Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Tate Bonnie Frances"'
Autor:
Kristin Kelly, Christopher John Helal, Tate Bonnie Frances, Mavis Diane Adam, Zhijun Kang, Marcia F. Peterson, Thomas G. Gant, Christopher B. Cooper, Michael K. Ahlijanian, Stanley William Kupchinsky, John C. Lucas, Frank S. Menniti, Sanner Mark Allen
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 14:5521-5525
High-throughput screening with cyclin-dependent kinase 5 (cdk5)/p25 led to the discovery of N-(5-isopropyl-thiazol-2-yl)isobutyramide (1). This compound is an equipotent inhibitor of cdk5 and cyclin-dependent kinase 2 (cdk2)/cyclin E (IC50 = ca. 320
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1a7b171a8387e73aea99641b4e26b53
https://doi.org/10.1016/j.bmcl.2004.09.006
https://doi.org/10.1016/j.bmcl.2004.09.006
Autor:
Paul DaSilva-Jardine, Josephine Spitzer, Michele H. Rosner, Samuel P. Simons, Diane M. Hargrove, Boris A. Chrunyk, Richard F. Hank, Phoebe Chiang, Ernest S. Paight, Swick Andrew Gordon, Robert L. Dow, Peter Cornelius, Gayle K. Schulte, Tate Bonnie Frances, Steven R. Schneider, Terrell A. Patterson, William P. Newsome, Jayvardhan Pandit, Mark Ammirati, Eunsun Lee, Dennis E. Danley, Peter K. LeMotte
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 13:379-382
In this communication, we wish to describe the discovery of a novel series of 6-azauracil-based thyromimetics that possess up to 100-fold selectivities for binding and functional activation of the beta(1)-isoform of the thyroid receptor family. Struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eedc13a957ab620f44d6f0b2eb9b7bf1
https://doi.org/10.1016/s0960-894x(02)00947-2
https://doi.org/10.1016/s0960-894x(02)00947-2
Publikováno v:
Analytical Biochemistry. 271:131-136
A novel method for characterizing the kinetics of protein kinase inhibitors is described. This method uses glycogen synthase kinase beta as the model protein kinase and looks at the shift in IC50 of inhibitors using the nonhydrolyzable ATP analog, be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef7b5ed4a6d31b32b800b27fac905d78
https://doi.org/10.1006/abio.1999.4126
https://doi.org/10.1006/abio.1999.4126