint" title="Model organism Aggregated Resources for Rare Variant ExpLoration." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MARRVEL', 'domain': 'marrvel.org'})">MARRVEL</a></dd>
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<dd><a href="https://monarchinitiative.org/NCBIGene:3295" class="mim-tip-hint" title="Monarch Initiative." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Monarch', 'domain': 'monarchinitiative.org'})">Monarch</a></dd>
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<div><a href="https://www.ncbi.nlm.nih.gov/gene/3295" class="mim-tip-hint" title="Gene-specific map, sequence, expression, structure, function, citation, and homology data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Gene', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Gene</a></div>
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<div><a href="https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_chrom=chr5&hgg_gene=ENST00000510025.7&hgg_start=119452497&hgg_end=119542332&hgg_type=knownGene" class="mim-tip-hint" title="UCSC Genome Bioinformatics; gene-specific structure and function information with links to other databases." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC', 'domain': 'genome.ucsc.edu'})">UCSC</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimClinicalResources">
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<span class="panel-title">
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<span class="small">
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<a href="#mimClinicalResourcesLinksFold" id="mimClinicalResourcesLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimClinicalResourcesLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Clinical Resources</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimClinicalResourcesLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel" aria-labelledby="clinicalResources">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://search.clinicalgenome.org/kb/gene-dosage/HGNC:5213" class="mim-tip-hint" title="A ClinGen curated resource of genes and regions of the genome that are dosage sensitive and should be targeted on a cytogenomic array." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinGen Dosage', 'domain': 'dosage.clinicalgenome.org'})">ClinGen Dosage</a></div>
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<div><a href="https://search.clinicalgenome.org/kb/genes/HGNC:5213" class="mim-tip-hint" title="A ClinGen curated resource of ratings for the strength of evidence supporting or refuting the clinical validity of the claim(s) that variation in a particular gene causes disease." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinGen Validity', 'domain': 'search.clinicalgenome.org'})">ClinGen Validity</a></div>
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<div><a href="https://medlineplus.gov/genetics/gene/hsd17b4" class="mim-tip-hint" title="Consumer-friendly information about the effects of genetic variation on human health." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MedlinePlus Genetics', 'domain': 'medlineplus.gov'})">MedlinePlus Genetics</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/gtr/all/tests/?term=601860[mim]" class="mim-tip-hint" title="Genetic Testing Registry." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GTR', 'domain': 'ncbi.nlm.nih.gov'})">GTR</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimVariation">
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<span class="panel-title">
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<span class="small">
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<a href="#mimVariationLinksFold" id="mimVariationLinksToggle" class=" mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<span id="mimVariationLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5">▼</span> Variation
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</a>
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</span>
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</span>
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</div>
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<div id="mimVariationLinksFold" class="panel-collapse collapse in mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.ncbi.nlm.nih.gov/clinvar?term=601860[MIM]" class="mim-tip-hint" title="ClinVar aggregates information about sequence variation and its relationship to human health." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">ClinVar</a></div>
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<div><a href="https://www.deciphergenomics.org/gene/HSD17B4/overview/clinical-info" class="mim-tip-hint" title="DECIPHER" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'DECIPHER', 'domain': 'DECIPHER'})">DECIPHER</a></div>
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<div><a href="https://gnomad.broadinstitute.org/gene/ENSG00000133835" class="mim-tip-hint" title="The Genome Aggregation Database (gnomAD), Broad Institute." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'gnomAD', 'domain': 'gnomad.broadinstitute.org'})">gnomAD</a></div>
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<div><a href="https://www.ebi.ac.uk/gwas/search?query=HSD17B4" class="mim-tip-hint" title="GWAS Catalog; NHGRI-EBI Catalog of published genome-wide association studies." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GWAS Catalog', 'domain': 'gwascatalog.org'})">GWAS Catalog </a></div>
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<div><a href="https://www.gwascentral.org/search?q=HSD17B4" class="mim-tip-hint" title="GWAS Central; summary level genotype-to-phenotype information from genetic association studies." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'GWAS Central', 'domain': 'gwascentral.org'})">GWAS Central </a></div>
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<div><a href="http://www.hgmd.cf.ac.uk/ac/gene.php?gene=HSD17B4" class="mim-tip-hint" title="Human Gene Mutation Database; published mutations causing or associated with human inherited disease; disease-associated/functional polymorphisms." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HGMD', 'domain': 'hgmd.cf.ac.uk'})">HGMD</a></div>
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<div><a href="http://databases.lovd.nl/shared/genes/HSD17B4" class="mim-tip-hint" title="A gene-specific database of variation." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Locus Specific DB', 'domain': 'locus-specific-db.org'})">Locus Specific DBs</a></div>
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<div><a href="https://evs.gs.washington.edu/EVS/PopStatsServlet?searchBy=Gene+Hugo&target=HSD17B4&upstreamSize=0&downstreamSize=0&x=0&y=0" class="mim-tip-hint" title="National Heart, Lung, and Blood Institute Exome Variant Server." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NHLBI EVS', 'domain': 'evs.gs.washington.edu'})">NHLBI EVS</a></div>
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<div><a href="https://www.pharmgkb.org/gene/PA29481" class="mim-tip-hint" title="Pharmacogenomics Knowledge Base; curated and annotated information regarding the effects of human genetic variations on drug response." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PharmGKB', 'domain': 'pharmgkb.org'})">PharmGKB</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimAnimalModels">
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<span class="panel-title">
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<span class="small">
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<a href="#mimAnimalModelsLinksFold" id="mimAnimalModelsLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimAnimalModelsLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Animal Models</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimAnimalModelsLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.alliancegenome.org/gene/HGNC:5213" class="mim-tip-hint" title="Search Across Species; explore model organism and human comparative genomics." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Alliance Genome', 'domain': 'alliancegenome.org'})">Alliance Genome</a></div>
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<div><a href="https://flybase.org/reports/FBgn0030731.html" class="mim-tip-hint" title="A Database of Drosophila Genes and Genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'FlyBase', 'domain': 'flybase.org'})">FlyBase</a></div>
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<div><a href="https://www.mousephenotype.org/data/genes/MGI:105089" class="mim-tip-hint" title="International Mouse Phenotyping Consortium." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'IMPC', 'domain': 'knockoutmouse.org'})">IMPC</a></div>
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<div><a href="http://v1.marrvel.org/search/gene/HSD17B4#HomologGenesPanel" class="mim-tip-hint" title="Model organism Aggregated Resources for Rare Variant ExpLoration." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MARRVEL', 'domain': 'marrvel.org'})">MARRVEL</a></div>
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<div><a href="http://www.informatics.jax.org/marker/MGI:105089" class="mim-tip-hint" title="Mouse Genome Informatics; international database resource for the laboratory mouse, including integrated genetic, genomic, and biological data." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MGI Mouse Gene', 'domain': 'informatics.jax.org'})">MGI Mouse Gene</a></div>
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<div><a href="https://www.mmrrc.org/catalog/StrainCatalogSearchForm.php?search_query=" class="mim-tip-hint" title="Mutant Mouse Resource & Research Centers." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'MMRRC', 'domain': 'mmrrc.org'})">MMRRC</a></div>
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<div><a href="https://www.ncbi.nlm.nih.gov/gene/3295/ortholog/" class="mim-tip-hint" title="Orthologous genes at NCBI." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'NCBI Orthologs', 'domain': 'ncbi.nlm.nih.gov'})">NCBI Orthologs</a></div>
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<div><a href="https://www.orthodb.org/?ncbi=3295" class="mim-tip-hint" title="Hierarchical catalogue of orthologs." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'OrthoDB', 'domain': 'orthodb.org'})">OrthoDB</a></div>
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<div><a href="mim#WormbaseGeneFold" id="mimWormbaseGeneToggle" data-toggle="collapse" class="mim-tip-hint mimTriangleToggle" title="Database of the biology and genome of Caenorhabditis elegans and related nematodes."><span id="mimWormbaseGeneToggleTriangle" class="small" style="margin-left: -0.8em;">►</span>Wormbase Gene</div>
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<div id="mimWormbaseGeneFold" class="collapse">
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<div style="margin-left: 0.5em;"><a href="https://wormbase.org/db/gene/gene?name=WBGene00000991;class=Gene" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Wormbase Gene', 'domain': 'wormbase.org'})">WBGene00000991 </a></div><div style="margin-left: 0.5em;"><a href="https://wormbase.org/db/gene/gene?name=WBGene00017123;class=Gene" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'Wormbase Gene', 'domain': 'wormbase.org'})">WBGene00017123 </a></div>
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</div>
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<div><a href="https://zfin.org/ZDB-GENE-040421-1" class="mim-tip-hint" title="The Zebrafish Model Organism Database." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ZFin', 'domain': 'zfin.org'})">ZFin</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimCellLines">
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<span class="panel-title">
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<span class="small">
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<a href="#mimCellLinesLinksFold" id="mimCellLinesLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimCellLinesLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Cell Lines</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimCellLinesLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://catalog.coriell.org/Search?q=OmimNum:601860" class="definition" title="Coriell Cell Repositories; cell cultures and DNA derived from cell cultures." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'CCR', 'domain': 'ccr.coriell.org'})">Coriell</a></div>
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</div>
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</div>
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</div>
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<div class="panel panel-default" style="margin-top: 0px; border-radius: 0px">
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<div class="panel-heading mim-panel-heading" role="tab" id="mimCellularPathways">
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<span class="panel-title">
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<span class="small">
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<a href="#mimCellularPathwaysLinksFold" id="mimCellularPathwaysLinksToggle" class="collapsed mimSingletonTriangleToggle" role="button" data-toggle="collapse" data-parent="#mimExternalLinksAccordion">
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<div style="display: table-row">
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<div id="mimCellularPathwaysLinksToggleTriangle" class="small mimSingletonTriangle" style="color: #337CB5; display: table-cell;">►</div>
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<div style="display: table-cell;">Cellular Pathways</div>
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</div>
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</a>
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</span>
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</span>
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</div>
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<div id="mimCellularPathwaysLinksFold" class="panel-collapse collapse mimLinksFold" role="tabpanel">
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<div class="panel-body small mim-panel-body">
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<div><a href="https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+hsa:3295" class="mim-tip-hint" title="Kyoto Encyclopedia of Genes and Genomes; diagrams of signaling pathways." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'KEGG', 'domain': 'genome.jp'})">KEGG</a></div>
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<div><a href="https://reactome.org/content/query?q=HSD17B4&species=Homo+sapiens&types=Reaction&types=Pathway&cluster=true" class="definition" title="Protein-specific information in the context of relevant cellular pathways." target="_blank" onclick="gtag('event', 'mim_outbound', {{'name': 'Reactome', 'domain': 'reactome.org'}})">Reactome</a></div>
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</div>
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</div>
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</div>
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</div>
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</div>
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</div>
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<span>
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<span class="mim-tip-bottom" qtip_title="<strong>Looking for this gene or this phenotype in other resources?</strong>" qtip_text="Select a related resource from the dropdown menu and click for a targeted link to information directly relevant.">
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</span>
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</span>
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</div>
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<div class="col-lg-8 col-lg-pull-2 col-md-8 col-md-pull-2 col-sm-8 col-sm-pull-2 col-xs-12">
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<div>
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<a id="title" class="mim-anchor"></a>
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<div>
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<a id="number" class="mim-anchor"></a>
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<div class="text-right">
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<a href="#" class="mim-tip-icd" qtip_title="<strong>ICD+</strong>" qtip_text="
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<strong>SNOMEDCT:</strong> 238068007<br />
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">ICD+</a>
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</div>
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<div>
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<span class="h3">
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<span class="mim-font mim-tip-hint" title="Gene description">
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<span class="text-danger"><strong>*</strong></span>
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601860
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</span>
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</span>
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</div>
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</div>
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<div>
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<a id="preferredTitle" class="mim-anchor"></a>
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<h3>
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<span class="mim-font">
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17-BETA-HYDROXYSTEROID DEHYDROGENASE IV; HSD17B4
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</span>
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</h3>
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</div>
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<div>
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<br />
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</div>
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<div>
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<a id="alternativeTitles" class="mim-anchor"></a>
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<div>
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<p>
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<span class="mim-font">
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<em>Alternative titles; symbols</em>
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</span>
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</p>
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</div>
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<div>
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<h4>
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<span class="mim-font">
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17-BETA-HSD IV<br />
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D-3-HYDROXYACYL-CoA DEHYDRATASE/D-3-HYDROXYACYL-CoA DEHYDROGENASE BIFUNCTIONAL PROTEIN<br />
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D-BIFUNCTIONAL PROTEIN, PEROXISOMAL<br />
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DBP, PEROXISOMAL<br />
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MULTIFUNCTIONAL PROTEIN 2; MFP2
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</span>
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</h4>
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</div>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<a id="approvedGeneSymbols" class="mim-anchor"></a>
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<p>
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<span class="mim-text-font">
