 Chaperonins
"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.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 0 | 1 | 1 | | 2004 | 0 | 1 | 1 | | 2009 | 1 | 0 | 1 | | 2016 | 0 | 1 | 1 | | 2022 | 0 | 1 | 1 |
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Below are the most recent publications written about "Chaperonins" by people in Profiles.
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Hassell D, Denney A, Singer E, Benson A, Roth A, Ceglowski J, Steingesser M, McMurray M. Chaperone requirements for de novo folding of Saccharomyces cerevisiae septins. Mol Biol Cell. 2022 10 01; 33(12):ar111.
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Panda AK, Chakraborty A, Nandi SK, Biswas A. The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3. Proteins. 2020 06; 88(6):759-774.
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Panda AK, Chakraborty A, Nandi SK, Kaushik A, Biswas A. The C-terminal extension of Mycobacterium tuberculosis Hsp16.3 regulates its oligomerization, subunit exchange dynamics and chaperone function. FEBS J. 2017 01; 284(2):277-300.
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Marino Gammazza A, Campanella C, Barone R, Caruso Bavisotto C, Gorska M, Wozniak M, Carini F, Cappello F, D'Anneo A, Lauricella M, Zummo G, Conway de Macario E, Macario AJ, Di Felice V. Doxorubicin anti-tumor mechanisms include Hsp60 post-translational modifications leading to the Hsp60/p53 complex dissociation and instauration of replicative senescence. Cancer Lett. 2017 01 28; 385:75-86.
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Bruns N, Pustelny K, Bergeron LM, Whitehead TA, Clark DS. Mechanical nanosensor based on FRET within a thermosome: damage-reporting polymeric materials. Angew Chem Int Ed Engl. 2009; 48(31):5666-9.
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Kahn NW, Rea SL, Moyle S, Kell A, Johnson TE. Proteasomal dysfunction activates the transcription factor SKN-1 and produces a selective oxidative-stress response in Caenorhabditis elegans. Biochem J. 2008 Jan 01; 409(1):205-13.
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George R, Kelly SM, Price NC, Erbse A, Fisher M, Lund PA. Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties. Biochem Biophys Res Commun. 2004 Nov 12; 324(2):822-8.
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Weber-Ban EU, Reid BG, Miranker AD, Horwich AL. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature. 1999 Sep 02; 401(6748):90-3.
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Andley UP, Mathur S, Griest TA, Petrash JM. Cloning, expression, and chaperone-like activity of human alphaA-crystallin. J Biol Chem. 1996 Dec 13; 271(50):31973-80.
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Kelson TL, Ohura T, Kraus JP. Chaperonin-mediated assembly of wild-type and mutant subunits of human propionyl-CoA carboxylase expressed in Escherichia coli. Hum Mol Genet. 1996 Mar; 5(3):331-7.
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