메뉴 건너뛰기




Volumn 4, Issue 4, 2008, Pages 194-215

Natural products as inhibitors of DNA related enzymes

Author keywords

DNA polymerases; Inhibitors; Natural products; Reverse transcriptase; Topoisomerases

Indexed keywords

ACLARUBICIN; ANTHRACYCLINE; ANTHRACYCLINE DERIVATIVE; BAICALIN; CAMPTOTHECIN DERIVATIVE; CATALPOL; CHROMONE DERIVATIVE; COUMARIN DERIVATIVE; DNA; DNA POLYMERASE; DNA TOPOISOMERASE; DOXORUBICIN; ENZYME INHIBITOR; FLAVONOID; IRIDOID; IRINOTECAN; LIPID; MASLINIC ACID; NATURAL PRODUCT; OLEIC ACID; PHYTOSTEROL; PROTOBERBERINE DERIVATIVE; PYRROLE DERIVATIVE; QUINONE DERIVATIVE; RNA DIRECTED DNA POLYMERASE INHIBITOR; SITOSTEROL; STIGMASTEROL; TANNIN DERIVATIVE; TRITERPENE DERIVATIVE; UNINDEXED DRUG;

EID: 65649095577     PISSN: 15734080     EISSN: None     Source Type: Journal    
DOI: 10.2174/157340808786733604     Document Type: Review
Times cited : (10)

