Alternative titles; symbols
Other entities represented in this entry:
HGNC Approved Gene Symbol: HNRNPA2B1
Cytogenetic location: 7p15.2 Genomic coordinates (GRCh38) : 7:26,189,927-26,200,746 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 7p15.2 | ?Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 2 | 615422 | Autosomal dominant | 3 |
| Oculopharyngeal muscular dystrophy 2 | 620460 | Autosomal dominant | 3 |
The HNRNPA2B1 gene encodes 2 major proteins, HNRNPA2 and HNRNPB1, through alternative splicing. HNRNPA/B proteins, such as HNRNPA2 and HNRNPB1, are involved in packaging nascent mRNA, in alternative splicing, and in cytoplasmic RNA trafficking, translation, and stabilization. HNRNPA2 and HNRNPB1 also appear to function in telomere maintenance, cell proliferation and differentiation, and glucose transport (Moran-Jones et al., 2005; Iwanaga et al., 2005).
By immunoscreening a HeLa cell cDNA expression library using mouse anti-A2 and anti-B1 antibodies, followed by screening a human osteosarcoma cDNA library, Burd et al. (1989) obtained full-length A2 and B1 clones. The B1 cDNA has a 36-nucleotide insertion near its 5-prime end relative to A2, but they are otherwise identical. The deduced A2 protein contains 341 amino acids, and the deduced B1 protein contains an in-frame 12-amino acid insert after glu2 compared with A2. Both proteins contain 2 consensus-type RNA-binding domains, followed by an extended C-terminal glycine-rich region. The insert in B1 introduces a putative nuclear localization signal. In vitro translation produced A2 and B1 proteins that comigrated with purified endogenous HeLa cell A2 and B1 at apparent molecular masses of 36 and 38 kD, respectively.
Biamonti et al. (1994) and Kozu et al. (1995) independently cloned HNRNPA2B1. Biamonti et al. (1994) determined that the 36-nucleotide insertion in the B1 transcript arises from inclusion of exon 2. Using Northern blot and RT-PCR analyses, Kozu et al. (1995) detected a 1.8-kb transcript representing total A2/B1 mRNA in all 3 human cell lines examined. The levels of B1 expression were about 2 to 5% of total A2/B1 levels in these cell lines. RT-PCR of mouse tissues suggested ubiquitous expression of both A2 and B1 transcripts.
Translational repression of glucose transporter-1 (GLUT1, or SLC2A1; 138140) in glioblastoma multiforme (GBM; 137800) is mediated by a specific RNA-binding protein that interacts with an AU-rich response element in the 3-prime UTR of the GLUT1 transcript. Hamilton et al. (1999) showed that HNRNPA2 and HNRNPL (603083) bound the 3-prime UTR of GLUT1 mRNA. Induction of brain ischemia in rats or hypoglycemic stress in 293 cells increased GLUT1 expression via mRNA stability. Polysomes isolated from ischemic rat brains or hypoglycemic 293 cells showed loss of HNRNPA2 and HNRNPL, suggesting that reduced levels of these RNA-binding proteins results in GLUT1 mRNA stability. Immunoprecipitation of polysomes from activated human T lymphocytes suggested that HNRNPA2 and HNRNPL form a complex in vivo.
Using pull-down assays and EMSA, Moran-Jones et al. (2005) identified Hnrnpa2 and Hnrnpa3 (605372) as the predominant single-stranded telomere repeat-binding proteins in rat brain. Using rat and human constructs, they identified 2 oligonucleotide-binding sites in HNRNPA2. One site bound single-stranded DNA (ssDNA) with little or no nucleotide sequence preference, whereas the second site bound specific RNA and DNA sequences. The latter site bound single-stranded TTAGGG telomere repeats and a cytoplasmic RNA-trafficking element (A2RE11). Mutation analysis indicated that the tandem RRM domains also bound the telomerase RNA (TERC; 602322), but the individual RRM domains did not. Full-length HNRNPA2, but not HNRNPA2 truncation mutants, protected telomeric DNA from DNase, suggesting that the glycine-rich domain as well as the RRM domains are required for telomere protection. Moran-Jones et al. (2005) proposed that HNRNPA2 can potentially bind telomeric DNA repeats and the RNA component of telomerase simultaneously, or that it may bind ssDNA in both sites and act as an intramolecular or intermolecular crosslink.
