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PMID: 8637592 Published · ppublish English Journal Article Review

Molecular chaperones in cellular protein folding.

Nature ·Vol. 381 ·No. 6583 ·1996-06-13 ·Pages 571-9

Hartl FU

Abstract

The folding of many newly synthesized proteins in the cell depends on a set of conserved proteins known as molecular chaperones. These prevent the formation of misfolded protein structures, both under normal conditions and when cells are exposed to stresses such as high temperature. Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.

MeSH Terms
Animals Chaperonins/physiology HSP70 Heat-Shock Proteins/physiology Humans Protein Folding
Chemicals
HSP70 Heat-Shock Proteins Chaperonins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Hartl F U
Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York 10021, USA.
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1996-06-13
Pages
571-9
Language
English
Region
England
NLM ID
0410462
Subset
IM
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