Structure, function, and mechanism of the Hsp90 molecular chaperone.
Pearl
L H
LH
Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK.
Prodromou
C
C
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors; D000255:Adenosine Triphosphate / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D011485:Protein Binding
D004791:Enzyme Inhibitors; D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases