"Chaperonin 60" 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 the barrel-like structure of the chaperonin complex. It is an oligomeric protein with a distinctive structure of fourteen subunits, arranged in two rings of seven subunits each. The protein was originally studied in BACTERIA where it is commonly referred to as GroEL protein.
| Descriptor ID |
D018834
|
| MeSH Number(s) |
D08.811.277.040.025.142.500.500 D12.776.580.216.210.590.750
|
| Concept/Terms |
Chaperonin 60- Chaperonin 60
- hsp60 Family
- Heat-Shock Proteins 60
- Heat Shock Proteins 60
- hsp60 Protein
- Heat-Shock Protein 60
- Heat Shock Protein 60
|
Below are MeSH descriptors whose meaning is more general than "Chaperonin 60".
Below are MeSH descriptors whose meaning is more specific than "Chaperonin 60".
This graph shows the total number of publications written about "Chaperonin 60" by people in this website by year, and whether "Chaperonin 60" was a major or minor topic of these publications.
To see the data from this visualization as text,
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 0 | 1 | 1 |
| 1996 | 1 | 0 | 1 |
| 1997 | 1 | 1 | 2 |
| 1998 | 0 | 1 | 1 |
| 2000 | 0 | 1 | 1 |
| 2001 | 1 | 0 | 1 |
| 2002 | 1 | 2 | 3 |
| 2003 | 0 | 3 | 3 |
| 2004 | 1 | 4 | 5 |
| 2005 | 0 | 2 | 2 |
| 2006 | 3 | 1 | 4 |
| 2007 | 0 | 1 | 1 |
| 2008 | 1 | 1 | 2 |
| 2009 | 1 | 0 | 1 |
| 2010 | 1 | 2 | 3 |
| 2011 | 0 | 2 | 2 |
| 2013 | 0 | 3 | 3 |
| 2016 | 0 | 1 | 1 |
| 2017 | 1 | 0 | 1 |
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Below are the most recent publications written about "Chaperonin 60" by people in Profiles.
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Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM. Proc Natl Acad Sci U S A. 2017 08 01; 114(31):8259-8264.
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Single-Particle Refinement and Variability Analysis in EMAN2.1. Methods Enzymol. 2016; 579:159-89.
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Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers. J Biol Chem. 2013 Jun 14; 288(24):17734-44.
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Robustness of Helicobacter pylori infection conferred by context-variable redundancy among cysteine-rich paralogs. PLoS One. 2013; 8(3):e59560.
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Survivability of immunoassay reagents exposed to the space radiation environment on board the ESA BIOPAN-6 platform as a prelude to performing immunoassays on Mars. Astrobiology. 2013 Jan; 13(1):92-102.
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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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Murine Sirt3 protein isoforms have variable half-lives. Gene. 2011 Nov 15; 488(1-2):46-51.
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Non-toxic cadmium concentrations induce vascular inflammation and promote atherosclerosis. Circ J. 2011; 75(10):2491-5.
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Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin. J Mol Biol. 2011 Jan 21; 405(3):831-9.
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Tracing conformational changes in proteins. BMC Struct Biol. 2010 May 17; 10 Suppl 1:S1.