Work

Molecular Chaperones and Protein Quality Control

Year: 2006

Type: review

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.

Source: Cell

DOI: 10.1016/j.cell.2006.04.014

Authors: Bernd Bukau, Jonathan Weissman, Arthur Horwich

Institutions: Heidelberg University, Howard Hughes Medical Institute, University of California, San Francisco, Scripps Research Institute, Yale University

Language: English

Topic: Heat shock proteins research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $11,400

OpenAlex ID: W2087689873

FWCI: 8.783

Cites: 50

Cited by: 1,589

Related to: 9