{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,28]],"date-time":"2026-03-28T02:07:34Z","timestamp":1774663654136,"version":"3.50.1"},"reference-count":38,"publisher":"Proceedings of the National Academy of Sciences","issue":"4","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2000,2,15]]},"abstract":"<jats:p>\n            Potent and selective inhibitors of inducible nitric oxide synthase (iNOS) (EC\n            <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"ec\" xlink:href=\"1.14.13.39\">1.14.13.39<\/jats:ext-link>\n            ) were identified in an encoded combinatorial chemical library that blocked human iNOS dimerization, and thereby NO production. In a cell-based iNOS assay (A-172 astrocytoma cells) the inhibitors had low-nanomolar IC\n            <jats:sub>50<\/jats:sub>\n            values and thus were &gt;1,000-fold more potent than the substrate-based direct iNOS inhibitors 1400W and\n            <jats:italic>N-<\/jats:italic>\n            methyl-\n            <jats:sc>l<\/jats:sc>\n            -arginine. Biochemical studies confirmed that inhibitors caused accumulation of iNOS monomers in mouse macrophage RAW 264.7 cells. High affinity (\n            <jats:italic>K<\/jats:italic>\n            <jats:sub>d<\/jats:sub>\n            \u2248 3 nM) of inhibitors for isolated iNOS monomers was confirmed by using a radioligand binding assay. Inhibitors were &gt;1,000-fold selective for iNOS versus endothelial NOS dimerization in a cell-based assay. The crystal structure of inhibitor bound to the monomeric iNOS oxygenase domain revealed inhibitor\u2013heme coordination and substantial perturbation of the substrate binding site and the dimerization interface, indicating that this small molecule acts by allosterically disrupting protein\u2013protein interactions at the dimer interface. These results provide a mechanism-based approach to highly selective iNOS inhibition. Inhibitors were active\n            <jats:italic>in vivo<\/jats:italic>\n            , with ED\n            <jats:sub>50<\/jats:sub>\n            values of &lt;2 mg\/kg in a rat model of endotoxin-induced systemic iNOS induction. Thus, this class of dimerization inhibitors has broad therapeutic potential in iNOS-mediated pathologies.\n          <\/jats:p>","DOI":"10.1073\/pnas.97.4.1506","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T14:32:33Z","timestamp":1027693953000},"page":"1506-1511","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":179,"title":["Allosteric inhibitors of inducible nitric oxide synthase dimerization discovered via combinatorial chemistry"],"prefix":"10.1073","volume":"97","author":[{"given":"Kirk","family":"McMillan","sequence":"first","affiliation":[{"name":"Pharmacopeia, Inc., Princeton, NJ 08512; and Discovery Research, Gene Therapy and Genomics, Cancer Research, and Department of Immunology, Berlex Biosciences, Richmond, CA 94804"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marc","family":"Adler","sequence":"additional","affiliation":[{"name":"Pharmacopeia, Inc., Princeton, NJ 08512; 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