Bicyclic and tricyclic thiophenes as protein tyrosine phosphatase 1B inhibitors

Autor:	Kenneth W. Foreman, David V. Erbe, Yan-Ling Zhang, Steven J. Kirincich, Zhao-Kui Wan, Alessandro Moretto, Eva Binnun, Douglas P. Wilson, Tam Steve Yik-Kai, S.K. Tam, Bruce Follows, Weixin Xu, Diane Joseph-McCarthy, Julie Lee, Michael J. Smith
Rok vydání:	2006
Předmět:	Models Molecular Molecular model Stereochemistry Clinical Biochemistry Pharmaceutical Science Thiophenes Protein tyrosine phosphatase Crystallography X-Ray Biochemistry Chemical synthesis Structure-Activity Relationship chemistry.chemical_compound Drug Discovery Structure–activity relationship Enzyme Inhibitors Molecular Biology chemistry.chemical_classification Molecular Structure biology Bicyclic molecule Chemistry Organic Chemistry Enzyme Enzyme inhibitor biology.protein Molecular Medicine Protein Tyrosine Phosphatases Lead compound hormones hormone substitutes and hormone antagonists
Zdroj:	Bioorganic & Medicinal Chemistry. 14:2162-2177
ISSN:	0968-0896
DOI:	10.1016/j.bmc.2005.11.005
Popis:	A novel pyridothiophene inhibitor of PTP1B was discovered by rational screening of phosphotyrosine mimics at high micromolar concentrations. The potency of this lead compound has been improved significantly by medicinal chemistry guided by X-ray crystallography and molecular modeling. Excellent consistency has been observed between structure-activity relationships and structural information from PTP1B-inhibitor complexes.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4f3ea9825417e657d8eab4182b3f9bb https://doi.org/10.1016/j.bmc.2005.11.005 Zobrazit plný text záznamu Full Text from ScienceDirect