Alternative titles; symbols
HGNC Approved Gene Symbol: SMARCA2
SNOMEDCT: 401046009;
Cytogenetic location: 9p24.3 Genomic coordinates (GRCh38) : 9:2,015,347-2,193,620 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 9p24.3 | Blepharophimosis-impaired intellectual development syndrome | 619293 | Autosomal dominant | 3 |
| Nicolaides-Baraitser syndrome | 601358 | Autosomal dominant | 3 |
The SMARCA2 gene encodes a helicase-related catalytic subunit of a complex involved in chromatin remodeling that regulates gene expression (summary by Cappuccio et al., 2020).
The yeast protein SNF2, also known as SWI2, is involved in transcriptional activation of numerous genes. It contains a domain that is highly conserved among several known helicases and is required for transcriptional activity. SNF2/SWI2 is highly homologous to the Drosophila protein 'brahma' (brm). In human cells, Muchardt and Yaniv (1993) identified SMARCA2, the homolog of yeast SNF2/SWI2 and Drosophila brm. The human SMARCA2 protein is 56% identical and 72% homologous to Drosophila brm. See also SMARCA1 (300012).
Koga et al. (2009) noted that the SMARCA2 gene contains 34 exons spanning 178.2 kb.
By interspecific backcross linkage analysis, Pilz et al. (1995) mapped the Snf2l2 gene to mouse chromosome 19. Muchardt et al. (1994) mapped the BRM gene in the human to chromosome 9p24-p23 by isotopic in situ hybridization. Ion et al. (1998) refined the localization of the SMARCA2 gene to chromosome 9p24.1 using a fluorescence in situ hybridization technique with fluorescently-labeled YACs. Koga et al. (2009) stated that the SMARCA2 gene maps to chromosome 9p24.3.
Muchardt et al. (1996) found that the human homolog of brm and another protein, BRG1 (603254), are phosphorylated during mitosis. Although the 2 proteins show nuclear localization during interphase, they are excluded from the condensed chromosomes during mitosis. They found that the level of BRM, but not BRG1, was strongly reduced during mitosis. Phosphorylation of BRM and BRG1 did not disrupt their association with SNF5 but correlated with a decreased affinity for the nuclear structure in early M phase. The authors suggested that chromosomal exclusion of the human SNF/SWI complex at the G2-M transition is part of the mechanism leading to transcriptional arrest during mitosis.
Mammalian SWI/SNF complexes are ATP-dependent chromatin remodeling enzymes that have been implicated in the regulation of gene expression, cell cycle control, and oncogenesis. MyoD (MYOD1; 159970) is a muscle-specific regulator capable of inducing myogenesis in numerous cell types. To ascertain the requirement for chromatin remodeling enzymes in cellular differentiation processes, de la Serna et al. (2001) examined MyoD-mediated induction of muscle differentiation in fibroblasts expressing dominant-negative versions of the human brahma-related gene-1 (BRG1; 603254) or human brahma, the ATPase subunits of 2 distinct SWI/SNF enzymes. They found that induction of the myogenic phenotype was completely abrogated in the presence of the mutant enzymes. They further demonstrated that failure to induce muscle-specific gene expression correlated with inhibition of chromatin remodeling in the promoter region of an endogenous muscle-specific gene. The results demonstrated that SWI/SNF enzymes promote MyoD-mediated muscle differentiation and indicated that these enzymes function by altering chromatin structure in promoter regions of endogenous, differentiation-specific loci.
Hakimi et al. (2002) reported the isolation of a human SNF2-containing chromatin remodeling complex that encompasses components of the cohesin and NURD (see 603526) complexes. They showed that the RAD21 (606462) subunit of the cohesin complex directly interacts with the ATPase subunit SNF2. Mapping of RAD21, SNF2, and Mi2 (see 603277) binding sites by chromatin immunoprecipitation experiments revealed the specific association of these 3 proteins with human DNA elements containing alu sequences. Hakimi et al. (2002) found a correlation between modification of histone tails and association of the SNF2/cohesin complex with chromatin. In addition, they showed that the association of the cohesin complex with chromatin can be regulated by the state of DNA methylation. Finally, they presented evidence pointing to a role for the ATPase activity of SNF2 in the loading of RAD21 on chromatin.
