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Volumn 44, Issue 34, 2005, Pages 11546-11554

Impact of the C-terminal domain of topoisomerase IIα on the DNA cleavage activity of the human enzyme

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CELLS; DNA; DRUG THERAPY; HYDROPHILICITY; MUTAGENESIS; PHOSPHORESCENCE; TUMORS;

EID: 23944501757     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050811l     Document Type: Article
Times cited : (41)

References (55)
  • 1
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang, J. C. (1996) DNA topoisomerases, Annu. Rev. Biochem. 65, 635-692.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 635-692
    • Wang, J.C.1
  • 2
    • 0031695155 scopus 로고    scopus 로고
    • Moving one DNA double helix through another by a type II DNA topoisomerase: The story of a simple molecular machine
    • Wang, J. C. (1998) Moving one DNA double helix through another by a type II DNA topoisomerase: the story of a simple molecular machine, Q. Rev. Biophys. 31, 107-144.
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 107-144
    • Wang, J.C.1
  • 3
    • 0032190561 scopus 로고    scopus 로고
    • Mechanism of action of eukaryotic topoisomerase II and drugs targeted to the enzyme
    • Burden, D. A., and Osheroff, N. (1998) Mechanism of action of eukaryotic topoisomerase II and drugs targeted to the enzyme, Biochim. Biophys. Acta 1400, 139-154.
    • (1998) Biochim. Biophys. Acta , vol.1400 , pp. 139-154
    • Burden, D.A.1    Osheroff, N.2
  • 4
    • 0032189942 scopus 로고    scopus 로고
    • Investigating the biological functions of DNA topoisomerases in eukaryotic cells
    • Nitiss, J. L. (1998) Investigating the biological functions of DNA topoisomerases in eukaryotic cells, Biochim. Biophys. Acta 1400, 63-81.
    • (1998) Biochim. Biophys. Acta , vol.1400 , pp. 63-81
    • Nitiss, J.L.1
  • 5
    • 0033628701 scopus 로고    scopus 로고
    • Topoisomerase II as a target for anticancer drugs: When enzymes stop being nice
    • Fortune, J. M., and Osheroff, N. (2000) Topoisomerase II as a target for anticancer drugs: when enzymes stop being nice, Prog. Nucleic Acid Res. Mol. Biol. 64, 221-253.
    • (2000) Prog. Nucleic Acid Res. Mol. Biol. , vol.64 , pp. 221-253
    • Fortune, J.M.1    Osheroff, N.2
  • 6
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: Structure, function, and mechanism
    • Champoux, J. J. (2001) DNA topoisomerases: Structure, Function, and Mechanism, Annu. Rev. Biochem. 70, 369-413.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 7
    • 0037870269 scopus 로고    scopus 로고
    • Stabilization of eukaryotic topoisomerase II-DNA cleavage complexes
    • Wilstermann, A. M., and Osheroff, N. (2003) Stabilization of eukaryotic topoisomerase II-DNA cleavage complexes, Curr. Top. Med. Chem. 3, 321-338.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 321-338
    • Wilstermann, A.M.1    Osheroff, N.2
  • 9
    • 0024432691 scopus 로고
    • Biochemical and pharmacological properties of p170 and p180 forms of topoisomerase II
    • Drake, F. H., Hofmann, G. A., Bartus, H. F., Mattern, M. R., Crooke, S. T., and Mirabelli, C. K. (1989) Biochemical and pharmacological properties of p170 and p180 forms of topoisomerase II, Biochemistry 28, 8154-8160.
    • (1989) Biochemistry , vol.28 , pp. 8154-8160
    • Drake, F.H.1    Hofmann, G.A.2    Bartus, H.F.3    Mattern, M.R.4    Crooke, S.T.5    Mirabelli, C.K.6
  • 10
    • 0023927993 scopus 로고
    • Proliferation-dependent regulation of DNA topoisomerase II in cultured human cells
    • Hsiang, Y. H., Wu, H. Y., and Liu, L. F. (1988) Proliferation-dependent regulation of DNA topoisomerase II in cultured human cells, Cancer Res. 48, 3230-3235.
    • (1988) Cancer Res. , vol.48 , pp. 3230-3235
    • Hsiang, Y.H.1    Wu, H.Y.2    Liu, L.F.3
  • 12
    • 0032032797 scopus 로고    scopus 로고
    • Eukaryotic DNA topoisomerase IIβ
    • Austin, C. A., and Marsh, K. L. (1998) Eukaryotic DNA topoisomerase IIβ, BioEssays 20, 215-226.
