"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
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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 |
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1995 | 0 | 1 | 1 |
2002 | 0 | 1 | 1 |
2003 | 0 | 2 | 2 |
2005 | 1 | 0 | 1 |
2014 | 0 | 1 | 1 |
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Below are the most recent publications written about "Chaperonins" by people in Profiles.
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Lim ET, Liu YP, Chan Y, Tiinamaija T, K?r?j?m?ki A, Madsen E, Altshuler DM, Raychaudhuri S, Groop L, Flannick J, Hirschhorn JN, Katsanis N, Daly MJ. A novel test for recessive contributions to complex diseases implicates Bardet-Biedl syndrome gene BBS10 in idiopathic type 2 diabetes and obesity. Am J Hum Genet. 2014 Nov 06; 95(5):509-20.
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Rachel RA, May-Simera HL, Veleri S, Gotoh N, Choi BY, Murga-Zamalloa C, McIntyre JC, Marek J, Lopez I, Hackett AN, Zhang J, Brooks M, den Hollander AI, Beales PL, Li T, Jacobson SG, Sood R, Martens JR, Liu P, Friedman TB, Khanna H, Koenekoop RK, Kelley MW, Swaroop A. Combining Cep290 and Mkks ciliopathy alleles in mice rescues sensory defects and restores ciliogenesis. J Clin Invest. 2012 Apr; 122(4):1233-45.
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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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Seoh HK, Weech M, Zhang N, Squires CL. rRNA antitermination functions with heat shock promoters. J Bacteriol. 2003 Nov; 185(21):6486-9.
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Sonna LA, Cullivan ML, Sheldon HK, Pratt RE, Lilly CM. Effect of hypoxia on gene expression by human hepatocytes (HepG2). Physiol Genomics. 2003 Feb 06; 12(3):195-207.
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Sonna LA, Gaffin SL, Pratt RE, Cullivan ML, Angel KC, Lilly CM. Effect of acute heat shock on gene expression by human peripheral blood mononuclear cells. J Appl Physiol (1985). 2002 May; 92(5):2208-20.
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Brown CR, Doxsey SJ, Hong-Brown LQ, Martin RL, Welch WJ. Molecular chaperones and the centrosome. A role for TCP-1 in microtubule nucleation. J Biol Chem. 1996 Jan 12; 271(2):824-32.
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Franke EK, Chen BX, Tatsis I, Diamanduros A, Erlanger BF, Luban J. Cyclophilin binding to the human immunodeficiency virus type 1 Gag polyprotein is mimicked by an anti-cyclosporine antibody. J Virol. 1995 Sep; 69(9):5821-3.
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Landry SJ, Gierasch LM. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Biochemistry. 1991 Jul 30; 30(30):7359-62.