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Volumn 56, Issue 15, 2008, Pages 6267-6277

Identification and characterization of topoisomerase II inhibitory peptides from soy protein hydrolysates

Author keywords

Dietary inhibitors; Molecular docking; Soy peptides; Topoisomerase II

Indexed keywords

DNA TOPOISOMERASE (ATP HYDROLYSING); ENZYME INHIBITOR; PANCREATIN; PEPSIN A; PEPTIDE; SOYBEAN PROTEIN;

EID: 50449084334     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf8005195     Document Type: Article
Times cited : (16)

References (50)
  • 1
    • 0000514613 scopus 로고    scopus 로고
    • Soybean seed composition
    • Verma, D. P. S, Shoemaker, R. C. Eds, CAB International: Wallingford, U.K
    • Nielsen, N. C. Soybean seed composition. In Soybean: Genetics, Molecular Biology and Biotechnology; Verma, D. P. S., Shoemaker, R. C. Eds.; CAB International: Wallingford, U.K., 1996; pp 127-163.
    • (1996) Soybean: Genetics, Molecular Biology and Biotechnology , pp. 127-163
    • Nielsen, N.C.1
  • 2
    • 0038397146 scopus 로고    scopus 로고
    • Food-derived bioactive peptides-opportunities for designing future foods
    • Korhonen, H.; Pihlanto, A. Food-derived bioactive peptides-opportunities for designing future foods. Curr. Pharm. Des. 2003, 9, 1297-1308.
    • (2003) Curr. Pharm. Des , vol.9 , pp. 1297-1308
    • Korhonen, H.1    Pihlanto, A.2
  • 3
    • 33748747614 scopus 로고    scopus 로고
    • A new frontier in soy bioactive peptides that may prevent age-related chronic diseases
    • Wang, W.; de Mejia, E. G. A new frontier in soy bioactive peptides that may prevent age-related chronic diseases. Compr. Rev. Food Sci. Food Saf. 2005, 4, 63-78.
    • (2005) Compr. Rev. Food Sci. Food Saf , vol.4 , pp. 63-78
    • Wang, W.1    de Mejia, E.G.2
  • 5
    • 0034705325 scopus 로고    scopus 로고
    • Peptide inhibitors of DNA cleavage by tyrosine recombinases and topoisomerases
    • Klemm, M.; Cheng, C.; Cassell, G.; Shuman, S.; Segall, A. M. Peptide inhibitors of DNA cleavage by tyrosine recombinases and topoisomerases. J. Mol. Biol. 2000, 299, 1203-1216.
    • (2000) J. Mol. Biol , vol.299 , pp. 1203-1216
    • Klemm, M.1    Cheng, C.2    Cassell, G.3    Shuman, S.4    Segall, A.M.5
  • 6
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • Wang, J. C. Cellular roles of DNA topoisomerases: a molecular perspective. Nat. Rev. Mol. Cell Biol. 2002, 3, 430-440.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 7
    • 0029842497 scopus 로고    scopus 로고
    • Method for quantifying expression of functionally active topoisomerase II in patients with leukaemia
    • Cattan, A.; Levett, D.; Douglas, E.; Middleton, P.; Taylor, P. Method for quantifying expression of functionally active topoisomerase II in patients with leukaemia. J. Clin. Pathol. 1996, 49, 848-852.
    • (1996) J. Clin. Pathol , vol.49 , pp. 848-852
    • Cattan, A.1    Levett, D.2    Douglas, E.3    Middleton, P.4    Taylor, P.5
  • 8
    • 15544391127 scopus 로고    scopus 로고
    • The cell cycle phases of DNA damage and repair initiated by topoisomerase II-targeting chemotherapeutic drugs
    • Potter, A. J.; Rabinovitch, P. S. The cell cycle phases of DNA damage and repair initiated by topoisomerase II-targeting chemotherapeutic drugs. Mutat. Res. 2005, 572, 27-44.
    • (2005) Mutat. Res , vol.572 , pp. 27-44
    • Potter, A.J.1    Rabinovitch, P.S.2
  • 9
    • 0041831131 scopus 로고    scopus 로고
    • Antitumor triptycene bisquinones: A novel synthetic class of dual inhibitors of DNA topoisomerase I and II activities
    • Wang, B.; Perchellet, E. M.; Wang, Y.; Tamura, M.; Hua, D. H.; Perchellet, J. H. Antitumor triptycene bisquinones: a novel synthetic class of dual inhibitors of DNA topoisomerase I and II activities. Anticancer Drugs 2003, 14, 503-514.