    • (1998) BioEssays , vol.20 , pp. 215-226
    • Austin, C.A.1    Marsh, K.L.2
  • 13
    • 0026147704 scopus 로고
    • Proliferation- and cell cycle-dependent differences in expression of the 170 kilodalton and 180 kilodalton forms of topoisomerase II in NIH-3T3 cells
    • Woessner, R. D., Mattern, M. R., Mirabelli, C. K., Johnson, R. K., and Drake, F. H. (1991) Proliferation- and cell cycle-dependent differences in expression of the 170 kilodalton and 180 kilodalton forms of topoisomerase II in NIH-3T3 cells. Cell Growth Differ. 2, 209-214.
    • (1991) Cell Growth Differ. , vol.2 , pp. 209-214
    • Woessner, R.D.1    Mattern, M.R.2    Mirabelli, C.K.3    Johnson, R.K.4    Drake, F.H.5
  • 14
    • 0034614266 scopus 로고    scopus 로고
    • DNA topoisomerase IIb and neural development
    • Yang, X., Li, W., Prescott, E. D., Burden, S. J., and Wang, J. C. (2000) DNA topoisomerase IIb and neural development, Science 287, 131-134.
    • (2000) Science , vol.287 , pp. 131-134
    • Yang, X.1    Li, W.2    Prescott, E.D.3    Burden, S.J.4    Wang, J.C.5
  • 15
    • 0030045003 scopus 로고    scopus 로고
    • Structure and mechanism of DNA topoisomerase II
    • Berger, J. M., Gamblin, S. J., Harrison, S. C., and Wang, J. C. (1996) Structure and mechanism of DNA topoisomerase II, Nature 379, 225-232.
    • (1996) Nature , vol.379 , pp. 225-232
    • Berger, J.M.1    Gamblin, S.J.2    Harrison, S.C.3    Wang, J.C.4
  • 16
    • 0032189963 scopus 로고    scopus 로고
    • Mutagenic properties of topoisomerase-targeted drugs
    • Baguley, B. C., and Ferguson, L. R. (1998) Mutagenic properties of topoisomerase-targeted drugs, Biochim. Biophys. Acta 1400, 213-222.
    • (1998) Biochim. Biophys. Acta , vol.1400 , pp. 213-222
    • Baguley, B.C.1    Ferguson, L.R.2
  • 17
    • 0032189081 scopus 로고    scopus 로고
    • Secondary leukemias induced by topoisomerase-targeted drugs
    • Felix, C. A. (1998) Secondary leukemias induced by topoisomerase-targeted drugs, Biochim. Biophys. Acta 1400, 233-255.
    • (1998) Biochim. Biophys. Acta , vol.1400 , pp. 233-255
    • Felix, C.A.1
  • 18
    • 0032189262 scopus 로고    scopus 로고
    • Cell death induced by topoisomerase-targeted drugs: More questions than answers
    • Kaufmann, S. H. (1998) Cell death induced by topoisomerase-targeted drugs: more questions than answers, Biochim. Biophys. Acta 1400, 195-211.
    • (1998) Biochim. Biophys. Acta , vol.1400 , pp. 195-211
    • Kaufmann, S.H.1
  • 19
    • 0002291316 scopus 로고    scopus 로고
    • Topoisomerase II inhibitors: The epipodophyllotoxins, m-AMSA, and the ellipticine derivatives
    • (Chabner, B. A., and Longo, D. L., Eds.), Lippincott-Raven Publishers, Philadelphia
    • Pommier, Y., Fesen, M. R., and Goldwasser, F. (1996) Topoisomerase II inhibitors: the epipodophyllotoxins, m-AMSA, and the ellipticine derivatives, in Cancer Chemotherapy and Biotherapy: Principles and Practice (Chabner, B. A., and Longo, D. L., Eds.) pp 435-461, Lippincott-Raven Publishers, Philadelphia.
    • (1996) Cancer Chemotherapy and Biotherapy: Principles and Practice , pp. 435-461
    • Pommier, Y.1    Fesen, M.R.2    Goldwasser, F.3
  • 20
    • 0032190407 scopus 로고    scopus 로고
    • Clinical applications of anticancer drugs targeted to topoisomerase II
    • Hande, K. R. (1998) Clinical applications of anticancer drugs targeted to topoisomerase II, Biochim. Biophys. Acta 1400, 173-184.
