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  Recent advances in understanding catalysis of protein folding by molecular chaperones

Balchin, D., Hayer-Hartl, M., & Hartl, F. U. (2020). Recent advances in understanding catalysis of protein folding by molecular chaperones. FEBS LETTERS. doi:10.1002/1873-3468.13844.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-A306-B Version Permalink: http://hdl.handle.net/21.11116/0000-0006-A307-A
Genre: Journal Article
Alternative Title : Review

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1873-3468.13844.pdf (Any fulltext), 989KB
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 Creators:
Balchin, David1, Author
Hayer-Hartl, Manajit2, Author              
Hartl, F. Ulrich2, Author              
Affiliations:
1external, ou_persistent22              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: HSP70 CHAPERONE; RESIDUAL STRUCTURE; POLYPEPTIDE FLUX; STRUCTURAL BASIS; TRIGGER FACTOR; NANO-CAGE; GROEL; DNAK; CONFORMATION; CONFINEMENTchaperonin; confinement; DnaK; GroEL; Hsp40; Hsp60; Hsp70; molecular chaperones; protein folding; protein misfolding;
 Abstract: Molecular chaperones are highly conserved proteins that promote proper folding of other proteinsin vivo. Diverse chaperone systems assistde novoprotein folding and trafficking, the assembly of oligomeric complexes, and recovery from stress-induced unfolding. A fundamental function of molecular chaperones is to inhibit unproductive protein interactions by recognizing and protecting hydrophobic surfaces that are exposed during folding or following proteotoxic stress. Beyond this basic principle, it is now clear that chaperones can also actively and specifically accelerate folding reactions in an ATP-dependent manner. We focus on the bacterial Hsp70 and chaperonin systems as paradigms, and review recent work that has advanced our understanding of how these chaperones act as catalysts of protein folding.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000539757200001
DOI: 10.1002/1873-3468.13844
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Title: FEBS LETTERS
Source Genre: Journal
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Publ. Info: 111 RIVER ST, HOBOKEN 07030-5774, NJ USA : WILEY
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 0014-5793