References (91)
  • 1
    • 0042844744 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the period 1981-2002
    • Newman, D.J.; Cragg, G.M.; Snader, K.M. Natural products as sources of new drugs over the period 1981-2002. J. Nat. Prod., 2003, 66, 1022-1037.
    • (2003) J. Nat. Prod , vol.66 , pp. 1022-1037
    • Newman, D.J.1    Cragg, G.M.2    Snader, K.M.3
  • 3
    • 0034664936 scopus 로고    scopus 로고
    • Novel triterpenoids inhibit both DNA polymerase and DNA topoisomerase
    • Mizushina, Y.; Iida, A.; Ohta, K.; Sugawara, F.; Sakaguchi, K. Novel triterpenoids inhibit both DNA polymerase and DNA topoisomerase. Biochem. J., 2000, 350, 757-763.
    • (2000) Biochem. J , vol.350 , pp. 757-763
    • Mizushina, Y.1    Iida, A.2    Ohta, K.3    Sugawara, F.4    Sakaguchi, K.5
  • 4
    • 0034739330 scopus 로고    scopus 로고
    • Cancer chemopreventative activity of an iridoid glycoside, 8-acetylharpagide, from Ajuga decumbens
    • Konoshima, T.; Takasaki, M.; Tokuda, H.; Nishino, H. Cancer chemopreventative activity of an iridoid glycoside, 8-acetylharpagide, from Ajuga decumbens. Cancer Lett., 2000, 157, 87-92.
    • (2000) Cancer Lett , vol.157 , pp. 87-92
    • Konoshima, T.1    Takasaki, M.2    Tokuda, H.3    Nishino, H.4
  • 5
    • 22744447495 scopus 로고    scopus 로고
    • Hamdi, H.; Castellon, R. Oleuropein, a non-toxic olive iridoid, is an anti-tumor agent and cytoskeleton disruptor. Biochem. Biophys. Res. Commun., 2005, 334, 769-778.
    • Hamdi, H.; Castellon, R. Oleuropein, a non-toxic olive iridoid, is an anti-tumor agent and cytoskeleton disruptor. Biochem. Biophys. Res. Commun., 2005, 334, 769-778.
  • 8
  • 9
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation
    • Li, Y.; Korolev, S.; Waksman, G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation. EMBO J., 1998, 17, 7514-7525.
    • (1998) EMBO J , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 10
    • 65649143674 scopus 로고    scopus 로고
    • Protein Data Bank, access code: 4KTQ.
    • Protein Data Bank, access code: 4KTQ.
  • 11
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • Ollis, D.L.; Brick, P.; Hamlin, R.; Xuong, N.G.; Steitz, T.A. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature, 1985, 313, 762-766.
    • (1985) Nature , vol.313 , pp. 762-766
    • Ollis, D.L.1    Brick, P.2    Hamlin, R.3    Xuong, N.G.4    Steitz, T.A.5
  • 12
    • 0027411261 scopus 로고
    • and RNA-dependent DNA polymerases
    • Steitz, T.A. DNA- and RNA-dependent DNA polymerases. Curr. Opin. Struct. Biol., 1993, 3, 31-38.
    • (1993) Curr. Opin. Struct. Biol , vol.3 , pp. 31-38
    • Steitz, T.A.D.1
  • 13
    • 0027220197 scopus 로고
    • Conformational coupling in DNA polymerase fidelity
    • Johnson, K.A. Conformational coupling in DNA polymerase fidelity. Annu. Rev. Biochem., 1993, 62, 685-713.
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 685-713
    • Johnson, K.A.1
  • 14
    • 65649144379 scopus 로고    scopus 로고
    • Protein Data Bank, access code: 1TV9.
    • Protein Data Bank, access code: 1TV9.
  • 15
    • 0032080334 scopus 로고    scopus 로고
    • Functional analysis of the amino-terminal 8-kDa domain of DNA polymerase β as revealed by site-directed mutagenesis
    • Prasad, R.J. Functional analysis of the amino-terminal 8-kDa domain of DNA polymerase β as revealed by site-directed mutagenesis. Biol. Chem., 1998, 273, 11121-11126.
    • (1998) Biol. Chem , vol.273 , pp. 11121-11126
    • Prasad, R.J.1
  • 16
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
    • Matsumoto, Y.; Kim, K. Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair. Science, 1995, 269, 699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 18
    • 0032822306 scopus 로고    scopus 로고
    • DNA polymerse β inhibitors from Sandoricum koetjape
    • Sun, D-A.; Starck, S.R.; Locke, E.P.; Hecht, S.M. DNA polymerse β inhibitors from Sandoricum koetjape. J. Nat. Prod., 1999, 62, 1110-1113.
    • (1999) J. Nat. Prod , vol.62 , pp. 1110-1113
    • Sun, D.-A.1    Starck, S.R.2    Locke, E.P.3    Hecht, S.M.4
  • 19
    • 0033759486 scopus 로고    scopus 로고
    • A new 7, 8-euphadien-type triterpenoid from Brackenridgea nitida and Bleasdalea bleasdalei that inhibits DNA polymerase β
    • Deng, J.-Z.; Starck, S.R.; Sun, D.-A.; Sabat, M.; Hecht, S.M. A new 7, 8-euphadien-type triterpenoid from Brackenridgea nitida and Bleasdalea bleasdalei that inhibits DNA polymerase β. J. Nat. Prod., 2000, 63, 1356-1360.
