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lüll Molecular chaperones and protein quality control Bukau B; Weissman J; Horwich ACell 2006[May]; 125 (3): 443-51In 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.|*Protein Folding[MESH]|Adenosine Triphosphate/metabolism[MESH]|Allosteric Regulation/physiology[MESH]|Animals[MESH]|Cytosol/metabolism[MESH]|Endopeptidase Clp[MESH]|Endoplasmic Reticulum/metabolism[MESH]|HSP70 Heat-Shock Proteins/metabolism[MESH]|Heat-Shock Proteins/metabolism[MESH]|Humans[MESH]|Molecular Chaperones/*metabolism[MESH]|Protein Biosynthesis/*physiology[MESH]|Proteins/chemistry/*metabolism[MESH]|Protozoan Proteins/metabolism[MESH] |