메뉴 건너뛰기




Volumn 31, Issue 18, 2003, Pages 5305-5316

Erratum: Functional dissection of the C-terminal domain of type II DNA topoisomerase from the kinetoplastid hemoflagellate Leishmania donovani (Nucleic Acids Research (2003) 31 (5305-5316) DOI: 10.1093/nar/gkg727);Functional dissection of the C-terminal domain of type II DNA topoisomerase from the kinetoplastid hemoflagellate Leishmania donovani

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTIINFECTIVE AGENT; ANTILEISHMANIAL AGENT; ANTINEOPLASTIC AGENT; ANTIPARASITIC AGENT; ANTIVIRUS AGENT; DNA TOPOISOMERASE (ATP HYDROLYSING); GYRASE INHIBITOR; KINETOPLAST DNA; PROTOZOAL PROTEIN;

EID: 0344875212     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkab171     Document Type: Erratum
Times cited : (26)

References (58)
  • 1
    • 0024592815 scopus 로고
    • Biochemical basis for interaction of type I and type II topoisomerases with DNA
    • Osheroff, N. (1989) Biochemical basis for interaction of type I and type II topoisomerases with DNA. Pharmacol. Ther., 41, 223-241.
    • (1989) Pharmacol. Ther. , vol.41 , pp. 223-241
    • Osheroff, N.1
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • Wang, J.C (2002) Cellular roles of DNA topoisomerases: a molecular perspective. Nature Rev. Mol. Cell. Biol., 3, 430-40.
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 5
    • 0025273205 scopus 로고
    • Segregation of recombined chromosomes in meiosis I requires DNA topoisomerase II
    • Rose, D., Thomas, W. and Holm, C. (1990) Segregation of recombined chromosomes in meiosis I requires DNA topoisomerase II. Cell, 60, 1009-1017.
    • (1990) Cell , vol.60 , pp. 1009-1017
    • Rose, D.1    Thomas, W.2    Holm, C.3
  • 7
    • 0024826968 scopus 로고
    • Preferential, cooperative binding of DNA topoisomerase II to scaffold-associated regions
    • Adachi, Y., Luke, M. and Laemmli, U.K. (1989) Preferential, cooperative binding of DNA topoisomerase II to scaffold-associated regions. EMBO J., 8, 3997-4006.
    • (1989) EMBO J. , vol.8 , pp. 3997-4006
    • Adachi, Y.1    Luke, M.2    Laemmli, U.K.3
  • 8
    • 0025966711 scopus 로고
    • Chromosome assembly in vitro: Topoisomerase II is required for condensation
    • Adachi, Y., Luke, M. and Laemmli, U.K. (1991) Chromosome assembly in vitro: topoisomerase II is required for condensation. Cell, 64, 137-148.
    • (1991) Cell , vol.64 , pp. 137-148
    • Adachi, Y.1    Luke, M.2    Laemmli, U.K.3
  • 9
    • 0018731640 scopus 로고
    • T4 DNA topoisomerase: A new ATP-dependent enzyme essential for initiation of T4 bacteriophage DNA replication
    • Liu, L.F., Liu, C.C. and Alberts, B.M. (1979) T4 DNA topoisomerase: a new ATP-dependent enzyme essential for initiation of T4 bacteriophage DNA replication. Nature, 281, 456-461.
    • (1979) Nature , vol.281 , pp. 456-461
    • Liu, L.F.1    Liu, C.C.2    Alberts, B.M.3
  • 10
  • 11
    • 0026441120 scopus 로고
    • Isolation of cDNA clones encoding the beta isozyme of human DNA topoisomerase II and localisation of the gene to chromosome 3p24
    • Jenkins, J.R., Ayton, P., Jones, T., Davies, S.L., Simmons, D.L., Harris, A.L., Sherr, D. and Hixon, I.D. (1992) Isolation of cDNA clones encoding the beta isozyme of human DNA topoisomerase II and localisation of the gene to chromosome 3p24. Nucleic Acids Res., 20, 5587-5592.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5587-5592
    • Jenkins, J.R.1    Ayton, P.2    Jones, T.3    Davies, S.L.4    Simmons, D.L.5    Harris, A.L.6    Sherr, D.7    Hixon, I.D.8
  • 12
    • 0030045003 scopus 로고    scopus 로고
    • Structure and mechanism of DNA topoisomerase II
    • Berger, J.M., Gramblin, 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    Gramblin, S.J.2    Harrison, S.C.3    Wang, J.C.4
  • 13
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus?
