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lüll Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs Blagosklonny MVLeukemia 2002[Apr]; 16 (4): 455-62Geldanamycin (GA), herbimycin A and radicicol bind heat-shock protein-90 (Hsp90) and destabilize its client proteins including v-Src, Bcr-Abl, Raf-1, ErbB2, some growth factor receptors and steroid receptors. Thus, Hsp90-active agents induce ubiquitination and proteasomal degradation of numerous oncoproteins. Depending on the cellular context, HSP90-active agents cause growth arrest, differentiation and apoptosis, or can prevent apoptosis. HSP-active agents are undergoing clinical trials. Like targets of most chemotherapeutics, Hsp90 is not a cancer-specific protein. By attacking a nonspecific target, HSP-90-active compounds still may preferentially kill certain tumor cells. How can this be achieved? How can therapeutic potentials be exploited? This article starts the discussion.|Animals[MESH]|Antibiotics, Antineoplastic/*pharmacology[MESH]|Benzoquinones[MESH]|Clinical Trials as Topic[MESH]|Growth Inhibitors/pharmacology[MESH]|HSP90 Heat-Shock Proteins/*antagonists & inhibitors[MESH]|Humans[MESH]|Lactams, Macrocyclic[MESH]|Neoplasms/drug therapy/*metabolism/pathology[MESH]|Oncogene Proteins/*metabolism[MESH]|Protein Kinases/metabolism[MESH]|Quinones/*pharmacology[MESH]|Receptors, Growth Factor/*metabolism[MESH]|Signal Transduction[MESH]|Transcription Factors/metabolism[MESH] |