Kadam and Emerson (2003) showed that BRG1 and BRM associate with different promoters during cellular proliferation and differentiation, and in response to specific signaling pathways by preferential interaction with certain classes of transcription factors. BRG1 binds to zinc finger proteins through a unique N-terminal domain that is not present in BRM. BRM interacts with 2 ankyrin repeat proteins that are critical components of Notch signal transduction. The authors concluded that BRG1 and BRM complexes may direct distinct cellular processes by recruitment to specific promoters through protein-protein interactions that are unique to each ATPase.
Harikrishnan et al. (2005) found that BRM associated with MECP2 (300005) in mouse fibroblasts and human T-lymphoblastic leukemia cells, and the association was functionally linked with repression. Promoter methylation specified the recruitment of MECP2 and BRM, and inhibition of methylation caused their release. The MECP2-BRM corepressor complex was directly recruited to the FMR1 gene (309550), and somatic knockdown in fragile X cells alleviated the repression. Harikrishnan et al. (2005) concluded that both MECP2 and components of the SWI/SNF complex are involved in gene repression.
Loe-Mie et al. (2010) showed that an SWI/SNF-centered network including the Smarca2 gene was modified by the downregulation of REST/NRSF (600571) in a mouse neuronal cell line. REST/NRSF downregulation also modified the levels of Smarce1 (603111), Smarcd3 (601737), and SWI/SNF interactors Hdac1 (601241), RcoR (607675), and Mecp2 (300005). Smarca2 downregulation generated an abnormal dendritic spine morphology that was an intermediate phenotype of schizophrenia (see 181500). The authors noted that 8 genomewide-supported schizophrenia-associated genes (SMARCA2; CSF2RA, 306250; HIST1H2BJ, 615044; NOTCH4, 164951; NRGN, 602350; SHOX, 312865; TCF4, 602272; and ZNF804A, 612282) are part of an interacting network; 5 of the 8 encode transcription regulators, and 3 (TCF4, SMARCA2, and CSF2RA) were modified at the level of expression when the REST/NRSF-SWI/SNF chromatin remodeling complex was experimentally manipulated in mouse cell lines and in transgenic mouse models. REST/NRSF-SWI/SNF deregulation also resulted in the differential expression of genes that are clustered in chromosomes, suggesting the induction of genomewide epigenetic changes. Loe-Mie et al. (2010) concluded that the SWI/SNF chromatin remodeling complex is a key component of the genetic architecture of schizophrenia.
Nicolaides-Baraitser Syndrome
In 36 of 44 individuals with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified de novo heterozygous missense mutations in the SMARCA2 gene (see, e.g., 600014.0001-600014.0012). The mutations clustered within sequences that encode ultraconserved motifs in the catalytic ATPase region of the protein. These alterations likely do not impair SWI/SNF complex assembly but may be associated with disrupted ATPase activity.
Wolff et al. (2012) reported 3 additional patients with SMARCA2 mutations causing Nicolaides-Baraitser syndrome. One was an in-frame deletion and 2 were missense mutations in the C-terminal helicase domain, in one patient resulting in a relative preservation of intellectual functioning despite classic dysmorphism (see 600014.0014).
Blepharophimosis-Impaired Intellectual Development Syndrome
In 14 patients with blepharophimosis-impaired intellectual development syndrome (BIS; 619293), Cappuccio et al. (2020) identified de novo heterozygous missense mutations in the SMARCA2 gene (see, e.g., 600014.0015-600014.0019). The mutations, which were found by genome, exome, or targeted sequencing and confirmed by Sanger sequencing, were not present in the gnomAD database. The mutations clustered in 2 regions located outside of the catalytic ATPase helicase domains. Some occurred in exons 8 or 9, corresponding to a region between the HSA and helicase ATP-binding domain, whereas others occurred in exon 19, mapping to the linker region located between the DExx helicase ATP-binding and helicase C-terminal domains. Structural analysis of the variants using the yeast homolog (Snf2) showed that the residues mutated in BIS are on an alpha-helix that is likely at the interface with other members of the SWI/SNF complex. Introduction of mutations corresponding to E929V and R937L (600014.0018 and 600014.0019) in yeast showed no growth abnormalities, being similar to wildtype. RNA-seq transcriptome analysis of blood derived from 2 patients (patients 1 and 9) showed some differential gene expression profiles compared to cells from patients with NCBRS. However, there was a close expression profile shared by BIS and NCBRS compared to controls. Cells from patients with BIS and NCBRS also showed some differences in methylation signature patterns. Additional functional studies of the variants were not performed. The authors concluded that SMARCA2 variants outside of the helicase domain result in a phenotypically and molecularly distinct disorder from NCBRS.
