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1
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0032189275
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DNA gyrase and topoisomerase IV: Biochemical activities, physiological roles during chromosome replication, and drug sensitivities
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This excellent review provides an especially good overview of topoisomerase biochemistry, and an introduction to intracellular action and quinolone mechanism
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Levine C, Hiasa H, Marians K DNA gyrase and topoisomerase IV: biochemical activities, physiological roles during chromosome replication, and drug sensitivities. Biochim Biophys Acta. 1400:1998;29-43. This excellent review provides an especially good overview of topoisomerase biochemistry, and an introduction to intracellular action and quinolone mechanism.
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(1998)
Biochim Biophys Acta
, vol.1400
, pp. 29-43
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Levine, C.1
Hiasa, H.2
Marians, K.3
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2
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0029904283
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DNA cleavage is not required for the binding of quinolone drugs to the DNA gyrase-DNA complex
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Critchlow SE, Maxwell A DNA cleavage is not required for the binding of quinolone drugs to the DNA gyrase-DNA complex. Biochemistry. 35:1996;7387-7393.
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(1996)
Biochemistry
, vol.35
, pp. 7387-7393
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Critchlow, S.E.1
Maxwell, A.2
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3
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0032575610
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Conformational changes in DNA gyrase revealed by limited proteolysis
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In this study with purified gyrase, ciprofloxacin is shown to alter the conformation of GyrB in quinolone/gyrase/DNA complexes in the absence of DNA cleavage. Also see [6]
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Kampranis S, Maxwell A Conformational changes in DNA gyrase revealed by limited proteolysis. J Biol Chem. 273:1998;22606-22614. In this study with purified gyrase, ciprofloxacin is shown to alter the conformation of GyrB in quinolone/gyrase/DNA complexes in the absence of DNA cleavage. Also see [6].
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(1998)
J Biol Chem
, vol.273
, pp. 22606-22614
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Kampranis, S.1
Maxwell, A.2
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4
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0032575668
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The DNA gyrase-quinolone complex, ATP hydrolysis and the mechanism of DNA cleavage
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The ATPase activity of gyrase in the presence of ciprofloxacin is used to dissect formation of quinolone/gyrase/DNA complex formation using kinetic analyses. Also see [6]
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Kampranis S, Maxwell A The DNA gyrase-quinolone complex, ATP hydrolysis and the mechanism of DNA cleavage. J Biol Chem. 173:1998;22615-22626. The ATPase activity of gyrase in the presence of ciprofloxacin is used to dissect formation of quinolone/gyrase/DNA complex formation using kinetic analyses. Also see [6].
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(1998)
J Biol Chem
, vol.173
, pp. 22615-22626
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Kampranis, S.1
Maxwell, A.2
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5
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0018384079
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DNA gyrase on the bacterial chromosome: DNA cleavage induced by oxolinic acid
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Snyder M, Drlica K DNA gyrase on the bacterial chromosome: DNA cleavage induced by oxolinic acid. J Mol Biol. 131:1979;287-302.
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(1979)
J Mol Biol
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Snyder, M.1
Drlica, K.2
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6
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0030962482
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Mechanism of quinolone action: A drug-induced structural perturbation of the DNA precedes strand cleavage by topoisomerase IV
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Marians K, Hiasa H Mechanism of quinolone action: a drug-induced structural perturbation of the DNA precedes strand cleavage by topoisomerase IV. J Biol Chem. 272:1997;9401-9409.
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(1997)
J Biol Chem
, vol.272
, pp. 9401-9409
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Marians, K.1
Hiasa, H.2
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8
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0024339376
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Double-stranded DNA cleavage/religation of eukaryotic topoisomerase II: Evidence for a nicked DNA intermediate
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Zechiedrich EL, Christiansen K, Andersen A, Westergaard O, Osheroff N Double-stranded DNA cleavage/religation of eukaryotic topoisomerase II: evidence for a nicked DNA intermediate. Biochemistry. 28:1989;6229-6236.
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Biochemistry
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Zechiedrich, E.L.1
Christiansen, K.2
Andersen, A.3
Westergaard, O.4
Osheroff, N.5
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9
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0024278509
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DNA gyrase on the bacterial chromosome: Oxolinic acid-induced DNA cleavage in the dnaA-gyrB region
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Franco R, Drlica K DNA gyrase on the bacterial chromosome: oxolinic acid-induced DNA cleavage in the dnaA-gyrB region. J Mol Biol. 201:1988;229-233.
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(1988)
J Mol Biol
, vol.201
, pp. 229-233
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Franco, R.1
Drlica, K.2
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10
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0032538454
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The mechanism of inhibition of topoisomerase IV by quinolone antibacterials
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This extensive physiological study of topoisomerase-IV-norfloxacin interactions provides evidence that topoisomerase IV acts behind replication forks. Use of gyrB and seqA mutants shows that topoisomerase IV-containing complexes can behave like gyrase-containing complexes by blocking replication immediately
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Khodursky A, Cozzarelli N The mechanism of inhibition of topoisomerase IV by quinolone antibacterials. J Biol Chem. 273:1998;27668-27677. This extensive physiological study of topoisomerase-IV-norfloxacin interactions provides evidence that topoisomerase IV acts behind replication forks. Use of gyrB and seqA mutants shows that topoisomerase IV-containing complexes can behave like gyrase-containing complexes by blocking replication immediately.