    • (2003) Anticancer Drugs , vol.14 , pp. 503-514
    • Wang, B.1    Perchellet, E.M.2    Wang, Y.3    Tamura, M.4    Hua, D.H.5    Perchellet, J.H.6
  • 10
    • 8344262388 scopus 로고    scopus 로고
    • AK37: The first pyridoacridine described capable of stabilizing the topoisomerase I cleavable complex
    • Marshall, K. M.; Holden, J. A.; Koller, A.; Kashman, Y.; Copp, B. R.; Barrows, L. R. AK37: the first pyridoacridine described capable of stabilizing the topoisomerase I cleavable complex. Anticancer Drugs 2004, 15, 907-913.
    • (2004) Anticancer Drugs , vol.15 , pp. 907-913
    • Marshall, K.M.1    Holden, J.A.2    Koller, A.3    Kashman, Y.4    Copp, B.R.5    Barrows, L.R.6
  • 12
    • 11144233212 scopus 로고    scopus 로고
    • Christmann-Franck, S.; Bertrand, H.; Goupil-Lamy, A.; derGarabedian, P. A.; Mauffret, O.; Hoffmann, R.; Fermandjian, S. Structure-based virtual screening: an application to human topoisomerase II. J. Med. Chem. 2004, 47, 6840-6853.
    • Christmann-Franck, S.; Bertrand, H.; Goupil-Lamy, A.; derGarabedian, P. A.; Mauffret, O.; Hoffmann, R.; Fermandjian, S. Structure-based virtual screening: an application to human topoisomerase II. J. Med. Chem. 2004, 47, 6840-6853.
  • 13
    • 34247627894 scopus 로고    scopus 로고
    • Single-molecule measurements of the opening and closing of the DNA gate by eukaryotic topoisomerase II
    • Smiley, R. D.; Collins, T. R. L.; Hammes, G. G.; Hsieh, T. Single-molecule measurements of the opening and closing of the DNA gate by eukaryotic topoisomerase II. Proc. Natl. Acad Sci. U.S.A. 2007, 104, 4840-4845.
    • (2007) Proc. Natl. Acad Sci. U.S.A , vol.104 , pp. 4840-4845
    • Smiley, R.D.1    Collins, T.R.L.2    Hammes, G.G.3    Hsieh, T.4
  • 14
    • 0022803528 scopus 로고
    • The DNA replication inhibitor microcin B17 is a forty-three-amino-acid protein containing sixty percent glycine
    • Davagnino, J.; Herrero, M.; Furlong, D.; Moreno, F.; Kolter, R. The DNA replication inhibitor microcin B17 is a forty-three-amino-acid protein containing sixty percent glycine. Proteins 1986, 1, 230-238.
    • (1986) Proteins , vol.1 , pp. 230-238
    • Davagnino, J.1    Herrero, M.2    Furlong, D.3    Moreno, F.4    Kolter, R.5
  • 15
    • 0025964113 scopus 로고
    • The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase
    • Vizan, J. L.; Hernandez-Chico, C.; del Castillo, I.; Moreno, F. The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase. EMBO J. 1991, 10, 467-476.
    • (1991) EMBO J , vol.10 , pp. 467-476
    • Vizan, J.L.1    Hernandez-Chico, C.2    del Castillo, I.3    Moreno, F.4
  • 17
    • 50449098531 scopus 로고    scopus 로고
    • Potent topoisomerase inhibition by synthetic cationic tetrapeptides constructed using unusual amino acids
    • Martin, L. M. Potent topoisomerase inhibition by synthetic cationic tetrapeptides constructed using unusual amino acids. Biopolymers 2003, 71, 398-398.
