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PMID: 15459659 Published · ppublish English Journal Article Review

Pathways of chaperone-mediated protein folding in the cytosol.

Nature reviews. Molecular cell biology ·Vol. 5 ·No. 10 ·2004-10-00 ·Pages 781-91

Young JC, Agashe VR, Siegers K, Hartl FU

Abstract

Cells are faced with the task of folding thousands of different polypeptides into a wide range of conformations. For many proteins, the folding process requires the action of molecular chaperones. In the cytosol of prokaryotic and eukaryotic cells, molecular chaperones of different structural classes form a network of pathways that can handle substrate polypeptides from the point of initial synthesis on ribosomes to the final stages of folding.

MeSH Terms
Animals Bacterial Proteins/metabolism Chaperonins/metabolism Cytoplasm/metabolism HSP70 Heat-Shock Proteins/metabolism HSP90 Heat-Shock Proteins/metabolism Models, Biological Molecular Chaperones/metabolism Protein Conformation Protein Folding Protein Transport Ribosomes/metabolism
Chemicals
Bacterial Proteins HSP70 Heat-Shock Proteins HSP90 Heat-Shock Proteins Molecular Chaperones Chaperonins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Young Jason C
Department of Biochemistry, McIntyre Medical Sciences Building, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec H3G 1Y6, Canada.
Agashe Vishwas R
Siegers Katja
Hartl F Ulrich
Article Info
Journal
Nature reviews. Molecular cell biology
Abbr.
Nat Rev Mol Cell Biol
ISSN
1471-0072
Published
2004-10-00
Pages
781-91
Language
English
Region
England
NLM ID
100962782
Subset
IM
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