DNA-dependent protein kinase (DNAPK; see 600899) is a multisubunit kinase involved in the repair of DNA double-strand breaks through nonhomologous end-joining. Iwanaga et al. (2005) found that HNRNPB1 interacted directly with the DNAPK subunit Ku70 (XRCC6; 152690) and inhibited DNAPK activity in a dose-dependent manner in vitro. Knockdown of HNRNPA2B1 in irradiated normal human bronchial epithelial cells reduced HNRNPB1 levels and enhanced recovery of DNA strand breaks compared with controls.
By yeast 2-hybrid analysis of a human brain cDNA library, Kosturko et al. (2006) found that mouse Hnrnpa2 interacted with human HNRNPE1 (PCBP1; 601209). They confirmed the interaction with in vivo and in vitro protein interaction assays. Hnrnpe1 colocalized with Hnrnpa2 and A2RE mRNA in granules in dendrites of rat oligodendrocytes. Overexpression of HNRNPE1 or microinjection of exogenous HNRNPE1 in rat neural cells inhibited translation of A2RE mRNA, but not translation of mutated A2RE mRNA. Excess HNRNPE1 added to an in vitro translation system reduced translation efficiency of A2RE mRNA in an Hnrnpa2-dependent manner. Kosturko et al. (2006) hypothesized that binding of HNRNPE1 to HNRNPA2 inhibits A2RE mRNA translation during granule transport.
A transgenic fly model of fragile X-associated tremor/ataxia syndrome (FXTAS; 300623) in which the 5-prime UTR of human FMR1 (309550) containing 90 CGG repeats is expressed specifically in the eye results in disorganized ommatidia, depigmentation, and progressive loss of photoreceptor neurons. Sofola et al. (2007) found that overexpression of human CUGBP1 (601074) suppressed the neurodegenerative eye phenotype in transgenic flies. CUGBP1 did not interact directly with the CGG repeats, but did so via HNRNPA2B1. Expression of the A2 isoform of human HNRNPA2B1, or the Drosophila orthologs, also suppressed the eye phenotype of FXTAS flies. Mouse Hnrnpa2b1 interacted directly with CGG repeat RNA (rCGG) in mouse cerebellar lysates, and increased repeat length increased the binding affinity. The interaction was most evident in cytoplasmic cerebellar lysates. Nuclear Hnrnpa2b1 showed little or no interaction with rCGG repeats, suggesting that protein modification, in either the nuclear or cytoplasmic compartment, affects the interaction.
Moran-Jones et al. (2009) found that HNRNPA2 promoted inclusion of TP53INP2 (617549) noncoding exon 2 in A2780 ovarian carcinoma cells, but only when cells were grown in a 3-dimensional substrate. Knockdown of exon 2-containing TP53INP2 transcripts via knockout of HNRNPA2 or via small interfering RNA targeting TP53INP2 exon 2 reduced cell migration through a 3-dimensional gel.
David et al. (2010) showed that 3 hnRNP proteins, polypyrimidine tract-binding protein (PTB, also known as hnRNPI; 600693), hnRNPA1 (164017), and hnRNPA2, bind repressively to sequences flanking exon 9 of the PKM2 gene (179050), resulting in exon 10 inclusion and expression of the PKM2 (embryonic) isoform. David et al. (2010) also demonstrated that the oncogenic transcription factor c-MYC (190080) upregulates transcription of PTB, hnRNPA1, and hnRNPA2, ensuring a high PKM2/PKM1 ratio. Establishing a relevance to cancer, David et al. (2010) showed that human gliomas (137800) overexpress c-Myc, PTB, hnRNPA1, and hnRNPA2 in a manner that correlates with PKM2 expression. David et al. (2010) concluded that their results defined a pathway that regulates an alternative splicing event required for tumor cell proliferation.
Kim et al. (2013) reported that HNRNPA2B1 has a C-terminal glycine-rich domain that is essential for activity and mediates interaction with TDP43 (605078). This low-complexity domain is predicted to be intrinsically unfolded and has an amino acid composition similar to that of yeast prion domains. Approximately 250 human proteins, including several RNA-binding proteins associated with neurodegenerative disease, harbor a similar distinctive prion-like domain (PrLD) enriched in uncharged polar amino acids and glycine. PrLDs in RNA-binding proteins are essential for the assembly of ribonucleoprotein granules. Kim et al. (2013) showed that HNRNPA2, the most abundant form of HNRNPA2B1, has an intrinsic tendency to assemble into self-seeding fibrils.
