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pubmed-article:16686528pubmed:abstractTextUsing the X-ray structure of human group X secreted phospholipase A(2) (hGX), we carried out structure-based design of indole-based inhibitors and prepared the compounds using a new synthetic route. The most potent compound inhibited hGX and the mouse orthologue with an IC(50) of 75 nM. This compound is the most potent hGX inhibitor reported to date and was also found to inhibit a subset of the other mouse and human sPLA(2)s.lld:pubmed
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pubmed-article:16686528pubmed:dateRevised2010-12-3lld:pubmed
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pubmed-article:16686528pubmed:articleTitleThe first potent inhibitor of mammalian group X secreted phospholipase A2: elucidation of sites for enhanced binding.lld:pubmed
pubmed-article:16686528pubmed:affiliationDepartment of Chemistry and Biochemistry, University of Washington, Seattle, Washington 98195, USA.lld:pubmed
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