"Chaperonins" 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 family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.
| Descriptor ID |
D018833
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| MeSH Number(s) |
D08.811.277.040.025.142 D12.776.580.216.210
|
| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Chaperonins".
Below are MeSH descriptors whose meaning is more specific than "Chaperonins".
This graph shows the total number of publications written about "Chaperonins" by people in this website by year, and whether "Chaperonins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2003 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
| 2012 | 1 | 0 | 1 |
| 2014 | 1 | 0 | 1 |
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Below are the most recent publications written about "Chaperonins" by people in Profiles.
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Horvat NK, Armstrong H, Lee BL, Mercier R, Wolmarans A, Knowles J, Spyracopoulos L, LaPointe P. A mutation in the catalytic loop of Hsp90 specifically impairs ATPase stimulation by Aha1p, but not Hch1p. J Mol Biol. 2014 Jun 12; 426(12):2379-92.
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Armstrong H, Wolmarans A, Mercier R, Mai B, LaPointe P. The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922. PLoS One. 2012; 7(11):e49322.
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Smirnova EV, Collingwood TS, Bisbal C, Tsygankova OM, Bogush M, Meinkoth JL, Henderson EE, Annan RS, Tsygankov AY. TULA proteins bind to ABCE-1, a host factor of HIV-1 assembly, and inhibit HIV-1 biogenesis in a UBA-dependent fashion. Virology. 2008 Mar 01; 372(1):10-23.
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Tomas CA, Welker NE, Papoutsakis ET. Overexpression of groESL in Clostridium acetobutylicum results in increased solvent production and tolerance, prolonged metabolism, and changes in the cell's transcriptional program. Appl Environ Microbiol. 2003 Aug; 69(8):4951-65.