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<strong><em>HGNC Approved Gene Symbol: <a href="https://www.genenames.org/tools/search/#!/genes?query=HSD17B4" class="mim-tip-hint" title="HUGO Gene Nomenclature Committee." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'HGNC', 'domain': 'genenames.org'})">HSD17B4</a></em></strong>
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</span>
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</p>
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</div>
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<div>
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<a id="cytogeneticLocation" class="mim-anchor"></a>
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<p>
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<span class="mim-text-font">
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<strong>
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<em>
|
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Cytogenetic location: <a href="/geneMap/5/392?start=-3&limit=10&highlight=392">5q23.1</a>
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Genomic coordinates <span class="small">(GRCh38)</span> : <a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&position=chr5:119452497-119542332&dgv=pack&knownGene=pack&omimGene=pack" class="mim-tip-hint" title="UCSC Genome Browser; reference sequences and working draft assemblies for a large collection of genomes." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'UCSC Genome Browser', 'domain': 'genome.ucsc.edu'})">5:119,452,497-119,542,332</a> </span>
|
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</em>
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</strong>
|
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<a href="https://www.ncbi.nlm.nih.gov/" target="_blank" class="small"> (from NCBI) </a>
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</span>
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</p>
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</div>
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<div>
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<br />
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</div>
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<div>
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<span class="glyphicon glyphicon-question-sign mim-tip-hint" title="OMIM PheneGene graphics depict relationships between phenotypes, groups of related phenotypes (Phenotypic Series), and genes.<br /><a href='/static/omim/pdf/OMIM_Graphics.pdf' target='_blank'>A quick reference overview and guide (PDF)</a>"></span>
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<span class="mim-tip-floating" qtip_title="<strong>Looking For More References?</strong>" qtip_text="Click the 'reference plus' icon <span class='glyphicon glyphicon-plus-sign'></span> at the end of each OMIM text paragraph to see more references related to the content of the preceding paragraph.">
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<p>The HSD17B4 gene encodes an enzyme involved in peroxisomal fatty acid beta-oxidation. It was first identified as a 17-beta-estradiol dehydrogenase (<a href="#14" class="mim-tip-reference" title="Leenders, F., Tesdorpf, J. G., Markus, M., Engel, T., Seedorf, U., Adamski, J. <strong>Porcine 80-kDa protein reveals intrinsic 17 beta-hydroxysteroid dehydrogenase, fatty acyl-CoA-hydratase/dehydrogenase, and sterol transfer activities.</strong> J. Biol. Chem. 271: 5438-5442, 1996.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8621399/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8621399</a>] [<a href="https://doi.org/10.1074/jbc.271.10.5438" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8621399">Leenders et al., 1996</a>; <a href="#25" class="mim-tip-reference" title="van Grunsven, E. G., van Berkel, E., Ijlst, L., Vreken, P., de Klerk, J. B. C., Adamski, J., Lemonde, H., Clayton, P. T., Cuebas, D. A., Wanders, R. J. A. <strong>Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency.</strong> Proc. Nat. Acad. Sci. 95: 2128-2133, 1998.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9482850/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9482850</a>] [<a href="https://doi.org/10.1073/pnas.95.5.2128" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9482850">van Grunsven et al., 1998</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?term=8621399+9482850" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>Multifunctional protein-2 (MFP2), also called D-bifunctional protein, catalyzes the second (hydration) and third (dehydrogenation) reactions of the peroxisomal beta-oxidation of fatty acids and fatty acid derivatives (summary by <a href="#4" class="mim-tip-reference" title="Ferdinandusse, S., Ylianttila, M. S., Gloerich, J., Koski, M. K., Oostheim, W., Waterham, H. R., Hiltunen, J. K., Wanders, R. J. A., Glumoff, T. <strong>Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis.</strong> Am. J. Hum. Genet. 78: 112-124, 2006.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/16385454/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">16385454</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=16385454[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1086/498880" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="16385454">Ferdinandusse et al., 2006</a>). The 2 enzymatic activities of MFP2, enoyl-CoA hydratase and D-3-hydroxyacyl-CoA dehydrogenase, are essential for the oxidation of a wide range of peroxisomal substrates (very long-chain acyl-CoAs, branched-chain acyl-CoAs including pristanoyl-CoA, and bile acid precursors) (summary by <a href="#15" class="mim-tip-reference" title="Lines, M. A., Jobling, R., Brady, L., Marshall, C. R., Scherer, S. W., Rodriguez, A. R., Lee, L., Lang, A. E., Mestre, T. A., Wanders, R. J. A., Ferdinandusse, S., Tarnopolsky, M. A. <strong>Peroxisomal D-bifunctional protein deficiency: three adults diagnosed by whole-exome sequencing.</strong> Neurology 82: 963-968, 2014.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/24553428/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">24553428</a>] [<a href="https://doi.org/10.1212/WNL.0000000000000219" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="24553428">Lines et al., 2014</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?term=24553428+16385454" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>See also the L-bifunctional peroxisomal protein (EHHADH; <a href="/entry/607037">607037</a>). The D- and L-bifunctional proteins have different substrate specificities. The D-bifunctional protein catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids and also acts in shortening cholesterol for bile acid formation. In contrast, the L-specific bifunctional protein does not have the latter 2 activities (<a href="#9" class="mim-tip-reference" title="Jiang, L. L., Kurosawa, T., Sato, M., Suzuki, Y., Hashimoto, T. <strong>Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein.</strong> J. Biochem. 121: 506-513, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9133619/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9133619</a>] [<a href="https://doi.org/10.1093/oxfordjournals.jbchem.a021615" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9133619">Jiang et al., 1997</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9133619" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p><a href="#1" class="mim-tip-reference" title="Adamski, J., Normand, T., Leenders, F., Monte, D., Begue, A., Stehelin, D., Jungblut, P. W., de Launoit, Y. <strong>Molecular cloning of a novel widely expressed human 80 kDa 17-beta-hydroxysteroid dehydrogenase IV.</strong> Biochem. J. 311: 437-443, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7487879/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7487879</a>] [<a href="https://doi.org/10.1042/bj3110437" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="7487879">Adamski et al. (1995)</a> cloned a fourth type of 17-beta-hydroxysteroid dehydrogenase, HSD17B4, from a human liver cDNA library. The HSD17B4 gene encodes a 736-amino acid polypeptide with a predicted molecular mass of approximately 80 kD and less than 25% identity with the 3 previously characterized 17-HSDs (HSD17B1, <a href="/entry/109684">109684</a>; HSD17B2, <a href="/entry/109685">109685</a>; and HSD17B3, <a href="/entry/605573">605573</a>). Northern blot analysis revealed that HSD17B4 is expressed in many tissues as an approximately 3.0-kb mRNA transcript, with highest expression in liver, heart, prostate, and testis. <a href="#1" class="mim-tip-reference" title="Adamski, J., Normand, T., Leenders, F., Monte, D., Begue, A., Stehelin, D., Jungblut, P. W., de Launoit, Y. <strong>Molecular cloning of a novel widely expressed human 80 kDa 17-beta-hydroxysteroid dehydrogenase IV.</strong> Biochem. J. 311: 437-443, 1995.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7487879/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7487879</a>] [<a href="https://doi.org/10.1042/bj3110437" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="7487879">Adamski et al. (1995)</a> overexpressed the gene in mammalian cells and found that HSD17B4 displays specific unidirectional oxidative 17-HSD activity. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=7487879" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#8" class="mim-tip-reference" title="Jiang, L. L., Kobayashi, A., Matsuura, H., Fukushima, H., Hashimoto, T. <strong>Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase.</strong> J. Biochem. 120: 624-632, 1996.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8902629/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8902629</a>] [<a href="https://doi.org/10.1093/oxfordjournals.jbchem.a021458" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8902629">Jiang et al. (1996)</a> purified and characterized a medium-chain enoyl-CoA hydratase from human liver. By immunohistochemistry, they confirmed the presence of the enzyme in peroxisomes of cultured human skin fibroblasts. <a href="#10" class="mim-tip-reference" title="Jiang, L. L., Miyazawa, S., Souri, M., Hashimoto, T. <strong>Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein.</strong> J. Biochem. 121: 364-369, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9089413/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9089413</a>] [<a href="https://doi.org/10.1093/oxfordjournals.jbchem.a021596" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9089413">Jiang et al. (1997)</a> determined the DNA and peptide sequences of medium-chain enoyl-CoA hydratase and found that it was identical to that of human 17-beta-hydroxysteroid dehydrogenase IV. The native enzyme is a 77-kD polypeptide. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=9089413+8902629" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>By analysis of the porcine enzyme, <a href="#14" class="mim-tip-reference" title="Leenders, F., Tesdorpf, J. G., Markus, M., Engel, T., Seedorf, U., Adamski, J. <strong>Porcine 80-kDa protein reveals intrinsic 17 beta-hydroxysteroid dehydrogenase, fatty acyl-CoA-hydratase/dehydrogenase, and sterol transfer activities.</strong> J. Biol. Chem. 271: 5438-5442, 1996.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8621399/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8621399</a>] [<a href="https://doi.org/10.1074/jbc.271.10.5438" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8621399">Leenders et al. (1996)</a> determined that the N-terminal region (residues 1-323) encodes the 17-steroid dehydrogenase activity, whereas the central region (residues 324-596) catalyzes the hydratase activity. The C-terminal portion facilitates the transfer of 7-dehydrocholesterol and phosphatidylcholine between membranes in vitro. The authors emphasized the unique ability of a single protein to catalyze different reactions. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=8621399" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p><a href="#12" class="mim-tip-reference" title="Leenders, F., Dolez, V., Begue, A., Moller, G., Gloeckner, J., de Launoit, Y., Adamski, J. <strong>Structure of the gene for the human 17-beta-hydroxysteroid dehydrogenase type IV.</strong> Mammalian Genome 9: 1036-1041, 1998.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9880674/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9880674</a>] [<a href="https://doi.org/10.1007/s003359900921" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9880674">Leenders et al. (1998)</a> found that the HSD17B4 gene contains 24 exons and spans more than 100 kb. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9880674" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p>By fluorescence in situ hybridization, <a href="#13" class="mim-tip-reference" title="Leenders, F., Prescher, G., Dolez, V., Begue, A., de Launoit, Y., Adamski, J. <strong>Assignment of human 17-beta-hydroxysteroid dehydrogenase IV to chromosome 5q2 by fluorescence in situ hybridization.</strong> Genomics 37: 403-404, 1996.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8938456/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8938456</a>] [<a href="https://doi.org/10.1006/geno.1996.0578" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="8938456">Leenders et al. (1996)</a> mapped the HSD17B4 gene to human chromosome 5q2. <a href="#19" class="mim-tip-reference" title="Novikov, D., Dieuaide-Noubhani, M., Vermeesch, J. R., Fournier, B., Mannaerts, G. P., Van Veldhoven, P. P. <strong>The human peroxisomal multifunctional protein involved in bile acid synthesis: activity measurement, deficiency in Zellweger syndrome and chromosome mapping.</strong> Biochim. Biophys. Acta 1360: 229-240, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9197465/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9197465</a>] [<a href="https://doi.org/10.1016/s0925-4439(97)00003-3" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9197465">Novikov et al. (1997)</a> mapped the HSD17B4 gene to chromosome 5q2.3 by FISH. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=9197465+8938456" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p>Due to the presence of 25-methyl and 24-hydroxyl groups, 4 stereoisomers of varanoyl-CoA are possible. By assaying subcellular fractions of human liver, <a href="#19" class="mim-tip-reference" title="Novikov, D., Dieuaide-Noubhani, M., Vermeesch, J. R., Fournier, B., Mannaerts, G. P., Van Veldhoven, P. P. <strong>The human peroxisomal multifunctional protein involved in bile acid synthesis: activity measurement, deficiency in Zellweger syndrome and chromosome mapping.</strong> Biochim. Biophys. Acta 1360: 229-240, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9197465/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9197465</a>] [<a href="https://doi.org/10.1016/s0925-4439(97)00003-3" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9197465">Novikov et al. (1997)</a> found that peroxisomal MFP2 catalyzed dehydrogenation of 24R,25R-varanoyl-CoA. By a hydratation reaction, MFP2 also catalyzed formation of 24R,25R-varanoyl-CoA. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9197465" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#7" class="mim-tip-reference" title="Green, V. L., Speirs, V., Landolt, A. M., Foy, P. M., Atkin, S. L. <strong>17-beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 expression and enzyme activity in human anterior pituitary adenomas.</strong> J. Clin. Endocr. Metab. 84: 1340-1345, 1999.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10199776/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10199776</a>] [<a href="https://doi.org/10.1210/jcem.84.4.5619" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="10199776">Green et al. (1999)</a> investigated HSD17B1, -2, -3, and -4 gene expression and HSD17B estrogenic activity in human anterior pituitary adenomas. HSD17B mRNA expression was studied by RT-PCR in 42 pituitary tumors and 3 normal pituitaries, HSD17B activity was studied in 11 tumors, and HSD17B1 was immunolocalized in vitro in 6 tumors. HSD17B1 gene expression was detected in 34 of 42 (81%) adenomas in all tumor subtypes; HSD17B2 mRNA was detected in 18 of 42 (43%) adenomas but not in prolactinomas; HSD17B3 mRNA was detected in 12 of 42 (29%) adenomas but not in corticotropinomas; and HSD17B4 was expressed in 20 of 42 (48%) adenomas by all adenoma subtypes. All 4 HSD17B isoforms were variably expressed in human anterior pituitary adenomas, which also showed HSD17B enzyme activity, suggesting that HSD17B may play an important role in regulating the local cellular levels of estradiol. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10199776" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p><strong><em>D-Bifunctional Protein Deficiency</em></strong></p><p>
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In 2 Japanese patients with D-bifunctional protein deficiency (<a href="/entry/261515">261515</a>), <a href="#22" class="mim-tip-reference" title="Suzuki, Y., Jiang, L. L., Souri, M., Miyazawa, S., Fukuda, S., Zhang, Z., Une, M., Shimozawa, N., Kondo, N., Orii, T., Hashimoto, T. <strong>D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified peroxisomal disorder.</strong> Am. J. Hum. Genet. 61: 1153-1162, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9345094/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9345094</a>] [<a href="https://doi.org/10.1086/301599" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9345094">Suzuki et al. (1997)</a> identified 2 different homozygous mutations in the HSD17B4 gene (<a href="#0001">601860.0001</a>; <a href="#0002">601860.0002</a>). The patients had previously been diagnosed with L-bifunctional protein deficiency by complementation analysis (<a href="#23" class="mim-tip-reference" title="Suzuki, Y., Shimozawa, N., Yajima, S., Tomatsu, S., Kondo, N., Nakada, Y., Akaboshi, S., Iai, M., Tanabe, Y., Hashimoto, T., Wanders, R. J. A., Schutgens, R. B. H., Moser, H. W., Orii, T. <strong>Novel subtype of peroxisomal acyl-CoA oxidase deficiency and bifunctional enzyme deficiency with detectable enzyme protein: identification by means of complementation analysis.</strong> Am. J. Hum. Genet. 54: 36-43, 1994.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8279468/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8279468</a>]" pmid="8279468">Suzuki et al., 1994</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?term=8279468+9345094" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>In an infant with a defect in peroxisomal beta-oxidation, <a href="#25" class="mim-tip-reference" title="van Grunsven, E. G., van Berkel, E., Ijlst, L., Vreken, P., de Klerk, J. B. C., Adamski, J., Lemonde, H., Clayton, P. T., Cuebas, D. A., Wanders, R. J. A. <strong>Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency.</strong> Proc. Nat. Acad. Sci. 95: 2128-2133, 1998.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9482850/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9482850</a>] [<a href="https://doi.org/10.1073/pnas.95.5.2128" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9482850">van Grunsven et al. (1998)</a> demonstrated D-bifunctional protein deficiency caused by a homozygous mutation in the HSD17B4 gene (<a href="#0003">601860.0003</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9482850" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>In a patient with D-bifunctional protein deficiency originally reported by <a href="#27" class="mim-tip-reference" title="Watkins, P. A., Chen, W. W., Harris, C. J., Hoefler, G., Hoefler, S., Blake, D. C., Jr., Balfe, A., Kelley, R. I., Moser, A. B., Beard, M. E., Moser, H. W. <strong>Peroxisomal bifunctional enzyme deficiency.</strong> J. Clin. Invest. 83: 771-777, 1989.