Novel thienopyrrole glycogen phosphorylase inhibitors: synthesis, in vitro SAR and crystallographic studies

Autor:	Michael Butters, Alan Martin Birch, Peter W. Kenny, Pawel Siedlecki, Paul Robert Owen Whittamore, Jennifer Whitehouse, Ludovic Otterbein, Matthew S. Addie, Andrew Pannifer, Melvyn J. Taylor, Paul M. Murray, Linda Godfrey, David Whalley, Andy Stocker, Jeremy S. Parker, Andrew David Morley, Nikos G. Oikonomakos, Kristy Readman, Linda A. Townsend, Stuart Norman Lile Bennett, Paul Schofield
Rok vydání:	2006
Předmět:	Stereochemistry Clinical Biochemistry Pharmaceutical Science Crystallography X-Ray Biochemistry Glycogen phosphorylase Structure-Activity Relationship Drug Discovery medicine Structure–activity relationship Transferase Animals Humans Pyrroles Phosphorylase kinase Molecular Biology chemistry.chemical_classification biology Chemistry Organic Chemistry Glycogen Phosphorylase In vitro Rats Crystallography medicine.anatomical_structure Enzyme Enzyme inhibitor Hepatocyte biology.protein Molecular Medicine Rabbits
Zdroj:	Bioorganic & Medicinal Chemistry Letters 16:21(Nov2006):5567-5571
ISSN:	0960-894X
Popis:	Two series of novel thienopyrrole inhibitors of recombinant human liver glycogen phosphorylase a (GPa) which are effective in reducing glucose output from rat hepatocytes are described. Representative compounds have been shown to bind at the dimer interface site of the rabbit muscle enzyme by X-ray crystallography.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a027fdd96a6fc9f365265c8ad7e44fb1 https://pubmed.ncbi.nlm.nih.gov/16945526 Zobrazit plný text záznamu Full Text from ScienceDirect