Retinoblastoma-Binding Protein 1
"Retinoblastoma-Binding Protein 1" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A ubiquitously expressed regulatory protein that contains a retinoblastoma protein binding domain and an AT-rich interactive domain. The protein may play a role in recruiting HISTONE DEACETYLASES to the site of RETINOBLASTOMA PROTEIN-containing transcriptional repressor complexes.
| Descriptor ID |
D056465
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| MeSH Number(s) |
D12.644.360.024.328.100 D12.776.157.057.158.100 D12.776.476.024.420.100 D12.776.660.769.100
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Retinoblastoma-Binding Protein 1".
Below are MeSH descriptors whose meaning is more specific than "Retinoblastoma-Binding Protein 1".
This graph shows the total number of publications written about "Retinoblastoma-Binding Protein 1" by people in this website by year, and whether "Retinoblastoma-Binding Protein 1" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2000 | 0 | 1 | 1 |
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Below are the most recent publications written about "Retinoblastoma-Binding Protein 1" by people in Profiles.
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Meehan WJ, Samant RS, Hopper JE, Carrozza MJ, Shevde LA, Workman JL, Eckert KA, Verderame MF, Welch DR. Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription. J Biol Chem. 2004 Jan 09; 279(2):1562-9.
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Robertson KD, Ait-Si-Ali S, Yokochi T, Wade PA, Jones PL, Wolffe AP. DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat Genet. 2000 Jul; 25(3):338-42.
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Lane ME, Elend M, Heidmann D, Herr A, Marzodko S, Herzig A, Lehner CF. A screen for modifiers of cyclin E function in Drosophila melanogaster identifies Cdk2 mutations, revealing the insignificance of putative phosphorylation sites in Cdk2. Genetics. 2000 May; 155(1):233-44.