Imidazole-containing diarylether and diarylsulfone inhibitors of farnesyl-protein transferase

Autor:	Rands E, Kenneth S. Koblan, Robert B. Lobell, Samuel L. Graham, Dongming Liu, Jackson B. Gibbs, J. Christopher Culberson, George D. Hartman, Theresa M. Williams, Nancy E. Kohl, Christopher J. Dinsmore, Oliff Allen I, Timothy J. O'Neill
Rok vydání:	1999
Předmět:	Magnetic Resonance Spectroscopy Molecular model Farnesyl Protein Transferase Stereochemistry Clinical Biochemistry Pharmaceutical Science Biochemistry Chemical synthesis Sulfone chemistry.chemical_compound Drug Discovery Transferase Humans Sulfones Enzyme Inhibitors Molecular Biology chemistry.chemical_classification Farnesyl-diphosphate farnesyltransferase Alkyl and Aryl Transferases biology Molecular Structure Organic Chemistry Imidazoles Enzyme chemistry Enzyme inhibitor biology.protein Molecular Medicine Ethers
Zdroj:	Bioorganicmedicinal chemistry letters. 9(23)
ISSN:	0960-894X
Popis:	The design and syntheses of non-thiol inhibitors of farnesyl-protein transferase are described. Optimization of cysteine-substituted diarylethers led to highly potent imidazole-containing diarylethers and diarylsulfones. Polar diaryl linkers dramatically improved potency and gave highly cell active compounds.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64e9d100b2f603dc26fa32d0b97700b3 https://pubmed.ncbi.nlm.nih.gov/10612589 Zobrazit plný text záznamu Full Text from ScienceDirect