Molecular chaperones in cellular protein folding Journal Article

  


Authors: Martin, J.; Hartl, F. U.
Article Title: Molecular chaperones in cellular protein folding
Abstract: The discovery of “molecular chaperones” has dramatically changed our concept of cellular protein folding. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformation in a reaction mediated by these versatile helper proteins. Understanding the structure and function of molecular chaperones is likely to yield useful applications for medicine and biotechnology in the future. Copyright © 1994 Cambridge University Press
Keywords: review; metabolism; biological model; models, biological; protein folding; bacterium; chaperone; bacteria; molecular chaperones; support, u.s. gov't, p.h.s.
Journal Title: BioEssays
Volume: 16
Issue: 9
ISSN: 0265-9247
Publisher: John Wiley & Sons  
Date Published: 1994-09-01
Start Page: 689
End Page: 692
Language: English
DOI: 10.1002/bies.950160916
PROVIDER: scopus
PUBMED: 7980496
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028501438&doi=10.1002%2fbies.950160916&partnerID=40&md5=e2e41fef2e90918fff578ab9c75e9c3b
Notes: Export Date: 14 January 2019 -- Article -- Source: Scopus
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MSK Authors
  1. F. Ulrich Hartl
    75 Hartl
  2. Jörg Martin
    12 Martin
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