Association with Schizophrenia
Koga et al. (2009) reported an association between schizophrenia (see 181500) and 3 SNPs in 2 linkage disequilibrium blocks of the SMARCA2 gene in the Japanese population. A risk allele of a missense polymorphism in exon 33 (D1546E; rs2296212) induced a lower nuclear localization efficiency of BRM, and risk alleles of intronic polymorphisms (rs3763627 and rs3793490) were associated with low SMARCA2 expression levels in the postmortem prefrontal cortex. The fold change of gene expression of 606 genes from schizophrenia prefrontal cortex samples (SMRI database) was significantly correlated with expression changes seen in transfected human T98G cells. Koga et al. (2009) proposed a role for BRM in the pathophysiology of schizophrenia.
Koga et al. (2009) generated Smarca2-knockout mice, which showed impaired social interaction and prepulse inhibition. Psychogenic drugs, such as MK-801 or methamphetamine, lowered Smarca2 expression, while antipsychotic drugs, such as haloperidol or olanzapine, increased Smarca2 expression in the brain of 4-week-old wildtype mice.
In a patient with typical features of Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a heterozygous C-to-T transition at nucleotide 3637 in exon 25 of the SMARCA2 gene, resulting in an arg-to-trp substitution at codon 1213 (R1213W). This mutation was not identified in 1,300 exomes of unaffected individuals.
In an individual with Nicolaides-Baraitser syndrome (NCBRS; 601358) who underwent whole-exome sequencing, Van Houdt et al. (2012) identified a heterozygous G-to-T transversion at nucleotide 3604 in exon 25 of the SMARCA2 gene, resulting in a gly-to-cys substitution at codon 1202 (G1202C). This mutation occurred de novo and was not found in 1,300 exomes of unaffected individuals.
In 2 unrelated individuals with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a heterozygous G-to-A transition at nucleotide 3476 in exon 25 of the SMARCA2 gene, resulting in an arg-to-gln substitution at codon 1159 (R1159Q). This mutation occurred as a de novo event in both individuals and was not identified in 1,300 exomes from unaffected individuals. Van Houdt et al. (2012) identified different mutations at this codon in other patients (600014.0005, 600014.0008).
In an individual with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a de novo heterozygous A-to-T transversion at nucleotide 3473 in exon 25 of the SMARCA2 gene, resulting in an asp-to-val substitution at codon 1158 (D1158V). This mutation was not present in 1,300 control exomes.
In an individual with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a de novo heterozygous C-to-G transversion at nucleotide 3475 in exon 25 of the SMARCA2 gene, resulting in an arg-to-gly substitution at codon 1159 (R1159G). This mutation was not present in 1,300 control exomes. Van Houdt et al. (2012) identified different mutations at this codon in other patients (600014.0003, 600014.0008).
In an individual with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a heterozygous G-to-T transversion at nucleotide 2642 in exon 18 of the SMARCA2 gene, resulting in a gly-to-val substitution at codon 881 (G881V). This mutation was not present in the patient's mother (no sample from the father was available), nor was it seen in 1,300 exomes from unaffected individuals.
In an individual with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a de novo heterozygous G-to-A transition at nucleotide 3485 in exon 25 of the SMARCA2 gene, resulting in an arg-to-his substitution at codon 1162 (R1162H). This mutation was not seen in 1,300 control exomes.
In an individual with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a heterozygous G-to-T transversion at nucleotide 3476 in exon 25 of the SMARCA2 gene, resulting in an arg-to-leu substitution at codon 1159 (R1159L). Neither parent was available for testing. This mutation was not identified in 1,300 control exomes. Van Houdt et al. (2012) identified different mutations at this codon in other patients (600014.0003, 600014.0005).