    • (2003) Biopolymers , vol.71 , pp. 398-398
    • Martin, L.M.1
  • 18
    • 33746531279 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max)
    • Gouda, K. G. M.; Gowda, L. R.; Rao, A. G. A.; Prakash, V. Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max). J. Agric. Food Chem. 2006, 54, 4568-4573.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 4568-4573
    • Gouda, K.G.M.1    Gowda, L.R.2    Rao, A.G.A.3    Prakash, V.4
  • 19
    • 34948841863 scopus 로고    scopus 로고
    • Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal
    • Yang, Y.; Tao, G.; Liu, P.; Liu, J. Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal. J. Agric. Food Chem. 2007, 55, 7891-7895.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 7891-7895
    • Yang, Y.1    Tao, G.2    Liu, P.3    Liu, J.4
  • 20
    • 35548970730 scopus 로고    scopus 로고
    • Antihypertensive effect of angiotensin I converting enzyme-inhibitory peptide from hydrolysates of bigeye tuna dark muscle Thunnus obesus
    • Qian, Z.; Je, J.; Kim, S. Antihypertensive effect of angiotensin I converting enzyme-inhibitory peptide from hydrolysates of bigeye tuna dark muscle Thunnus obesus. J. Agric. Food Chem. 2007, 55, 8398-8403.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 8398-8403
    • Qian, Z.1    Je, J.2    Kim, S.3
  • 21
    • 12144288141 scopus 로고    scopus 로고
    • Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates
    • Megias, C.; Yust, M. M.; Pedroche, J.; Lquari, H.; Giron-Calle, J.; Alaiz, M.; Millan, F.; Vioque, J. Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates. J. Agric. Food Chem. 2004, 52, 1928-1932.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 1928-1932
    • Megias, C.1    Yust, M.M.2    Pedroche, J.3    Lquari, H.4    Giron-Calle, J.5    Alaiz, M.6    Millan, F.7    Vioque, J.8
  • 22
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • Adler-Nissen, J. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agric. Food Chem. 1979, 27, 1256-1262.
    • (1979) J. Agric. Food Chem , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 23
    • 33746923472 scopus 로고    scopus 로고
    • Catalytic inhibition of human DNA topoisomerase by phenolic compounds in Ardisia compressa extracts and their effect on human colon cancer cells
    • Gonzalez de Mejía, E.; Chandra, S.; Ramírez-Mares, M.; Wang, W. Catalytic inhibition of human DNA topoisomerase by phenolic compounds in Ardisia compressa extracts and their effect on human colon cancer cells. Food Chem. Toxicol. 2006, 44, 1191-1203.
    • (2006) Food Chem. Toxicol , vol.44 , pp. 1191-1203
    • Gonzalez de Mejía, E.1    Chandra, S.2    Ramírez-Mares, M.3    Wang, W.4
  • 25
    • 0141591551 scopus 로고    scopus 로고
    • Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187
    • Classen, S.; Olland, S.; Berger, J. M. Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 10629-10634.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 10629-10634
    • Classen, S.1    Olland, S.2    Berger, J.M.3
  • 26
    • 0041784950 scopus 로고    scopus 로고
    • MacKerell, A. D., Jr.; Bashford, D.; Bellott, M.; Dunbrack, R. L., Jr.; Evanseck, J. D.; Field, M. J.; Fischer, S.; Gao, J.; Guo, H.; Ha, S.; Joseph-McCarthy, D.; Kuchnir, L.; Kuczera, K.; Lau, F. T. K.; Mattes, C.; Michnick, S.; Ngo, T.; Nguyen, D. T.; Prodhom, B.; Reiher, W. E., III; Roux, B.; Schlenkrich, M.; Smith, J. C.; Stote, R.; Straub, J.; Watanabe, M.; Wiórkiewicz-Kuczera, J.; Yin, D.; Karplus, M. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 1998, 102, 3586-3616.
    • MacKerell, A. D., Jr.; Bashford, D.; Bellott, M.; Dunbrack, R. L., Jr.; Evanseck, J. D.; Field, M. J.; Fischer, S.; Gao, J.; Guo, H.; Ha, S.; Joseph-McCarthy, D.; Kuchnir, L.; Kuczera, K.; Lau, F. T. K.; Mattes, C.; Michnick, S.; Ngo, T.; Nguyen, D. T.; Prodhom, B.; Reiher, W. E., III; Roux, B.; Schlenkrich, M.; Smith, J. C.; Stote, R.; Straub, J.; Watanabe, M.; Wiórkiewicz-Kuczera, J.; Yin, D.; Karplus, M. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 1998, 102, 3586-3616.
  • 27
    • 0037571112 scopus 로고    scopus 로고
    • Halgren, T. A. Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J. Comput. Chem. 1996, 17, 490-519.
    • Halgren, T. A. Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J. Comput. Chem. 1996, 17, 490-519.
  • 28
    • 0141705688 scopus 로고    scopus 로고
    • Molecular docking of substrates and inhibitors in the catalytic site of CYP6B1, an insect cytochrome P450 monooxygenase
    • Baudry, J.; Li, W.; Pan, L.; Berenbaum, M. R.; Schuler, M. A. Molecular docking of substrates and inhibitors in the catalytic site of CYP6B1, an insect cytochrome P450 monooxygenase. Protein Eng. 2003, 16, 577-587.
