ArticleStructure (London, England : 1993)2016
Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence Motif.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- RBM protein family: Focusing on the occurrence, progression and treatment of cancer.Medical oncology (Northwood, London, England) · 2026Review
- Shared genetic architecture between stroke and blood lipids: a large-scale genome-wide cross-trait analysis.Human genomics · 2025Article
- Structural basis for specific RNA recognition by the alternative splicing factor RBM5.Nature communications · 2023Article
- RBM6 splicing factor promotes homologous recombination repair of double-strand breaks and modulates sensitivity to chemotherapeutic drugs.Nucleic acids research · 2021Article
- Sequestration of RBM10 in Nuclear Bodies: Targeting Sequences and Biological Significance.International journal of molecular sciences · 2021Article
- Do polyproline II helix associations modulate biomolecular condensates?FEBS open bio · 2021Review
- Review
- RBM10: Harmful or helpful-many factors to consider.Journal of cellular biochemistry · 2018Review
- Article
- Article
- The acidic domain is a unique structural feature of the splicing factor SYNCRIP.Protein science : a publication of the Protein Society · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The OCtamer REpeat (OCRE) has been annotated as a 42-residue sequence motif with 12 tyrosine residues in the spliceosome trans-regulatory elements RBM5 and RBM10 (RBM [RNA-binding motif]), which are known to regulate alternative splicing of Fas and Bcl-x pre-mRNA transcripts. Nuclear magnetic resonance structure determination showed that the RBM10 OCRE sequence motif is part of a 55-residue globular domain containing 16 aromatic amino acids, which consists of an anti-parallel arrangement of six β strands, with the first five strands containing complete or incomplete Tyr triplets. This OCRE globular domain is a distinctive component of RBM10 and is more widely conserved in RBM10s across the animal kingdom than the ubiquitous RNA recognition components. It is also found in the functionally related RBM5. Thus, it appears that the three-dimensional structure of the globular OCRE domain, rather than the 42-residue OCRE sequence motif alone, confers specificity on RBM10 intermolecular interactions in the spliceosome.
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Registered trials
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