    • Dingwall, C. and Laskey, R.A. (1991) Nuclear targeting sequences - a consensus? Trends Biochem. Sci., 16, 478-481.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 14
    • 0028114974 scopus 로고
    • Serine 1524 is a major site of phosphorylation on human topoisomerase II alpha protein in vivo and is a substrate for casein kinase II in vitro
    • Wells, N.J., Addison, C.N., Fry, A.M., Ganapathi, R. and Hixon, I.D. (1994) Serine 1524 is a major site of phosphorylation on human topoisomerase II alpha protein in vivo and is a substrate for casein kinase II in vitro. J. Biol. Chem., 269, 29746-29751.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29746-29751
    • Wells, N.J.1    Addison, C.N.2    Fry, A.M.3    Ganapathi, R.4    Hixon, I.D.5
  • 16
    • 0033543661 scopus 로고    scopus 로고
    • Using a biochemical approach to identify the primary dimerisation regions in human DNA topoisomerase II alpha
    • Bjergbaek, L., Jensen, S., Westergaard, O. and Andersen, A.H. (1999) Using a biochemical approach to identify the primary dimerisation regions in human DNA topoisomerase II alpha. J. Biol. Chem., 274, 26529-26536.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26529-26536
    • Bjergbaek, L.1    Jensen, S.2    Westergaard, O.3    Andersen, A.H.4
  • 17
    • 0029072779 scopus 로고
    • Expression, domain structure and enzymatic properties of an active recombinant human DNA topoisomerse II β
    • Austin, C.A., Marsh, K.L. Wasserman, R.A., Willmore, E., Sayer, P.J., Wang, J.C. and Fisher, M.L. (1995). Expression, domain structure and enzymatic properties of an active recombinant human DNA topoisomerse II β. J. Biol. Chem., 270, 15739-15746.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15739-15746
    • Austin, C.A.1    Marsh, K.L.2    Wasserman, R.A.3    Willmore, E.4    Sayer, P.J.5    Wang, J.C.6    Fisher, M.L.7
  • 18
    • 0028137895 scopus 로고
    • Linker insertion mutagenesis of Drosophila topoisomerase II. Probing the structure of eukaryotic topoisomerase II
    • Lee, M.P. and Hsieh, T.S. (1994) Linker insertion mutagenesis of Drosophila topoisomerase II. Probing the structure of eukaryotic topoisomerase II. J. Mol. Biol., 235, 436-447.
    • (1994) J. Mol. Biol. , vol.235 , pp. 436-447
    • Lee, M.P.1    Hsieh, T.S.2
  • 19
    • 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
  • 20
    • 0025838305 scopus 로고
    • Proteolysis patterns of epitopically labeled yeast topoisomerase II suggest an allosteric transition in the enzyme induced by ATP binding
    • Lindsley, J.E. and Wang, J.C. (1991) Proteolysis patterns of epitopically labeled yeast topoisomerase II suggest an allosteric transition in the enzyme induced by ATP binding. Proc. Natl Acad. Sci. USA, 88, 10485-10489.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10485-10489
    • Lindsley, J.E.1    Wang, J.C.2
  • 21
    • 0025758726 scopus 로고
    • The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein
    • Reece, R.J. and Maxwell, A. (1991) The C-terminal domain of the Escherichia coli DNA gyrase A subunit is a DNA-binding protein. Nucleic Acids Res., 19, 1399-1405.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1399-1405
    • Reece, R.J.1    Maxwell, A.2
  • 22
    • 0026448670 scopus 로고
    • The capture of a DNA double helix by an ATP-dependent protein clamp: A key step in DNA transport by type II DNA topoisomerases
    • Roca, J. and Wang, J.C. (1992) The capture of a DNA double helix by an ATP-dependent protein clamp: a key step in DNA transport by type II DNA topoisomerases. Cell, 71, 833-840.