    • (1998) Biochim. Biophys. Acta , vol.1400 , pp. 173-184
    • Hande, K.R.1
  • 21
    • 0032168167 scopus 로고    scopus 로고
    • Etoposide: Four decades of development of a topoisomerase II inhibitor
    • Hande, K. R. (1998) Etoposide: four decades of development of a topoisomerase II inhibitor, Eur. J. Cancer 34, 1514-1521.
    • (1998) Eur. J. Cancer , vol.34 , pp. 1514-1521
    • Hande, K.R.1
  • 22
    • 0032411481 scopus 로고    scopus 로고
    • The critical role of chromosome translocations in human leukemias
    • Rowley, J. D. (1998) The critical role of chromosome translocations in human leukemias, Annu. Rev. Genet. 32, 495-519.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 495-519
    • Rowley, J.D.1
  • 23
    • 0035056832 scopus 로고    scopus 로고
    • Leukemias related to treatment with DNA topoisomerase II inhibitors
    • Felix, C. A. (2001) Leukemias related to treatment with DNA topoisomerase II inhibitors, Med. Pediatr. Oncol. 36, 525-535.
    • (2001) Med. Pediatr. Oncol. , vol.36 , pp. 525-535
    • Felix, C.A.1
  • 24
    • 0037063170 scopus 로고    scopus 로고
    • MLL-SEPTIN6 fusion recurs in novel translocation of chromosomes 3, X, and 11 in infant acute myelomonocytic leukaemia and in t(X;11) in infant acute myeloid leukaemia, and MLL genomic breakpoint in complex MLL-SEPTIN6 rearrangement is a DNA topoisomerase II cleavage site
    • Slater, D. J., Hilgenfeld, E., Rappaport, E. F., Shah, N., Meek, R. G., Williams, W. R., Lovett, B. D., Osheroff, N., Autar, R. S., Ried, T., and Felix, C. A. (2002) MLL-SEPTIN6 fusion recurs in novel translocation of chromosomes 3, X, and 11 in infant acute myelomonocytic leukaemia and in t(X;11) in infant acute myeloid leukaemia, and MLL genomic breakpoint in complex MLL-SEPTIN6 rearrangement is a DNA topoisomerase II cleavage site, Oncogene 21, 4706-4714.
    • (2002) Oncogene , vol.21 , pp. 4706-4714
    • Slater, D.J.1    Hilgenfeld, E.2    Rappaport, E.F.3    Shah, N.4    Meek, R.G.5    Williams, W.R.6    Lovett, B.D.7    Osheroff, N.8    Autar, R.S.9    Ried, T.10    Felix, C.A.11
  • 27
    • 16844382731 scopus 로고    scopus 로고
    • Insights into leukemogenesis from therapy-related leukemia
    • Pedersen-Bjergaard, J. (2005) Insights into leukemogenesis from therapy-related leukemia, N. Engl. J. Med. 352, 1591-1594.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1591-1594
    • Pedersen-Bjergaard, J.1
  • 28
    • 0034629090 scopus 로고    scopus 로고
    • Topoisomerase II from chlorella virus PBCV-1. Characterization of the smallest known type II topoisomerase
    • Lavrukhin, O. V., Fortune, J. M., Wood, T. G., Burbank, D. E., Van Etten, J. L., Osheroff, N., and Lloyd, R. S. (2000) Topoisomerase II from chlorella virus PBCV-1. Characterization of the smallest known type II topoisomerase, J. Biol. Chem. 275, 6915-6921.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6915-6921
    • Lavrukhin, O.V.1    Fortune, J.M.2    Wood, T.G.3    Burbank, D.E.4    Van Etten, J.L.5    Osheroff, N.6    Lloyd, R.S.7
  • 29
    • 0035968227 scopus 로고    scopus 로고
    • Topoisomerase II from Chlorella virus PBCV-1 has an exceptionally high DNA cleavage activity
    • Fortune, J. M., Lavrukhin, O. V., Gurnon, J. R., Van Etten, J. L., Lloyd, R. S., and Osheroff, N. (2001) Topoisomerase II from Chlorella virus PBCV-1 has an exceptionally high DNA cleavage activity, J. Biol. Chem. 276, 24401-24408.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24401-24408
    • Fortune, J.M.1    Lavrukhin, O.V.2    Gurnon, J.R.3    Van Etten, J.L.4    Lloyd, R.S.5    Osheroff, N.6
  • 31
    • 14844359841 scopus 로고    scopus 로고
    • Chlorella virus Marburg topoisomerase II: High DNA cleavage activity as a characteristic of chlorella virus type II enzymes
    • Dickey, J. S., Choi, T. J., Van Etten, J. L., and Osheroff, N. (2005) Chlorella virus Marburg topoisomerase II: high DNA cleavage activity as a characteristic of chlorella virus type II enzymes, Biochemistry 44, 3899-3908.
