Inhibition Hsp90 as a special way to inhibit protein kinases

• Autorzy: Csermely P , Soti C.
• Języki publikacji: EN

Słowa kluczowe

EN

heat shock; inhibition; molecular chaperone; protein kinase

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2003
• Tom: 08
• Numer: 2A
• Opis fizyczny: p.514-515

Twórcy

autor

Csermely P

• Semmelweis University, Budapest 8, Hungary

autor

Soti C.

Bibliografia

• 1.Csermely, P., Schnaider, T., Sőti, Cs., Prohászka, Z. and Nardai, G. The 90-kDa molecular chaperone family: structure, function and clinical applications. A comprehensive review. Pharmacol. Ther. 79 (1998) 129-168.
• 2. Schnaider, T., Somogyi, J., Csermely, P. and Szamel, M. The Hsp90-specific inhibitor, geldanamycin, selectively disrupts kinase-mediated signalling events of T lymphocyte activation. Cell Stress Chaperones 5 (2000) 52-61.
• 3. Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol. Med. 8 (2002) S55-S61.
• 4. Harvey, S.A., Jensen, K.O., Elmore, L.W. and Holt, S.E. Pharmacological approaches to defining the role of chaperones in aging and prostate cancer progression. Cell Stress Chaperones 7 (2002) 230-234.
• 5. Soga, S., Kozawa, T., Narumi, H., Akinaga, S., Irie, K., Matsumoto, K., Sharma, S.V., Nakano, H., Mizukami, T. and Hara, M. Radicicol leads to selective depletion of raf kinase and disrupts K-Ras-activated aberrant signaling pathway. J. Biol. Chem. 273 (1998) 822-828.
• 6. Chiosis, G., Lucas, B., Shtil, A., Huezo, H. and Rosen, N. Development of a purine/scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase. Bioorg. Med. Chem. 10 (2002) 3555-3564.
• 7. Sőti, Cs., Rácz, A. and Csermely, P. A nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90: N-terminal nucleotide binding unmasks a C-terminal binding pocket. J. Biol. Chem. 277 (2002) 7066-7075.