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2921319/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2921319</a>] [<a href="https://doi.org/10.1172/JCI113956" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2921319">Watkins et al. (1989)</a>, <a href="#26" class="mim-tip-reference" title="van Grunsven, E. G., van Berkel, E., Mooijer, P. A. W., Watkins, P. A., Moser, H. W., Suzuki, Y., Jiang, L. L., Hashimoto, T., Hoefler, G., Adamski, J., Wanders, R. J. A. <strong>Peroxisomal bifunctional protein deficiency revisited: resolution of its true enzymatic and molecular basis.</strong> Am. J. Hum. Genet. 64: 99-107, 1999.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9915948/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9915948</a>] [<a href="https://doi.org/10.1086/302180" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9915948">van Grunsven et al. (1999)</a> identified a homozygous 2-bp deletion in the HSD17B4 gene (<a href="#0007">601860.0007</a>). The patient was originally thought to have L-bifunctional protein deficiency based on immunoblot analysis of postmortem liver tissue. However, reanalysis showed accumulation of both very long chain fatty acids and bile acid intermediates, which was hard to reconcile with an isolated deficiency of the L-bifunctional protein. The results suggested that most, if not all, patients whose peroxisomal disorder had been diagnosed as L-bifunctional protein deficiency were in fact cases of D-bifunctional protein deficiency. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=2921319+9915948" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#18" class="mim-tip-reference" title="Nakano, K., Zhang, Z., Shimozawa, N., Kondo, N., Ishii, N., Funatsuka, M., Shirakawa, S., Itoh, M., Takashima, S., Une, M., Kana-aki, R. R., Mukai, K., Osawa, M., Suzuki, Y. <strong>D-bifunctional protein deficiency with fetal ascites, polyhydramnios, and contractures of hands and toes.</strong> J. Pediat. 139: 865-867, 2001.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11743515/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11743515</a>] [<a href="https://doi.org/10.1067/mpd.2001.119170" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11743515">Nakano et al. (2001)</a> reported a patient with D-bifunctional protein deficiency who was compound heterozygous for 2 mutations in the HSD17B4 gene (<a href="#0001">601860.0001</a> and <a href="#0005">601860.0005</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=11743515" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#3" class="mim-tip-reference" title="Ferdinandusse, S., van Grunsven, E. G., Oostheim, W., Denis, S., Hogenhout, E. M., Ijlst, L., van Roermund, C. W. T., Waterham, H. R., Goldfischer, S., Wanders, R. J. A. <strong>Reinvestigation of peroxisomal 3-ketoacyl-CoA thiolase deficiency: identification of the true defect at the level of D-bifunctional protein.</strong> Am. J. Hum. Genet. 70: 1589-1593, 2002.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11992265/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11992265</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=11992265[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1086/340970" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11992265">Ferdinandusse et al. (2002)</a> reinvestigated the patient of <a href="#6" class="mim-tip-reference" title="Goldfischer, S., Collins, J., Rapin, I., Neumann, P., Neglia, W., Spiro, A. J., Ishii, T., Roels, F., Vamecq, J., Van Hoof, F. <strong>Pseudo-Zellweger syndrome: deficiencies in several peroxisomal oxidative activities.</strong> J. Pediat. 108: 25-32, 1986.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2868085/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2868085</a>] [<a href="https://doi.org/10.1016/s0022-3476(86)80764-8" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2868085">Goldfischer et al. (1986)</a>, who was the only patient ever reported with a presumed deficiency of peroxisomal 3-ketoacyl-CoA thiolase (<a href="/entry/604054">604054</a>). Molecular analysis identified a homozygous deletion in the HSD17B4 gene (<a href="#0006">601860.0006</a>), confirming a diagnosis of D-bifunctional protein deficiency. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=2868085+11992265" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#4" class="mim-tip-reference" title="Ferdinandusse, S., Ylianttila, M. S., Gloerich, J., Koski, M. K., Oostheim, W., Waterham, H. R., Hiltunen, J. K., Wanders, R. J. A., Glumoff, T. <strong>Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis.</strong> Am. J. Hum. Genet. 78: 112-124, 2006.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/16385454/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">16385454</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=16385454[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1086/498880" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="16385454">Ferdinandusse et al. (2006)</a> reported the mutational spectrum of DBP deficiency on the basis of molecular analysis in 110 patients. They identified 61 different mutations by DBP cDNA analysis, 48 of which had not been previously reported. The predicted effects of the different disease-causing amino acid changes in protein structure were determined using the crystal structures. The effects ranged from the replacement of catalytic amino acid residues or residues in direct contact with the substrate or cofactor to disturbances of protein folding or dimerization of the subunits. To study whether there is a genotype-phenotype correlation for DBP deficiency, these structure-based analyses were combined with extensive biochemical analyses of patient material (cultured skin fibroblasts and plasma) and available clinical information on the patients. They found that the effect of the mutations identified in patients with a relatively mild clinical and biochemical presentation was less detrimental to the protein structure than the effect of mutations identified in those with a very severe presentation. These results suggested that the amount of residual DBP activity correlates with the severity of the phenotype. Thus the data indicated that on the basis of the predicted effect of mutations on protein structure, a genotype-phenotype correlation exists for DBP deficiency. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=16385454" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#4" class="mim-tip-reference" title="Ferdinandusse, S., Ylianttila, M. S., Gloerich, J., Koski, M. K., Oostheim, W., Waterham, H. R., Hiltunen, J. K., Wanders, R. J. A., Glumoff, T. <strong>Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis.</strong> Am. J. Hum. Genet. 78: 112-124, 2006.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/16385454/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">16385454</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=16385454[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1086/498880" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="16385454">Ferdinandusse et al. (2006)</a> found that the missense mutation G16S (<a href="#0003">601860.0003</a>) is by far the most common mutation causing DBP deficiency (type III), which had in their study an allele frequency of approximately 24% and was detected in 28 of the 110 patients. The second most common mutation causing DBP deficiency (type II) was the missense mutation N457Y (<a href="#0004">601860.0004</a>), which had an allele frequency of approximately 11% and was found in 13 patients. Of 5 patients for whom homozygosity was checked, 2 turned out to be heterozygotes at the genomic level. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=16385454" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>In DBP type I-deficient patients, <a href="#4" class="mim-tip-reference" title="Ferdinandusse, S., Ylianttila, M. S., Gloerich, J., Koski, M. K., Oostheim, W., Waterham, H. R., Hiltunen, J. K., Wanders, R. J. A., Glumoff, T. <strong>Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis.</strong> Am. J. Hum. Genet. 78: 112-124, 2006.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/16385454/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">16385454</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=16385454[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1086/498880" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="16385454">Ferdinandusse et al. (2006)</a> found only deletions, insertions, and nonsense mutations. All deletions resulted in a truncated protein, except for 3 large in-frame deletions. Two patients with DBP type-II deficiency had in-frame deletions in the hydratase unit. All other DBP type II-deficient patients had missense mutations in the coding region of the DBP hydratase unit. DBP type III deficiency was predominantly caused by missense mutations and, in 2 cases, by a 1-amino acid deletion in the coding region of the dehydrogenase unit. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=16385454" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><strong><em>Perrault Syndrome 1</em></strong></p><p>
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<a href="#20" class="mim-tip-reference" title="Pierce, S. B., Walsh, T., Chisholm, K. M., Lee, M, K., Thornton, A. M., Fiumara, A., Opitz, J. M., Levy-Lahad, E., Klevit, R. E., King, M.-C. <strong>Mutations in the DBP-deficiency protein HSD17B4 cause ovarian dysgenesis, hearing loss, and ataxia of Perrault syndrome.</strong> Am. J. Hum. Genet. 87: 282-288, 2010.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/20673864/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">20673864</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=20673864[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1016/j.ajhg.2010.07.007" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="20673864">Pierce et al. (2010)</a> performed whole-exome sequencing of genomic DNA from a woman with Perrault syndrome-1 (PRLTS1; <a href="/entry/233400">233400</a>), which is characterized by ovarian dysgenesis and sensorineural deafness, originally described by <a href="#16" class="mim-tip-reference" title="McCarthy, D. J., Opitz, J. M. <strong>Perrault syndrome in sisters.</strong> Am. J. Med. Genet. 22: 629-631, 1985.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/4061497/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">4061497</a>] [<a href="https://doi.org/10.1002/ajmg.1320220324" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="4061497">McCarthy and Opitz (1985)</a> and identified 2 rare variants in the HSD17B4 gene (<a href="#0008">601860.0008</a> and <a href="#0009">601860.0009</a>). Sequencing revealed that both the proband and her affected sister were compound heterozygous for the missense (Y217C) and nonsense (Y568X) mutations, and that their unaffected mother was heterozygous for the missense mutation. <a href="#20" class="mim-tip-reference" title="Pierce, S. B., Walsh, T., Chisholm, K. M., Lee, M, K., Thornton, A. M., Fiumara, A., Opitz, J. M., Levy-Lahad, E., Klevit, R. E., King, M.-C. <strong>Mutations in the DBP-deficiency protein HSD17B4 cause ovarian dysgenesis, hearing loss, and ataxia of Perrault syndrome.</strong> Am. J. Hum. Genet. 87: 282-288, 2010.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/20673864/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">20673864</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=20673864[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1016/j.ajhg.2010.07.007" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="20673864">Pierce et al. (2010)</a> noted that Perrault syndrome and DBP deficiency overlap clinically, and suggested that mutations in HSD17B4 leading to DBP deficiency that is mild enough to allow survival to the age of puberty are likely to cause ovarian dysgenesis in females in addition to the known neurologic defects. The authors predicted that because the affected sisters were likely to express only protein with the Y217C mutation, they would have so-called type III DBP deficiency, with a defect in dehydrogenase activity. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=20673864+4061497" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>In 2 brothers of European descent with Perrault syndrome, <a href="#17" class="mim-tip-reference" title="McMillan, H. J., Worthylake, T., Schwartzentruber, J., Gottlieb, C. C., Lawrence, S. E., MacKenzie, A., Beaulieu, C. L., Mooyer, P. A. W., FORGE Canada Consortium, Wanders, R. J. A., Majewski, J., Bulman, D. E., Geraghty, M. T., Ferdinandusse, S., Boycott, K. M. <strong>Specific combination of compound heterozygous mutations in 17-beta-hydroxysteroid dehydrogenase type 4 (HD17B4) defines a new subtype of D-bifunctional protein deficiency.</strong> Orphanet J. Rare Dis. 7: 90, 2012. Note: Electronic Article.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/23181892/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">23181892</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=23181892[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1186/1750-1172-7-90" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="23181892">McMillan et al. (2012)</a> identified compound heterozygous mutations in the HSD17B4 gene (A34V, <a href="#0010">601860.0010</a> and I516T, <a href="#0011">601860.0011</a>). Each mutation affected a different domain, dehydrogenase and hydratase, respectively. The mutations, which were found by exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=23181892" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p>In 3 Italian sibs with Perrault syndrome, <a href="#15" class="mim-tip-reference" title="Lines, M. A., Jobling, R., Brady, L., Marshall, C. R., Scherer, S. W., Rodriguez, A. R., Lee, L., Lang, A. E., Mestre, T. A., Wanders, R. J. A., Ferdinandusse, S., Tarnopolsky, M. A. <strong>Peroxisomal D-bifunctional protein deficiency: three adults diagnosed by whole-exome sequencing.</strong> Neurology 82: 963-968, 2014.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/24553428/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">24553428</a>] [<a href="https://doi.org/10.1212/WNL.0000000000000219" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="24553428">Lines et al. (2014)</a> identified compound heterozygous missense mutations in the HSD17B4 gene (P513L, <a href="#0012">601860.0012</a> and R543P, <a href="#0013">601860.0013</a>), both affecting the hydratase domain. The mutations were found by whole-exome sequencing. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=24553428" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p><a href="#2" class="mim-tip-reference" title="Baes, M., Huyghe, S., Carmeliet, P., Declercq, P. E., Collen, D., Mannaerts, G. P., Van Veldhoven, P. P. <strong>Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids.</strong> J. Biol. Chem. 275: 16329-16336, 2000.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10748062/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10748062</a>] [<a href="https://doi.org/10.1074/jbc.M001994200" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="10748062">Baes et al. (2000)</a> obtained Mfp2 -/- mice at the expected mendelian ratio. At birth, Mfp2 -/- mice were indistinguishable from wildtype or Mfp2 +/- littermates, but Mfp2 -/- pups failed to thrive, and about one-third died within the first 12 days of life. At weaning, surviving Mfp2 -/- pups resumed weight gain. Adult Mfp2 -/-females were fertile, but Mfp2 -/- males were subfertile. Mfp2 -/- mice accumulated very long chain fatty acids in brain and liver phospholipids, as well as immature C27 bile acids in bile. Dietary supplementation with phytol, a tetramethyl-branched fatty alcohol, revealed accumulation of branched chain fatty acids in Mfp2 -/- mice, concomitant with severe weight loss and development of cataracts and ataxia. Oxidation of long chain fatty acids was enhanced in liver of Mfp2 -/- mice, suggesting compensatory increased Mfp1 (EHHADH; <a href="/entry/607037">607037</a>) activity. Mature C24 bile acids were found in adult Mfp2 -/- mice, suggesting bile acid formation by alternative pathways. <a href="#2" class="mim-tip-reference" title="Baes, M., Huyghe, S., Carmeliet, P., Declercq, P. E., Collen, D., Mannaerts, G. P., Van Veldhoven, P. P. <strong>Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids.</strong> J. Biol. Chem. 275: 16329-16336, 2000.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10748062/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10748062</a>] [<a href="https://doi.org/10.1074/jbc.M001994200" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="10748062">Baes et al. (2000)</a> concluded that MFP2 degrades 2-methyl-branched fatty acids, bile acid intermediates, and very long chain fatty acids. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10748062" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=601860[MIM]" class="btn btn-default mim-tip-hint" role="button" title="ClinVar aggregates information about sequence variation and its relationship to human health." target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">ClinVar</a>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs1554065670 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs1554065670;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs1554065670" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs1554065670" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<p>In a Japanese patient with D-bifunctional protein deficiency (<a href="/entry/261515">261515</a>), <a href="#22" class="mim-tip-reference" title="Suzuki, Y., Jiang, L. L., Souri, M., Miyazawa, S., Fukuda, S., Zhang, Z., Une, M., Shimozawa, N., Kondo, N., Orii, T., Hashimoto, T. <strong>D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified peroxisomal disorder.</strong> Am. J. Hum. Genet. 61: 1153-1162, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9345094/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9345094</a>] [<a href="https://doi.org/10.1086/301599" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9345094">Suzuki et al. (1997)</a> identified a 52-bp deletion in the HSD17B4 gene, resulting in a 17-amino acid deletion and premature termination. Studies of postmortem liver tissue confirmed absence of the activity and immunoreactivity of D-bifunctional protein. The patient was previously thought to have L-bifunctional protein deficiency (<a href="#23" class="mim-tip-reference" title="Suzuki, Y., Shimozawa, N., Yajima, S., Tomatsu, S., Kondo, N., Nakada, Y., Akaboshi, S., Iai, M., Tanabe, Y., Hashimoto, T., Wanders, R. J. A., Schutgens, R. B. H., Moser, H. W., Orii, T. <strong>Novel subtype of peroxisomal acyl-CoA oxidase deficiency and bifunctional enzyme deficiency with detectable enzyme protein: identification by means of complementation analysis.</strong> Am. J. Hum. Genet. 54: 36-43, 1994.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8279468/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8279468</a>]" pmid="8279468">Suzuki et al., 1994</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?term=8279468+9345094" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<p>In a Japanese patient with D-bifunctional protein deficiency (<a href="/entry/261515">261515</a>), <a href="#22" class="mim-tip-reference" title="Suzuki, Y., Jiang, L. L., Souri, M., Miyazawa, S., Fukuda, S., Zhang, Z., Une, M., Shimozawa, N., Kondo, N., Orii, T., Hashimoto, T. <strong>D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified peroxisomal disorder.</strong> Am. J. Hum. Genet. 61: 1153-1162, 1997.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9345094/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9345094</a>] [<a href="https://doi.org/10.1086/301599" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9345094">Suzuki et al. (1997)</a> identified a 237-bp deletion in the HSD17B4 gene, resulting in a 79-amino acid deletion. Studies of postmortem liver tissue confirmed absence of the activity and immunoreactivity of D-bifunctional protein. The patient was previously thought to have L-bifunctional protein deficiency (<a href="#23" class="mim-tip-reference" title="Suzuki, Y., Shimozawa, N., Yajima, S., Tomatsu, S., Kondo, N., Nakada, Y., Akaboshi, S., Iai, M., Tanabe, Y., Hashimoto, T., Wanders, R. J. A., Schutgens, R. B. H., Moser, H. W., Orii, T. <strong>Novel subtype of peroxisomal acyl-CoA oxidase deficiency and bifunctional enzyme deficiency with detectable enzyme protein: identification by means of complementation analysis.</strong> Am. J. Hum. Genet. 54: 36-43, 1994.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8279468/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8279468</a>]" pmid="8279468">Suzuki et al., 1994</a>). <a href="https://pubmed.ncbi.nlm.nih.gov/?term=8279468+9345094" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs137853096 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs137853096;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs137853096?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs137853096" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs137853096" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000008094 OR RCV000415821 OR RCV000688945 OR RCV000779455 OR RCV001197145 OR RCV002512888 OR RCV005031420" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000008094, RCV000415821, RCV000688945, RCV000779455, RCV001197145, RCV002512888, RCV005031420" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000008094...</a>
