Molecular chaperones: the busy life of Hsp90
- PMID: 10322107
- DOI: 10.1016/s0960-9822(99)80203-6
Molecular chaperones: the busy life of Hsp90
Abstract
The heat shock protein Hsp90 is a molecular chaperone which assists the refolding of misfolded proteins, but also has highly selective functions in normal metabolism. These dual functions enable Hsp90 to connect environmental conditions with developmental processes and to buffer genetic changes.
Similar articles
-
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.EMBO J. 1996 Jun 17;15(12):2969-79. EMBO J. 1996. PMID: 8670798 Free PMC article.
-
Heat shock protein 90: its inhibition and function.Philos Trans R Soc Lond B Biol Sci. 2018 Jan 19;373(1738):20160527. doi: 10.1098/rstb.2016.0527. Philos Trans R Soc Lond B Biol Sci. 2018. PMID: 29203712 Free PMC article. Review.
-
Cdc37 goes beyond Hsp90 and kinases.Cell Stress Chaperones. 2003 Summer;8(2):114-9. doi: 10.1379/1466-1268(2003)008<0114:cgbhak>2.0.co;2. Cell Stress Chaperones. 2003. PMID: 14627196 Free PMC article. Review.
-
Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding.Eur J Biochem. 2001 Apr;268(8):2520-4. doi: 10.1046/j.1432-1327.2001.02145.x. Eur J Biochem. 2001. PMID: 11298772
-
Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90.Life Sci. 2000 Aug 11;67(12):1455-65. doi: 10.1016/s0024-3205(00)00735-9. Life Sci. 2000. PMID: 10983842
Cited by
-
Novel aspects of macromolecular repair and relationship to human disease.J Mol Med (Berl). 2004 May;82(5):280-97. doi: 10.1007/s00109-004-0528-1. Epub 2004 Feb 24. J Mol Med (Berl). 2004. PMID: 14985856 Review.
-
The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme.Mol Cell Biol. 2001 Dec;21(23):7923-32. doi: 10.1128/MCB.21.23.7923-7932.2001. Mol Cell Biol. 2001. PMID: 11689685 Free PMC article.
-
Isolation and quantification of the heat shock protein 90 alpha and beta isoforms from rat liver.Protoplasma. 2001;218(1-2):54-6. doi: 10.1007/BF01288360. Protoplasma. 2001. PMID: 11732320
-
Quantitative trait symmetry independent of Hsp90 buffering: distinct modes of genetic canalization and developmental stability.Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13396-401. doi: 10.1073/pnas.1835613100. Epub 2003 Oct 31. Proc Natl Acad Sci U S A. 2003. PMID: 14595030 Free PMC article.
-
Global Dynamics of Yeast Hsp90 Middle and C-Terminal Dimer Studied by Advanced Sampling Simulations.Front Mol Biosci. 2019 Sep 27;6:93. doi: 10.3389/fmolb.2019.00093. eCollection 2019. Front Mol Biosci. 2019. PMID: 31681792 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
