Recombinant Human Selenoprotein N (SEPN1)

1. Case Report: rigid spine muscular dystrophy 1 in a compound heterozygote with two novel mutations in SEPN1 gene; a novel missense mutation (c.1384T>C; p.Sec462Arg) and a novel nonsense mutation (c.1525C>T; p.Gln509Ter), inherited from his father and mother respectively. PMID: 27863379
2. We report two previously undescribed mutations in SEPN1. Our study adds two novel homozygous mutations to the number of reported pathogenic SEPN1 variants. PMID: 26780752
3. The physiological function of SelN in muscle tissue and the pathogenesis leading to SEPN1-related myopathies. [Review] PMID: 22527882
4. Data show that the spectrum of severity of SEPN1-related myopathiesis wider than previously reported. PMID: 21670436
5. Data show that Argonaute 2 expression is critical for stem cells to escape senescence by downregulating miR10b and miR23b, and that selenoprotein N1 is also involved in ATSC survival and self-renewal through ROS-mediated p38 MAPK inactivation. PMID: 21241449
6. this series of patients illustrates the clinical, histopathological and MRI findings of SEPN1-related myopathy. It also adds new mutations to the limited number of fully described pathogenic SEPN1 variants. PMID: 20937510
7. Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease PMID: 12192640
8. A new SEPN1 point mutation, 943g->A causing G315S was found in a rigid spine muscular dystrophy patient with cor pulmonale. PMID: 15668457
9. SEPN1 mutation analysis revealed that the patient was a compound heterozygote: a previously described insertion (713-714 insA), and a novel nonsense mutation (R439stop). PMID: 15792869
10. Two patients with 'Dropped head syndrome' due to mutations in SEPN1 genes. PMID: 15961312
11. SEPN1 is the second genetic cause of CFTD and the first cause of autosomal recessive CFTD to be identified to our knowledge. CFTD is the fourth clinicopathological presentation that can be associated with mutations in SEPN1. PMID: 16365872
12. identification of this mutation affecting a conserved base in the selenocysteine insertion sequence functional motif thereby reveals the structural basis for a novel pathological mechanism leading to SEPN1-related myopathy PMID: 16498447
13. We report on the possible molecular mechanism behind these mutations in SEPN1. Our study clarifies molecular mechanisms of this muscular disorder. PMID: 16779558
14. SEPN1 and RYR1 are required for the same cellular differentiation events and are needed for normal calcium fluxes PMID: 18713863
15. Data highlights the importance of the SRE element during SelN expression and illustrates a novel molecular mechanism by which point mutations may lead to SEPN1-related myopathy. PMID: 19067361
16. SelN plays a key role in redox homeostasis and human cell protection against oxidative stress. PMID: 19557870
17. The Alu-derived exon 3 of human SEPN1 acquired its muscle-specific splicing activity after the divergence of humans and chimpanzees, suggesting its potential role in human evolution. PMID: 18841251

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HGNC: 15999

OMIM: 255310

KEGG: hsa:57190

STRING: 9606.ENSP00000355141

UniGene: Hs.323396