    • (2005) Biochemistry , vol.44 , pp. 3899-3908
    • Dickey, J.S.1    Choi, T.J.2    Van Etten, J.L.3    Osheroff, N.4
  • 32
    • 0031574263 scopus 로고    scopus 로고
    • Bipartite nuclear localization signals in the C terminus of human topoisomerase IIα
    • Mirski, S. E., Gerlach, J. H., Cummings, H. J., Zirngibl, R., Greer, P. A., and Cole, S. P. (1997) Bipartite nuclear localization signals in the C terminus of human topoisomerase IIα, Exp. Cell Res. 237, 452-455.
    • (1997) Exp. Cell Res. , vol.237 , pp. 452-455
    • Mirski, S.E.1    Gerlach, J.H.2    Cummings, H.J.3    Zirngibl, R.4    Greer, P.A.5    Cole, S.P.6
  • 34
    • 2442611949 scopus 로고    scopus 로고
    • The C-terminal domain of DNA gyrase A adopts a DNA-bending beta-pinwheel fold
    • Corbett, K. D., Shultzaberger, R. K., and Berger, J. M. (2004) The C-terminal domain of DNA gyrase A adopts a DNA-bending beta-pinwheel fold, Proc. Natl. Acad. Sci. U.S.A. 101, 7293-7298.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7293-7298
    • Corbett, K.D.1    Shultzaberger, R.K.2    Berger, J.M.3
  • 35
    • 0037093648 scopus 로고    scopus 로고
    • C-terminal domain of gyrase A is predicted to have a beta-propeller structure
    • Qi, Y., Pei, J., and Grishin, N. V. (2002) C-terminal domain of gyrase A is predicted to have a beta-propeller structure, Proteins 47, 258-264.
    • (2002) Proteins , vol.47 , pp. 258-264
    • Qi, Y.1    Pei, J.2    Grishin, N.V.3
  • 36
    • 7444230947 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of ParC protein from Bacillus stearothermophilus
    • Hsieh, T. J., and Chan, N. L. (2004) Crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of ParC protein from Bacillus stearothermophilus, Acta Crystallogr., Sect. D: Biol. Crystallogr. 60, 564-566.
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 564-566
    • Hsieh, T.J.1    Chan, N.L.2
  • 37
    • 11244308067 scopus 로고    scopus 로고
    • Structure of the topoisomerase IV C-terminal domain: A broken beta-propeller implies a role as geometry facilitator in catalysis
    • Hsieh, T. J., Farh, L., Huang, W. M., and Chan, N. L. (2004) Structure of the topoisomerase IV C-terminal domain: a broken beta-propeller implies a role as geometry facilitator in catalysis, J. Biol. Chem. 279, 55587-55593.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55587-55593
    • Hsieh, T.J.1    Farh, L.2    Huang, W.M.3    Chan, N.L.4
  • 38
    • 0026046957 scopus 로고
    • A functional 125-kDa core polypeptide of fission yeast DNA topoisomerase II
    • Shiozaki, K., and Yanagida, M. (1991) A functional 125-kDa core polypeptide of fission yeast DNA topoisomerase II, Mol. Cell. Biol. 11, 6093-6102.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6093-6102
    • Shiozaki, K.1    Yanagida, M.2
  • 39
    • 0027454490 scopus 로고
    • Function of the hydrophilic carboxyl terminus of type II DNA topoisomerase from Drosophila melanogaster. I. In vitro studies
    • Crenshaw, D. G., and Hsieh, T. (1993) Function of the hydrophilic carboxyl terminus of type II DNA topoisomerase from Drosophila melanogaster. I. In vitro studies, J. Biol. Chem. 268, 21328-21334.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21328-21334
    • Crenshaw, D.G.1    Hsieh, T.2
  • 40
    • 0027452353 scopus 로고
    • Function of the hydrophilic carboxyl terminus of type II DNA topoisomerase from Drosophila melanogasler. II. In vivo studies
    • Crenshaw, D. G., and Hsieh, T. (1993) Function of the hydrophilic carboxyl terminus of type II DNA topoisomerase from Drosophila melanogasler. II. In vivo studies, J. Biol. Chem. 268, 21335-21343.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21335-21343
    • Crenshaw, D.G.1    Hsieh, T.2
  • 41
    • 0028345885 scopus 로고
    • The C-terminal domain of Saccharomyces cerevisiae DNA topoisomerase II
    • Caron, P. R., Watt, P., and Wang, J. C. (1994) The C-terminal domain of Saccharomyces cerevisiae DNA topoisomerase II, Mol. Cell. Biol., 3197-3207.