    • (1992) Cell , vol.71 , pp. 833-840
    • Roca, J.1    Wang, J.C.2
  • 23
    • 0037226127 scopus 로고    scopus 로고
    • Protozomics: Trypanosomatid parasite genetics comes of age
    • Beverly, S.M. (2003) Protozomics: trypanosomatid parasite genetics comes of age. Nature Rev. Gen., 4, 11-19.
    • (2003) Nature Rev. Gen. , vol.4 , pp. 11-19
    • Beverly, S.M.1
  • 24
    • 0025174166 scopus 로고
    • The TOP2 gene of Trypanosoma brucei: A single copy gene that shares extensive homology with other TOP2 genes encoding eukaryotic DNA topoisomerase II
    • Strauss, P.R. and Wang, J.C. (1990) The TOP2 gene of Trypanosoma brucei: a single copy gene that shares extensive homology with other TOP2 genes encoding eukaryotic DNA topoisomerase II. Mol. Biochem. Parasitol., 38, 141-150.
    • (1990) Mol. Biochem. Parasitol. , vol.38 , pp. 141-150
    • Strauss, P.R.1    Wang, J.C.2
  • 25
    • 0026757877 scopus 로고
    • Cloning and characterisation of the gene encoding Trypanosoma cruzi DNA topoisomerase II
    • Fragosso, S.P. and Goldenberg, S. (1992) Cloning and characterisation of the gene encoding Trypanosoma cruzi DNA topoisomerase II. Mol. Biochem. Parasitol., 55, 127-135.
    • (1992) Mol. Biochem. Parasitol. , vol.55 , pp. 127-135
    • Fragosso, S.P.1    Goldenberg, S.2
  • 26
    • 0026595197 scopus 로고
    • Molecular cloning and expression of the gene encoding the kinetoplast-associated type II DNA topoisomerase of Crithidia fasciculata
    • Pasion, S.G., Hines, J.C., Aebersold, R. and Ray, D.S. (1992) Molecular cloning and expression of the gene encoding the kinetoplast-associated type II DNA topoisomerase of Crithidia fasciculata. Mol. Biochem. Parasitol., 50, 57-68.
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 57-68
    • Pasion, S.G.1    Hines, J.C.2    Aebersold, R.3    Ray, D.S.4
  • 27
    • 0023505005 scopus 로고
    • Decatenation of kinetoplast DNA by an ATP-dependent DNA topoisomerase from the kinetoplast hemoflagellate Leishmania donovani
    • Chakraborty, A.K. and Majumder, H.K. (1987) Decatenation of kinetoplast DNA by an ATP-dependent DNA topoisomerase from the kinetoplast hemoflagellate Leishmania donovani. Mol. Biochem. Parasitol., 26, 215-224.
    • (1987) Mol. Biochem. Parasitol. , vol.26 , pp. 215-224
    • Chakraborty, A.K.1    Majumder, H.K.2
  • 28
    • 0025937195 scopus 로고
    • An ATP independent catenating enzyme from the kinetoplast hemoflagellate Leishmania donovani
    • Chakraborty, A.K. and Majumder, H.K. (1991) An ATP independent catenating enzyme from the kinetoplast hemoflagellate Leishmania donovani. Biochem. Biophys. Res. Commun., 180, 279-285.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 279-285
    • Chakraborty, A.K.1    Majumder, H.K.2
  • 29
    • 0035339610 scopus 로고    scopus 로고
    • Characterisation of the gene encoding type II DNA topoisomerase from Leishmania donovani: A key molecular target in anti leishmanial therapy
    • Das, A., Dasgupta, A., Sharma, S., Ghosh, M., Sengupta, T., Bandopadhyay, S. and Majumder, H.K. (2001) Characterisation of the gene encoding type II DNA topoisomerase from Leishmania donovani: a key molecular target in anti leishmanial therapy. Nucleic Acids Res., 29, 1844-1851.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1844-1851
    • Das, A.1    Dasgupta, A.2    Sharma, S.3    Ghosh, M.4    Sengupta, T.5    Bandopadhyay, S.6    Majumder, H.K.7
  • 30
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991) Getting started with yeast. Methods Enzymol., 194, 3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 31
    • 0023275830 scopus 로고
    • A family of yeast expression vectors containing the phage f1 intergenic region
    • Vernet, T., Dignard, D. and Thomas, D.Y. (1987) A family of yeast expression vectors containing the phage f1 intergenic region. Gene, 52, 225-233.