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<p>In an infant with a D-bifunctional protein deficiency (<a href="/entry/261515">261515</a>), <a href="#25" class="mim-tip-reference" title="van Grunsven, E. G., van Berkel, E., Ijlst, L., Vreken, P., de Klerk, J. B. C., Adamski, J., Lemonde, H., Clayton, P. T., Cuebas, D. A., Wanders, R. J. A. <strong>Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency.</strong> Proc. Nat. Acad. Sci. 95: 2128-2133, 1998.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9482850/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9482850</a>] [<a href="https://doi.org/10.1073/pnas.95.5.2128" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9482850">van Grunsven et al. (1998)</a> identified a 46G-A transition in the HSD17B4 gene, resulting in a gly16-to-ser (G16S) substitution within an important loop of the Rossman fold forming the NAD(+)-binding site. Biochemical analysis showed that the 3-hydroxyacyl-CoA dehydrogenase activity of the D-bifunctional protein was completely inactive, whereas the enoyl-CoA hydratase component was active. Their findings showed that the D-bifunctional protein plays an essential role in the peroxisomal beta-oxidation pathway that cannot be compensated for by the L-specific bifunctional protein. Both parents were heterozygous for the mutation. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9482850" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p><p><a href="#26" class="mim-tip-reference" title="van Grunsven, E. G., van Berkel, E., Mooijer, P. A. W., Watkins, P. A., Moser, H. W., Suzuki, Y., Jiang, L. L., Hashimoto, T., Hoefler, G., Adamski, J., Wanders, R. J. A. <strong>Peroxisomal bifunctional protein deficiency revisited: resolution of its true enzymatic and molecular basis.</strong> Am. J. Hum. Genet. 64: 99-107, 1999.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9915948/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9915948</a>] [<a href="https://doi.org/10.1086/302180" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9915948">Van Grunsven et al. (1999)</a> demonstrated the G16S mutation in 9 additional patients previously thought to have deficiency of L-bifunctional protein on the basis of complementation studies. The findings confirmed D-bifunctional protein deficiency in these cases. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9915948" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<strong>.0004 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
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HSD17B4, ASN457TYR
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs137853097 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs137853097;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs137853097?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs137853097" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs137853097" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000008095 OR RCV000385297 OR RCV000477799 OR RCV000684773 OR RCV001002204" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000008095, RCV000385297, RCV000477799, RCV000684773, RCV001002204" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000008095...</a>
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<p>In 2 unrelated patients with D-bifunctional protein deficiency (<a href="/entry/261515">261515</a>), <a href="#24" class="mim-tip-reference" title="van Grunsven, E. G., Mooijer, P. A. W., Aubourg, P., Wanders, R. J. A. <strong>Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency.</strong> Hum. Molec. Genet. 8: 1509-1516, 1999.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10400999/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10400999</a>] [<a href="https://doi.org/10.1093/hmg/8.8.1509" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="10400999">van Grunsven et al. (1999)</a> identified a homozygous 1369A-T transversion in the HSD17B4 gene, resulting in an asn457-to-tyr (N457Y) substitution. Both patients had an isolated defect of the enoyl-CoA hydratase domain of the D-bifunctional protein. Both patients had abnormalities of peroxisomal beta-oxidation with elevated very long chain fatty acids and branch chain fatty acids, but normal levels of bile acid intermediates. Both patients were born of consanguineous parents. Sequence analysis of the D-bifunctional protein cDNA of 15 control subjects of Caucasian origin did not identify the N457Y mutation. Expression of the N457Y mutation in Saccharomyces cerevisiae confirmed that it is the disease-causing mutation. Immunoblot analysis of patient fibroblast homogenates showed that the protein levels of full-length D-bifunctional protein were strongly reduced, while the enoyl-CoA hydratase component produced after processing within the peroxisome was undetectable, indicating that the mutation leads to an unstable protein. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10400999" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a id="0005" class="mim-anchor"></a>
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<span class="mim-font">
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<strong>.0005 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
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HSD17B4, ARG106PRO
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs25640 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs25640;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs25640?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs25640" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs25640" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<span class="mim-text-font">
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000008096" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000008096" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000008096</a>
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<p>In a male patient with D-bifunctional protein deficiency (<a href="/entry/261515">261515</a>), <a href="#18" class="mim-tip-reference" title="Nakano, K., Zhang, Z., Shimozawa, N., Kondo, N., Ishii, N., Funatsuka, M., Shirakawa, S., Itoh, M., Takashima, S., Une, M., Kana-aki, R. R., Mukai, K., Osawa, M., Suzuki, Y. <strong>D-bifunctional protein deficiency with fetal ascites, polyhydramnios, and contractures of hands and toes.</strong> J. Pediat. 139: 865-867, 2001.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11743515/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11743515</a>] [<a href="https://doi.org/10.1067/mpd.2001.119170" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11743515">Nakano et al. (2001)</a> identified compound heterozygosity for 2 mutations in the HSD17B4 gene: a 317G-C transversion, resulting in an arg106-to-pro (R106P) substitution, and a 52-bp deletion (<a href="#0001">601860.0001</a>). The mutations were associated with complete loss of function of the protein. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=11743515" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a id="0006" class="mim-anchor"></a>
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<h4>
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<span class="mim-font">
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<strong>.0006 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
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</span>
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</h4>
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HSD17B4, 138-BP DEL
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000008097" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000008097" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000008097</a>
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<p>In a patient with D-bifunctional protein deficiency (<a href="/entry/261515">261515</a>), <a href="#3" class="mim-tip-reference" title="Ferdinandusse, S., van Grunsven, E. G., Oostheim, W., Denis, S., Hogenhout, E. M., Ijlst, L., van Roermund, C. W. T., Waterham, H. R., Goldfischer, S., Wanders, R. J. A. <strong>Reinvestigation of peroxisomal 3-ketoacyl-CoA thiolase deficiency: identification of the true defect at the level of D-bifunctional protein.</strong> Am. J. Hum. Genet. 70: 1589-1593, 2002.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11992265/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11992265</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=11992265[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1086/340970" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="11992265">Ferdinandusse et al. (2002)</a> identified a homozygous 138-bp deletion in the HSD17B4 gene extending from basepair 145 in exon 3 through the first 63 basepairs of intron 3 of the DBP gene. This deletion resulted in skipping of exon 3. The patient had originally been reported by <a href="#6" class="mim-tip-reference" title="Goldfischer, S., Collins, J., Rapin, I., Neumann, P., Neglia, W., Spiro, A. J., Ishii, T., Roels, F., Vamecq, J., Van Hoof, F. <strong>Pseudo-Zellweger syndrome: deficiencies in several peroxisomal oxidative activities.</strong> J. Pediat. 108: 25-32, 1986.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2868085/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2868085</a>] [<a href="https://doi.org/10.1016/s0022-3476(86)80764-8" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2868085">Goldfischer et al. (1986)</a> and <a href="#21" class="mim-tip-reference" title="Schram, A. W., Goldfischer, S., van Roermund, C. W. T., Brouwer-Kelder, E. M., Collins, J., Hashimoto, T., Heymans, H. S. A., van den Bosch, H., Schutgens, R. B. H., Tager, J. M., Wanders, R. J. A. <strong>Human peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency.</strong> Proc. Nat. Acad. Sci. 84: 2494-2496, 1987.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2882519/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2882519</a>] [<a href="https://doi.org/10.1073/pnas.84.8.2494" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2882519">Schram et al. (1987)</a> as the only patient ever reported to have peroxisomal 3-ketoacyl-CoA thiolase (<a href="/entry/604054">604054</a>) deficiency. However, reanalysis showed normal thiolase and absence of the D-bifunctional protein in brain tissue. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=2882519+2868085+11992265" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a id="0007" class="mim-anchor"></a>
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<h4>
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<strong>.0007 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
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</h4>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs775832137 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs775832137;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs775832137?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs775832137" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs775832137" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000008098" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000008098" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000008098</a>
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<p>In a patient with D-bifunctional protein deficiency (<a href="/entry/261515">261515</a>) originally reported by <a href="#27" class="mim-tip-reference" title="Watkins, P. A., Chen, W. W., Harris, C. J., Hoefler, G., Hoefler, S., Blake, D. C., Jr., Balfe, A., Kelley, R. I., Moser, A. B., Beard, M. E., Moser, H. W. <strong>Peroxisomal bifunctional enzyme deficiency.</strong> J. Clin. Invest. 83: 771-777, 1989.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2921319/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2921319</a>] [<a href="https://doi.org/10.1172/JCI113956" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="2921319">Watkins et al. (1989)</a>, <a href="#26" class="mim-tip-reference" title="van Grunsven, E. G., van Berkel, E., Mooijer, P. A. W., Watkins, P. A., Moser, H. W., Suzuki, Y., Jiang, L. L., Hashimoto, T., Hoefler, G., Adamski, J., Wanders, R. J. A. <strong>Peroxisomal bifunctional protein deficiency revisited: resolution of its true enzymatic and molecular basis.</strong> Am. J. Hum. Genet. 64: 99-107, 1999.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9915948/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9915948</a>] [<a href="https://doi.org/10.1086/302180" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="9915948">van Grunsven et al. (1999)</a> identified a homozygous 2-bp deletion (422delAG) in the HSD17B4 gene, resulting in a premature stop codon at position 490 and a shortened protein of 163 amino acids. The patient was originally thought to have L-bifunctional protein deficiency. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=2921319+9915948" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs387906825 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs387906825;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs387906825" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs387906825" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000023152 OR RCV002513181 OR RCV003330398" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000023152, RCV002513181, RCV003330398" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000023152...</a>
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<p>In 2 sisters with Perrault syndrome (PRLTS1; <a href="/entry/233400">233400</a>), previously described by <a href="#16" class="mim-tip-reference" title="McCarthy, D. J., Opitz, J. M. <strong>Perrault syndrome in sisters.</strong> Am. J. Med. Genet. 22: 629-631, 1985.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/4061497/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">4061497</a>] [<a href="https://doi.org/10.1002/ajmg.1320220324" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="4061497">McCarthy and Opitz (1985)</a> and <a href="#5" class="mim-tip-reference" title="Fiumara, A., Sorge, G., Toscano, A., Parano, E., Pavone, L., Opitz, J. M. <strong>Perrault syndrome: evidence for progressive nervous system involvement.</strong> Am. J. Med. Genet. 128A: 246-249, 2004.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/15216544/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">15216544</a>] [<a href="https://doi.org/10.1002/ajmg.a.20616" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="15216544">Fiumara et al. (2004)</a>, <a href="#20" class="mim-tip-reference" title="Pierce, S. B., Walsh, T., Chisholm, K. M., Lee, M, K., Thornton, A. M., Fiumara, A., Opitz, J. M., Levy-Lahad, E., Klevit, R. E., King, M.-C. <strong>Mutations in the DBP-deficiency protein HSD17B4 cause ovarian dysgenesis, hearing loss, and ataxia of Perrault syndrome.</strong> Am. J. Hum. Genet. 87: 282-288, 2010.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/20673864/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">20673864</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=20673864[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1016/j.ajhg.2010.07.007" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="20673864">Pierce et al. (2010)</a> identified compound heterozygosity for a 605A-G transition in exon 9 of the HSD17B4 gene, resulting in a tyr217-to-cys (Y217C) substitution in a very highly conserved region of the protein, and a 1704T-A transversion in exon 20, resulting in a tyr568-to-ter (Y568X; <a href="#0009">601860.0009</a>) substitution. Their unaffected mother was found to be heterozygous for the Y217C mutation, and neither mutation was detected in 1,092 control individuals. Expression analysis using lymphoblast cDNA showed that Y568X transcript was expressed at very low levels relative to the Y217C transcript, suggesting that Y568X undergoes nonsense-mediated decay, whereas Y217C is more stably expressed. <a href="https://pubmed.ncbi.nlm.nih.gov/?term=20673864+15216544+4061497" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs1038744864 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs1038744864;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs1038744864?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs1038744864" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs1038744864" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000023153 OR RCV000811384 OR RCV001260323 OR RCV001556667 OR RCV002538095 OR RCV005047098" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000023153, RCV000811384, RCV001260323, RCV001556667, RCV002538095, RCV005047098" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000023153...</a>
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<p>For discussion of the tyr568-to-ter (Y568X) mutation in the HSD17B4 gene that was found in compound heterozygous state in 2 sisters with Perrault syndrome (PRLTS1; <a href="/entry/233400">233400</a>) by <a href="#20" class="mim-tip-reference" title="Pierce, S. B., Walsh, T., Chisholm, K. M., Lee, M, K., Thornton, A. M., Fiumara, A., Opitz, J. M., Levy-Lahad, E., Klevit, R. E., King, M.-C. <strong>Mutations in the DBP-deficiency protein HSD17B4 cause ovarian dysgenesis, hearing loss, and ataxia of Perrault syndrome.</strong> Am. J. Hum. Genet. 87: 282-288, 2010.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/20673864/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">20673864</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=20673864[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1016/j.ajhg.2010.07.007" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="20673864">Pierce et al. (2010)</a>, see <a href="#0008">601860.0008</a>. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=20673864" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs587777442 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs587777442;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs587777442?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs587777442" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs587777442" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000125465 OR RCV001092766 OR RCV001810425 OR RCV003764860 OR RCV004567068" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000125465, RCV001092766, RCV001810425, RCV003764860, RCV004567068" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000125465...</a>
