Ontology highlight
ABSTRACT:
SUBMITTER: McMillan K
PROVIDER: S-EPMC26464 | biostudies-literature | 2000 Feb
REPOSITORIES: biostudies-literature
McMillan K K Adler M M Auld D S DS Baldwin J J JJ Blasko E E Browne L J LJ Chelsky D D Davey D D Dolle R E RE Eagen K A KA Erickson S S Feldman R I RI Glaser C B CB Mallari C C Morrissey M M MM Ohlmeyer M H MH Pan G G Parkinson J F JF Phillips G B GB Polokoff M A MA Sigal N H NH Vergona R R Whitlow M M Young T A TA Devlin J J JJ
Proceedings of the National Academy of Sciences of the United States of America 20000201 4
Potent and selective inhibitors of inducible nitric oxide synthase (iNOS) (EC ) 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(50) values and thus were >1,000-fold more potent than the substrate-based direct iNOS inhibitors 1400W and N-methyl-l-arginine. Biochemical studies confirmed that inhibitors caused accumulation of iNOS mon ...[more]