    • (1987) Gene , vol.52 , pp. 225-233
    • Vernet, T.1    Dignard, D.2    Thomas, D.Y.3
  • 32
    • 0026599048 scopus 로고
    • One-step transformation of yeast in stationary phase
    • Chen, D.C., Yang, B.C. and Kuo, T.T. (1992) One-step transformation of yeast in stationary phase. Curr. Genet., 21, 83-84.
    • (1992) Curr. Genet. , vol.21 , pp. 83-84
    • Chen, D.C.1    Yang, B.C.2    Kuo, T.T.3
  • 33
    • 0034637574 scopus 로고    scopus 로고
    • Assignment of functional amino acids around the active site of human DNA topoisomerase II alpha
    • Okada, Y., Ito, Y., Kikuchi, A., Nimura, Y., Yoshida, S. and Suzuki, M. (2000) Assignment of functional amino acids around the active site of human DNA topoisomerase II alpha. J. Biol. Chem., 275, 24630-24638.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24630-24638
    • Okada, Y.1    Ito, Y.2    Kikuchi, A.3    Nimura, Y.4    Yoshida, S.5    Suzuki, M.6
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 37
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and Swiss Pdb Viewer: An environment for comparitive protein modeling
    • Guex, N. and Peitsch, M.C. (1997) SWISS-MODEL and Swiss Pdb Viewer: an environment for comparitive protein modeling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 39
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 29-32
    • Koradi, R., Billeter, M. and Wuthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph., 14, 51-55, 29-32.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-46809.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-46809
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 0026746446 scopus 로고
    • Characterisation of cDNA encoding the mouse DNA topoisomerase II that can complement the budding yeast top2 mutation
    • Adachi, N., Miyaike, M., Ikeda, H. and Kikuchi, A. (1992) Characterisation of cDNA encoding the mouse DNA topoisomerase II that can complement the budding yeast top2 mutation. Nucleic Acids Res., 20, 5297-5303.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5297-5303
    • Adachi, N.1    Miyaike, M.2    Ikeda, H.3    Kikuchi, A.4
  • 42
    • 0030747269 scopus 로고    scopus 로고
    • Cellular distribution of mammalian DNA topoisomerase II is determined by its catalytically dispensable C-terminal domain
    • Adachi, N., Miyaike, M., Kato, S., Kanamaru, R., Koyama, H. and Kikuchi, A. (1997) Cellular distribution of mammalian DNA topoisomerase II is determined by its catalytically dispensable C-terminal domain. Nucleic Acids Res., 25, 3135-3142.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3135-3142
    • Adachi, N.1    Miyaike, M.2    Kato, S.3    Kanamaru, R.4    Koyama, H.5    Kikuchi, A.6
  • 43
    • 0028678214 scopus 로고
    • Appendix II: Alignment of primary sequences of DNA topoisomerases
    • Caron, P.R. and Wang, J.C. (1994) Appendix II: alignment of primary sequences of DNA topoisomerases. Adv. Pharmacol., 29B, 271-297.
    • (1994) Adv. Pharmacol. , vol.29 B , pp. 271-297
    • Caron, P.R.1    Wang, J.C.2
  • 44
    • 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
  • 45
    • 0023681467 scopus 로고
    • Functional expression of a Drosophila gene in yeast: Genetic complementation of DNA topoisomerase II
    • Wyckoff, E. and Hsieh, T.S. (1988) Functional expression of a Drosophila gene in yeast: genetic complementation of DNA topoisomerase II. Proc. Natl Acad. Sci. USA, 85, 6272-6276.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6272-6276
    • Wyckoff, E.1    Hsieh, T.S.2
  • 46
    • 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
  • 47
    • 0029360551 scopus 로고
    • DNA topoisomerase II mutations and resistance to anti-tumor drugs
    • Vassetzky, Y.S., Alghisi, G.C. and Gasser, S.M. (1995) DNA topoisomerase II mutations and resistance to anti-tumor drugs. Bioessays, 17, 767-774.