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(1998)
J Biol Chem
, vol.273
, pp. 27668-27677
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Khodursky, A.1
Cozzarelli, N.2
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11
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0026712869
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The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication
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Adams D, Shekhtman E, Zechiedrich E, Schmid M, Cozzarelli N The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication. Cell. 71:1992;277-288.
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(1992)
Cell
, vol.71
, pp. 277-288
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Adams, D.1
Shekhtman, E.2
Zechiedrich, E.3
Schmid, M.4
Cozzarelli, N.5
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13
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0032544699
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The structure of supercoiled intermediates in DNA replication
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Using small bacterial plasmids, experimental support is provided for precatenanes forming behind replication forks
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Peter B, Ullsperger C, Hiasa H, Marians K, Cozzarelli N The structure of supercoiled intermediates in DNA replication. Cell. 94:1998;819-827. Using small bacterial plasmids, experimental support is provided for precatenanes forming behind replication forks.
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(1998)
Cell
, vol.94
, pp. 819-827
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Peter, B.1
Ullsperger, C.2
Hiasa, H.3
Marians, K.4
Cozzarelli, N.5
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14
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0029991326
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DNA gyrase and topoisomerase IV on the bacterial chromosome: Quinolone-induced DNA cleavage
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Chen C-R, Malik M, Snyder M, Drlica K DNA gyrase and topoisomerase IV on the bacterial chromosome: quinolone-induced DNA cleavage. J Mol Biol. 258:1996;627-637.
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(1996)
J Mol Biol
, vol.258
, pp. 627-637
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Chen, C.-R.1
Malik, M.2
Snyder, M.3
Drlica, K.4
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15
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0342377454
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Bipolar localization of Bacillus subtilis topoisomerase IV, an enzyme required for chromosome segregation
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Fluorescence microscopy is used to show that topoisomerase IV is localized to specific cellular regions
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Huang WM, Libbey J, VanderHoeven P, Yu SX Bipolar localization of Bacillus subtilis topoisomerase IV, an enzyme required for chromosome segregation. Proc Natl Acad Sci USA. 95:1998;4652-4657. Fluorescence microscopy is used to show that topoisomerase IV is localized to specific cellular regions.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 4652-4657
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Huang, W.M.1
Libbey, J.2
Vanderhoeven, P.3
Yu, S.X.4
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16
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0343240577
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Chromosomes in living Escherichia coli cells are segregated into domains of supercoiling
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Sinden RR, Pettijohn DE Chromosomes in living Escherichia coli cells are segregated into domains of supercoiling. Proc Natl Acad Sci USA. 78:1981;224-228.
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Proc Natl Acad Sci USA
, vol.78
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Sinden, R.R.1
Pettijohn, D.E.2
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17
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0031712188
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Gyrase and topo IV modulate chromosome domain size in vivo
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Chromosome barriers to DNA slithering and branch migration were detected by failure of recombination between widely spaced res sites of γδ. Mutations in gyrase and topoisomerase IV increase the barriers
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Staczek P, Higgins NP Gyrase and topo IV modulate chromosome domain size in vivo. Mol Microbiol. 29:1998;1435-1448. Chromosome barriers to DNA slithering and branch migration were detected by failure of recombination between widely spaced res sites of γδ. Mutations in gyrase and topoisomerase IV increase the barriers.
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(1998)
Mol Microbiol
, vol.29
, pp. 1435-1448
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Staczek, P.1
Higgins, N.P.2
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18
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0021966486
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Localization of topoisomerase II in mitotic chromosomes
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Earnshaw WC, Heck MMS Localization of topoisomerase II in mitotic chromosomes. J Cell Biol. 100:1985;1716-1725.
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(1985)
J Cell Biol
, vol.100
, pp. 1716-1725
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Earnshaw, W.C.1
Heck, M.M.S.2
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19
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0021958085
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Topoisomerase II is a structural component of mitotic chromosome scaffolds
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Earnshaw WC, Halligan B, Cooke CA, Heck MMS, Liu LF Topoisomerase II is a structural component of mitotic chromosome scaffolds. J Cell Biol. 100:1985;1706-1715.
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(1985)
J Cell Biol
, vol.100
, pp. 1706-1715
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Earnshaw, W.C.1
Halligan, B.2
Cooke, C.A.3
Heck, M.M.S.4
Liu, L.F.5
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20
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0033582466
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In vitro evolution of preferred topoisomerase II DNA cleavage sites
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Nucleotide sequences likely to be preferred topoisomerase II cleavage sites were identified. This paper may guide similar studies with bacterial type II topoisomerases
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Burden DA, Osheroff N In vitro evolution of preferred topoisomerase II DNA cleavage sites. J Biol Chem. 274:1999;5227-5235. Nucleotide sequences likely to be preferred topoisomerase II cleavage sites were identified. This paper may guide similar studies with bacterial type II topoisomerases.