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<p>In 2 teenaged brothers of European descent with Perrault syndrome (PRLTS1; <a href="/entry/233400">233400</a>), <a href="#17" class="mim-tip-reference" title="McMillan, H. J., Worthylake, T., Schwartzentruber, J., Gottlieb, C. C., Lawrence, S. E., MacKenzie, A., Beaulieu, C. L., Mooyer, P. A. W., FORGE Canada Consortium, Wanders, R. J. A., Majewski, J., Bulman, D. E., Geraghty, M. T., Ferdinandusse, S., Boycott, K. M. <strong>Specific combination of compound heterozygous mutations in 17-beta-hydroxysteroid dehydrogenase type 4 (HD17B4) defines a new subtype of D-bifunctional protein deficiency.</strong> Orphanet J. Rare Dis. 7: 90, 2012. Note: Electronic Article.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/23181892/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">23181892</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=23181892[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1186/1750-1172-7-90" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="23181892">McMillan et al. (2012)</a> identified compound heterozygous mutations in the HSD17B4 gene: a c.101C-T transition, resulting in an ala34-to-val (A34V) substitution in the dehydrogenase domain, and a c.1547T-C transition, resulting in an ile516-to-thr (I516T; <a href="#0011">601860.0011</a>) substitution in the hydratase domain. The mutations, which were found by exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. <a href="#17" class="mim-tip-reference" title="McMillan, H. J., Worthylake, T., Schwartzentruber, J., Gottlieb, C. C., Lawrence, S. E., MacKenzie, A., Beaulieu, C. L., Mooyer, P. A. W., FORGE Canada Consortium, Wanders, R. J. A., Majewski, J., Bulman, D. E., Geraghty, M. T., Ferdinandusse, S., Boycott, K. M. <strong>Specific combination of compound heterozygous mutations in 17-beta-hydroxysteroid dehydrogenase type 4 (HD17B4) defines a new subtype of D-bifunctional protein deficiency.</strong> Orphanet J. Rare Dis. 7: 90, 2012. Note: Electronic Article.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/23181892/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">23181892</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=23181892[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1186/1750-1172-7-90" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="23181892">McMillan et al. (2012)</a> postulated that the relatively mild phenotype was due to the fact that only 1 of the functional HSD17B4 domains was affected on each allele. There was reduced but detectable DBP hydratase and dehydrogenase activity, with some reduction of pristanic acid beta-oxidation in patient fibroblasts. The 45-kD DBP fragment was not detected by immunoblot analysis; however, peroxisomes and plasma very long-chain and branched fatty acids were normal. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=23181892" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs587777443 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs587777443;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs587777443" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs587777443" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000125466 OR RCV000672665 OR RCV000825530 OR RCV001849905 OR RCV003144135 OR RCV005031635" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000125466, RCV000672665, RCV000825530, RCV001849905, RCV003144135, RCV005031635" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000125466...</a>
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<p>For discussion of the ile516-to-thr (I516T) mutation in the HSD17B4 gene that was found in compound heterozygous state in 2 brothers with Perrault syndrome (PRLTS1; <a href="/entry/233400">233400</a>) by <a href="#17" class="mim-tip-reference" title="McMillan, H. J., Worthylake, T., Schwartzentruber, J., Gottlieb, C. C., Lawrence, S. E., MacKenzie, A., Beaulieu, C. L., Mooyer, P. A. W., FORGE Canada Consortium, Wanders, R. J. A., Majewski, J., Bulman, D. E., Geraghty, M. T., Ferdinandusse, S., Boycott, K. M. <strong>Specific combination of compound heterozygous mutations in 17-beta-hydroxysteroid dehydrogenase type 4 (HD17B4) defines a new subtype of D-bifunctional protein deficiency.</strong> Orphanet J. Rare Dis. 7: 90, 2012. Note: Electronic Article.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/23181892/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">23181892</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=23181892[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>] [<a href="https://doi.org/10.1186/1750-1172-7-90" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="23181892">McMillan et al. (2012)</a>, see <a href="#0010">601860.0010</a>. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=23181892" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown">rs587777444 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs587777444;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs587777444" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs587777444" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000125467 OR RCV000675096" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000125467, RCV000675096" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000125467...</a>
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<p>In 3 Italian sibs, including 2 sisters, with Perrault syndrome (PRLTS1; <a href="/entry/233400">233400</a>), <a href="#15" class="mim-tip-reference" title="Lines, M. A., Jobling, R., Brady, L., Marshall, C. R., Scherer, S. W., Rodriguez, A. R., Lee, L., Lang, A. E., Mestre, T. A., Wanders, R. J. A., Ferdinandusse, S., Tarnopolsky, M. A. <strong>Peroxisomal D-bifunctional protein deficiency: three adults diagnosed by whole-exome sequencing.</strong> Neurology 82: 963-968, 2014.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/24553428/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">24553428</a>] [<a href="https://doi.org/10.1212/WNL.0000000000000219" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="24553428">Lines et al. (2014)</a> identified compound heterozygous mutations in the HSD17B4 gene: a c.1537C-A transversion, resulting in a pro513-to-leu (P513L) substitution, and a c.1628G-C transversion, resulting in an arg543-to-pro (R543P; <a href="#0013">601860.0013</a>) substitution. The mutations, which were found by whole-exome sequencing, occurred at highly conserved residues within the active site of the hydratase domain and segregated with the disorder in the family. They were filtered against the dbSNP, 1000 Genomes Project, and Exome Variant Server databases, as well as 130 local control exomes. Immunoblot analysis of patient cells showed markedly reduced DBP enoyl-CoA hydratase activity, as well as absence of the 45-kD posttranslational fragment containing the hydratase domain. Laboratory studies of all patients showed increased serum total bile acids, but phytanic and very long-chain fatty acids were normal. Patient fibroblasts showed decreased beta-oxidation of pristanic acid. Peroxisome morphology was normal. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=24553428" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<div class="btn-group"> <button type="button" class="btn btn-default btn-xs dropdown-toggle mim-font" data-toggle="dropdown"><span class="text-primary">●</span> rs201009485 <span class="caret"></span></button> <ul class="dropdown-menu"> <li><a href="https://www.ensembl.org/Homo_sapiens/Variation/Summary?v=rs201009485;toggle_HGVS_names=open" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'ensembl.org'})">Ensembl</a></li> <li><a href="https://gnomad.broadinstitute.org/variant/rs201009485?dataset=gnomad_r2_1" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'gnomad.broadinstitute.org'})" style="padding-left: 8px;"><span class="text-primary">●</span> gnomAD</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/snp/?term=rs201009485" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'www.ncbi.nlm.nih.gov'})">NCBI</a></li> <li><a href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&db=hg38&clinvar=pack&omimAvSnp=pack&position=rs201009485" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'dbSNP', 'domain': 'genome.ucsc.edu'})">UCSC</a></li> </ul> </div>
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<a href="https://www.ncbi.nlm.nih.gov/clinvar?term=RCV000125468 OR RCV000730879 OR RCV001849906 OR RCV003467098" target="_blank" class="btn btn-default btn-xs mim-tip-hint" title="RCV000125468, RCV000730879, RCV001849906, RCV003467098" onclick="gtag('event', 'mim_outbound', {'name': 'ClinVar', 'domain': 'ncbi.nlm.nih.gov'})">RCV000125468...</a>
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<p>For discussion of the arg543-to-pro (R543P) mutation in the HSD17B4 gene that was found in compound heterozygous state in sibs with Perrault syndrome (PRLTS1; <a href="/entry/233400">233400</a>) by <a href="#15" class="mim-tip-reference" title="Lines, M. A., Jobling, R., Brady, L., Marshall, C. R., Scherer, S. W., Rodriguez, A. R., Lee, L., Lang, A. E., Mestre, T. A., Wanders, R. J. A., Ferdinandusse, S., Tarnopolsky, M. A. <strong>Peroxisomal D-bifunctional protein deficiency: three adults diagnosed by whole-exome sequencing.</strong> Neurology 82: 963-968, 2014.[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/24553428/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">24553428</a>] [<a href="https://doi.org/10.1212/WNL.0000000000000219" target="_blank" onclick="gtag('event', 'mim_outbound', {'destination': 'Publisher'})">Full Text</a>]" pmid="24553428">Lines et al. (2014)</a>, see <a href="#0012">601860.0012</a>. <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=24553428" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})"><span class="glyphicon glyphicon-plus-sign mim-tip-hint" title="Click this 'reference-plus' icon to see articles related to this paragraph in PubMed."></span></a></p>
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<a href="#Lazarow1976" class="mim-tip-reference" title="Lazarow, P. B., de Duve, C. <strong>A fatty acyl-CoA oxidizing system in rat liver peroxisomes: enhancement by clofibrate, a hypolipidemic drug.</strong> Proc. Nat. Acad. Sci. 73: 2043-2046, 1976.">Lazarow and de Duve (1976)</a>
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Adamski, J., Normand, T., Leenders, F., Monte, D., Begue, A., Stehelin, D., Jungblut, P. W., de Launoit, Y.
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<strong>Molecular cloning of a novel widely expressed human 80 kDa 17-beta-hydroxysteroid dehydrogenase IV.</strong>
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Biochem. J. 311: 437-443, 1995.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/7487879/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">7487879</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=7487879" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1042/bj3110437" target="_blank">Full Text</a>]
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Baes, M., Huyghe, S., Carmeliet, P., Declercq, P. E., Collen, D., Mannaerts, G. P., Van Veldhoven, P. P.
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<strong>Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids.</strong>
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J. Biol. Chem. 275: 16329-16336, 2000.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10748062/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10748062</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10748062" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1074/jbc.M001994200" target="_blank">Full Text</a>]
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Ferdinandusse, S., van Grunsven, E. G., Oostheim, W., Denis, S., Hogenhout, E. M., Ijlst, L., van Roermund, C. W. T., Waterham, H. R., Goldfischer, S., Wanders, R. J. A.
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<strong>Reinvestigation of peroxisomal 3-ketoacyl-CoA thiolase deficiency: identification of the true defect at the level of D-bifunctional protein.</strong>
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Am. J. Hum. Genet. 70: 1589-1593, 2002.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/11992265/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">11992265</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=11992265[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=11992265" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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Ferdinandusse, S., Ylianttila, M. S., Gloerich, J., Koski, M. K., Oostheim, W., Waterham, H. R., Hiltunen, J. K., Wanders, R. J. A., Glumoff, T.
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<strong>Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis.</strong>
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Am. J. Hum. Genet. 78: 112-124, 2006.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/16385454/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">16385454</a>, <a href="https://www.ncbi.nlm.nih.gov/pmc/?term=16385454[PMID]&report=imagesdocsum" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Image', 'domain': 'ncbi.nlm.nih.gov'})">images</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=16385454" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1086/498880" target="_blank">Full Text</a>]
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Fiumara, A., Sorge, G., Toscano, A., Parano, E., Pavone, L., Opitz, J. M.
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<strong>Perrault syndrome: evidence for progressive nervous system involvement.</strong>
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Am. J. Med. Genet. 128A: 246-249, 2004.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/15216544/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">15216544</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=15216544" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1002/ajmg.a.20616" target="_blank">Full Text</a>]
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Goldfischer, S., Collins, J., Rapin, I., Neumann, P., Neglia, W., Spiro, A. J., Ishii, T., Roels, F., Vamecq, J., Van Hoof, F.
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<strong>Pseudo-Zellweger syndrome: deficiencies in several peroxisomal oxidative activities.</strong>
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J. Pediat. 108: 25-32, 1986.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2868085/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2868085</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=2868085" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1016/s0022-3476(86)80764-8" target="_blank">Full Text</a>]
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Green, V. L., Speirs, V., Landolt, A. M., Foy, P. M., Atkin, S. L.
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<strong>17-beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 expression and enzyme activity in human anterior pituitary adenomas.</strong>
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J. Clin. Endocr. Metab. 84: 1340-1345, 1999.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/8279468/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">8279468</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=8279468" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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</p>
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</li>
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<li>
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<a id="24" class="mim-anchor"></a>
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<a id="van Grunsven1999" class="mim-anchor"></a>
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<div class="">
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<p class="mim-text-font">
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van Grunsven, E. G., Mooijer, P. A. W., Aubourg, P., Wanders, R. J. A.
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<strong>Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency.</strong>
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Hum. Molec. Genet. 8: 1509-1516, 1999.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/10400999/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">10400999</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=10400999" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1093/hmg/8.8.1509" target="_blank">Full Text</a>]
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</p>
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</div>
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<li>
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<a id="25" class="mim-anchor"></a>
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<a id="van Grunsven1998" class="mim-anchor"></a>
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<div class="">
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<p class="mim-text-font">
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van Grunsven, E. G., van Berkel, E., Ijlst, L., Vreken, P., de Klerk, J. B. C., Adamski, J., Lemonde, H., Clayton, P. T., Cuebas, D. A., Wanders, R. J. A.
|
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<strong>Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency.</strong>
|
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Proc. Nat. Acad. Sci. 95: 2128-2133, 1998.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9482850/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9482850</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9482850" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1073/pnas.95.5.2128" target="_blank">Full Text</a>]
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</p>
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</div>
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<li>
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<a id="26" class="mim-anchor"></a>
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<a id="van Grunsven1999" class="mim-anchor"></a>
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<div class="">
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<p class="mim-text-font">
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van Grunsven, E. G., van Berkel, E., Mooijer, P. A. W., Watkins, P. A., Moser, H. W., Suzuki, Y., Jiang, L. L., Hashimoto, T., Hoefler, G., Adamski, J., Wanders, R. J. A.
|
|
<strong>Peroxisomal bifunctional protein deficiency revisited: resolution of its true enzymatic and molecular basis.</strong>
|
|
Am. J. Hum. Genet. 64: 99-107, 1999.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/9915948/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">9915948</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=9915948" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1086/302180" target="_blank">Full Text</a>]
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</p>
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</div>
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</li>
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<li>
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<a id="27" class="mim-anchor"></a>
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<a id="Watkins1989" class="mim-anchor"></a>
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<div class="">
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<p class="mim-text-font">
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Watkins, P. A., Chen, W. W., Harris, C. J., Hoefler, G., Hoefler, S., Blake, D. C., Jr., Balfe, A., Kelley, R. I., Moser, A. B., Beard, M. E., Moser, H. W.
|
|
<strong>Peroxisomal bifunctional enzyme deficiency.</strong>
|
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J. Clin. Invest. 83: 771-777, 1989.