In 3 unrelated individuals with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a heterozygous C-to-T transition at nucleotide 2648 in exon 18 of the SMARCA2 gene, resulting in a pro-to-leu substitution at codon 883 (P883L). In one individual the mutation was shown to have occurred de novo; parents of the other 2 individuals were unavailable for testing. This mutation was not seen in 1,300 control exomes.
In 3 unrelated individuals with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a heterozygous C-to-T transition at nucleotide 3602 in exon 25 of the SMARCA2 gene, resulting in a ala-to-val substitution at codon 1201 (A1201V). In 2 of the patients the mutation was confirmed to have occurred de novo. The mutation was not seen in 1,300 control exomes.
In an individual with Nicolaides-Baraitser syndrome (NCBRS; 601358), Van Houdt et al. (2012) identified a heterozygous de novo C-to-T transition at nucleotide 2815 in exon 19 of the SMARCA2 gene, resulting in a his-to-tyr substitution at codon 939 (H939Y). This mutation was not seen in 1,300 control exomes.
In monozygotic twins with Nicolaides-Baraitser syndrome (NCBRS; 601358), originally reported by Sousa et al. (2009), Van Houdt et al. (2012) identified a G-to-C transversion at nucleotide 2255 in exon 15 of the SMARCA2 gene, resulting in a gly-to-ala substitution at codon 752 (G752A). Neither parent was available for testing. This mutation was not seen in 1,300 control exomes.
In an individual with Nicolaides-Baraitser syndrome (NCBRS; 601358), Tsurusaki et al. (2012) detected a 55-kb interstitial deletion of SMARCA2 arising as a de novo occurrence. The deletion resulted in skipping of exons 20 through 27. The patient, subject 19, did not have sparse hair but did have developmental delay, hypotonia, and microcephaly, as well as vision problems, hearing loss, and seizures. He was noted to be hirsute, with thick eyebrows, long eyelashes, and abnormal dentition, and had a coarse facial appearance with flat nasal bridge, broad nose, wide mouth, thick lips, and abnormal ears. Spinal anomalies, delayed bone age, feeding problems, and intestinal anomalies were also present. Although the phenotype of the patient was classified as Coffin-Siris syndrome (135900), the patient lacked absent/hypoplastic fifth phalanx of hands or feet and corresponding nails.
In a 9-year-old boy with Nicolaides-Baraitser syndrome (NCBRS; 601358), Wolff et al. (2012) detected a heterozygous de novo G-to-A transition at nucleotide 3395 in the SMARCA2 gene, resulting in a gly-to-asp substitution at codon 1132 (G1132D). The glycine at position 1132 resides in the helicase domain and is conserved among species from human to zebrafish. Birth parameters were at the tenth percentile and height was at the fifth percentile at 9 years of age. Wolff et al. (2012) reported that the child had a borderline IQ of 74 with relatively good verbal skills and no autistic features. Dysmorphologic features typical of Nicolaides-Baraitser syndrome were present.
In a 9-year-old girl (patient 1) with blepharophimosis-impaired intellectual development syndrome (BIS; 619293), Cappuccio et al. (2020) identified a de novo heterozygous c.1514G-A transition (c.1514G-A, NM_001289396) in exon 8 of the SMARCA2 gene, resulting in an arg505-to-gln (R505Q) substitution at a conserved residue between the HSA and helicase ATP-binding domains. The mutation, which was found by exome sequencing and confirmed by Sanger sequencing, was not present in the gnomAD database.
In 2 girls (patients 3 and 4) with blepharophimosis-impaired intellectual development syndrome (BIS; 619293), Cappuccio et al. (2020) identified a de novo heterozygous c.1574G-A transition (c.1574G-A, NM_001289396) in exon 9 of the SMARCA2 gene, resulting in an arg525-to-his (R525H) substitution at a conserved residue between the HSA and helicase ATP-binding domains. The mutation, which was found by exome sequencing and confirmed by Sanger sequencing, was not present in the gnomAD database.
