Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Edgar H. Ulm"'
Autor:
Karen Lundgren, Roy Grecko, Srinivas Rao Kasibhatla, Kevin Hong, Adeela Kamal, Rachel Lough, Gregg Timony, Lawrence C. Fritz, Edgar H. Ulm, Marco A. Biamonte, Patricia Karjian, David J. Busch, Marcus F. Boehm, Robert K. Mansfield, Francis Burrows, John Brekken, Yingqing Ran, John Sensintaffar
Publikováno v:
Journal of Medicinal Chemistry. 50:2767-2778
Heat shock protein 90 (Hsp90) is a molecular chaperone protein implicated in stabilizing the conformation and maintaining the function of many cell-signaling proteins. Many oncogenic proteins are more dependent on Hsp90 in maintaining their conformat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::256512d0ba0657d93f9e55a9f6d48e83
https://doi.org/10.1021/jm050752+
https://doi.org/10.1021/jm050752+
Autor:
Kevin Hong, Adeela Kamal, Yingqing Ran, Jiandong Shi, Marcus F. Boehm, Karen Lundgren, Gregg Timony, Khang Vu, Edgar H. Ulm, Francis Burrows, Roy Grecko, Rachel Lough, Srinivas Rao Kasibhatla, John Sensintaffar, David J. Busch, Jean-Yves Le Brazidec, Marco A. Biamonte, Robert K. Mansfield, Junhua Fan, Lin Zhang
Publikováno v:
Journal of Medicinal Chemistry. 49:5352-5362
We report on the discovery of benzo- and pyridino- thiazolothiopurines as potent heat shock protein 90 inhibitors. The benzothiazole moiety is exceptionally sensitive to substitutions on the aromatic ring with a 7'-substituent essential for activity.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a30163f614c02b6f0a966897c679719
https://doi.org/10.1021/jm051146h
https://doi.org/10.1021/jm051146h
Autor:
Edgar H. Ulm, Theodore C. Vassil, Eugene D. Thorsett, William J. Greenlee, Arthur A. Patchett, Elbert E. Harris, E. R. Peterson
Publikováno v:
Proceedings of the National Academy of Sciences. 79:2176-2180
Several phosphonamides, phosphoramides, and phosphates having the general structure R-Y-P(O)(OH)-X-CH(CH3)-CO-Pro have been synthesized and tested for inhibition of angiotensin-converting enzyme (dipeptidyl carboxypeptidase; peptidyl-dipeptide hydrol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::943b5066530d7aa2ef5915b5532866df
https://doi.org/10.1073/pnas.79.7.2176
https://doi.org/10.1073/pnas.79.7.2176
Autor:
Charles S. Sweet, Edgar H. Ulm
Publikováno v:
Cardiovascular Drug Reviews. 2:1-17
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::72f11b10556c9c0ec279c47cf004024f
https://doi.org/10.1111/j.1527-3466.1984.tb00455.x
https://doi.org/10.1111/j.1527-3466.1984.tb00455.x
Autor:
Daniel F. Veber, Carl D. Bennett, LaMont Bi, Joshua S. Boger, Terry W. Schorn, Edgar H. Ulm, Edward H. Blaine, Payne Linda S, Carl F. Homnick
Publikováno v:
Regulatory Peptides. 10:8-13
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e58a9ad000824fbe1d3ceb5965b76db
https://doi.org/10.1016/0167-0115(85)90210-1
https://doi.org/10.1016/0167-0115(85)90210-1
Autor:
Charles S. Sweet, Edgar H. Ulm
Publikováno v:
Cardiovascular Drug Reviews. 6:181-191
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15e468e41d129e0429d71e9a4c0fbbe8
https://doi.org/10.1111/j.1527-3466.1988.tb00375.x
https://doi.org/10.1111/j.1527-3466.1988.tb00375.x
Publikováno v:
Journal of Biological Chemistry. 250:4996-5002
Dialyzed rabbit liver cytosol was specifically freed of endogenous fructose-1,6-diphosphatase by immunoadsorption on a column of Sepharose-immobilized anti-fructose-1,6-diphosphatase. This material increased the specific activity of homogeneous enzym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8fec9bd2649c10fc28ca491a64f84373
https://doi.org/10.1016/s0021-9258(19)41268-4
https://doi.org/10.1016/s0021-9258(19)41268-4
Autor:
Martin Poe, B. E. Evans, Robert M. DiPardo, Edgar H. Ulm, Kenneth E. Rittle, LaMont Bi, Joshua S. Boger, Lynch Rj, Mark G. Bock, George P. Vlasuk
Publikováno v:
Journal of Medicinal Chemistry. 30:1853-1857
A series of statine-containing tetrapeptides, systematically modified at the carboxy terminus with various hydrophobic aromatic groups, is described. These compounds were tested in vitro for their ability to inhibit porcine, human plasma, and purifie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31ff585bee2b4ee64a80dc3570ef1642
https://doi.org/10.1021/jm00393a029
https://doi.org/10.1021/jm00393a029
Publikováno v:
Journal of Biological Chemistry. 248:5555-5561
Homogeneous rabbit liver fructose 1,6-diphosphatase (specific activity of 35 at pH 7.3 and 30°) was activated by various fatty acids, of which oleate was the most effective. In the absence of oleate or other activators, the enzyme had a pH optimum a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f15c352340a33e5b298c76b580e9c74f
https://doi.org/10.1016/s0021-9258(19)43540-0
https://doi.org/10.1016/s0021-9258(19)43540-0
Autor:
Edward H. Blaine, LaMont Bi, Kenneth E. Rittle, M. G. Bock, Edgar H. Ulm, M. Poe, C. D. Bennett, Joshua S. Boger, D. F. Veber, Robert M. DiPardo, I. I. Stabilito, G. M. Fanelli, B. E. Evans
Publikováno v:
Chemischer Informationsdienst. 17
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::861f0718929b181627344bd7b00f83e6
https://doi.org/10.1002/chin.198613318
https://doi.org/10.1002/chin.198613318