The role of heat-shock proteins as molecular chaperones.
Recent studies have revealed that protein folding and assembly events in vivo require the participation of accessory components, now being referred to as 'molecular chaperones'. A number of chaperones have been identified as members of the heat-shock (or stress) protein family. This review discusses the roles of two classes of chaperones, the heat-shock protein 70 and groEL/ES families, in facilitating protein maturation, and describes how such events are perturbed in the cell subjected to metabolic stress.
University of California, San Francisco.
W J
WJ
Welch
D001426:Bacterial Proteins / Q000378:metabolism; D002352:Carrier Proteins / Q000378:metabolism*; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins / Q000378:metabolism*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational
D001426:Bacterial Proteins; D002352:Carrier Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins