| Literature DB >> 28492317 |
Emiliano Tamanini1, Ildiko M Buck1, Gianni Chessari1, Elisabetta Chiarparin1, James E H Day1, Martyn Frederickson1, Charlotte M Griffiths-Jones1, Keisha Hearn1, Tom D Heightman1, Aman Iqbal1, Christopher N Johnson1, Edward J Lewis1, Vanessa Martins1, Torren Peakman1, Michael Reader1, Sharna J Rich1, George A Ward1, Pamela A Williams1, Nicola E Wilsher1.
Abstract
XIAP and cIAP1 are members of the inhibitor of apoptosis protein (IAP) family and are key regulators of anti-apoptotic and pro-survival signaling pathways. Overexpression of IAPs occurs in various cancers and has been associated with tumor progression and resistance to treatment. Structure-based drug design (SBDD) guided by structural information from X-ray crystallography, computational studies, and NMR solution conformational analysis was successfully applied to a fragment-derived lead resulting in AT-IAP, a potent, orally bioavailable, dual antagonist of XIAP and cIAP1 and a structurally novel chemical probe for IAP biology.Entities:
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Year: 2017 PMID： 28492317 DOI： 10.1021/acs.jmedchem.6b01877
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446