Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Katherine M. Welsh"'
Autor:
Varney Michael D, Charlotte A. Bartlett, Stephanie Webber, Catharine A. Morse, Ward W. Smith, Cheryl A. Janson, Cindy L. Palmer, Deal Judith G, Katherine M. Welsh
Publikováno v:
Journal of Medicinal Chemistry. 38:1892-1903
The design, synthesis, and biochemical and biological evaluations of a novel series of 2,6-diaminobenz[cd]indole-containing inhibitors of human thymidylate synthase (TS) are described. The compounds are characterized by having either a pyridine or py
Autor:
Marta Perego, Conrad Hanstein, Philippe Glaser, James A. Hoch, Katherine M. Welsh, Tsotne Djavakhishvili
Publikováno v:
Cell. 79:1047-1055
The initiation of sporulation in B. subtilis is regulated by the Spo0A transcription factor, which is activated by phosphorylation to control developmental switching from the vegetative to the sporulation state. The level of phosphorylation of Spo0A
Autor:
Stephan T. Freer, M. Rami Reddy, Jones Terence R, Katherine M. Welsh, Russell J. Bacquet, Dominic Zichi, David A. Matthews
Publikováno v:
Journal of the American Chemical Society. 114:10117-10122
The thermodynamic cycle perturbation approach, in conjunction with molecular dynamics simulations, has been used to calculate relative binding free energies for the closely related inhibitors 10-propargyl-5,8-dideazafolic acid (PDDF) and 10-formyl-5,
Autor:
C. A. Morse, Deal Judith G, Marzoni Gifford P, Russell J. Bacquet, Varney Michael D, Katherine M. Welsh, Cynthia Louise Palmer, Carol L. J. Booth, Charlotte A. Bartlett, Stephanie Webber
Publikováno v:
Journal of Medicinal Chemistry. 35:663-676
The X-ray crystal-structure-based design, synthesis, and biological activity of a novel family of benz[cd]indole-containing inhibitors of thymidylate synthase (TS) are described. The structure-activity of the lead compound was studied by conceptually
Autor:
Zuzana Hostomska, Cheryl A. Janson, Katherine M. Welsh, Daniel R. Knighton, Chen-Chen Kan, David A. Matthews, Eleanor F. Howland
Publikováno v:
Nature structural biology. 1(3)
The bifunctional enzyme dihydrofolate reductase-thymidylate synthase catalyses both the reductive methylation of 2'-deoxyuridylate and the subsequent reduction of dihydrofolate to yield 2'-deoxythymidylate and tetrahydrofolate at two spacially discre
Autor:
Mary Ann M. Fuhry, Ward W. Smith, David A. Matthews, Katherine M. Welsh, Dzuy T. Nguyen, S R Jordan, Cheryl A. Janson, Siegfried Reich, Mark J. Pino, Stephanie Webber
Publikováno v:
Journal of medicinal chemistry. 35(5)
Antifolate inhibitors of thymidylate synthase (TS) have primarily been based on the structure of folic acid. This paper describes the identification and development of novel 6,7-imidazotetrahydroquinoline TS inhibitors by iterative ligand design, syn
Autor:
Barry S. Cooperman, Katherine M. Welsh
Publikováno v:
Biochemistry. 23:4947-4955
Equilibrium dialysis and 113Cd2+ NMR studies in the presence of inorganic phosphate (Pi) provide clear evidence for the existence of four well-defined Cd2+ sites per yeast inorganic pyrophosphatase subunit. Parallel 31P NMR studies demonstrate the ex
Publikováno v:
Biochemistry. 23:797-801
In this work, we show that adenosine 5'-O-(3-thiotriphosphate) (ATP gamma S) is a substrate for yeast inorganic pyrophosphatase (PPase) (EC 3.6.1.1) and further, using chirally labeled [gamma-17O,18O]ATP gamma S, that enzyme-catalyzed hydrolysis to p
Publikováno v:
Biochemistry. 22:2243-2248
Autor:
Judith P. Klinman, Katherine M. Welsh
Publikováno v:
Biochemical and Biophysical Research Communications. 70:878-884
Analyses for zinc in high specific activity preparations of yeast alcohol dehydrogenase (YADH) indicate a metal content of 1.8–1.9 moles of zinc per mole of enzyme subunit. This zinc content is observed for YADH prepared from Bakers yeast by recrys