 Chaperonin 60
"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
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| Concept/Terms |
Chaperonin 60- Chaperonin 60
- hsp60 Protein
- hsp60 Family
- Heat-Shock Protein 60
- Heat Shock Protein 60
- Heat-Shock Proteins 60
- Heat Shock Proteins 60
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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, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1992 | 0 | 1 | 1 | | 1994 | 0 | 1 | 1 | | 1995 | 1 | 0 | 1 | | 1996 | 1 | 0 | 1 | | 1997 | 0 | 1 | 1 | | 2001 | 0 | 1 | 1 | | 2003 | 1 | 0 | 1 | | 2014 | 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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Burbulla LF, Fitzgerald JC, Stegen K, Westermeier J, Thost AK, Kato H, Mokranjac D, Sauerwald J, Martins LM, Woitalla D, Rapaport D, Riess O, Proikas-Cezanne T, Rasse TM, Krüger R. Mitochondrial proteolytic stress induced by loss of mortalin function is rescued by Parkin and PINK1. Cell Death Dis. 2014 Apr 17; 5:e1180.
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Antonopoulos DA, Russell WM, White BA. Phylogenetic reconstruction of Gram-positive organisms based on comparative sequence analysis of molecular chaperones from the ruminal microorganism Ruminococcus flavefaciens FD-1. FEMS Microbiol Lett. 2003 Oct 10; 227(1):1-7.
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Garrido C, Gurbuxani S, Ravagnan L, Kroemer G. Heat shock proteins: endogenous modulators of apoptotic cell death. Biochem Biophys Res Commun. 2001 Aug 24; 286(3):433-42.
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Matouschek A, Azem A, Ratliff K, Glick BS, Schmid K, Schatz G. Active unfolding of precursor proteins during mitochondrial protein import. EMBO J. 1997 Nov 17; 16(22):6727-36.
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Rospert S, Looser R, Dubaquie Y, Matouschek A, Glick BS, Schatz G. Hsp60-independent protein folding in the matrix of yeast mitochondria. EMBO J. 1996 Feb 15; 15(4):764-74.
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Sanyal A, Harington A, Herbert CJ, Groudinsky O, Slonimski PP, Tung B, Getz GS. Heat shock protein HSP60 can alleviate the phenotype of mitochondrial RNA-deficient temperature-sensitive mna2 pet mutants. Mol Gen Genet. 1995 Jan 06; 246(1):56-64.
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Wachter C, Schatz G, Glick BS. Protein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix. Mol Biol Cell. 1994 Apr; 5(4):465-74.
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Glick BS, Brandt A, Cunningham K, Müller S, Hallberg RL, Schatz G. Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell. 1992 May 29; 69(5):809-22.
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