Potent and selective Aurora inhibitors identified by the expansion of a Novel scaffold for protein kinase inhibition

Autor:	Paolo Cappella, Daniele Fancelli, Cornel Catana, Patrizia Carpinelli, Alexander D. Cameron, Barbara Forte, and Anna Vulpetti, Aurelio Marsiglio, Simona Bindi, Maria Laura Giorgini, Valeria Pittalà, Chiara Soncini, Dino Severino, Paola Vianello, D. Berta, Fulvia Roletto, Patrizia Giordano, Sergio Mantegani, Paola Storici, Mario Varasi, Juergen Moll, Roberto Tonani, M. Meroni
Jazyk:	angličtina
Rok vydání:	2005
Předmět:	Models Molecular Aurora inhibitor Antineoplastic Agents Protein Serine-Threonine Kinases Piperazines Cell Line Structure-Activity Relationship Adenosine Triphosphate Aurora kinase Aurora Kinases Cell Line Tumor Drug Discovery Combinatorial Chemistry Techniques Humans Structure–activity relationship Pyrroles Cytotoxicity Protein kinase A Cell Proliferation Binding Sites biology Kinase Chemistry Bridged Bicyclo Compounds Heterocyclic Biochemistry Enzyme inhibitor biology.protein Molecular Medicine Drug Screening Assays Antitumor Signal transduction Protein Binding
Popis:	Potent and selective Aurora kinase inhibitors were identified from the combinatorial expansion of the 1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazole bi-cycle, a novel and versatile scaffold designed to target the ATP pocket of protein kinases. The most potent compound reported in this study had an IC(50) of 0.027 microM in the enzymatic assay for Aur-A inhibition and IC(50)s between 0.05 microM and 0.5 microM for the inhibition of proliferation of different tumor cell lines.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2969e30ed7075e89dcd470afde1746f4 http://hdl.handle.net/20.500.11769/54844 Zobrazit plný text záznamu