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[PubMed: <a href="https://pubmed.ncbi.nlm.nih.gov/2921319/" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">2921319</a>, <a href="https://pubmed.ncbi.nlm.nih.gov/?cmd=link&linkname=pubmed_pubmed&from_uid=2921319" target="_blank" onclick="gtag('event', 'mim_outbound', {'name': 'PubMed Related', 'domain': 'pubmed.ncbi.nlm.nih.gov'})">related citations</a>]
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[<a href="https://doi.org/10.1172/JCI113956" target="_blank">Full Text</a>]
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</p>
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</div>
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</ol>
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<div>
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<br />
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</div>
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<div>
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<a id="contributors" class="mim-anchor"></a>
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<div class="row">
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<div class="col-lg-2 col-md-2 col-sm-4 col-xs-4">
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<span class="mim-text-font">
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<a href="#mimCollapseContributors" role="button" data-toggle="collapse"> Contributors: </a>
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</div>
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<div class="col-lg-6 col-md-6 col-sm-6 col-xs-6">
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<span class="mim-text-font">
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Patricia A. Hartz - updated : 8/7/2015
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</span>
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</div>
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</div>
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<div class="row collapse" id="mimCollapseContributors">
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<div class="col-lg-offset-2 col-md-offset-4 col-sm-offset-4 col-xs-offset-2 col-lg-6 col-md-6 col-sm-6 col-xs-6">
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<span class="mim-text-font">
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Cassandra L. Kniffin - updated : 6/4/2014<br>Marla J. F. O'Neill - updated : 2/24/2011<br>Victor A. McKusick - updated : 12/29/2005<br>Cassandra L. Kniffin - reorganized : 12/8/2005<br>Cassandra L. Kniffin - updated : 12/7/2005<br>Victor A. McKusick - updated : 6/12/2002<br>Ada Hamosh - updated : 1/29/2002<br>John A. Phillips, III - updated : 9/30/1999<br>Ada Hamosh - updated : 8/9/1999<br>Sonja A. Rasmussen - updated : 6/30/1999<br>Victor A. McKusick - updated : 2/26/1999<br>Victor A. McKusick - updated : 2/9/1999<br>Victor A. McKusick - updated : 12/3/1997
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</span>
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<a id="creationDate" class="mim-anchor"></a>
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<div class="row">
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<div class="col-lg-2 col-md-2 col-sm-4 col-xs-4">
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<span class="text-nowrap mim-text-font">
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Creation Date:
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</span>
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</div>
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<div class="col-lg-6 col-md-6 col-sm-6 col-xs-6">
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<span class="mim-text-font">
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Jennifer P. Macke : 3/24/1997
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</span>
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</div>
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</div>
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<div>
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<a id="editHistory" class="mim-anchor"></a>
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<div class="col-lg-2 col-md-2 col-sm-4 col-xs-4">
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<span class="text-nowrap mim-text-font">
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<a href="#mimCollapseEditHistory" role="button" data-toggle="collapse"> Edit History: </a>
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</span>
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</div>
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<div class="col-lg-6 col-md-6 col-sm-6 col-xs-6">
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<span class="mim-text-font">
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alopez : 08/25/2015
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</span>
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<div class="row collapse" id="mimCollapseEditHistory">
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<div class="col-lg-offset-2 col-md-offset-2 col-sm-offset-4 col-xs-offset-4 col-lg-6 col-md-6 col-sm-6 col-xs-6">
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<span class="mim-text-font">
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mgross : 8/24/2015<br>mcolton : 8/7/2015<br>mcolton : 7/21/2015<br>alopez : 6/16/2014<br>mcolton : 6/5/2014<br>ckniffin : 6/4/2014<br>carol : 9/17/2013<br>alopez : 11/15/2012<br>ckniffin : 11/14/2012<br>alopez : 10/8/2012<br>wwang : 2/25/2011<br>terry : 2/24/2011<br>alopez : 5/4/2006<br>terry : 12/29/2005<br>carol : 12/8/2005<br>ckniffin : 12/7/2005<br>carol : 11/30/2005<br>carol : 11/30/2005<br>tkritzer : 1/20/2005<br>carol : 11/18/2004<br>cwells : 11/7/2003<br>tkritzer : 7/10/2003<br>carol : 4/18/2003<br>alopez : 6/17/2002<br>terry : 6/12/2002<br>alopez : 1/31/2002<br>terry : 1/29/2002<br>alopez : 2/2/2001<br>mgross : 9/30/1999<br>alopez : 8/17/1999<br>terry : 8/9/1999<br>kayiaros : 6/30/1999<br>kayiaros : 6/29/1999<br>carol : 2/27/1999<br>terry : 2/26/1999<br>carol : 2/17/1999<br>terry : 2/9/1999<br>joanna : 5/15/1998<br>carol : 4/7/1998<br>terry : 3/28/1998<br>dholmes : 12/29/1997<br>terry : 12/4/1997<br>terry : 12/3/1997<br>alopez : 7/16/1997
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</span>
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</div>
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<h3>
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<span class="mim-font">
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<strong>*</strong> 601860
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</span>
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</h3>
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</div>
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<div>
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<h3>
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<span class="mim-font">
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17-BETA-HYDROXYSTEROID DEHYDROGENASE IV; HSD17B4
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</span>
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</h3>
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</div>
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<div>
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<br />
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<div>
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<div >
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<p>
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<span class="mim-font">
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<em>Alternative titles; symbols</em>
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</span>
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</p>
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<div>
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<h4>
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<span class="mim-font">
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17-BETA-HSD IV<br />
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D-3-HYDROXYACYL-CoA DEHYDRATASE/D-3-HYDROXYACYL-CoA DEHYDROGENASE BIFUNCTIONAL PROTEIN<br />
|
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D-BIFUNCTIONAL PROTEIN, PEROXISOMAL<br />
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DBP, PEROXISOMAL<br />
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MULTIFUNCTIONAL PROTEIN 2; MFP2
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</span>
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</h4>
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</div>
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</div>
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<div>
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<br />
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</div>
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<span class="mim-text-font">
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<strong><em>HGNC Approved Gene Symbol: HSD17B4</em></strong>
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</span>
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</p>
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<div>
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<p>
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<span class="mim-text-font">
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<strong>SNOMEDCT:</strong> 238068007;
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<span class="mim-text-font">
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<strong>
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<em>
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Cytogenetic location: 5q23.1
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Genomic coordinates <span class="small">(GRCh38)</span> : 5:119,452,497-119,542,332 </span>
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</em>
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</strong>
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<span class="small">(from NCBI)</span>
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</span>
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</p>
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</div>
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<div>
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</div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>Gene-Phenotype Relationships</strong>
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</span>
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</h4>
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<div>
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<table class="table table-bordered table-condensed small mim-table-padding">
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<thead>
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<tr class="active">
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<th>
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Location
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</th>
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<th>
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Phenotype
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</th>
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<th>
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Phenotype <br /> MIM number
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</th>
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<th>
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Inheritance
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</th>
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<th>
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Phenotype <br /> mapping key
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</th>
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</tr>
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</thead>
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<tbody>
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<tr>
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<td rowspan="2">
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<span class="mim-font">
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5q23.1
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</span>
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</td>
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<td>
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<span class="mim-font">
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D-bifunctional protein deficiency
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</span>
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</td>
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<td>
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<span class="mim-font">
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261515
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</span>
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</td>
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<td>
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<span class="mim-font">
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Autosomal recessive
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</span>
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</td>
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<td>
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<span class="mim-font">
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3
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</span>
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</td>
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<tr>
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<td>
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<span class="mim-font">
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Perrault syndrome 1
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</span>
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</td>
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<td>
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<span class="mim-font">
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233400
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</span>
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</td>
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<td>
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<span class="mim-font">
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Autosomal recessive
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</span>
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</td>
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<td>
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<span class="mim-font">
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3
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</span>
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</td>
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</table>
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<div>
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<br />
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</div>
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<div>
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<h4>
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<span class="mim-font">
|
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<strong>TEXT</strong>
|
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</span>
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</h4>
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<div>
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<h4>
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<span class="mim-font">
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<strong>Description</strong>
|
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<p>The HSD17B4 gene encodes an enzyme involved in peroxisomal fatty acid beta-oxidation. It was first identified as a 17-beta-estradiol dehydrogenase (Leenders et al., 1996; van Grunsven et al., 1998). </p><p>Multifunctional protein-2 (MFP2), also called D-bifunctional protein, catalyzes the second (hydration) and third (dehydrogenation) reactions of the peroxisomal beta-oxidation of fatty acids and fatty acid derivatives (summary by Ferdinandusse et al., 2006). The 2 enzymatic activities of MFP2, enoyl-CoA hydratase and D-3-hydroxyacyl-CoA dehydrogenase, are essential for the oxidation of a wide range of peroxisomal substrates (very long-chain acyl-CoAs, branched-chain acyl-CoAs including pristanoyl-CoA, and bile acid precursors) (summary by Lines et al., 2014). </p><p>See also the L-bifunctional peroxisomal protein (EHHADH; 607037). The D- and L-bifunctional proteins have different substrate specificities. The D-bifunctional protein catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids and also acts in shortening cholesterol for bile acid formation. In contrast, the L-specific bifunctional protein does not have the latter 2 activities (Jiang et al., 1997). </p>
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</span>
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<div>
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<br />
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</div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>Cloning and Expression</strong>
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<p>Adamski et al. (1995) cloned a fourth type of 17-beta-hydroxysteroid dehydrogenase, HSD17B4, from a human liver cDNA library. The HSD17B4 gene encodes a 736-amino acid polypeptide with a predicted molecular mass of approximately 80 kD and less than 25% identity with the 3 previously characterized 17-HSDs (HSD17B1, 109684; HSD17B2, 109685; and HSD17B3, 605573). Northern blot analysis revealed that HSD17B4 is expressed in many tissues as an approximately 3.0-kb mRNA transcript, with highest expression in liver, heart, prostate, and testis. Adamski et al. (1995) overexpressed the gene in mammalian cells and found that HSD17B4 displays specific unidirectional oxidative 17-HSD activity. </p><p>Jiang et al. (1996) purified and characterized a medium-chain enoyl-CoA hydratase from human liver. By immunohistochemistry, they confirmed the presence of the enzyme in peroxisomes of cultured human skin fibroblasts. Jiang et al. (1997) determined the DNA and peptide sequences of medium-chain enoyl-CoA hydratase and found that it was identical to that of human 17-beta-hydroxysteroid dehydrogenase IV. The native enzyme is a 77-kD polypeptide. </p><p>By analysis of the porcine enzyme, Leenders et al. (1996) determined that the N-terminal region (residues 1-323) encodes the 17-steroid dehydrogenase activity, whereas the central region (residues 324-596) catalyzes the hydratase activity. The C-terminal portion facilitates the transfer of 7-dehydrocholesterol and phosphatidylcholine between membranes in vitro. The authors emphasized the unique ability of a single protein to catalyze different reactions. </p>
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</span>
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<div>
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<br />
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</div>
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<div>
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<h4>
|
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<span class="mim-font">
|
|
<strong>Gene Structure</strong>
|
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<p>Leenders et al. (1998) found that the HSD17B4 gene contains 24 exons and spans more than 100 kb. </p>
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</span>
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<div>
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<br />
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</div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>Mapping</strong>
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<p>By fluorescence in situ hybridization, Leenders et al. (1996) mapped the HSD17B4 gene to human chromosome 5q2. Novikov et al. (1997) mapped the HSD17B4 gene to chromosome 5q2.3 by FISH. </p>
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</span>
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<div>
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<br />
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</div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>Gene Function</strong>
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<p>Due to the presence of 25-methyl and 24-hydroxyl groups, 4 stereoisomers of varanoyl-CoA are possible. By assaying subcellular fractions of human liver, Novikov et al. (1997) found that peroxisomal MFP2 catalyzed dehydrogenation of 24R,25R-varanoyl-CoA. By a hydratation reaction, MFP2 also catalyzed formation of 24R,25R-varanoyl-CoA. </p><p>Green et al. (1999) investigated HSD17B1, -2, -3, and -4 gene expression and HSD17B estrogenic activity in human anterior pituitary adenomas. HSD17B mRNA expression was studied by RT-PCR in 42 pituitary tumors and 3 normal pituitaries, HSD17B activity was studied in 11 tumors, and HSD17B1 was immunolocalized in vitro in 6 tumors. HSD17B1 gene expression was detected in 34 of 42 (81%) adenomas in all tumor subtypes; HSD17B2 mRNA was detected in 18 of 42 (43%) adenomas but not in prolactinomas; HSD17B3 mRNA was detected in 12 of 42 (29%) adenomas but not in corticotropinomas; and HSD17B4 was expressed in 20 of 42 (48%) adenomas by all adenoma subtypes. All 4 HSD17B isoforms were variably expressed in human anterior pituitary adenomas, which also showed HSD17B enzyme activity, suggesting that HSD17B may play an important role in regulating the local cellular levels of estradiol. </p>
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</span>
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<div>
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<br />
