Discovery and design of benzimidazolone based inhibitors of p38 MAP kinase

Autor:	Christopher Ronald Sarko, Antonio J.M. Jr Barbosa, Kevin Chungeng Qian, Mark Stephen Ralph, Neil Moss, Ming-Hong Hao, Daniel R. Goldberg, Tazmeen N. Fadra, Faith Corbo Gaenzler, Fariba Soleymanzadeh, Rachel R. Kroe, Pingrong Liu, Abdelhakim Hammach
Rok vydání:	2006
Předmět:	Models Molecular Molecular model Protein Conformation High-throughput screening Clinical Biochemistry Molecular Conformation Pharmaceutical Science Crystallography X-Ray Biochemistry p38 Mitogen-Activated Protein Kinases Structure-Activity Relationship Drug Discovery Enzyme Inhibitors Protein kinase A Molecular Biology chemistry.chemical_classification biology Bicyclic molecule Chemistry Organic Chemistry Enzyme Enzyme inhibitor Mitogen-activated protein kinase biology.protein Molecular Medicine Benzimidazoles Signal transduction
Zdroj:	Bioorganicmedicinal chemistry letters. 16(24)
ISSN:	0960-894X
Popis:	A new class of benzimidazolone p38 MAP kinase inhibitors was discovered through high-throughput screening. X-ray crystallographic data of the lead molecule with p38 were used to design analogues with improved binding affinity and potency in a cell assay of LPS-induced TNFalpha production. Herein, we report the SAR of this new class of p38 inhibitors.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0981a6403bb9e04689fd0c9d2113d72d https://pubmed.ncbi.nlm.nih.gov/17010605 Zobrazit plný text záznamu Full Text from ScienceDirect