Wang et al. (2019) reported that HNRNPA2B1 recognizes pathogenic DNA and amplifies interferon-alpha/beta production. Upon DNA virus infection, nuclear-localized HNRNPA2B1 senses viral DNA, homodimerizes, and is then demethylated at arginine-226 by the arginine demethylase JMJD6 (604914). This results in HNRNPA2B1 translocation to the cytoplasm, where it activates the TANK-binding kinase-1 (TBK1; 604834)-interferon regulatory factor-3 (IRF3; 603734) pathway, leading to IFN-alpha (147660)/beta (147640) production. Additionally, HNRNPA2B1 facilitates N6-methyladenosine (m6A) modification and nucleocytoplasmic trafficking of CGAS (613973), IFI16 (147586), and STING (612374) mRNAs. This, in turn, amplifies the activation of cytoplasmic TBK1-IRF3 mediated by these factors. Wang et al. (2019) concluded that HNRNPA2B1 plays important roles in initiating IFN-alpha/beta production and enhancing STING-dependent cytoplasmic antiviral signaling.
Biamonti et al. (1994) determined that the HNRNPA2B1 gene contains 12 exons, including an alternatively spliced 36-nucleotide mini-exon specific for the B1 protein. The intron/exon organization of HNRNPA2B1 is identical to that of the HNRNPA1 gene over its entire length, indicating a common origin by gene duplication.
Kozu et al. (1995) determined that the HNRNPA2B1 gene spans over 9 kb. The 5-prime region is GC rich and contains several binding sites for ubiquitous transcription factors, including 7 H4TF1 elements and 2 CCAAT boxes, but no TATA sequence. The 3-prime region contains a pyrimidine-rich RNA degradation motif prior to the polyadenylation signal. Intron 8 contains an Alu repeat that is not found in the HNRNPA1 gene.
Biamonti et al. (1994) mapped the HNRNPA2B1 gene to chromosome 7p15 by fluorescence in situ hybridization.
Inclusion Body Myopathy With Early-Onset Paget Disease And Frontotemporal Dementia 2
In a family (family 1, previously described by Waggoner et al. (2002)) with dominantly inherited degeneration of muscle, bone, brain, and motor neurons (IBMPFD2; 615422), Kim et al. (2013) identified a heterozygous missense mutation in the HNRNPA2B1 gene that altered a conserved aspartic acid at position 290 of the short (A2) isoform and 302 of the long (B1) isoform (D290V; 600124.0001). Kim et al. (2013) showed that the intrinsic tendency of HNRNPA2, the most abundant form of HNRNPA2B1, and HNRNPA1 (164017) to assemble into self-seeding fibrils is exacerbated by disease mutations. The pathogenic mutations strengthen a 'steric zipper' motif in the prion-like domain (PrLD) that accelerates the formation of self-seeding fibrils that cross-seed polymerization of wildtype HNRNP. Notably, disease mutations promoted excess incorporation of HNRNPA2 and HNRNPA1 into stress granules and drove the formation of cytoplasmic inclusions in animal models that recapitulated the human pathology. Kim et al. (2013) concluded that dysregulated polymerization caused by a potent mutant steric zipper motif in a PrLD can initiate degenerative disease.
By sequencing coding exons of the HNRNPA2B1 gene, Le Ber et al. (2014) failed to identify pathogenic mutations in a cohort of 17 unrelated French patients with sporadic or familial occurrence of multiple system proteinopathy manifest as frontotemporal lobar degeneration (FTLD) and/or amyotrophic lateral sclerosis (ALS) that segregated with Paget disease of bone (PDB), and/or inclusion body myositis (IBM). No mutations were found in 60 probands with FTLD or FTLD/ALS. By sequencing the prion-like domain of the HNRNPA2B1 gene, Seelen et al. (2014) also failed to identify any nonsynonymous mutations in 135 patients with familial ALS, 1,084 patients with sporadic ALS, 68 patients with familial FTLD, 74 patients with sporadic FTLD, and 31 patients with sporadic IBM. A splice site mutation (c.695A-G) was found in 1 patient with familial FTD, but functional studies and segregation analysis were not performed. All patients were from the Netherlands. The findings of both studies suggested that mutations in HNRNPA2B1 are a very rare cause of this spectrum of diseases.
