Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Keith A, Eagen"'
Autor:
Damian Arnaiz, Gary Phillips, Shawn David Erickson, Marc Whitlow, Margaret Kenrick, James J. Devlin, Gonghua Pan, Cecile Santos, William J. Guilford, Robert G. Wei, Marc Adler, Kurt W. Saionz, Bin Ye, Ron Vergona, John Parkinson, Zuchun Spring Zhao, David D. Davey, Michael Ohlmeyer, Babu Subramanyam, Vidyadhar M. Paradkar, Mark A. Polokoff, Keith A. Eagen, Michael M. Morrissey
Publikováno v:
Journal of Medicinal Chemistry. 50:1146-1157
By the screening of a combinatorial library for inhibitors of nitric oxide (NO) formation by the inducible isoform of nitric oxide synthase (iNOS) using a whole-cell assay, 2-(imidazol-1-yl)pyrimidines were identified. Compounds were found to inhibit
Autor:
Howard P, Ng, Brad O, Buckman, Keith A, Eagen, William J, Guilford, Monica J, Kochanny, Raju, Mohan, Kenneth J, Shaw, Shung C, Wu, Dao, Lentz, Amy, Liang, Lan, Trinh, Elena, Ho, David, Smith, Babu, Subramanyam, Ron, Vergona, Janette, Walters, Kathy A, White, Mark E, Sullivan, Michael M, Morrissey, Gary B, Phillips
Publikováno v:
Bioorganicmedicinal chemistry. 10(3)
A novel series of triaryloxypyridines have been designed to inhibit factor Xa, a serine protease strategically located in the coagulation cascade. Inhibitor 5e has a K(I) against factor Xa of 0.12nM and is greater than 8000- and 2000-fold selective o
Autor:
Kirk Mcmillan, Gonghua Pan, Michael M. Morrissey, Leslie J. Browne, Mark A. Polokoff, Baldwin John J, Ronald Vergona, Gary Phillips, Marc Adler, Michael Ohlmeyer, David D. Davey, John Parkinson, Cornell Mallari, Charles B. Glaser, Nolan H. Sigal, Shawn David Erickson, Keith A. Eagen, James J. Devlin, Tish A. Young, Ronald E. Dolle, Eric Blasko, Daniel Chelsky, Richard I. Feldman, Douglas S. Auld, Marc Whitlow
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 97(4)
Potent and selective inhibitors of inducible nitric oxide synthase (iNOS) (EC 1.14.13.39 ) 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