Evaluation of series of isobenzofuranone dimers as PKCα ligands: implication for the distance between the two ligand binding sites

Autor:	Yuichi Hashimoto, Yoshiyasu Baba, Takeshi Yanagisawa, Satoshi Mayumi, Go Hirai, Hidekazu Kawasaki, Mikiko Sodeoka, Yosuke Ogoshi
Rok vydání:	2004
Předmět:	Protein Kinase C-alpha Stereochemistry Dimer Clinical Biochemistry Pharmaceutical Science Plasma protein binding Ligands Biochemistry Structure-Activity Relationship chemistry.chemical_compound Drug Discovery Humans Enzyme Inhibitors Binding site Molecular Biology Protein Kinase C Protein kinase C Benzofurans Binding Sites Dose-Response Relationship Drug Organic Chemistry Ligand (biochemistry) Intracellular signal transduction chemistry Drug Design Molecular Medicine lipids (amino acids peptides and proteins) Signal transduction Dimerization Linker Protein Binding
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 14:2969-2972
ISSN:	0960-894X
DOI:	10.1016/j.bmcl.2004.02.098
Popis:	Protein kinase C (PKC) is a family of enzymes, which play important roles in intracellular signal transduction. To examine the distance between the two ligand binding sites (C1A and C1B) of PKC, we designed and synthesized two series of isobenzofuranone dimers. Peak binding activities were observed for the C3-acyl chain dimers having a C10-C12 linker and for the C7 dimers having a C14-C16.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d27013a3e716c2b2d19683e4412ef1be https://doi.org/10.1016/j.bmcl.2004.02.098 Zobrazit plný text záznamu Full Text from ScienceDirect