"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
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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.
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Year | Major Topic | Minor Topic | Total |
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1994 | 1 | 1 | 2 |
1999 | 1 | 0 | 1 |
2000 | 2 | 0 | 2 |
2001 | 1 | 0 | 1 |
2002 | 1 | 0 | 1 |
2004 | 0 | 1 | 1 |
2005 | 1 | 0 | 1 |
2008 | 0 | 1 | 1 |
2010 | 0 | 1 | 1 |
2015 | 0 | 1 | 1 |
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Below are the most recent publications written about "Chaperonin 60" by people in Profiles.
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Cho Y, Zhang X, Pobre KF, Liu Y, Powers DL, Kelly JW, Gierasch LM, Powers ET. Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli. Cell Rep. 2015 Apr 14; 11(2):321-33.
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Shiryaev SA, Cieplak P, Aleshin AE, Sun Q, Zhu W, Motamedchaboki K, Sloutsky A, Strongin AY. Matrix metalloproteinase proteolysis of the mycobacterial HSP65 protein as a potential source of immunogenic peptides in human tuberculosis. FEBS J. 2011 Sep; 278(18):3277-86.
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Wood KL, Nunley DR, Moffatt-Bruce S, Pope-Harman A, Huang Q, Shamo EN, Phillips GS, Baran C, Batra S, Marsh CB, Doseff AI. The role of heat shock protein 27 in bronchiolitis obliterans syndrome after lung transplantation. J Heart Lung Transplant. 2010 Jul; 29(7):786-91.
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Kaltashov IA, Abzalimov RR. Do ionic charges in ESI MS provide useful information on macromolecular structure? J Am Soc Mass Spectrom. 2008 Sep; 19(9):1239-46.
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Swain JF, Gierasch LM. First glimpses of a chaperonin-bound folding intermediate. Proc Natl Acad Sci U S A. 2005 Sep 27; 102(39):13715-6.
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Wilson-Fritch L, Nicoloro S, Chouinard M, Lazar MA, Chui PC, Leszyk J, Straubhaar J, Czech MP, Corvera S. Mitochondrial remodeling in adipose tissue associated with obesity and treatment with rosiglitazone. J Clin Invest. 2004 Nov; 114(9):1281-9.
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Yoneda T, Benedetti C, Urano F, Clark SG, Harding HP, Ron D. Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones. J Cell Sci. 2004 Aug 15; 117(Pt 18):4055-66.
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Gierasch LM. Caught in the act: how ATP binding triggers cooperative conformational changes in a molecular machine. Mol Cell. 2002 Jan; 9(1):3-5.
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Sasu S, LaVerda D, Qureshi N, Golenbock DT, Beasley D. Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via toll-like receptor 4 and p44/p42 mitogen-activated protein kinase activation. Circ Res. 2001 Aug 03; 89(3):244-50.
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Feltham JL, Gierasch LM. GroEL-substrate interactions: molding the fold, or folding the mold? Cell. 2000 Jan 21; 100(2):193-6.