In 2 girls (patients 5 and 6) with blepharophimosis-impaired intellectual development syndrome (BIS; 619293), Cappuccio et al. (2020) identified a de novo heterozygous c.1573C-T transition (c.1573C-T, NM_001289396) in exon 9 of the SMARCA2 gene, resulting in an arg525-to-cys (R525C) substitution at a conserved residue between the HSA and helicase ATP-binding domain. The mutation, which was found by exome sequencing and confirmed by Sanger sequencing, was not present in the gnomAD database.
In a 9-year-old boy (patient 9) with blepharophimosis-impaired intellectual development syndrome (BIS; 619293), Cappuccio et al. (2020) identified a de novo heterozygous c.2786A-T transversion (c.2786A-T, NM_001289396) in exon 19 of the SMARCA2 gene, resulting in a glu929-to-val (E929V) substitution at a conserved residue in the linker region between the DExx helicase ATP-binding and helicase C-terminal domains. The mutation, which was found by targeted sequencing and confirmed by Sanger sequencing, was not present in the gnomAD database.
In 2 boys (patients 12 and 13) with blepharophimosis-impaired intellectual development syndrome (BIS; 619293), Cappuccio et al. (2020) identified a de novo heterozygous c.2810G-T transversion (c.2810G-T, NM_001289396) in exon 19 of the SMARCA2 gene, resulting in an arg937-to-leu (R937L) substitution at a conserved residue in the linker region between the DExx helicase ATP-binding and helicase C-terminal domains. The mutation, which was found by exome sequencing and confirmed by Sanger sequencing, was not present in the gnomAD database.
Cappuccio, G., Sayou, C., Le Tanno, P., Tisserant, E., Bruel, A.-L., El Kennani, S., Sa, J., Low, K. J., Dias, C., Havlovicova, M., Hancarova, M., Eichler, E. E., and 36 others. De novo SMARCA2 variants clustered outside the helicase domain cause a new recognizable syndrome with intellectual disability and blepharophimosis distinct from Nicolaides-Baraitser syndrome. Genet. Med. 22: 1838-185, 2020. [PubMed: 32694869] [Full Text: https://doi.org/10.1038/s41436-020-0898-y]
de la Serna, I. L., Carlson, K. A., Imbalzano, A. N. Mammalian SWI/SNF complexes promote MyoD-mediated muscle differentiation. Nature Genet. 27: 187-190, 2001. [PubMed: 11175787] [Full Text: https://doi.org/10.1038/84826]
Hakimi, M.-A., Bochar, D. A., Schmiesing, J. A., Dong, Y., Barak, O. G., Speicher, D. W., Yokomori, K., Shiekhattar, R. A chromatin remodelling complex that loads cohesin onto human chromosomes. Nature 418: 994-998, 2002. [PubMed: 12198550] [Full Text: https://doi.org/10.1038/nature01024]
Harikrishnan, K. N., Chow, M. Z., Baker, E. K., Pal, S., Bassal, S., Brasacchio, D., Wang, L., Craig, J. M., Jones, P. L., Sif, S., El-Osta, A. Brahma links the SWI/SNF chromatin-remodeling complex with MeCP2-dependent transcriptional silencing. Nature Genet. 37: 254-264, 2005. [PubMed: 15696166] [Full Text: https://doi.org/10.1038/ng1516]
Ion, R., Telvi, L., Chaussain, J.-L., Barbet, J. P., Nunes, M., Safar, A., Rethore, M.-O., Fellous, M., McElreavey, K. Failure of testicular development associated with a rearrangement of 9p24.1 proximal to the SNF2 gene. Hum. Genet. 102: 151-156, 1998. [PubMed: 9521582] [Full Text: https://doi.org/10.1007/s004390050669]