    • (1995) Bioessays , vol.17 , pp. 767-774
    • Vassetzky, Y.S.1    Alghisi, G.C.2    Gasser, S.M.3
  • 48
    • 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.S. (1993) Function of the hydrophilic carboxyl terminus of type II DNA topoisomerase from Drosophila melanogaster. I. In vitro studies. J. Biol. Chem., 268, 21335-21343.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21335-21343
    • Crenshaw, D.G.1    Hsieh, T.S.2
  • 49
    • 0026607164 scopus 로고
    • Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase II in vivo
    • Cardenas, M.E., Dang, Q., Glover, C.V.C. and Gasser, S.M. (1992) Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase II in vivo. EMBO J., 11, 1785-1796.
    • (1992) EMBO J. , vol.11 , pp. 1785-1796
    • Cardenas, M.E.1    Dang, Q.2    Glover, C.V.C.3    Gasser, S.M.4
  • 50
    • 0034029541 scopus 로고    scopus 로고
    • During both interface and mitosis, DNA topoisomerase II interacts with DNA as well as RNA through the protein's C-terminal domain
    • Rzepecki, R. and Fisher, P.A. (2000) During both interface and mitosis, DNA topoisomerase II interacts with DNA as well as RNA through the protein's C-terminal domain. J. Cell Sci., 113, 1635-1647.
    • (2000) J. Cell Sci. , vol.113 , pp. 1635-1647
    • Rzepecki, R.1    Fisher, P.A.2
  • 51
    • 0026046957 scopus 로고
    • A functional 125-kDa polypeptide of fission yeast DNA topoisomerase II
    • Shiozaki, K. and Yanagida, M. (1991) A functional 125-kDa 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
  • 52
    • 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., 14, 3197-3207.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 3197-3207
    • Caron, P.R.1    Watt, P.2    Wang, J.C.3
  • 53
    • 0032488285 scopus 로고    scopus 로고
    • Trial of oral miltefosine for visceral leishmaniasis
    • Sunder, S. (1998) Trial of oral miltefosine for visceral leishmaniasis. Lancet, 352, 1821-1823.
    • (1998) Lancet , vol.352 , pp. 1821-1823
    • Sunder, S.1
  • 55
    • 0024533317 scopus 로고
    • Mechanism of quinolone inhibition of DNA gyrase. Appearance of unique norfloxacin binding sites in enzyme-DNA complexes
    • Shen, L.L., Kuhlbrenner, W.E., Weigl, D. and Baranowski, J. (1989) Mechanism of quinolone inhibition of DNA gyrase. Appearance of unique norfloxacin binding sites in enzyme-DNA complexes. J. Biol. Chem., 264, 2973-2978.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2973-2978
    • Shen, L.L.1    Kuhlbrenner, W.E.2    Weigl, D.3    Baranowski, J.4
  • 56
    • 0032977819 scopus 로고    scopus 로고
    • Mechanism of inhibition of a pox virus topoisomerase by the marine natural product Sansalvamide
    • Hwang, Y., Rowley, D., Rhodes, D., Gertsch, J., Fenical, W. and Bushman, F. (1999) Mechanism of inhibition of a pox virus topoisomerase by the marine natural product Sansalvamide. Mol. Pharmacol., 55, 1049-1053.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 1049-1053
    • Hwang, Y.1    Rowley, D.2    Rhodes, D.3    Gertsch, J.4    Fenical, W.5    Bushman, F.6
  • 57
    • 0034199017 scopus 로고    scopus 로고
    • Luteolin, an abundant dietary component is a potent antileishmanial agent that acts by inducing topoisomerase II-mediated kinetoplast DNA cleavage leading to apoptosis
    • Mittra, B., RoyChowdhury, A. and Majumder, H.K (2000) Luteolin, an abundant dietary component is a potent antileishmanial agent that acts by inducing topoisomerase II-mediated kinetoplast DNA cleavage leading to apoptosis. Mol. Med., 6, 527-541.
    • (2000) Mol. Med. , vol.6 , pp. 527-541
    • Mittra, B.1    RoyChowdhury, A.2    Majumder, H.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.