Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Terrence M. Ciccarone"'
Autor:
Terrence M. Ciccarone, Hans E. Huber, Samuel L. Graham, Ronald G. Robinson, Jeffrey S. Taylor, Lorena S. Beese, Michelle Ellis-Hutchings, Robert B. Lobell, Nancy E. Kohl, Anthony W. Shaw, Eileen S. Walsh, Nancy N. Tsou, Desolms S Jane, Christine Fernandes, Suzanne C. Mactough, Kelly Hamilton, Carolyn A. Buser
Publikováno v:
Journal of Medicinal Chemistry. 46:2973-2984
A series of novel diaryl ether lactams have been identified as very potent dual inhibitors of protein farnesyltransferase (FTase) and protein geranylgeranyltransferase I (GGTase-I), enzymes involved in the prenylation of Ras. The structure of the com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7157b39100cc527794d744d80896dbd
https://doi.org/10.1021/jm020587n
https://doi.org/10.1021/jm020587n
Autor:
Joseph P. Davide, Robert B. Lobell, Kelly Hamilton, Kenneth S. Koblan, Ronald G. Robinson, Nancy E. Kohl, S. Jane Desolms, Samuel L. Graham, S. C. Mactough, John H. Hutchinson, Anthony W. Shaw, Terrence M. Ciccarone, Marc Abrams
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 11:1257-1260
Imidazolemethyl diaryl ethers are potent inhibitors of farnesyl-protein transferase. The SNAr displacement reaction used to prepare these diaryl ethers was amenable to rapid parallel synthesis of FPTase inhibitors. The use of a broad range of commerc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a97313784c223cafc9cb62933fc9a131
https://doi.org/10.1016/s0960-894x(01)00162-7
https://doi.org/10.1016/s0960-894x(01)00162-7
Autor:
Kenneth S. Koblan, Christopher J. Dinsmore, Jackson B. Gibbs, S. C. Mactough, J. Christopher Culberson, Terrence M. Ciccarone, Nancy E. Kohl, Samuel L. Graham, Daksha Shah, Timothy J. O'Neill, Oliff Allen I, Theresa M. Williams, George D. Hartman
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 9:1991-1996
The design and syntheses of non-thiol inhibitors of farnesyl-protein transferase are described. Substitutions on an imidazolylmethyl-AMBA-methionine template gave a highly potent and cell-active inhibitor.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3c372403f5e249be893cf49da7881c4
https://doi.org/10.1016/s0960-894x(99)00323-6
https://doi.org/10.1016/s0960-894x(99)00323-6
Autor:
Julie A. O'Brien, M E Goldman, S K Balani, V V Sardana, Terrence M. Ciccarone, C. S. Rooney, S. C. Mactough, Jon H. Condra, P. S. Anderson, William A. Schleif, Theresa M. Williams, Emilio A. Emini, Theoharides Anthony D, L. R. Kauffman, William J. Greenlee
Publikováno v:
ChemInform. 25
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::35f2712e1a446f4ef9e5b372da9f871c
https://doi.org/10.1002/chin.199410163
https://doi.org/10.1002/chin.199410163
Autor:
William J. Greenlee, S K Balani, L. R. Kauffman, Mark E. Goldman, Clarence S. Rooney, Jon H. Condra, Emilio A. Emini, S. C. Mactough, Terrence M. Ciccarone, Theresa M. Williams
Publikováno v:
Journal of medicinal chemistry. 36(9)
A series of highly potent, structurally novel, non-nucleoside RT inhibitors has been described. Low nanomolar concentrations of 5-chloro-3-(phenylsulfonyl)-indole-2-carboxamide (1) inhibit the HIV-1 RT enzyme in vitro and HTLVIIIb viral spread in MT-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cc6ccdc5cee375b7a1784cc0e52b4e3
https://pubmed.ncbi.nlm.nih.gov/7683725
https://pubmed.ncbi.nlm.nih.gov/7683725
Autor:
Paul L. Darke, Terrence M. Ciccarone, Patricia K. Lumma, Roger M. Freidinger, Victor M. Garsky, Irving S. Sigal, Stephen F. Brady, Daniel F. Veber, Ruth F. Nutt, Chih-Tai Leu
Publikováno v:
Biochemical and biophysical research communications. 156(1)
The mature proteins of retroviruses originate as a result of proteolytic cleavages of polyprotein precursors. Retroviruses encode proteases responsible for several of these processing events, making them potential antiviral drug targets. A 99-amino a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e472e5f6e0b9493f52d6ccad48cb888
https://pubmed.ncbi.nlm.nih.gov/3052448
https://pubmed.ncbi.nlm.nih.gov/3052448