title: Chaperones and protein folding.
abstract: Chaperones are centrally involved in the control of protein structure, function, localization and transport. A flurry of scientific activity continues to examine the molecular nature of chaperone-substrate recognition and the role of auxiliary chaperones (cohort proteins) and small molecules that expedite these processes. Chaperones have been implicated in processes as diverse as protein secretion, nuclear transport, thermotolerance, the steroid receptor signal transduction pathway, T-cell receptor and major histocompatibility complex class I and II multimeric assembly and bacterial virulence.
authors.affiliation: Départment de Biochimie Médicale, Université de Genève, Switzerland.
authors.forename: W L
authors.initials: WL
authors.lastname: Kelley
authors.forename: C
authors.initials: C
authors.lastname: Georgopoulos
mesh_terms: D000591:Amino Acid Isomerases / Q000502:physiology; D000818:Animals; D006360:Heat-Shock Proteins / Q000096:biosynthesis; D007109:Immunity / Q000502:physiology; D011487:Protein Conformation; D011506:Proteins / Q000502:physiology*; D011956:Receptors, Cell Surface / Q000502:physiology
chemical_list: D006360:Heat-Shock Proteins; D011506:Proteins; D011956:Receptors, Cell Surface; D000591:Amino Acid Isomerases