Potent inhibitors of Huntingtin protein aggregation in a cell-based assay

Autor:	Maria Laura Cremona, Ai Yamamoto, Udo Többen, Dusica Vidovic, Yuli Xie, Nathalie Aulner, Donald W. Landry, Caty Chung, Lars Branden, Gangli Gong, Katherine M. Myers, Alison Rinderspacher, Stephan C. Schürer, Yidong Liu, Monique Andersen, Shi Xian Deng
Rok vydání:	2009
Předmět:	Huntingtin Chemistry Pharmaceutical High-throughput screening Clinical Biochemistry Drug Evaluation Preclinical Pharmaceutical Science Nerve Tissue Proteins Biochemistry Article Inhibitory Concentration 50 Structure-Activity Relationship chemistry.chemical_compound Drug Discovery Quinazoline Huntingtin Protein Combinatorial Chemistry Techniques Humans Structure–activity relationship Nuclear protein Molecular Biology Molecular Structure Drug discovery Chemistry Organic Chemistry Nuclear Proteins Small molecule Models Chemical Drug Design Quinazolines Molecular Medicine Peptides
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 19:1715-1717
ISSN:	0960-894X
DOI:	10.1016/j.bmcl.2009.01.087
Popis:	A quinazoline that decreases polyglutamine aggregate burden in a cell-based assay was identified from a high-throughput screen of a chemical-compound library, provided by the NIH Molecular Libraries Small Molecule Repository (MLSMR). A structure and activity study yielded leads with submicromolar potency.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67daaa3c56cc2d76ef345cc1d9ff49ad https://doi.org/10.1016/j.bmcl.2009.01.087 Zobrazit plný text záznamu Full Text from ScienceDirect