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(1999)
J Biol Chem
, vol.274
, pp. 5227-5235
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Burden, D.A.1
Osheroff, N.2
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21
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0029859964
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DNA strand cleavage is required for replication fork arrest by a frozen topoisomerase-quinolone-DNA ternary complex
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Hiasa H, Yousef D, Marians K DNA strand cleavage is required for replication fork arrest by a frozen topoisomerase-quinolone-DNA ternary complex. J Biol Chem. 271:1996;26424-26429.
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J Biol Chem
, vol.271
, pp. 26424-26429
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Hiasa, H.1
Yousef, D.2
Marians, K.3
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22
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0024420685
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Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptothecin
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Hsiang YH, Lihou MG, Liu LF Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptothecin. Cancer Res. 49:1989;5077-5082.
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Hsiang, Y.H.1
Lihou, M.G.2
Liu, L.F.3
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23
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0001369472
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Mechanism of action of nalidixic acid on Escherichia coli. II. Inhibition of deoxyribonucleic acid synthesis
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Goss W, Deitz W, Cook T Mechanism of action of nalidixic acid on Escherichia coli. II. Inhibition of deoxyribonucleic acid synthesis. J Bacteriol. 89:1965;1068-1074.
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Goss, W.1
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Cook, T.3
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24
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0013867055
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Mechanism of action of nalidixic acid on Escherichia coli. III. Conditions required for lethality
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Deitz WH, Cook TM, Goss WA Mechanism of action of nalidixic acid on Escherichia coli. III. Conditions required for lethality. J Bacteriol. 91:1966;768-773.
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J Bacteriol
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Deitz, W.H.1
Cook, T.M.2
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25
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0031459911
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DNA topoisomerase targets of the fluoroquinolones: A strategy for avoiding bacterial resistance
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Zhao X, Xu C, Domagala J, Drlica K DNA topoisomerase targets of the fluoroquinolones: a strategy for avoiding bacterial resistance. Proc Natl Acad Sci USA. 94:1997;13991-13996.
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(1997)
Proc Natl Acad Sci USA
, vol.94
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Zhao, X.1
Xu, C.2
Domagala, J.3
Drlica, K.4
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27
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0027524110
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A single point mutation in the DNA gyrase A protein greatly reduces binding of fluoroquinolones to the gyrase-DNA complex
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Willmott CJ, Maxwell A A single point mutation in the DNA gyrase A protein greatly reduces binding of fluoroquinolones to the gyrase-DNA complex. Antimicrob Agents Chemother. 37:1993;126-127.
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Antimicrob Agents Chemother
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Willmott, C.J.1
Maxwell, A.2
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28
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0022509231
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Effects of DNA gyrase inhibitors in Escherichia coli topoisomerase I mutants
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Pruss G, Franco R, Chevalier S, Manes S, Drlica K Effects of DNA gyrase inhibitors in Escherichia coli topoisomerase I mutants. J Bacteriol. 168:1986;276-282.
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(1986)
J Bacteriol
, vol.168
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Pruss, G.1
Franco, R.2
Chevalier, S.3
Manes, S.4
Drlica, K.5
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29
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0000301456
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Crystal structure of the breakage-reunion domain of DNA gyrase
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Morais Cabral JHM, Jackson AP, Smith CV, Shikotra N, Maxwell A, Liddington RC Crystal structure of the breakage-reunion domain of DNA gyrase. Nature. 388:1997;903-906.
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Nature
, vol.388
, pp. 903-906
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Morais Cabral, J.H.M.1
Jackson, A.P.2
Smith, C.V.3
Shikotra, N.4
Maxwell, A.5
Liddington, R.C.6
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30
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0032803964
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Effect of fluoroquinolone concentration on selection of resistant mutants of Mycobacterium bovis BCG and Staphylococcus aureus
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A complex relationship between quinolone concentration and recovery of resistant mutants is described that allows fluoroquinolones of different structure to be compared. Introduced is mutant prevention concentration (MPC), a concept that can help prevent the selection of resistance during antibiotic therapy
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Dong Y, Zhao X, Domagala J, Drlica K Effect of fluoroquinolone concentration on selection of resistant mutants of Mycobacterium bovis BCG and Staphylococcus aureus. Antimicrob Agents Chemother. 43:1999;1756-1758. A complex relationship between quinolone concentration and recovery of resistant mutants is described that allows fluoroquinolones of different structure to be compared. Introduced is mutant prevention concentration (MPC), a concept that can help prevent the selection of resistance during antibiotic therapy.
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(1999)
Antimicrob Agents Chemother
, vol.43
, pp. 1756-1758
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Dong, Y.1
Zhao, X.2
Domagala, J.3
Drlica, K.4
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