Oculopharyngeal Muscular Dystrophy 2
In 11 patients from 10 unrelated families with oculopharyngeal muscular dystrophy-2 (OPMD2; 620460), Kim et al. (2022) identified heterozygous frameshift mutations in the last coding exon of the HNRNPA2B1 gene that affected both isoforms (see, e.g., 600124.0002-600124.0005). The mutations, which were found by exome sequencing, were not present in the gnomAD database. The mutations occurred de novo in 7 patients and were presumed to be de novo in 2; only 1 family (family 4) showed autosomal dominant inheritance of the mutation. All mutations occurred in the highly conserved M9 nuclear localization signal in the C-terminal LCD domain. The mutations all resulted in the same frameshift with a common C-terminal extension sequence. The mutant mRNAs escaped nonsense-mediated mRNA decay and resulted in the production of novel transcripts and proteins that showed aberrant accumulation in the cytoplasm of cells expressing the mutations. The mutations did not increase the propensity of the HNRNPA2 protein to fibrillize. In vitro studies of some of the mutations showed that they impaired the interaction between HNRNPA2 and its nuclear transport receptor TNPO1 (602901), suggesting a loss-of-function effect. However, the mutations caused increased apoptotic cell death in differentiating myoblasts, consistent with a toxic gain-of-function mechanism. The findings added to the growing spectrum of neuromuscular disorders caused by mutations in RNA-binding proteins (RBPs).
In affected members of a family (family 1) segregating autosomal dominant inclusion body myopathy with Paget disease of the bone and frontotemporal dementia (IBMPFD2; 615422), Kim et al. (2013) identified an 869A-T transversion in the A2 isoform of the HNRNPA2B1 gene (905A-T in the B1 isoform) resulting in an aspartic acid-to-valine substitution at codon 290 (D290V; ASP302VAL, D302V in the B1 isoform). This was the family originally reported by Waggoner et al. (2002). The aspartic acid at this position is evolutionarily conserved to Drosophila, and is centered in a motif, the prion-like domain (PrLD), that is conserved in multiple human paralogs of the HNRNP A/B family. The mutation segregated with the disease in the family and was not identified in the NHLBI Exome Sequencing Project. In another family with a similar phenotype, Kim et al. (2013) detected an aspartic acid-to-valine substitution at the analogous residue of HNRNPA1 (164017.0001).
In a 12-year-old boy (P1) with oculopharyngeal muscular dystrophy-2 (OPMD2; 620460), Kim et al. (2022) identified a de novo heterozygous 1-bp deletion (c.992delG, NM_002137) in the last coding exon affecting both isoforms of the HNRNPA2B1 gene. The deletion resulted in frameshift and extension of the reading frame (Gly331GlufsTer28). The mutation, which was found by exome sequencing, was not present in the gnomAD database. The mutation occurred in the highly conserved M9 nuclear localization signal in the C-terminal LCD domain. The transcript escaped nonsense-mediated mRNA decay and resulted in the production of a novel protein that showed aberrant accumulation in the cytoplasm of cells expressing the mutation. In vitro studies showed that the variant impaired the interaction between HNRNPA2 and its nuclear transport receptor TNPO1 (602901), suggesting a loss-of-function effect. However, the mutation caused increased apoptotic cell death in differentiating myoblasts, consistent with a toxic gain-of-function mechanism. The patient had onset of symptoms at 2 years of age.
In a 17-year-old boy (P2) with oculopharyngeal muscular dystrophy-2 (OPMD2; 620460), Kim et al. (2022) identified a de novo heterozygous 1-bp deletion (c.981delA, NM_002137) in the last coding exon affecting both isoforms of the HNRNPA2B1 gene. The deletion resulted in frameshift and extension of the reading frame (Gly328AlafsTer31). The mutation, which was found by exome sequencing, was not present in the gnomAD database. The mutation occurred in the highly conserved M9 nuclear localization signal in the C-terminal LCD domain. The transcript escaped nonsense-mediated mRNA decay and resulted in the production of a novel protein that showed aberrant accumulation in the cytoplasm of cells expressing the mutation. In vitro studies showed that the variant impaired the interaction between HNRNPA2 and its nuclear transport receptor TNPO1 (602901), suggesting a loss-of-function effect. However, the mutation caused increased apoptotic cell death in differentiating myoblasts, consistent with a toxic gain-of-function mechanism. The patient had onset of symptoms at 5 years of age.
