DIARYLETHER INHIBITORS OF FARNESYL-PROTEIN TRANSFERASE
| Autor: | Theresa M. Williams, Rands E, Nancy E. Kohl, George D. Hartman, Samuel L. Graham, Kelly Hamilton, Timothy J. O'Neill, Oliff Allen I, Christopher J. Dinsmore, Kenneth S. Koblan, Jackson B. Gibbs |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
chemistry.chemical_classification
Farnesyl-diphosphate farnesyltransferase biology Farnesyl Protein Transferase Tetrapeptide medicine.drug_class Stereochemistry Organic Chemistry Clinical Biochemistry Pharmaceutical Science Carboxamide Biochemistry Chemical synthesis Enzyme chemistry Enzyme inhibitor Drug Discovery medicine biology.protein Molecular Medicine Transferase Molecular Biology |
| Zdroj: | Bioorganic & Medicinal Chemistry Letters. 7:1345-1348 |
| ISSN: | 0960-894X |
| DOI: | 10.1016/s0960-894x(97)00225-4 |
| Popis: | The design and synthesis of simple nonpeptide inhibitors of farnesyl-protein transferase (FTase) are described. Cysteine-derived diarylether frameworks are appropriate structural replacements for the C -terminal tetrapeptide portion of the Ras protein, and possess in vitro potency against FTase. Inhibitory activity is dependent on the ring-substitution pattern, and does not require the presence of a C -terminal carboxylate group. © 1997 Elsevier Science Ltd. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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