| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10596594 | Bioorganic & Medicinal Chemistry Letters | 2012 | 7 Pages |
Abstract
A potent inhibitor of PI3Kδ that is ⩾200 fold selective for the remaining three Class I PI3K isoforms and additional kinases is described. The hypothesis for selectivity is illustrated through structure activity relationships and crystal structures of compounds bound to a K802T mutant of PI3Kγ. Pharmacokinetic data in rats and mice support the use of 3 as a useful tool compound to use for in vivo studies.
Keywords
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Daniel P. Sutherlin, Stewart Baker, Angelina Bisconte, Paul M. Blaney, Anthony Brown, Bryan K. Chan, David Chantry, Georgette Castanedo, Paul DePledge, Paul Goldsmith, David M. Goldstein, Timothy Hancox, Jasmit Kaur, David Knowles, Rama Kondru,