title: Hsp90: a specialized but essential protein-folding tool.
abstract: Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy.
authors.affiliation: Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D-82152, Germany.
authors.forename: J C
authors.initials: JC
authors.lastname: Young
authors.forename: I
authors.initials: I
authors.lastname: Moarefi
authors.forename: F U
authors.initials: FU
authors.lastname: Hartl
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D003600:Cytosol / Q000378:metabolism; D019143:Evolution, Molecular; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology; D011506:Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology
chemical_list: D018841:HSP90 Heat-Shock Proteins; D011506:Proteins; D000251:Adenosine Triphosphatases