Kadam, S., Emerson, B. M. Transcriptional specificity of human SWI/SNF BRG1 and BRM chromatin remodeling complexes. Molec. Cell 11: 377-389, 2003. [PubMed: 12620226] [Full Text: https://doi.org/10.1016/s1097-2765(03)00034-0]
Koga, M., Ishiguro, H., Yazaki, S., Horiuchi, Y., Arai, M., Niizato, K., Iritani, S., Itokawa, M., Inada, T., Iwata, N., Ozaki, N., Ujike, H., and 11 others. Involvement of SMARCA2/BRM in the SWI/SNF chromatin-remodeling complex in schizophrenia. Hum. Molec. Genet. 18: 2483-2494, 2009. [PubMed: 19363039] [Full Text: https://doi.org/10.1093/hmg/ddp166]
Loe-Mie, Y., Lepagnol-Bestel, A.-M., Maussion, G., Doron-Faigenboim, A., Imbeaud, S., Delacroix, H., Aggerbeck, L., Pupko, T., Gorwood, P., Simonneau, M., Moalic, J.-M. SMARCA2 and other genome-wide supported schizophrenia-associated genes: regulation by REST/NRSF, network organization and primate-specific evolution. Hum. Molec. Genet. 19: 2841-2857, 2010. [PubMed: 20457675] [Full Text: https://doi.org/10.1093/hmg/ddq184]
Muchardt, C., Reyes, J. C., Bourachot, B., Leguoy, E., Yaniv, M. The hbrm and BRG-1 proteins, components of the human SNF/SWI complex, are phosphorylated and excluded from the condensed chromosomes during mitosis. EMBO J. 15: 3394-3402, 1996. [PubMed: 8670841]
Muchardt, C., Yaniv, M., Mattei, M.-G. Assignment of HBRM, the human homolog of S. cerevisiae SNF2/SWI2 and Drosophila brm genes, to chromosome region 9p23-p24, by in situ hybridization. Mammalian Genome 5: 241-243, 1994. [PubMed: 8012116] [Full Text: https://doi.org/10.1007/BF00360554]
Muchardt, C., Yaniv, M. A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. EMBO J. 12: 4279-4290, 1993. [PubMed: 8223438] [Full Text: https://doi.org/10.1002/j.1460-2075.1993.tb06112.x]
Pilz, A., Woodward, K., Povey, S., Abbott, C. Comparative mapping of 50 human chromosome 9 loci in the laboratory mouse. Genomics 25: 139-149, 1995. [PubMed: 7774911] [Full Text: https://doi.org/10.1016/0888-7543(95)80119-7]
Sousa, S. B., Abdul-Rahman, O. A., Bottani, A., Cormier-Daire, V., Fryer, A., Gillessen-Kaesbach, G., Horn, D., Josifova, D., Kuechler, A., Lees, M., MacDermot, K., Magee, A., and 9 others. Nicolaides-Baraitser syndrome: delineation of the phenotype. Am. J. Med. Genet. 149A: 1628-1640, 2009. [PubMed: 19606471] [Full Text: https://doi.org/10.1002/ajmg.a.32956]
Tsurusaki, Y., Okamoto, N., Ohashi, H., Kosho, T., Imai, Y., Hibi-Ko, Y., Kaname, T., Naritomi, K., Kawame, H., Wakui, K., Fukushima, Y., Homma, T., and 19 others. Mutations affecting components of the SWI/SNF complex cause Coffin-Siris syndrome. Nature Genet. 44: 376-378, 2012. [PubMed: 22426308] [Full Text: https://doi.org/10.1038/ng.2219]
Van Houdt, J. K. J., Nowakowska, B. A., Sousa, S. B., van Schaik, B. D. C., Seuntjens, E., Avonce, N., Sifrim, A., Abdul-Rahman, O. A., van den Boogaard, M.-J. H., Bottani, A., Castori, M., Cormier-Daire, V., and 37 others. Heterozygous missense mutations in SMARCA2 cause Nicolaides-Baraitser syndrome. Nature Genet. 44: 445-449, 2012. [PubMed: 22366787] [Full Text: https://doi.org/10.1038/ng.1105]
Wolff, D., Endele, S., Azzarello-Burri, S., Hoyer, J., Zweier, M., Schanze, I., Schmitt, B., Rauch, A., Reis, A., Zweier, C. In-frame deletion and missense mutations of the C-terminal helicase domain of SMARCA2 in three patients with Nicolaides-Baraitser syndrome. Molec. Syndromol. 2: 237-244, 2012. [PubMed: 22822383] [Full Text: https://doi.org/10.1159/000337323]