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</div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>Molecular Genetics</strong>
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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<p><strong><em>D-Bifunctional Protein Deficiency</em></strong></p><p>
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|
In 2 Japanese patients with D-bifunctional protein deficiency (261515), Suzuki et al. (1997) identified 2 different homozygous mutations in the HSD17B4 gene (601860.0001; 601860.0002). The patients had previously been diagnosed with L-bifunctional protein deficiency by complementation analysis (Suzuki et al., 1994). </p><p>In an infant with a defect in peroxisomal beta-oxidation, van Grunsven et al. (1998) demonstrated D-bifunctional protein deficiency caused by a homozygous mutation in the HSD17B4 gene (601860.0003). </p><p>In a patient with D-bifunctional protein deficiency originally reported by Watkins et al. (1989), van Grunsven et al. (1999) identified a homozygous 2-bp deletion in the HSD17B4 gene (601860.0007). The patient was originally thought to have L-bifunctional protein deficiency based on immunoblot analysis of postmortem liver tissue. However, reanalysis showed accumulation of both very long chain fatty acids and bile acid intermediates, which was hard to reconcile with an isolated deficiency of the L-bifunctional protein. The results suggested that most, if not all, patients whose peroxisomal disorder had been diagnosed as L-bifunctional protein deficiency were in fact cases of D-bifunctional protein deficiency. </p><p>Nakano et al. (2001) reported a patient with D-bifunctional protein deficiency who was compound heterozygous for 2 mutations in the HSD17B4 gene (601860.0001 and 601860.0005). </p><p>Ferdinandusse et al. (2002) reinvestigated the patient of Goldfischer et al. (1986), who was the only patient ever reported with a presumed deficiency of peroxisomal 3-ketoacyl-CoA thiolase (604054). Molecular analysis identified a homozygous deletion in the HSD17B4 gene (601860.0006), confirming a diagnosis of D-bifunctional protein deficiency. </p><p>Ferdinandusse et al. (2006) reported the mutational spectrum of DBP deficiency on the basis of molecular analysis in 110 patients. They identified 61 different mutations by DBP cDNA analysis, 48 of which had not been previously reported. The predicted effects of the different disease-causing amino acid changes in protein structure were determined using the crystal structures. The effects ranged from the replacement of catalytic amino acid residues or residues in direct contact with the substrate or cofactor to disturbances of protein folding or dimerization of the subunits. To study whether there is a genotype-phenotype correlation for DBP deficiency, these structure-based analyses were combined with extensive biochemical analyses of patient material (cultured skin fibroblasts and plasma) and available clinical information on the patients. They found that the effect of the mutations identified in patients with a relatively mild clinical and biochemical presentation was less detrimental to the protein structure than the effect of mutations identified in those with a very severe presentation. These results suggested that the amount of residual DBP activity correlates with the severity of the phenotype. Thus the data indicated that on the basis of the predicted effect of mutations on protein structure, a genotype-phenotype correlation exists for DBP deficiency. </p><p>Ferdinandusse et al. (2006) found that the missense mutation G16S (601860.0003) is by far the most common mutation causing DBP deficiency (type III), which had in their study an allele frequency of approximately 24% and was detected in 28 of the 110 patients. The second most common mutation causing DBP deficiency (type II) was the missense mutation N457Y (601860.0004), which had an allele frequency of approximately 11% and was found in 13 patients. Of 5 patients for whom homozygosity was checked, 2 turned out to be heterozygotes at the genomic level. </p><p>In DBP type I-deficient patients, Ferdinandusse et al. (2006) found only deletions, insertions, and nonsense mutations. All deletions resulted in a truncated protein, except for 3 large in-frame deletions. Two patients with DBP type-II deficiency had in-frame deletions in the hydratase unit. All other DBP type II-deficient patients had missense mutations in the coding region of the DBP hydratase unit. DBP type III deficiency was predominantly caused by missense mutations and, in 2 cases, by a 1-amino acid deletion in the coding region of the dehydrogenase unit. </p><p><strong><em>Perrault Syndrome 1</em></strong></p><p>
|
|
Pierce et al. (2010) performed whole-exome sequencing of genomic DNA from a woman with Perrault syndrome-1 (PRLTS1; 233400), which is characterized by ovarian dysgenesis and sensorineural deafness, originally described by McCarthy and Opitz (1985) and identified 2 rare variants in the HSD17B4 gene (601860.0008 and 601860.0009). Sequencing revealed that both the proband and her affected sister were compound heterozygous for the missense (Y217C) and nonsense (Y568X) mutations, and that their unaffected mother was heterozygous for the missense mutation. Pierce et al. (2010) noted that Perrault syndrome and DBP deficiency overlap clinically, and suggested that mutations in HSD17B4 leading to DBP deficiency that is mild enough to allow survival to the age of puberty are likely to cause ovarian dysgenesis in females in addition to the known neurologic defects. The authors predicted that because the affected sisters were likely to express only protein with the Y217C mutation, they would have so-called type III DBP deficiency, with a defect in dehydrogenase activity. </p><p>In 2 brothers of European descent with Perrault syndrome, McMillan et al. (2012) identified compound heterozygous mutations in the HSD17B4 gene (A34V, 601860.0010 and I516T, 601860.0011). Each mutation affected a different domain, dehydrogenase and hydratase, respectively. The mutations, which were found by exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. </p><p>In 3 Italian sibs with Perrault syndrome, Lines et al. (2014) identified compound heterozygous missense mutations in the HSD17B4 gene (P513L, 601860.0012 and R543P, 601860.0013), both affecting the hydratase domain. The mutations were found by whole-exome sequencing. </p>
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</span>
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<div>
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<br />
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</div>
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<div>
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<h4>
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<span class="mim-font">
|
|
<strong>Animal Model</strong>
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</span>
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</h4>
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</div>
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<span class="mim-text-font">
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|
<p>Baes et al. (2000) obtained Mfp2 -/- mice at the expected mendelian ratio. At birth, Mfp2 -/- mice were indistinguishable from wildtype or Mfp2 +/- littermates, but Mfp2 -/- pups failed to thrive, and about one-third died within the first 12 days of life. At weaning, surviving Mfp2 -/- pups resumed weight gain. Adult Mfp2 -/-females were fertile, but Mfp2 -/- males were subfertile. Mfp2 -/- mice accumulated very long chain fatty acids in brain and liver phospholipids, as well as immature C27 bile acids in bile. Dietary supplementation with phytol, a tetramethyl-branched fatty alcohol, revealed accumulation of branched chain fatty acids in Mfp2 -/- mice, concomitant with severe weight loss and development of cataracts and ataxia. Oxidation of long chain fatty acids was enhanced in liver of Mfp2 -/- mice, suggesting compensatory increased Mfp1 (EHHADH; 607037) activity. Mature C24 bile acids were found in adult Mfp2 -/- mice, suggesting bile acid formation by alternative pathways. Baes et al. (2000) concluded that MFP2 degrades 2-methyl-branched fatty acids, bile acid intermediates, and very long chain fatty acids. </p>
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</span>
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<div>
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<br />
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</div>
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</div>
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<div>
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<h4>
|
|
<span class="mim-font">
|
|
<strong>ALLELIC VARIANTS</strong>
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</span>
|
|
<strong>13 Selected Examples):</strong>
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</span>
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</h4>
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<div>
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<p />
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</div>
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<div>
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<div>
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<h4>
|
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<span class="mim-font">
|
|
<strong>.0001 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
|
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</span>
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</h4>
|
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</div>
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<div>
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<span class="mim-text-font">
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|
HSD17B4, 52-BP DEL
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<br />
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SNP: rs1554065670,
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|
|
ClinVar: RCV000008092
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</span>
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</div>
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<div>
|
|
<span class="mim-text-font">
|
|
<p>In a Japanese patient with D-bifunctional protein deficiency (261515), Suzuki et al. (1997) identified a 52-bp deletion in the HSD17B4 gene, resulting in a 17-amino acid deletion and premature termination. Studies of postmortem liver tissue confirmed absence of the activity and immunoreactivity of D-bifunctional protein. The patient was previously thought to have L-bifunctional protein deficiency (Suzuki et al., 1994). </p>
|
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</span>
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</div>
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<div>
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|
<br />
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|
</div>
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</div>
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<div>
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|
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<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0002 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
|
|
</span>
|
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</h4>
|
|
</div>
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<div>
|
|
<span class="mim-text-font">
|
|
|
|
HSD17B4, 237-BP DEL
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|
<br />
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|
|
SNP: rs1554065254,
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|
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|
|
|
|
ClinVar: RCV000008093
|
|
|
|
|
|
</span>
|
|
</div>
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|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a Japanese patient with D-bifunctional protein deficiency (261515), Suzuki et al. (1997) identified a 237-bp deletion in the HSD17B4 gene, resulting in a 79-amino acid deletion. Studies of postmortem liver tissue confirmed absence of the activity and immunoreactivity of D-bifunctional protein. The patient was previously thought to have L-bifunctional protein deficiency (Suzuki et al., 1994). </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
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|
|
</div>
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|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0003 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
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|
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|
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|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
HSD17B4, GLY16SER
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|
|
|
<br />
|
|
|
|
SNP: rs137853096,
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|
|
|
|
|
gnomAD: rs137853096,
|
|
|
|
|
|
ClinVar: RCV000008094, RCV000415821, RCV000688945, RCV000779455, RCV001197145, RCV002512888, RCV005031420
|
|
|
|
|
|
</span>
|
|
</div>
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|
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|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In an infant with a D-bifunctional protein deficiency (261515), van Grunsven et al. (1998) identified a 46G-A transition in the HSD17B4 gene, resulting in a gly16-to-ser (G16S) substitution within an important loop of the Rossman fold forming the NAD(+)-binding site. Biochemical analysis showed that the 3-hydroxyacyl-CoA dehydrogenase activity of the D-bifunctional protein was completely inactive, whereas the enoyl-CoA hydratase component was active. Their findings showed that the D-bifunctional protein plays an essential role in the peroxisomal beta-oxidation pathway that cannot be compensated for by the L-specific bifunctional protein. Both parents were heterozygous for the mutation. </p><p>Van Grunsven et al. (1999) demonstrated the G16S mutation in 9 additional patients previously thought to have deficiency of L-bifunctional protein on the basis of complementation studies. The findings confirmed D-bifunctional protein deficiency in these cases. </p>
|
|
</span>
|
|
</div>
|
|
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|
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|
|
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<div>
|
|
<br />
|
|
</div>
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|
|
|
</div>
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<div>
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|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0004 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
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|
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|
|
|
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|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
HSD17B4, ASN457TYR
|
|
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|
|
|
<br />
|
|
|
|
SNP: rs137853097,
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|
|
|
|
|
gnomAD: rs137853097,
|
|
|
|
|
|
ClinVar: RCV000008095, RCV000385297, RCV000477799, RCV000684773, RCV001002204
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In 2 unrelated patients with D-bifunctional protein deficiency (261515), van Grunsven et al. (1999) identified a homozygous 1369A-T transversion in the HSD17B4 gene, resulting in an asn457-to-tyr (N457Y) substitution. Both patients had an isolated defect of the enoyl-CoA hydratase domain of the D-bifunctional protein. Both patients had abnormalities of peroxisomal beta-oxidation with elevated very long chain fatty acids and branch chain fatty acids, but normal levels of bile acid intermediates. Both patients were born of consanguineous parents. Sequence analysis of the D-bifunctional protein cDNA of 15 control subjects of Caucasian origin did not identify the N457Y mutation. Expression of the N457Y mutation in Saccharomyces cerevisiae confirmed that it is the disease-causing mutation. Immunoblot analysis of patient fibroblast homogenates showed that the protein levels of full-length D-bifunctional protein were strongly reduced, while the enoyl-CoA hydratase component produced after processing within the peroxisome was undetectable, indicating that the mutation leads to an unstable protein. </p>
|
|
</span>
|
|
</div>
|
|
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<div>
|
|
<br />
|
|
</div>
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|
|
|
</div>
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|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0005 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
HSD17B4, ARG106PRO
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|
|
|
|
|
<br />
|
|
|
|
SNP: rs25640,
|
|
|
|
|
|
gnomAD: rs25640,
|
|
|
|
|
|
ClinVar: RCV000008096
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a male patient with D-bifunctional protein deficiency (261515), Nakano et al. (2001) identified compound heterozygosity for 2 mutations in the HSD17B4 gene: a 317G-C transversion, resulting in an arg106-to-pro (R106P) substitution, and a 52-bp deletion (601860.0001). The mutations were associated with complete loss of function of the protein. </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
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|
|
<div>
|
|
<br />
|
|
</div>
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|
|
</div>
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|
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|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0006 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
|
|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
HSD17B4, 138-BP DEL
|
|
|
|
|
|
<br />
|
|
|
|
|
|
|
|
ClinVar: RCV000008097
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a patient with D-bifunctional protein deficiency (261515), Ferdinandusse et al. (2002) identified a homozygous 138-bp deletion in the HSD17B4 gene extending from basepair 145 in exon 3 through the first 63 basepairs of intron 3 of the DBP gene. This deletion resulted in skipping of exon 3. The patient had originally been reported by Goldfischer et al. (1986) and Schram et al. (1987) as the only patient ever reported to have peroxisomal 3-ketoacyl-CoA thiolase (604054) deficiency. However, reanalysis showed normal thiolase and absence of the D-bifunctional protein in brain tissue. </p>
|
|
</span>
|
|
</div>
|
|
|
|
|
|
|
|
<div>
|
|
<br />
|
|
</div>
|
|
|
|
</div>
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|
|
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|
|
<div>
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0007 D-BIFUNCTIONAL PROTEIN DEFICIENCY</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
|
|
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|
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
|
|
HSD17B4, 2-BP DEL, 422AG
|
|
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|
|
|
<br />
|
|
|
|
SNP: rs775832137,
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|
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|
|
|
gnomAD: rs775832137,
|
|
|
|
|
|
ClinVar: RCV000008098
|
|
|
|
|
|
</span>
|
|
</div>
|
|
|
|
|
|
<div>
|
|
<span class="mim-text-font">
|
|
<p>In a patient with D-bifunctional protein deficiency (261515) originally reported by Watkins et al. (1989), van Grunsven et al. (1999) identified a homozygous 2-bp deletion (422delAG) in the HSD17B4 gene, resulting in a premature stop codon at position 490 and a shortened protein of 163 amino acids. The patient was originally thought to have L-bifunctional protein deficiency. </p>
|
|
</span>
|
|
</div>
|
|
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|
<div>
|
|
<br />
|
|
</div>
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|
|
</div>
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<div>
|
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|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>.0008 PERRAULT SYNDROME 1</strong>
|
|
</span>
|
|
</h4>
|
|
</div>
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<div>
|
|
<span class="mim-text-font">
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|
HSD17B4, TYR217CYS
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|
|
<br />
|
|
|
|
SNP: rs387906825,
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|
|
|
|
ClinVar: RCV000023152, RCV002513181, RCV003330398
|
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|
</span>
|
|
</div>
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<div>
|
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<span class="mim-text-font">
|
|
<p>In 2 sisters with Perrault syndrome (PRLTS1; 233400), previously described by McCarthy and Opitz (1985) and Fiumara et al. (2004), Pierce et al. (2010) identified compound heterozygosity for a 605A-G transition in exon 9 of the HSD17B4 gene, resulting in a tyr217-to-cys (Y217C) substitution in a very highly conserved region of the protein, and a 1704T-A transversion in exon 20, resulting in a tyr568-to-ter (Y568X; 601860.0009) substitution. Their unaffected mother was found to be heterozygous for the Y217C mutation, and neither mutation was detected in 1,092 control individuals. Expression analysis using lymphoblast cDNA showed that Y568X transcript was expressed at very low levels relative to the Y217C transcript, suggesting that Y568X undergoes nonsense-mediated decay, whereas Y217C is more stably expressed. </p>
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</span>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>.0009 PERRAULT SYNDROME 1</strong>
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</span>
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</h4>
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</div>
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<div>
