Autor: |
Taveras AG; Schering-Plough Research Institute, Kenilworth, NJ 07033, USA., Remiszewski SW, Doll RJ, Cesarz D, Huang EC, Kirschmeier P, Pramanik BN, Snow ME, Wang YS, del Rosario JD, Vibulbhan B, Bauer BB, Brown JE, Carr D, Catino J, Evans CA, Girijavallabhan V, Heimark L, James L, Liberles S, Nash C, Perkins L, Senior MM, Tsarbopoulos A, Webber SE, et. al. |
Jazyk: |
angličtina |
Zdroj: |
Bioorganic & medicinal chemistry [Bioorg Med Chem] 1997 Jan; Vol. 5 (1), pp. 125-33. |
DOI: |
10.1016/s0968-0896(96)00202-7 |
Abstrakt: |
The nucleotide exchange process is one of the key activation steps regulating the ras protein. This report describes the development of potent, non-nucleotide, small organic inhibitors of the ras nucleotide exchange process. These inhibitors bind to the ras protein in a previously unidentified binding pocket, without displacing bound nucleotide. This report also describes the development and use of mass spectrometry, NMR spectroscopy and molecular modeling techniques to elucidate the structure of a drug-protein complex, and aid in designing new ras inhibitor targets. |
Databáze: |
MEDLINE |
Externí odkaz: |
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