    • (1994) Mol. Cell. Biol. , pp. 3197-3207
    • Caron, P.R.1    Watt, P.2    Wang, J.C.3
  • 42
    • 0017867183 scopus 로고
    • The replication of kinetoplast DNA networks in Crithidia fasciculata
    • Englund, P. T. (1978) The replication of kinetoplast DNA networks in Crithidia fasciculata, Cell 14, 157-168.
    • (1978) Cell , vol.14 , pp. 157-168
    • Englund, P.T.1
  • 43
    • 0027275284 scopus 로고
    • Use of yeast in the study of anticancer drugs targeting DNA topoisomerases: Expression of a functional recombinant human DNA topoisomerase II alpha in yeast
    • Wasserman, R. A., Austin, C. A., Fisher, L. M., and Wang, J. C. (1993) Use of yeast in the study of anticancer drugs targeting DNA topoisomerases: expression of a functional recombinant human DNA topoisomerase II alpha in yeast, Cancer Res. 53, 3591-3596.
    • (1993) Cancer Res. , vol.53 , pp. 3591-3596
    • Wasserman, R.A.1    Austin, C.A.2    Fisher, L.M.3    Wang, J.C.4
  • 44
    • 0030958484 scopus 로고    scopus 로고
    • Spontaneous DNA lesions poison human topoisomerase IIα and stimulate cleavage proximal to leukemic 11q23 chromosomal breakpoints
    • Kingma, P. S., Greider, C. A., and Osheroff, N. (1997) Spontaneous DNA lesions poison human topoisomerase IIα and stimulate cleavage proximal to leukemic 11q23 chromosomal breakpoints, Biochemistry 36, 5934-5939.
    • (1997) Biochemistry , vol.36 , pp. 5934-5939
    • Kingma, P.S.1    Greider, C.A.2    Osheroff, N.3
  • 45
    • 0019877297 scopus 로고
    • A homogeneous type II DNA topoisomerase from HeLa cell nuclei
    • Miller, K. G., Liu, L. F., and Englund, P. T. (1981) A homogeneous type II DNA topoisomerase from HeLa cell nuclei, J. Biol. Chem. 256, 9334-9339.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9334-9339
    • Miller, K.G.1    Liu, L.F.2    Englund, P.T.3
  • 46
    • 0032504157 scopus 로고    scopus 로고
    • Merbarone inhibits the catalytic activity of human topoisomerase IIα by blocking DNA cleavage
    • Fortune, J. M., and Osheroff, N. (1998) Merbarone inhibits the catalytic activity of human topoisomerase IIα by blocking DNA cleavage, J. Biol. Chem. 273, 17643-17650.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17643-17650
    • Fortune, J.M.1    Osheroff, N.2
  • 47
    • 1642494897 scopus 로고    scopus 로고
    • Cobalt enhances DNA cleavage mediated by human topoisomerase II alpha in vitro and in cultured cells
    • Baldwin, E. L., Byl, J. A., and Osheroff, N. (2004) Cobalt enhances DNA cleavage mediated by human topoisomerase II alpha in vitro and in cultured cells. Biochemistry 43, 728-735.
    • (2004) Biochemistry , vol.43 , pp. 728-735
    • Baldwin, E.L.1    Byl, J.A.2    Osheroff, N.3
  • 48
    • 0037172804 scopus 로고    scopus 로고
    • A unique type II topoisomerase mutant that is hypersensitive to a broad range of cleavage-inducing antitumor agents
    • O'Reilly, E. K., and Kreuzer, K. N. (2002) A unique type II topoisomerase mutant that is hypersensitive to a broad range of cleavage-inducing antitumor agents, Biochemistry 41, 7989-7997.