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<span class="mim-text-font">
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HSD17B4, TYR568TER
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<br />
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SNP: rs1038744864,
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gnomAD: rs1038744864,
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ClinVar: RCV000023153, RCV000811384, RCV001260323, RCV001556667, RCV002538095, RCV005047098
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</span>
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</div>
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<div>
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<span class="mim-text-font">
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<p>For discussion of the tyr568-to-ter (Y568X) mutation in the HSD17B4 gene that was found in compound heterozygous state in 2 sisters with Perrault syndrome (PRLTS1; 233400) by Pierce et al. (2010), see 601860.0008. </p>
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</span>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>.0010 PERRAULT SYNDROME 1</strong>
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</span>
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</h4>
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</div>
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<div>
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<span class="mim-text-font">
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HSD17B4, ALA34VAL
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<br />
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SNP: rs587777442,
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gnomAD: rs587777442,
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ClinVar: RCV000125465, RCV001092766, RCV001810425, RCV003764860, RCV004567068
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</span>
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</div>
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<div>
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<span class="mim-text-font">
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<p>In 2 teenaged brothers of European descent with Perrault syndrome (PRLTS1; 233400), McMillan et al. (2012) identified compound heterozygous mutations in the HSD17B4 gene: a c.101C-T transition, resulting in an ala34-to-val (A34V) substitution in the dehydrogenase domain, and a c.1547T-C transition, resulting in an ile516-to-thr (I516T; 601860.0011) substitution in the hydratase domain. The mutations, which were found by exome sequencing and confirmed by Sanger sequencing, segregated with the disorder in the family. McMillan et al. (2012) postulated that the relatively mild phenotype was due to the fact that only 1 of the functional HSD17B4 domains was affected on each allele. There was reduced but detectable DBP hydratase and dehydrogenase activity, with some reduction of pristanic acid beta-oxidation in patient fibroblasts. The 45-kD DBP fragment was not detected by immunoblot analysis; however, peroxisomes and plasma very long-chain and branched fatty acids were normal. </p>
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</span>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<div>
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<h4>
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<span class="mim-font">
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<strong>.0011 PERRAULT SYNDROME 1</strong>
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</span>
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</h4>
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</div>
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<div>
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<span class="mim-text-font">
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HSD17B4, ILE516THR
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<br />
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SNP: rs587777443,
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ClinVar: RCV000125466, RCV000672665, RCV000825530, RCV001849905, RCV003144135, RCV005031635
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</span>
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</div>
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<div>
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<span class="mim-text-font">
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<p>For discussion of the ile516-to-thr (I516T) mutation in the HSD17B4 gene that was found in compound heterozygous state in 2 brothers with Perrault syndrome (PRLTS1; 233400) by McMillan et al. (2012), see 601860.0010. </p>
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</span>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<div>
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<h4>
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<span class="mim-font">
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|
<strong>.0012 PERRAULT SYNDROME 1</strong>
|
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</span>
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</h4>
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</div>
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<div>
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<span class="mim-text-font">
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HSD17B4, PRO513LEU
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<br />
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SNP: rs587777444,
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ClinVar: RCV000125467, RCV000675096
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</span>
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</div>
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<div>
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<span class="mim-text-font">
|
|
<p>In 3 Italian sibs, including 2 sisters, with Perrault syndrome (PRLTS1; 233400), Lines et al. (2014) identified compound heterozygous mutations in the HSD17B4 gene: a c.1537C-A transversion, resulting in a pro513-to-leu (P513L) substitution, and a c.1628G-C transversion, resulting in an arg543-to-pro (R543P; 601860.0013) substitution. The mutations, which were found by whole-exome sequencing, occurred at highly conserved residues within the active site of the hydratase domain and segregated with the disorder in the family. They were filtered against the dbSNP, 1000 Genomes Project, and Exome Variant Server databases, as well as 130 local control exomes. Immunoblot analysis of patient cells showed markedly reduced DBP enoyl-CoA hydratase activity, as well as absence of the 45-kD posttranslational fragment containing the hydratase domain. Laboratory studies of all patients showed increased serum total bile acids, but phytanic and very long-chain fatty acids were normal. Patient fibroblasts showed decreased beta-oxidation of pristanic acid. Peroxisome morphology was normal. </p>
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</span>
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</div>
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<div>
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<br />
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</div>
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</div>
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<div>
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<div>
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<h4>
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<span class="mim-font">
|
|
<strong>.0013 PERRAULT SYNDROME 1</strong>
|
|
</span>
|
|
</h4>
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</div>
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<div>
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<span class="mim-text-font">
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HSD17B4, ARG543PRO
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<br />
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SNP: rs201009485,
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gnomAD: rs201009485,
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|
|
|
ClinVar: RCV000125468, RCV000730879, RCV001849906, RCV003467098
|
|
|
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</span>
|
|
</div>
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|
<div>
|
|
<span class="mim-text-font">
|
|
<p>For discussion of the arg543-to-pro (R543P) mutation in the HSD17B4 gene that was found in compound heterozygous state in sibs with Perrault syndrome (PRLTS1; 233400) by Lines et al. (2014), see 601860.0012. </p>
|
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</span>
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</div>
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<div>
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<br />
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</div>
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</div>
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</div>
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<div>
|
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<h4>
|
|
<span class="mim-font">
|
|
<strong>See Also:</strong>
|
|
</span>
|
|
</h4>
|
|
<span class="mim-text-font">
|
|
Lazarow and de Duve (1976)
|
|
</span>
|
|
<div>
|
|
<br />
|
|
</div>
|
|
</div>
|
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|
|
|
|
|
|
|
|
<div>
|
|
<h4>
|
|
<span class="mim-font">
|
|
<strong>REFERENCES</strong>
|
|
</span>
|
|
</h4>
|
|
<div>
|
|
<p />
|
|
</div>
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<div>
|
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<ol>
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<li>
|
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<p class="mim-text-font">
|
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Adamski, J., Normand, T., Leenders, F., Monte, D., Begue, A., Stehelin, D., Jungblut, P. W., de Launoit, Y.
|
|
<strong>Molecular cloning of a novel widely expressed human 80 kDa 17-beta-hydroxysteroid dehydrogenase IV.</strong>
|
|
Biochem. J. 311: 437-443, 1995.
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[PubMed: 7487879]
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[Full Text: https://doi.org/10.1042/bj3110437]
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</p>
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</li>
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<li>
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<p class="mim-text-font">
|
|
Baes, M., Huyghe, S., Carmeliet, P., Declercq, P. E., Collen, D., Mannaerts, G. P., Van Veldhoven, P. P.
|
|
<strong>Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids.</strong>
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J. Biol. Chem. 275: 16329-16336, 2000.
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[PubMed: 10748062]
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[Full Text: https://doi.org/10.1074/jbc.M001994200]
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</p>
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</li>
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<li>
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<p class="mim-text-font">
|
|
Ferdinandusse, S., van Grunsven, E. G., Oostheim, W., Denis, S., Hogenhout, E. M., Ijlst, L., van Roermund, C. W. T., Waterham, H. R., Goldfischer, S., Wanders, R. J. A.
|
|
<strong>Reinvestigation of peroxisomal 3-ketoacyl-CoA thiolase deficiency: identification of the true defect at the level of D-bifunctional protein.</strong>
|
|
Am. J. Hum. Genet. 70: 1589-1593, 2002.
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[PubMed: 11992265]
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[Full Text: https://doi.org/10.1086/340970]
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</p>
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</li>
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<li>
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<p class="mim-text-font">
|
|
Ferdinandusse, S., Ylianttila, M. S., Gloerich, J., Koski, M. K., Oostheim, W., Waterham, H. R., Hiltunen, J. K., Wanders, R. J. A., Glumoff, T.
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|
<strong>Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis.</strong>
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Am. J. Hum. Genet. 78: 112-124, 2006.
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[PubMed: 16385454]
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[Full Text: https://doi.org/10.1086/498880]
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</p>
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</li>
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<li>
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<p class="mim-text-font">
|
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Fiumara, A., Sorge, G., Toscano, A., Parano, E., Pavone, L., Opitz, J. M.
|
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<strong>Perrault syndrome: evidence for progressive nervous system involvement.</strong>
|
|
Am. J. Med. Genet. 128A: 246-249, 2004.
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[PubMed: 15216544]
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[Full Text: https://doi.org/10.1002/ajmg.a.20616]
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</p>
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</li>
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<li>
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<p class="mim-text-font">
|
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Goldfischer, S., Collins, J., Rapin, I., Neumann, P., Neglia, W., Spiro, A. J., Ishii, T., Roels, F., Vamecq, J., Van Hoof, F.
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<strong>Pseudo-Zellweger syndrome: deficiencies in several peroxisomal oxidative activities.</strong>
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J. Pediat. 108: 25-32, 1986.
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[PubMed: 2868085]
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[Full Text: https://doi.org/10.1016/s0022-3476(86)80764-8]
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</p>
|
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</li>
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<li>
|
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<p class="mim-text-font">
|
|
Green, V. L., Speirs, V., Landolt, A. M., Foy, P. M., Atkin, S. L.
|
|
<strong>17-beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 expression and enzyme activity in human anterior pituitary adenomas.</strong>
|
|
J. Clin. Endocr. Metab. 84: 1340-1345, 1999.
|
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[PubMed: 10199776]
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[Full Text: https://doi.org/10.1210/jcem.84.4.5619]
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</p>
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</li>
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<li>
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<p class="mim-text-font">
|
|
Jiang, L. L., Kobayashi, A., Matsuura, H., Fukushima, H., Hashimoto, T.
|
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<strong>Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase.</strong>
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J. Biochem. 120: 624-632, 1996.
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[PubMed: 8902629]
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[Full Text: https://doi.org/10.1093/oxfordjournals.jbchem.a021458]
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</p>
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</li>
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<li>
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<p class="mim-text-font">
|
|
Jiang, L. L., Kurosawa, T., Sato, M., Suzuki, Y., Hashimoto, T.
|
|
<strong>Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein.</strong>
|
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J. Biochem. 121: 506-513, 1997.
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[PubMed: 9133619]
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[Full Text: https://doi.org/10.1093/oxfordjournals.jbchem.a021615]
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</p>
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</li>
|
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<li>
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<p class="mim-text-font">
|
|
Jiang, L. L., Miyazawa, S., Souri, M., Hashimoto, T.
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<strong>Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein.</strong>
|
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J. Biochem. 121: 364-369, 1997.
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[PubMed: 9089413]
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|
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|
|
[Full Text: https://doi.org/10.1093/oxfordjournals.jbchem.a021596]
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</p>
|
|
</li>
|
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<li>
|
|
<p class="mim-text-font">
|
|
Lazarow, P. B., de Duve, C.
|
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<strong>A fatty acyl-CoA oxidizing system in rat liver peroxisomes: enhancement by clofibrate, a hypolipidemic drug.</strong>
|
|
Proc. Nat. Acad. Sci. 73: 2043-2046, 1976.
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|
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|
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[PubMed: 180535]
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|
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[Full Text: https://doi.org/10.1073/pnas.73.6.2043]
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</p>
|
|
</li>
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<li>
|
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<p class="mim-text-font">
|
|
Leenders, F., Dolez, V., Begue, A., Moller, G., Gloeckner, J., de Launoit, Y., Adamski, J.
|
|
<strong>Structure of the gene for the human 17-beta-hydroxysteroid dehydrogenase type IV.</strong>
|
|
Mammalian Genome 9: 1036-1041, 1998.
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|
|
|
|
[PubMed: 9880674]
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|
|
|
|
|
[Full Text: https://doi.org/10.1007/s003359900921]
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|
|
</p>
|
|
</li>
|
|
|
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<li>
|
|
<p class="mim-text-font">
|
|
Leenders, F., Prescher, G., Dolez, V., Begue, A., de Launoit, Y., Adamski, J.
|
|
<strong>Assignment of human 17-beta-hydroxysteroid dehydrogenase IV to chromosome 5q2 by fluorescence in situ hybridization.</strong>
|
|
Genomics 37: 403-404, 1996.
|
|
|
|
|
|
[PubMed: 8938456]
|
|
|
|
|
|
[Full Text: https://doi.org/10.1006/geno.1996.0578]
|
|
|
|
|
|
</p>
|
|
</li>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
Leenders, F., Tesdorpf, J. G., Markus, M., Engel, T., Seedorf, U., Adamski, J.
|
|
<strong>Porcine 80-kDa protein reveals intrinsic 17 beta-hydroxysteroid dehydrogenase, fatty acyl-CoA-hydratase/dehydrogenase, and sterol transfer activities.</strong>
|
|
J. Biol. Chem. 271: 5438-5442, 1996.
|
|
|
|
|
|
[PubMed: 8621399]
|
|
|
|
|
|
[Full Text: https://doi.org/10.1074/jbc.271.10.5438]
|
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|
|
</p>
|
|
</li>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
Lines, M. A., Jobling, R., Brady, L., Marshall, C. R., Scherer, S. W., Rodriguez, A. R., Lee, L., Lang, A. E., Mestre, T. A., Wanders, R. J. A., Ferdinandusse, S., Tarnopolsky, M. A.
|
|
<strong>Peroxisomal D-bifunctional protein deficiency: three adults diagnosed by whole-exome sequencing.</strong>
|
|
Neurology 82: 963-968, 2014.
|
|
|
|
|
|
[PubMed: 24553428]
|
|
|
|
|
|
[Full Text: https://doi.org/10.1212/WNL.0000000000000219]
|
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|
|
</p>
|
|
</li>
|
|
|
|
<li>
|
|
<p class="mim-text-font">
|
|
McCarthy, D. J., Opitz, J. M.
|
|
<strong>Perrault syndrome in sisters.</strong>
|
|
Am. J. Med. Genet. 22: 629-631, 1985.
|
|
|
|
|
|
[PubMed: 4061497]
|
|
|
|
|
|
[Full Text: https://doi.org/10.1002/ajmg.1320220324]
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</p>
|
|
</li>
|
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<li>
|
|
<p class="mim-text-font">
|
|
McMillan, H. J., Worthylake, T., Schwartzentruber, J., Gottlieb, C. C., Lawrence, S. E., MacKenzie, A., Beaulieu, C. L., Mooyer, P. A. W., FORGE Canada Consortium, Wanders, R. J. A., Majewski, J., Bulman, D. E., Geraghty, M. T., Ferdinandusse, S., Boycott, K. M.
|
|
<strong>Specific combination of compound heterozygous mutations in 17-beta-hydroxysteroid dehydrogenase type 4 (HD17B4) defines a new subtype of D-bifunctional protein deficiency.</strong>
|
|
Orphanet J. Rare Dis. 7: 90, 2012. Note: Electronic Article.
|
|
|
|
|
|
[PubMed: 23181892]
|
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<strong>Human peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency.</strong>
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Suzuki, Y., Jiang, L. L., Souri, M., Miyazawa, S., Fukuda, S., Zhang, Z., Une, M., Shimozawa, N., Kondo, N., Orii, T., Hashimoto, T.
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Suzuki, Y., Shimozawa, N., Yajima, S., Tomatsu, S., Kondo, N., Nakada, Y., Akaboshi, S., Iai, M., Tanabe, Y., Hashimoto, T., Wanders, R. J. A., Schutgens, R. B. H., Moser, H. W., Orii, T.
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van Grunsven, E. G., van Berkel, E., Mooijer, P. A. W., Watkins, P. A., Moser, H. W., Suzuki, Y., Jiang, L. L., Hashimoto, T., Hoefler, G., Adamski, J., Wanders, R. J. A.
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Watkins, P. A., Chen, W. W., Harris, C. J., Hoefler, G., Hoefler, S., Blake, D. C., Jr., Balfe, A., Kelley, R. I., Moser, A. B., Beard, M. E., Moser, H. W.
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