Protein Quality Control: Chaperones Culling Corrupt Conformations

Files

McClellan_2005_NCB.pdf (349.75 KB)

Date

2005-08

Authors

Journal Title

Journal ISSN

Volume Title

Publisher

Nature Publishing Group

Abstract

Achieving the correct balance between folding and degradation of misfolded proteins is critical for cell viability. The importance of defining the mechanisms and factors that mediate cytoplasmic quality control is underscored by the growing list of diseases associated with protein misfolding and aggregation. Molecular chaperones assist protein folding and also facilitate degradation of misfolded polypeptides by the ubiquitin–proteasome system. Here we discuss emerging links between folding and degradation machineries and highlight challenges for future research.

Description

Keywords

Proteins, Cytoplasm, Protoplasm, Molecular chaperones, Peptide hormones, Ubiquitin, Proteins -- Analysis

Citation

Nature Cell Biology. Aug2005, Vol. 7 Issue 8, p736-741. 6p. DOI: 10.1038/ncb0805-736

URI

http://hdl.handle.net/11209/10522

DOI

Collections

Science, Mathematics, & Computing