title: Molecular chaperones and protein quality control.
abstract: In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for protein quality control in the endoplasmic reticulum; and provide new insight into two classes of molecular chaperones, the Hsp70 system and the AAA+ (Hsp100) unfoldases.
authors: Zentrum fur Molekulare Biologie, Universität Heidelberg, 69120 Heidelberg, Germany.
authors: Bernd
authors: B
authors: Bukau
authors: Jonathan
authors: J
authors: Weissman
authors: Arthur
authors: A
authors: Horwich