In 2 sisters (family 4, P4 and P5) with oculopharyngeal muscular dystrophy-2 (OPMD2; 620460), Kim et al. (2022) identified a heterozygous 1-bp deletion (c.966delA, NM_002137) in the last coding exon affecting both isoforms of the HNRNPA2B1 gene. The deletion resulted in frameshift and extension of the reading frame (Asn323ThrfsTer36). The mutation, which was found by exome sequencing, was not present in the gnomAD database. The mutation occurred in the highly conserved M9 nuclear localization signal in the C-terminal LCD domain. The transcript escaped nonsense-mediated mRNA decay and resulted in the production of a novel protein that showed aberrant accumulation in the cytoplasm of cells expressing the mutation. In vitro studies showed that the variant impaired the interaction between HNRNPA2 and its nuclear transport receptor TNPO1 (602901), suggesting a loss-of-function effect. However, the mutation caused increased apoptotic cell death in differentiating myoblasts, consistent with a toxic gain-of-function mechanism. The patients had onset of symptoms in their late teens.
In 2 unrelated girls (P7 and P10) with oculopharyngeal muscular dystrophy-2 (OPMD2; 620460), Kim et al. (2022) identified a de novo heterozygous 2-bp duplication (c.996_997dupTG, NM_002137) in the last coding exon affecting both isoforms of the HNRNPA2B1 gene. The duplication resulted in frameshift and extension of the reading frame (Gly333ValfsTer27). The mutation, which was found by exome sequencing, was not present in the gnomAD database. The mutation occurred in the highly conserved M9 nuclear localization signal in the C-terminal LCD domain and was predicted to escape nonsense-mediated mRNA decay. Both patients had a severe form of the disorder with onset of symptoms in infancy or early childhood, respiratory insufficiency, dysphagia requiring tube-feeding, and loss of independent ambulation in the first decade.
Biamonti, G., Ruggiu, M., Saccone, S., Della Valle, G., Riva, S. Two homologous genes, originated by duplication, encode the human hnRNP proteins A2 and A1. Nucleic Acids Res. 22: 1996-2002, 1994. [PubMed: 8029005] [Full Text: https://doi.org/10.1093/nar/22.11.1996]
Burd, C. G., Swanson, M. S., Gorlach, M., Dreyfuss, G. Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts. Proc. Nat. Acad. Sci. 86: 9788-9792, 1989. [PubMed: 2557628] [Full Text: https://doi.org/10.1073/pnas.86.24.9788]
David, C. J., Chen, M., Assanah, M., Canoll, P., Manley, J. L. HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer. Nature 463: 364-368, 2010. [PubMed: 20010808] [Full Text: https://doi.org/10.1038/nature08697]
Hamilton, B. J., Nichols, R. C., Tsukamoto, H., Boado, R. J., Pardridge, W. M., Rigby, W. F. C. hnRNP A2 and hnRNP L bind the 3-prime UTR of glucose transporter 1 mRNA and exist as a complex in vivo. Biochem. Biophys. Res. Commun. 261: 646-651, 1999. [PubMed: 10441480] [Full Text: https://doi.org/10.1006/bbrc.1999.1040]
Iwanaga, K., Sueoka, N., Sato, A., Hayashi, S., Sueoka, E. Heterogeneous nuclear ribonucleoprotein B1 protein impairs DNA repair mediated through the inhibition of DNA-dependent protein kinase activity. Biochem. Biophys. Res. Commun. 333: 888-895, 2005. [PubMed: 15964549] [Full Text: https://doi.org/10.1016/j.bbrc.2005.05.180]
Kim, H. J., Kim, N. C., Wang, Y.-D., Scarborough, E. A., Moore, J., Diaz, Z., MacLea, K. S., Freibaum, B., Li, S., Molliex, A., and 25 others. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 495: 467-473, 2013. [PubMed: 23455423] [Full Text: https://doi.org/10.1038/nature11922]