    • (2003) Protein Eng , vol.16 , pp. 577-587
    • Baudry, J.1    Li, W.2    Pan, L.3    Berenbaum, M.R.4    Schuler, M.A.5
  • 29
    • 19944402532 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein
    • Lo, W. M. Y.; Li-Chan, E. C. Y. Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein. J. Agric. Food Chem. 2005, 53, 3369-3376.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 3369-3376
    • Lo, W.M.Y.1    Li-Chan, E.C.Y.2
  • 30
    • 35448950270 scopus 로고    scopus 로고
    • Mechanism of inhibition of DNA gyrase by ES-1273, a novel DNA gyrase inhibitor
    • Oyamada, Y.; Yamagishi, J.; Kihara, T.; Yoshida, H.; Wachi, M.; Ito, H. Mechanism of inhibition of DNA gyrase by ES-1273, a novel DNA gyrase inhibitor. Microbiol. Immunol. 2007, 51, 977-984.
    • (2007) Microbiol. Immunol , vol.51 , pp. 977-984
    • Oyamada, Y.1    Yamagishi, J.2    Kihara, T.3    Yoshida, H.4    Wachi, M.5    Ito, H.6
  • 31
    • 13244277961 scopus 로고    scopus 로고
    • Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulin. Identification of active peptides by HPLC-MS/MS
    • Hernandez-Ledesma, B.; Davalos, A.; Bartolome, B.; Amigo, L. Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulin. Identification of active peptides by HPLC-MS/MS. J. Agric. Food Chem. 2005, 53, 588-593.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 588-593
    • Hernandez-Ledesma, B.1    Davalos, A.2    Bartolome, B.3    Amigo, L.4
  • 32
    • 33748124256 scopus 로고    scopus 로고
    • Identification and characterization of novel angiotensin-converting enzyme inhibitors obtained from goat milk
    • Geerlings, A.; Villar, I. C.; Zarco, F. H.; Sanchez, M.; Vera, R.; Gomez, A. Z.; Boza, J.; Duarte, J. Identification and characterization of novel angiotensin-converting enzyme inhibitors obtained from goat milk. J. Dairy Sci. 2006, 89, 3326-3335.
    • (2006) J. Dairy Sci , vol.89 , pp. 3326-3335
    • Geerlings, A.1    Villar, I.C.2    Zarco, F.H.3    Sanchez, M.4    Vera, R.5    Gomez, A.Z.6    Boza, J.7    Duarte, J.8
  • 33
    • 33746531279 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max)
    • Gouda, K. G. M.; Gowda, L. R.; Rao, A. G. A.; Prakash, V. Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max). J. Agric. Food Chem. 2006, 54, 4568-4573.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 4568-4573
    • Gouda, K.G.M.1    Gowda, L.R.2    Rao, A.G.A.3    Prakash, V.4
  • 34
  • 36
    • 0034845801 scopus 로고    scopus 로고
    • Sequence verification of oligonucleotides by electrospray quadrupole time-of flight mass spectrometry
    • Ni, J.; Chan, K. Sequence verification of oligonucleotides by electrospray quadrupole time-of flight mass spectrometry. Rapid Commun. Mass Spectrom. 2001, 15, 1600-1608.
    • (2001) Rapid Commun. Mass Spectrom , vol.15 , pp. 1600-1608
    • Ni, J.1    Chan, K.2
  • 37
    • 0030796836 scopus 로고    scopus 로고
    • A novel geometry mass spectrometer, the Q-TOF, for low-femtomol/attomole-range biopolymer sequencing
    • Morris, H. R.; Paxton, T.; Panico, M.; McDowell, R.; Dell, A. A novel geometry mass spectrometer, the Q-TOF, for low-femtomol/attomole-range biopolymer sequencing. J. Protein Chem. 1997, 16, 469-479.
    • (1997) J. Protein Chem , vol.16 , pp. 469-479
    • Morris, H.R.1    Paxton, T.2    Panico, M.3    McDowell, R.4    Dell, A.5
  • 38
    • 34848859979 scopus 로고    scopus 로고
    • Peptic and tryptic hydrolysis of native and heated whey protein to reduce its antigenicity
    • Kim, S. B.; Ki, K. S.; Khan, M. A.; Lee, W. S.; Lee, H. J.; Ahn, B. S.; Kim, H. S. Peptic and tryptic hydrolysis of native and heated whey protein to reduce its antigenicity. J. Dairy Sci. 2007, 90, 4043-4050.
