UNIGE document Scientific Article
previous document  unige:7377  next document
add to browser collection

Molecular chaperones: How J domains turn on Hsp70s

Published in Current Biology. 1999, vol. 9, no. 8, p. R305-308
Abstract Molecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding and assembly. They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the 'J domains' of these 'cochaperones' activate substrate binding by Hsp70 molecules.
Keywords Binding SitesHSP40 Heat-Shock ProteinsHSP70 Heat-Shock Proteins/metabolismHeat-Shock Proteins/chemistry/metabolism/physiologyMolecular Chaperones/metabolism/ physiologyProtein BindingProtein Structure, Tertiary
PMID: 10226023
Full text
Article - document accessible for UNIGE members only Limited access to UNIGE
(ISO format)
KELLEY, William. Molecular chaperones: How J domains turn on Hsp70s. In: Current Biology, 1999, vol. 9, n° 8, p. R305-308. doi: 10.1016/s0960-9822(99)80185-7 https://archive-ouverte.unige.ch/unige:7377

353 hits

0 download


Deposited on : 2010-06-21

Export document
Format :
Citation style :