Zobrazeno 1 - 9
of 9
pro vyhledávání: '"J. V. Tuttle"'
Autor:
K. L. Powell, Margaret Tisdale, G. Darby, G. Appleyard, D. J. Nelson, D. J. M. Purifoy, W. Al Nakib, J. N. Stables, J. V. Tuttle, S. Nusinoff-Lehrman
Publikováno v:
Antiviral Chemistry and Chemotherapy. 4:281-287
A series of 2′-deoxy-2′-fluororibosides were evaluated for anti-influenza activity in cell culture and in the mouse pneumonia model. Many were found to be potent inhibitors of Influenza A, in chick embryo fibroblast cells (IC50's 0.1–2.9 μM),
Publikováno v:
The Journal of biological chemistry. 265(6)
The diphosphate of the antiherpetic agent acyclovir [9-[(2-hydroxyethoxy)methyl]guanine] has been shown to inhibit purine nucleoside phosphorylase with unique potency (Tuttle, J. V., and Krenitsky, T. A. (1984) J. Biol. Chem. 259, 4065-4069). A major
Autor:
T A Krenitsky, J V Tuttle
Publikováno v:
Journal of Biological Chemistry. 259:4065-4069
Acyclovir (9-(2-hydroxyethoxymethyl)guanine), the clinically useful antiherpetic agent, is an "acyclic" analogue of 2'-deoxyguanosine. Purine nucleoside phosphorylase partially purified from human erythrocytes did not catalyze detectable phosphorolys
Autor:
T A Krenitsky, J V Tuttle
Publikováno v:
Journal of Biological Chemistry. 255:909-916
Autor:
J V, Tuttle, T A, Krenitsky
Publikováno v:
The Journal of biological chemistry. 259(7)
Acyclovir (9-(2-hydroxyethoxymethyl)guanine), the clinically useful antiherpetic agent, is an "acyclic" analogue of 2'-deoxyguanosine. Purine nucleoside phosphorylase partially purified from human erythrocytes did not catalyze detectable phosphorolys
Publikováno v:
Advances in experimental medicine and biology.
Autor:
D J, Nelson, S W, LaFon, J V, Tuttle, W H, Miller, R L, Miller, T A, Krenitsky, G B, Elion, R L, Berens, J J, Marr
Publikováno v:
The Journal of biological chemistry. 254(22)
Autor:
T A, Krenitsky, J V, Tuttle, G W, Koszalka, I S, Chen, L M, Beacham, J L, Rideout, G B, Elion
Publikováno v:
The Journal of biological chemistry. 251(13)
Kinetic constants were determined for 34 nucleoside substrates of deoxycytidine kinase (EC 2.7.1.74) from calf thymus. Substrate efficiency was assessed by the ratio of Vmax to Km. Inhibition constants were determined for 61 nonsubstrate nucleosides
Autor:
J V, Tuttle, T A, Krenitsky
Publikováno v:
The Journal of biological chemistry. 255(3)