    • (2007) J. Dairy Sci , vol.90 , pp. 4043-4050
    • Kim, S.B.1    Ki, K.S.2    Khan, M.A.3    Lee, W.S.4    Lee, H.J.5    Ahn, B.S.6    Kim, H.S.7
  • 39
  • 41
    • 0003054359 scopus 로고    scopus 로고
    • Agronomic characteristics, production, and marketing
    • Chapman and Hall: New York
    • Liu, K. S. Agronomic characteristics, production, and marketing. In Soybeans: Chemistry, Technology and Utilization; Chapman and Hall: New York, 1997; pp 1-24.
    • (1997) Soybeans: Chemistry, Technology and Utilization , pp. 1-24
    • Liu, K.S.1
  • 42
    • 0026428621 scopus 로고
    • Crystal structure of an N-terminal fragment of the DNA gyrase B protein
    • Wigley, D. B.; Davies, G. J.; Dodson, E. J.; Maxwell, A.; Dodson, G. Crystal structure of an N-terminal fragment of the DNA gyrase B protein. Nature 1991, 351, 624-629.
    • (1991) Nature , vol.351 , pp. 624-629
    • Wigley, D.B.1    Davies, G.J.2    Dodson, E.J.3    Maxwell, A.4    Dodson, G.5
  • 43
    • 0030045003 scopus 로고    scopus 로고
    • Structure and mechanism of DNA topoisomerase II
    • Berger, J. M.; Gamblin, S. J.; Harrison, S. C.; Wang, J. C. Structure and mechanism of DNA topoisomerase II. Nature 1996, 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
  • 45
    • 0034737716 scopus 로고    scopus 로고
    • Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center
    • Brino, L.; Urzhumtsev, A.; Mousli, M.; Bronner, C.; Mitschier, A.; Oudet, P.; Moras, D. Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center. J. Biol. Chem. 2000, 275, 9468-9475.
    • (2000) J. Biol. Chem , vol.275 , pp. 9468-9475
    • Brino, L.1    Urzhumtsev, A.2    Mousli, M.3    Bronner, C.4    Mitschier, A.5    Oudet, P.6    Moras, D.7
  • 46
    • 0032947158 scopus 로고    scopus 로고
    • Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands
    • Fass, D.; Bogden, C. E.; Berger, J. M. Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. Nat. Struct. Biol. 1999, 6, 322-326.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 322-326
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 47
    • 27744591551 scopus 로고    scopus 로고
    • Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase
    • Wei, H.; Ruthenburg, A. J.; Bechis, S. K.; Verdine, G. L. Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase. J. Biol. Chem. 2005, 280, 37041-37047.
    • (2005) J. Biol. Chem , vol.280 , pp. 37041-37047
    • Wei, H.1    Ruthenburg, A.J.2    Bechis, S.K.3    Verdine, G.L.4
  • 48
    • 28844455588 scopus 로고    scopus 로고
    • Recent advances in understanding structure-function relationships in the type II topoisomerase mechanism
    • Schoeffler, A. J.; Berger, J. M. Recent advances in understanding structure-function relationships in the type II topoisomerase mechanism. Biochem. Soc. Trans. 2005, 33, 1465-1470.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 1465-1470
    • Schoeffler, A.J.1    Berger, J.M.2
  • 49
    • 35748968504 scopus 로고    scopus 로고
    • DNA topoisomerase II structures and anthracycline activity: Insights into ternary complex formation
    • Dal Ben, D.; Palumbo, M.; Zagotto, G.; Capranico, G.; Moro, S. DNA topoisomerase II structures and anthracycline activity: insights into ternary complex formation. Curr. Pharm. Des. 2007, 13, 2766-2780.
    • (2007) Curr. Pharm. Des , vol.13 , pp. 2766-2780
    • Dal Ben, D.1    Palumbo, M.2    Zagotto, G.3    Capranico, G.4    Moro, S.5
  • 50
    • 33745216445 scopus 로고    scopus 로고
    • Topoisomerase research of kinetoplastid parasite Leishmania, with special reference to development of therapeutics
    • Das, B. B.; Sen, N.; Dasgupta, S. B.; Ganguly, A.; Das, R.; Majumder, H. K. Topoisomerase research of kinetoplastid parasite Leishmania, with special reference to development of therapeutics. Indian J. Med. Res. 2006, 123, 221-232.
    • (2006) Indian J. Med. Res , vol.123 , pp. 221-232
    • Das, B.B.1    Sen, N.2    Dasgupta, S.B.3    Ganguly, A.4    Das, R.5    Majumder, H.K.6


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