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  Molecular chaperones in protein folding: the art of avoiding sticky situations

Hartl, F. U., Hlodan, R., & Langer, T. (1994). Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem Sci, 19(1), 20-5.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-6FCA-6 Version Permalink: https://hdl.handle.net/21.11116/0000-000B-6FCB-5
Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/7908149 (Any fulltext)
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 Creators:
Hartl, F. U., Author
Hlodan, R., Author
Langer, T.1, Author           
Affiliations:
1Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_3393994              

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Free keywords: Animals Bacterial Proteins/physiology Chaperonins Fungal Proteins/physiology Heat-Shock Proteins/*physiology Humans *Protein Folding Proteins
 Abstract: Molecular chaperones are a class of proteins that interact with the non-native conformations of other proteins. The major role of chaperones of the Hsp70 and Hsp60 families is to prevent aggregation of newly synthesized polypeptides and then to mediate their folding to the native state. As a result of functional studies of these proteins, there has been a revision of the long-held view that protein folding in the cell is a spontaneous process.

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 Dates: 1994-011994-01-01
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: 7908149
ISSN: 0968-0004 (Print)0968-0004 (Linking)
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Title: Trends Biochem Sci
Source Genre: Journal
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Pages: - Volume / Issue: 19 (1) Sequence Number: - Start / End Page: 20 - 5 Identifier: -