[Heat shock protein 90: novel target for cancer therapy].
The molecular chaperone heat shock protein 90 (Hsp90) is important in maintaining the conformation, stability, and function of many proteins involved in cell surviving. Hsp90 is of interest as an anticancer drug target because of its importance in maintaining the function of key oncogenic client proteins. Hsp90 inhibitors also have shown promising antitumor activity in vitro and in vivo preclinical model systems. One Hsp90 inhibitor, 17-allylamio-17- desmethoxygeldanamycin (17-AAG), is currently in clinical trial.
Chen
Yi
Y
Division of Anti-tumor Pharmacology, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Science, Chinese Academy of Sciences, Shanghai, 201203, PR China.
Ding
Jian
J
D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology*; D016227:Benzoquinones; D018841:HSP90 Heat-Shock Proteins / Q000037:antagonists & inhibitors / Q000187:drug effects* / Q000502:physiology; D006801:Humans; D047029:Lactams, Macrocyclic; D009369:Neoplasms / Q000188:drug therapy* / Q000473:pathology; D011809:Quinones / Q000494:pharmacology; D017828:Rifabutin / Q000031:analogs & derivatives* / Q000494:pharmacology
D000970:Antineoplastic Agents; D016227:Benzoquinones; D018841:HSP90 Heat-Shock Proteins; D047029:Lactams, Macrocyclic; D011809:Quinones; D017828:Rifabutin; C112765:tanespimycin; C001277:geldanamycin