    • (2002) Biochemistry , vol.41 , pp. 7989-7997
    • O'Reilly, E.K.1    Kreuzer, K.N.2
  • 49
    • 0025305782 scopus 로고
    • Stabilization of the topoisomerase II-DNA cleavage complex by antineoplastic drugs: Inhibition of enzyme-mediated DNA religation by 4′-(9-acridinylamino)methanesulfon-m-anisidide
    • Robinson, M. J., and Osheroff, N. (1990) Stabilization of the topoisomerase II-DNA cleavage complex by antineoplastic drugs: inhibition of enzyme-mediated DNA religation by 4′-(9-acridinylamino)methanesulfon-m- anisidide, Biochemistry 29, 2511-2515.
    • (1990) Biochemistry , vol.29 , pp. 2511-2515
    • Robinson, M.J.1    Osheroff, N.2
  • 50
    • 18544393471 scopus 로고    scopus 로고
    • Binding of etoposide to topoisomerase II in the absence of DNA: Decreased affinity as a mechanism of drug resistance
    • Kingma, P. S., Burden, D. A., and Osheroff, N. (1999) Binding of etoposide to topoisomerase II in the absence of DNA: decreased affinity as a mechanism of drug resistance, Biochemistry 38, 3457-3461.
    • (1999) Biochemistry , vol.38 , pp. 3457-3461
    • Kingma, P.S.1    Burden, D.A.2    Osheroff, N.3
  • 51
    • 0024395605 scopus 로고
    • Effect of antineoplastic agents on the DNA cleavage/religation reaction of eukaryotic topoisomerase II: Inhibition of DNA religation by etoposide
    • Osheroff, N. (1989) Effect of antineoplastic agents on the DNA cleavage/religation reaction of eukaryotic topoisomerase II: inhibition of DNA religation by etoposide, Biochemistry 28, 6157-6160.
    • (1989) Biochemistry , vol.28 , pp. 6157-6160
    • Osheroff, N.1
  • 52
    • 6344226531 scopus 로고    scopus 로고
    • DNA ligation catalyzed by human topoisomerase II alpha
    • Bromberg, K. D., Velez-Cruz, R., Burgin, A. B., and Osheroff, N. (2004) DNA ligation catalyzed by human topoisomerase II alpha, Biochemistry 43, 13416-13423.
    • (2004) Biochemistry , vol.43 , pp. 13416-13423
    • Bromberg, K.D.1    Velez-Cruz, R.2    Burgin, A.B.3    Osheroff, N.4
  • 53
    • 0024398661 scopus 로고
    • Tryptic fragments of the Escherichia coli DNA gyrase A protein
    • Reece, R. J., and Maxwell, A. (1989) Tryptic fragments of the Escherichia coli DNA gyrase A protein, J. Biol. Chem. 264, 19648-19653.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19648-19653
    • Reece, R.J.1    Maxwell, A.2
  • 54
    • 0344875212 scopus 로고    scopus 로고
    • Functional dissection of the C-terminal domain of type II DNA topoisomerase from the kinetoplastid hemoflagellate Leishmania donovani
    • Sengupta, T., Mukherjee, M., Mandal, C., Das, A., and Majumder, H. K. (2003) Functional dissection of the C-terminal domain of type II DNA topoisomerase from the kinetoplastid hemoflagellate Leishmania donovani, Nucleic Acids Res. 31, 5305-5316.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5305-5316
    • Sengupta, T.1    Mukherjee, M.2    Mandal, C.3    Das, A.4    Majumder, H.K.5
  • 55
    • 0034988263 scopus 로고    scopus 로고
    • Co-localization of chicken DNA topoisomerase IIalpha, but not beta, with sites of DNA replication and possible involvement of a C-terminal region of alpha through its binding to PCNA
    • Niimi, A., Suka, N., Harata, M., Kikuchi, A., and Mizuno, S. (2001) Co-localization of chicken DNA topoisomerase IIalpha, but not beta, with sites of DNA replication and possible involvement of a C-terminal region of alpha through its binding to PCNA, Chromosoma 110, 102-114.
    • (2001) Chromosoma , vol.110 , pp. 102-114
    • Niimi, A.1    Suka, N.2    Harata, M.3    Kikuchi, A.4    Mizuno, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.