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Effect of antineoplastic agents on the DNA cleavage/religation reaction of eukaryotic topoisomerase II: inhibition of DNA religation by etoposide.
Osheroff N. Osheroff N. Biochemistry. 1989 Jul 25;28(15):6157-60. doi: 10.1021/bi00441a005. Biochemistry. 1989. PMID: 2551366
By employing a topoisomerase II mediated DNA religation assay [Osheroff, N. & Zechiedrich, E.L. (1987) Biochemistry 26, 4303-4309], etoposide was found to stabilize the enzyme-DNA cleavage complex (at least in part) by inhibiting the enzyme's ability to religate …
By employing a topoisomerase II mediated DNA religation assay [Osheroff, N. & Zechiedrich, E.L. (1987) Biochemistry 26, 43 …
A role for the passage helix in the DNA cleavage reaction of eukaryotic topoisomerase II. A two-site model for enzyme-mediated DNA cleavage.
Corbett AH, Zechiedrich EL, Osheroff N. Corbett AH, et al. Among authors: osheroff n. J Biol Chem. 1992 Jan 15;267(2):683-6. J Biol Chem. 1992. PMID: 1309770
Eukaryotic topoisomerase II is capable of binding two separate nucleic acid helices prior to its DNA cleavage and strand passage events (Zechiedrich, E. L., and Osheroff, N (1990) EMBO J. 9, 4555-4562). Presumably, one of these helices represents the helix that the …
Eukaryotic topoisomerase II is capable of binding two separate nucleic acid helices prior to its DNA cleavage and strand passage events (Zec …
Intrinsic intermolecular DNA ligation activity of eukaryotic topoisomerase II. Potential roles in recombination.
Gale KC, Osheroff N. Gale KC, et al. Among authors: osheroff n. J Biol Chem. 1992 Jun 15;267(17):12090-7. J Biol Chem. 1992. PMID: 1318309
Drosophila melanogaster topoisomerase II is capable of joining phi X174 (+) strand DNA that it has cleaved to duplex oligonucleotide acceptor molecules by an intermolecular ligation reaction (Gale, K. C. and Osheroff, N. (1990) Biochemistry 29, 9538-9545). In order …
Drosophila melanogaster topoisomerase II is capable of joining phi X174 (+) strand DNA that it has cleaved to duplex oligonucleotide accepto …
Cytotoxicity of quinolones toward eukaryotic cells. Identification of topoisomerase II as the primary cellular target for the quinolone CP-115,953 in yeast.
Elsea SH, Osheroff N, Nitiss JL. Elsea SH, et al. Among authors: osheroff n. J Biol Chem. 1992 Jul 5;267(19):13150-3. J Biol Chem. 1992. PMID: 1320012
., Gootz, T. D., McGuirk, P. R., Moynihan, M., Sutcliffe, J. A., and Osheroff, N. (1991) J. Biol. Chem. 266, 14585-14592). Although the quinolone is highly toxic to mammalian cells in culture, its mechanism of cytotoxic action is not known. ...
., Gootz, T. D., McGuirk, P. R., Moynihan, M., Sutcliffe, J. A., and Osheroff, N. (1991) J. Biol. Chem. 266, 14585-14592). Alt …
Effects of novel fluoroquinolones on the catalytic activities of eukaryotic topoisomerase II: Influence of the C-8 fluorine group.
Robinson MJ, Martin BA, Gootz TD, McGuirk PR, Osheroff N. Robinson MJ, et al. Among authors: osheroff n. Antimicrob Agents Chemother. 1992 Apr;36(4):751-6. doi: 10.1128/aac.36.4.751. Antimicrob Agents Chemother. 1992. PMID: 1323952 Free PMC article.
Martin, T.D. Gootz, P.R. McGuirk, M. Moynihan, J.A. Sutcliffe, and N. Osheroff, J. Biol. Chem. 266:14585-14592, 1991) demonstrated that novel 6,8-difluoroquinolones were potent effectors of eukaryotic topoisomerase II. ...Further comparisons of CP-115,955 with CP-11 …
Martin, T.D. Gootz, P.R. McGuirk, M. Moynihan, J.A. Sutcliffe, and N. Osheroff, J. Biol. Chem. 266:14585-14592, 1991) demonstr …
Effect of casein kinase II-mediated phosphorylation on the catalytic cycle of topoisomerase II. Regulation of enzyme activity by enhancement of ATP hydrolysis.
Corbett AH, DeVore RF, Osheroff N. Corbett AH, et al. Among authors: osheroff n. J Biol Chem. 1992 Oct 5;267(28):20513-8. J Biol Chem. 1992. PMID: 1328202
The catalytic activity of topoisomerase II is stimulated approximately 2-3-fold following phosphorylation by casein kinase II (Ackerman, P., Glover, C. V. C., and Osheroff, N. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 3164-3168). ...
The catalytic activity of topoisomerase II is stimulated approximately 2-3-fold following phosphorylation by casein kinase II (Ackerman, P., …
Catalytic function of DNA topoisomerase II.
Osheroff N, Zechiedrich EL, Gale KC. Osheroff N, et al. Bioessays. 1991 Jun;13(6):269-73. doi: 10.1002/bies.950130603. Bioessays. 1991. PMID: 1654050 Review.
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