"Chaperonin 10" 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 group I chaperonin protein that forms a lid-like structure which encloses the non-polar cavity of the chaperonin complex. The protein was originally studied in BACTERIA where it is commonly referred to as GroES protein.
| Descriptor ID |
D018835
|
| MeSH Number(s) |
D12.776.580.216.210.590.500
|
| Concept/Terms |
Chaperonin 10- Chaperonin 10
- Heat-Shock Proteins 10
- Heat Shock Proteins 10
- hsp10 Protein
- Heat-Shock Protein 10
- Heat Shock Protein 10
- hsp10 Family
|
Below are MeSH descriptors whose meaning is more general than "Chaperonin 10".
Below are MeSH descriptors whose meaning is more specific than "Chaperonin 10".
This graph shows the total number of publications written about "Chaperonin 10" by people in this website by year, and whether "Chaperonin 10" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2002 | 1 | 0 | 1 |
| 2004 | 0 | 1 | 1 |
| 2006 | 1 | 0 | 1 |
| 2008 | 0 | 1 | 1 |
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Below are the most recent publications written about "Chaperonin 10" by people in Profiles.
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Visualizing GroEL/ES in the act of encapsulating a folding protein. Cell. 2013 Jun 06; 153(6):1354-65.
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Comparison of Segger and other methods for segmentation and rigid-body docking of molecular components in cryo-EM density maps. Biopolymers. 2012 Sep; 97(9):742-60.
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Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions. J Struct Biol. 2010 Jun; 170(3):427-38.
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Location and flexibility of the unique C-terminal tail of Aquifex aeolicus co-chaperonin protein 10 as derived by cryo-electron microscopy and biophysical techniques. J Mol Biol. 2008 Sep 05; 381(3):707-17.
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De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure. 2008 Mar; 16(3):441-8.
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An expanded conformation of single-ring GroEL-GroES complex encapsulates an 86 kDa substrate. Structure. 2006 Nov; 14(11):1711-22.
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A chaperone network controls the heat shock response in E. coli. Genes Dev. 2004 Nov 15; 18(22):2812-21.
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Directed evolution of substrate-optimized GroEL/S chaperonins. Cell. 2002 Dec 27; 111(7):1027-39.
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GroEL-GroES-mediated protein folding requires an intact central cavity. Proc Natl Acad Sci U S A. 1998 Oct 13; 95(21):12163-8.
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Protein chaperones and protein folding. Curr Opin Biotechnol. 1994 Oct; 5(5):534-9.