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PMID: 11470816 Published · ppublish English Journal Article Review

Hsp90: a specialized but essential protein-folding tool.

The Journal of cell biology ·Vol. 154 ·No. 2 ·2001-07-23 ·Pages 267-73

Young JC, Moarefi I, Hartl FU

Abstract

Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy.

MeSH Terms
Adenosine Triphosphatases/metabolism Animals Cytosol/metabolism Evolution, Molecular HSP90 Heat-Shock Proteins/metabolism Humans Models, Molecular Protein Folding Protein Structure, Tertiary/physiology Proteins/metabolism Signal Transduction/physiology
Chemicals
HSP90 Heat-Shock Proteins Proteins Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Young J C
Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D-82152, Germany.
Moarefi I
Hartl F U
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74 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.200104079
Published
2001-07-23
Pages
267-73
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2150759
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.200104079 PMC Full Text View journal details
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