Hsp90: The vulnerable chaperone Journal Article
| Authors: | Chiosis, G.; Vilenchik, M.; Kim, J.; Solit, D. |
| Article Title: | Hsp90: The vulnerable chaperone |
| Abstract: | The molecular chaperone Hsp90 has emerged as an important target in cancer treatment because of its roles in maintaining transformation and regulating the function of proteins involved in apoptotic, survival and growth pathways. Many Hsp90 inhibitors function by binding to the N-terminal ATP pocket, but the chaperone has many other vulnerable points. Agents that interact with its C-terminus or modify its post-translational status represent additional ways of interfering with chaperone activity. This review will discuss several emerging classes of Hsp90 inhibitors and their modes of action. |
| Keywords: | clinical trial; review; cisplatin; antineoplastic agents; protein function; neoplasms; animals; cell survival; complex formation; apoptosis; liver toxicity; cell growth; carboxy terminal sequence; nausea; odor; protein binding; alkylating agent; melphalan; drug discovery; cancer therapy; antiinfective agent; protein processing; heat shock protein 90; hsp90 heat-shock proteins; purine derivative; oxaliplatin; structure analysis; steroid receptor; drug binding; protein inhibitor; acetylation; geldanamycin; radicicol; chaperone; ansamycin derivative; fr 901228; hsp90 chaperone; pyrazole; 17aag; hypericin; humans; human; anti-cancer therapy; cct018159; hsp90 posttranslational modifications; pu24fcl; herbimycin |
| Journal Title: | Drug Discovery Today |
| Volume: | 9 |
| Issue: | 20 |
| ISSN: | 1359-6446 |
| Publisher: | Elsevier Inc. |
| Date Published: | 2004-10-15 |
| Start Page: | 881 |
| End Page: | 888 |
| Language: | English |
| DOI: | 10.1016/s1359-6446(04)03245-3 |
| PROVIDER: | scopus |
| PUBMED: | 15475321 |
| DOI/URL: | |
| Notes: | Drug Discov. Today -- Cited By (since 1996):154 -- Export Date: 16 June 2014 -- CODEN: DDTOF -- Source: Scopus |
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