Peptide Termination Factors
"Peptide Termination Factors" 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.
Proteins that are involved in the peptide chain termination reaction (PEPTIDE CHAIN TERMINATION, TRANSLATIONAL) on RIBOSOMES. They include codon-specific class-I release factors, which recognize stop signals (TERMINATOR CODON) in the MESSENGER RNA; and codon-nonspecific class-II release factors.
| Descriptor ID |
D010454
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| MeSH Number(s) |
D12.776.835.862
|
| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Peptide Termination Factors".
Below are MeSH descriptors whose meaning is more specific than "Peptide Termination Factors".
This graph shows the total number of publications written about "Peptide Termination Factors" by people in this website by year, and whether "Peptide Termination Factors" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2003 | 1 | 0 | 1 |
| 2005 | 0 | 1 | 1 |
| 2008 | 0 | 1 | 1 |
| 2012 | 2 | 1 | 3 |
| 2015 | 0 | 1 | 1 |
| 2017 | 1 | 0 | 1 |
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Below are the most recent publications written about "Peptide Termination Factors" by people in Profiles.
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Iwakura N, Yokoyama T, Quaglia F, Mitsuoka K, Mio K, Shigematsu H, Shirouzu M, Kaji A, Kaji H. Chemical and structural characterization of a model Post-Termination Complex (PoTC) for the ribosome recycling reaction: Evidence for the release of the mRNA by RRF and EF-G. PLoS One. 2017; 12(5):e0177972.
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Sweeny EA, Jackrel ME, Go MS, Sochor MA, Razzo BM, DeSantis ME, Gupta K, Shorter J. The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation. Mol Cell. 2015 Mar 05; 57(5):836-849.
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Hashimoto Y, Hosoda N, Datta P, Alnemri ES, Hoshino S. Translation termination factor eRF3 is targeted for caspase-mediated proteolytic cleavage and degradation during DNA damage-induced apoptosis. Apoptosis. 2012 Dec; 17(12):1287-99.
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Kurata S, Shen B, Liu JO, Takeuchi N, Kaji A, Kaji H. Possible steps of complete disassembly of post-termination complex by yeast eEF3 deduced from inhibition by translocation inhibitors. Nucleic Acids Res. 2013 Jan 07; 41(1):264-76.
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Vivanco-Dom?nguez S, Bueno-Mart?nez J, Le?n-Avila G, Iwakura N, Kaji A, Kaji H, Guarneros G. Protein synthesis factors (RF1, RF2, RF3, RRF, and tmRNA) and peptidyl-tRNA hydrolase rescue stalled ribosomes at sense codons. J Mol Biol. 2012 Apr 13; 417(5):425-39.
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Feng BY, Toyama BH, Wille H, Colby DW, Collins SR, May BC, Prusiner SB, Weissman J, Shoichet BK. Small-molecule aggregates inhibit amyloid polymerization. Nat Chem Biol. 2008 Mar; 4(3):197-9.
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Golovina TN, Morrison SE, Eisenlohr LC. The impact of misfolding versus targeted degradation on the efficiency of the MHC class I-restricted antigen processing. J Immunol. 2005 Mar 01; 174(5):2763-9.
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Hegde R, Srinivasula SM, Datta P, Madesh M, Wassell R, Zhang Z, Cheong N, Nejmeh J, Fernandes-Alnemri T, Hoshino S, Alnemri ES. The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein. J Biol Chem. 2003 Oct 03; 278(40):38699-706.
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Chu ML, Mann K, Deutzmann R, Pribula-Conway D, Hsu-Chen CC, Bernard MP, Timpl R. Characterization of three constituent chains of collagen type VI by peptide sequences and cDNA clones. Eur J Biochem. 1987 Oct 15; 168(2):309-17.