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  Molecular chaperones in the cytosol: from nascent chain to folded protein

Hartl, F. U., & Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science, 295(5561), 1852-1858.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-6F8C-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-6F8D-C
Genre: Journal Article
Alternative Title : Science

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 Creators:
Hartl, F. U.1, Author              
Hayer-Hartl, M.2, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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 Abstract: Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent protein misfolding and aggregation in the crowded environment of the cell. Nascent chain-binding chaperones, including trigger factor, Hsp70, and prefoldin, stabilize elongating chains on ribosomes in a nonaggregated state. Folding in the cytosol is achieved either on controlled chain release from these factors or after transfer of newly synthesized proteins to downstream chaperones, such as the chaperonins. These are large, cylindrical complexes that provide a central compartment for a single protein chain to fold unimpaired by aggregation. Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.

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Language(s): eng - English
 Dates: 2002-03-08
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 39147
ISI: 000174299500028
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Title: Science
  Alternative Title : Science
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 295 (5561) Sequence Number: - Start / End Page: 1852 - 1858 Identifier: ISSN: 0036-8075