Zobrazeno 1 - 8
of 8
pro vyhledávání: '"D. M. Delisle"'
Autor:
Meador J rd, Clifford E. Ford, Edward L. Brown, Chan F, Johnson T, Reich Siegfried Heinz, Kephart Se, Rose Ann Ferre, D. M. Delisle, David A. Matthews, Susan L. Binford, Shella A. Fuhrman, Amy K. Patick, Thomas F. Hendrickson, Stephen T. Worland, Wallace Michael B
Publikováno v:
Journal of Medicinal Chemistry. 43:1670-1683
A series of nonpeptide benzamide-containing inhibitors of human rhinovirus (HRV) 3C protease was identified using structure-based design. The design, synthesis, and biological evaluation of these inhibitors are reported. A Michael acceptor was combin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ff54ee5dd72ac29a93d73bc2f8db304
https://doi.org/10.1021/jm9903242
https://doi.org/10.1021/jm9903242
Autor:
A.K. Ganguly, Taveras Arthur G, Robert M. Aust, Doll Ronald J, Mark E. Snow, W. Sisson, Birendra N. Pramanik, D. M. Delisle, Charles R. Kissinger, Shella A. Fuhrman, Mary M. Senior, Bancha Vibulbhan, Yu-Sen Wang, C.A. Evans, Paul Kirschmeier, Stacy W. Remiszewski, B.B. Bauer, Louise M. Perkins, V. Girijavallabhan, D. Cesarz, Robert A. Love, Joseph J. Catino, Eric C. Huang, C. Nash, Joan E. Brown, Larry Heimark, Donna Carr, Linda James, E. Villafranca, Anthony Tsarbopoulos, Edward L. Brown, S.E. Webber, Thomas F. Hendrickson, Stephen D. Liberles, J. del Rosario
Publikováno v:
Bioorganic & Medicinal Chemistry. 5:125-133
The nucleotide exchange process is one of the key activation steps regulating the ras protein. This report describes the development of potent, non-nucleotide, small organic inhibitors of the ras nucleotide exchange process. These inhibitors bind to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc28878387c5048a407d3b0e5a227d3a
https://doi.org/10.1016/s0968-0896(96)00202-7
https://doi.org/10.1016/s0968-0896(96)00202-7
Autor:
Edward L. Brown, Susan L. Binford, Amy K. Patick, Shella A. Fuhrman, Rose Ann Ferre, D. M. Delisle, R. A. Love, Jayashree Tikhe, Stephen E. Webber, James W. Meador, Thomas F. Hendrickson, David A. Matthews, Stephen T. Worland, Clifford E. Ford
Publikováno v:
Journal of Medicinal Chemistry. 39:5072-5082
The design, synthesis, and biological evaluation of reversible, nonpeptidic inhibitors of human rhinovirus (HRV) 3C protease (3CP) are reported. A novel series of 2,3-dioxindoles (isatins) were designed that utilized a combination of protein structur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afb4276743bdc1e96c88b9e79ec6479e
https://doi.org/10.1021/jm960603e
https://doi.org/10.1021/jm960603e
Autor:
R. A. Love, Stephen T. Worland, D. M. Delisle, Jayashree Tikhe, Edward L. Brown, Susan L. Binford, Thomas F. Hendrickson, Rose Ann Ferre, Shella A. Fuhrman, David A. Matthews, James W. Meador, Clifford E. Ford, Amy K. Patick, Stephen E. Webber
Publikováno v:
ChemInform. 28
The design, synthesis, and biological evaluation of reversible, nonpeptidic inhibitors of human rhinovirus (HRV) 3C protease (3CP) are reported. A novel series of 2,3-dioxindoles (isatins) were designed that utilized a combination of protein structur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1bce72203ce2bbeeb2279001653ec46
https://doi.org/10.1002/chin.199716148
https://doi.org/10.1002/chin.199716148
Autor:
D. A. Matthews, P. S. Dragovich, S. E. Webber, S. A. Fuhrman, A. K. Patick, L. S. Zalman, T. F. Hendrickson, R. A. Love, T. J. Prins, J. T. Marakovits, R. Zhou, J. Tikhe, C. E. Ford, J. W. Meador, R. A. Ferre, E. L. Brown, S. L. Binford, M. A. Brothers, D. M. DeLisle, S. T. Worland
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 96(20)
Human rhinoviruses, the most important etiologic agents of the common cold, are messenger-active single-stranded monocistronic RNA viruses that have evolved a highly complex cascade of proteolytic processing events to control viral gene expression an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edabbff518962190e09debad63ef7ac8
https://pubmed.ncbi.nlm.nih.gov/10500114
https://pubmed.ncbi.nlm.nih.gov/10500114
Autor:
Paul Kirschmeier, Thomas F. Hendrickson, Remiszewski Stacy W, Wess A. Sisson, Doll Ronald J, Birendra N. Pramanik, Ashit K. Ganguly, David Cesarz, and Anthony Tsarbopoulos, Steve E. Webber, Eric C. Huang, Yu-Sen Wang, Joan E. Brown, Viyyoor M. Girijavallabhan, Robert A. Love, Bancha Vibulbhan, Taveras Arthur G, Robert M. Aust, Mark E. Snow, J. del Rosario, Edward L. Brown, Shella A. Fuhrman, Larry Heimark, and J. Ernest Villafranca, Charles R. Kissinger, D. M. Delisle
Publikováno v:
Biochemistry. 37(45)
Mutated, tumorigenic Ras is present in a variety of human tumors. Compounds that inhibit tumorigenic Ras function may be useful in the treatment of Ras-related tumors. The interaction of a novel GDP exchange inhibitor (SCH-54292) with the Ras-GDP pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8588dd08523ce1eb52765428eb0f1de
https://pubmed.ncbi.nlm.nih.gov/9843367
https://pubmed.ncbi.nlm.nih.gov/9843367
Publikováno v:
Journal of Biological Chemistry. 261:13247-13251
A superoxide-forming oxidase from activated human neutrophil membranes was solubilized by two slightly different methods, then purified by "dye-affinity" chromatography. Kinetic studies of the purified preparations gave Vmax values of 5-10 mumol of O
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4ea77b13b23abceb340e1c7a9d53160c
https://doi.org/10.1016/s0021-9258(18)69297-x
https://doi.org/10.1016/s0021-9258(18)69297-x
Publikováno v:
The Journal of biological chemistry. 261(28)
A superoxide-forming oxidase from activated human neutrophil membranes was solubilized by two slightly different methods, then purified by "dye-affinity" chromatography. Kinetic studies of the purified preparations gave Vmax values of 5-10 mumol of O
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::96d7c2d24e3a4031aa3abf01e2cd00f7
https://pubmed.ncbi.nlm.nih.gov/3759962
https://pubmed.ncbi.nlm.nih.gov/3759962