    • (2000) J. Nat. Prod , vol.63 , pp. 1356-1360
    • Deng, J.-Z.1    Starck, S.R.2    Sun, D.-A.3    Sabat, M.4    Hecht, S.M.5
  • 20
    • 0031881255 scopus 로고    scopus 로고
    • Fomitellic Acids, Triterpenoid inhibitors of eukaryotic DNA polymerases from a basidiomycete, Fomitella fraxinea
    • Tanaka, N.; Kitamura, A.; Mizushina, Y.; Sugawara, F.; Sakaguchi, K. Fomitellic Acids, Triterpenoid inhibitors of eukaryotic DNA polymerases from a basidiomycete, Fomitella fraxinea. J. Nat. Prod., 1998, 61, 193-197.
    • (1998) J. Nat. Prod , vol.61 , pp. 193-197
    • Tanaka, N.1    Kitamura, A.2    Mizushina, Y.3    Sugawara, F.4    Sakaguchi, K.5
  • 21
    • 0033427655 scopus 로고    scopus 로고
    • DNA polymerase β inhibitors from Baeckea gunniana
    • Deng, J.-Z.; Starck, S.R.; Hecht, S.M. DNA polymerase β inhibitors from Baeckea gunniana. J. Nat. Prod., 1999, 62, 1624-1626.
    • (1999) J. Nat. Prod , vol.62 , pp. 1624-1626
    • Deng, J.-Z.1    Starck, S.R.2    Hecht, S.M.3
  • 23
    • 0000334719 scopus 로고    scopus 로고
    • DNA polymerase and topoisomerase II inhibitors from Psoralea corylifolia
    • Sun, N.J.; Woo, S.H.; Cassady, J.M.; Snapka R.M. DNA polymerase and topoisomerase II inhibitors from Psoralea corylifolia. J. Nat. Prod., 1998, 61, 362-366.
    • (1998) J. Nat. Prod , vol.61 , pp. 362-366
    • Sun, N.J.1    Woo, S.H.2    Cassady, J.M.3    Snapka, R.M.4
  • 24
    • 0032890604 scopus 로고    scopus 로고
    • Bis-5-alkylresorcinols from Panopsis rubescens that inhibit DNA polymerase β
    • Deng, J-Z.; Starck, S.R.; Hecht, S.M. Bis-5-alkylresorcinols from Panopsis rubescens that inhibit DNA polymerase β. J. Nat. Prod., 1999, 62, 477-480.
    • (1999) J. Nat. Prod , vol.62 , pp. 477-480
    • Deng, J.-Z.1    Starck, S.R.2    Hecht, S.M.3
  • 27
    • 33947588087 scopus 로고    scopus 로고
    • Kamisuki, S.; Ishimaru, C.; Onoda, K.; Kuriyama, I.; Ida, N.; Sugawara, F.; Yoshida, H.; Mizushina, Y. Nodulisporol and nodulisporone, novel specific inhibitors of human DNA polymerase λ from a fungus, Nodulisporium sp. Bioorg. Med. Chem., 2007, 15, 3109-3114.
    • Kamisuki, S.; Ishimaru, C.; Onoda, K.; Kuriyama, I.; Ida, N.; Sugawara, F.; Yoshida, H.; Mizushina, Y. Nodulisporol and nodulisporone, novel specific inhibitors of human DNA polymerase λ from a fungus, Nodulisporium sp. Bioorg. Med. Chem., 2007, 15, 3109-3114.
  • 30
    • 0029114736 scopus 로고
    • Flavocristamides A and B, new DNA polymerases α inhibitors from a marine bacterium Flavobacterium sp
    • Kobayashi, J.; Mikami, S.; Shigemori, H.; Takao, T.; Shimonishi, Y.; Izuta, S.; Yoshida, S. Flavocristamides A and B, new DNA polymerases α inhibitors from a marine bacterium Flavobacterium sp. Tetrahedron, 1995, 51, 10487-10490.
    • (1995) Tetrahedron , vol.51 , pp. 10487-10490
    • Kobayashi, J.1    Mikami, S.2    Shigemori, H.3    Takao, T.4    Shimonishi, Y.5    Izuta, S.6    Yoshida, S.7
  • 35
    • 3042716233 scopus 로고    scopus 로고
    • Plant sterols as selective DNA polymerase β lyase inhibitors and potentiators of bleomycin cytotoxicity
    • Li, S.-S.; Gao, Z.; Feng, X.; Jones, S.H.; Hecht, S.M. Plant sterols as selective DNA polymerase β lyase inhibitors and potentiators of bleomycin cytotoxicity. Bioorg. Med. Chem., 2004, 12, 4253-4258.
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 4253-4258
    • Li, S.-S.1    Gao, Z.2    Feng, X.3    Jones, S.H.4    Hecht, S.M.5
  • 37
    • 40949083456 scopus 로고    scopus 로고
    • 1-Deoxyrubralactone, a novel specific inhibitor of families X and Y of eukaryotic DNA polymerases from a fungal strain derived from sea algae
    • Naganuma, M.; Nishida, M.; Kuramochi, K.; Sugawara, F.; Yoshida, H.; Mizushina, Y. 1-Deoxyrubralactone, a novel specific inhibitor of families X and Y of eukaryotic DNA polymerases from a fungal strain derived from sea algae. Bioorg. Med. Chem., 2008, 16, 2939-2944.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 2939-2944
    • Naganuma, M.1    Nishida, M.2    Kuramochi, K.3    Sugawara, F.4    Yoshida, H.5    Mizushina, Y.6
  • 41
    • 42149089140 scopus 로고    scopus 로고
    • Novel azaphilones, kasanosins A and B, which are specific inhibitors of eukaryotic DNA polymerases β and λ from Talaromyces sp
    • Kimura, T.; Nishida, M.; Kuramochi, K.; Sugawara, F.; Yoshida, H.; Mizushina, Y. Novel azaphilones, kasanosins A and B, which are specific inhibitors of eukaryotic DNA polymerases β and λ from Talaromyces sp. Bioorg. Med. Chem., 2008, 16, 4594-4599.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 4594-4599