Kim, H. J., Mohassel, P., Donkervoort, S., Guo, L., O'Donovan, K., Coughlin, M., Lornage, X., Foulds, N., Hammans, S. R., Foley, A. R., Fare, C. M., Ford, A. F., and 46 others. Heterozygous frameshift variants in HNRNPA2B1 cause early-onset oculopharyngeal muscular dystrophy. Nature Commun. 13: 2306, 2022. [PubMed: 35484142] [Full Text: https://doi.org/10.1038/s41467-022-30015-1]
Kosturko, L. D., Maggipinto, M. J., Korza, G., Lee, J. W., Carson, J. H., Barbarese, E. Heterogeneous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs. Molec. Biol. Cell 17: 3521-3533, 2006. [PubMed: 16775011] [Full Text: https://doi.org/10.1091/mbc.e05-10-0946]
Kozu, T., Henrich, B., Schafer, K. P. Structure and expression of the gene (HNRPA2B1) encoding the human hnRNP protein A2/B1. Genomics 25: 365-371, 1995. [PubMed: 7789969] [Full Text: https://doi.org/10.1016/0888-7543(95)80035-k]
Le Ber, I., Van Bortel, I., Nicolas, G., Bouya-Ahmed, K., Camuzat, A., Wallon, D., De Septenville, A., Latouche, M., Lattante, S., Kabashi, E., Jornea, L., Hannequin, D., Brice, A., French research Network on FTLD/FTLD-ALS. hnRNPA2B1 and hnRNPA1 mutations are rare in patients with 'multisystem proteinopathy' and frontotemporal lobar degeneration phenotypes. Neurobiol. Aging 35: 934.e5-6, 2014. [PubMed: 24119545] [Full Text: https://doi.org/10.1016/j.neurobiolaging.2013.09.016]
Moran-Jones, K., Grindlay, J., Jones, M., Smith, R., Norman, J. C. hnRNP A2 regulates alternative mRNA splicing of TP53INP2 to control invasive cell migration. Cancer Res. 69: 9219-9227, 2009. [PubMed: 19934309] [Full Text: https://doi.org/10.1158/0008-5472.CAN-09-1852]
Moran-Jones, K., Wayman, L., Kennedy, D. D., Reddel, R. R., Sara, S., Snee, M. J., Smith, R. hnRNP A2, a potential ssDNA/RNA molecular adapter at the telomere. Nucleic Acids Res. 33: 486-496, 2005. [PubMed: 15659580] [Full Text: https://doi.org/10.1093/nar/gki203]
Seelen, M., Visser, A. E., Overste, D. J., Kim, H. J., Palud, A., Wong, T. H., van Swieten, J. C., Scheltens, P., Voermans, N. C., Baas, F., de Jong, J. M. B. V., van der Kooi, A. J., de Visser, M., Veldink, J. H., Taylor, J. P., Van Es, M. A., van den Berg, L. H. No mutations in hnRNPA1 and hnRNPA2B1 in Dutch patients with amyotrophic lateral sclerosis, frontotemporal dementia, and inclusion body myopathy. Neurobiol. Aging 35: 1956.e9-1956.e11, 2014. [PubMed: 24612671] [Full Text: https://doi.org/10.1016/j.neurobiolaging.2014.01.152]
Sofola, O. A., Jin, P., Qin, Y., Duan, R., Liu, H., de Haro, M., Nelson, D. L., Botas, J. RNA-binding proteins hnRNP A2/B1 and CUGBP1 suppress fragile X CGG premutation repeat-induced neurodegeneration in a Drosophila model of FXTAS. Neuron 55: 565-571, 2007. [PubMed: 17698010] [Full Text: https://doi.org/10.1016/j.neuron.2007.07.021]
Waggoner, B., Kovach, M. J., Winkelman, M., Cai, D., Khardori, R., Gelber, D., Kimonis, V. E. Heterogeneity in familial dominant Paget disease of bone and muscular dystrophy. Am. J. Med. Genet. 108: 187-191, 2002. [PubMed: 11891683] [Full Text: https://doi.org/10.1002/ajmg.10199]
Wang, L., Wen, M., Cao, X. Nuclear hnRNPA2B1 initiates and amplifies the innate immune response to DNA viruses. Science 365: eaav0758, 2019. Note: Electronic Article. [PubMed: 31320558] [Full Text: https://doi.org/10.1126/science.aav0758]