    • Kimura, T.1    Nishida, M.2    Kuramochi, K.3    Sugawara, F.4    Yoshida, H.5    Mizushina, Y.6
  • 45
    • 0032769164 scopus 로고    scopus 로고
    • Harbanic acid, a novel and potent DNA polymerase β inhibitor from Hardwickia binata
    • Deng, J.-Z.; Starck, S.R.; Hecht, S.M.; Ijames, C.F.; Hemling, M.E. Harbanic acid, a novel and potent DNA polymerase β inhibitor from Hardwickia binata. J. Nat. Prod., 1999, 62, 1000-1002.
    • (1999) J. Nat. Prod , vol.62 , pp. 1000-1002
    • Deng, J.-Z.1    Starck, S.R.2    Hecht, S.M.3    Ijames, C.F.4    Hemling, M.E.5
  • 47
    • 0344010645 scopus 로고    scopus 로고
    • Modified limonoids from the leaves of Sandoricum koetjape
    • Ismail, I.; Ito, H.; Hatano, T.; Taniguchi, S.; Yoshida, T. Modified limonoids from the leaves of Sandoricum koetjape. Phytochemistry, 2003, 641, 345-1349.
    • (2003) Phytochemistry , vol.641 , pp. 345-1349
    • Ismail, I.1    Ito, H.2    Hatano, T.3    Taniguchi, S.4    Yoshida, T.5
  • 48
    • 0030159368 scopus 로고    scopus 로고
    • Seco-eremophilane derivatives from rhizomes of Petasites Japonicus
    • Yaoita, Y.; Kikuchi, M. Seco-eremophilane derivatives from rhizomes of Petasites Japonicus. Phytochemistry, 1996, 42, 751-755.
    • (1996) Phytochemistry , vol.42 , pp. 751-755
    • Yaoita, Y.1    Kikuchi, M.2
  • 49
    • 38849168110 scopus 로고    scopus 로고
    • Neuroprotective effect of methanolic extracts of Allium cepa on ischemia and reperfusion-induced cerebral injury
    • Shri, R.; Singh, K. Neuroprotective effect of methanolic extracts of Allium cepa on ischemia and reperfusion-induced cerebral injury. Fitoterapia, 2008, 79, 86-96.
    • (2008) Fitoterapia , vol.79 , pp. 86-96
    • Shri, R.1    Singh, K.2
  • 50
    • 49449118509 scopus 로고    scopus 로고
    • Effect of green and black teas (Camellia sinensis L.) on the characteristic microflora of yogurt during fermentation and refrigerated storage
    • Jaziri, I.; Ben Slama, M.; Mhadhbi, H.; Urdaci, M.; Hamdi, M. Effect of green and black teas (Camellia sinensis L.) on the characteristic microflora of yogurt during fermentation and refrigerated storage. Food Chem., 2009, 112, 614-620.
    • (2009) Food Chem , vol.112 , pp. 614-620
    • Jaziri, I.1    Ben Slama, M.2    Mhadhbi, H.3    Urdaci, M.4    Hamdi, M.5
  • 51
    • 0000576165 scopus 로고
    • Preparations containing DNA gyrase activity has been extensively purified from Escherichia coli
    • Gellert, M.; Mizuchi, K.; O'Dea, M.H.; Nash, H.A. Preparations containing DNA gyrase activity has been extensively purified from Escherichia coli. Proc. Natl. Acad. Sci. USA, 1976, 73, 3872-3876.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3872-3876
    • Gellert, M.1    Mizuchi, K.2    O'Dea, M.H.3    Nash, H.A.4
  • 52
    • 0019877297 scopus 로고
    • A homogeneous type II DNA topoisomerase from HeLa cell nuclei
    • Miller, K.G.; Liu, L.F.; Englund, P.T. A homogeneous type II DNA topoisomerase from HeLa cell nuclei. J. Biol. Chem., 1981, 256, 9334-9339.
    • (1981) J. Biol. Chem , vol.256 , pp. 9334-9339
    • Miller, K.G.1    Liu, L.F.2    Englund, P.T.3
  • 53
    • 65649086949 scopus 로고    scopus 로고
    • Protein Data Bank, access code: 1EJ9.
    • Protein Data Bank, access code: 1EJ9.
  • 54
    • 0035808334 scopus 로고    scopus 로고
    • The role of Histidine 632 in catalysis by human topoisomerase I
    • Yang, Z.; Champoux, J.J. The role of Histidine 632 in catalysis by human topoisomerase I. J. Biol. Chem., 2001, 276, 677-685.
    • (2001) J. Biol. Chem , vol.276 , pp. 677-685
    • Yang, Z.1    Champoux, J.J.2
  • 55
    • 0032489634 scopus 로고    scopus 로고
    • Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA
    • Redinbo, M.R.; Stewart, L.; Kuhn, P.; Champoux, J.J.; Hol, W.G.J. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science, 1998, 279, 1504-1513.
    • (1998) Science , vol.279 , pp. 1504-1513
    • Redinbo, M.R.1    Stewart, L.2    Kuhn, P.3    Champoux, J.J.4    Hol, W.G.J.5
  • 56
    • 0034643810 scopus 로고    scopus 로고
    • Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA
    • Redinbo, M.R.; Champoux, J.J.; Hol, W.G.J. Novel insights into catalytic mechanism from a crystal structure of human topoisomerase I in complex with DNA. Biochemistry, 2000, 39, 6832-6840.
    • (2000) Biochemistry , vol.39 , pp. 6832-6840
    • Redinbo, M.R.1    Champoux, J.J.2    Hol, W.G.J.3
  • 57
    • 0037212083 scopus 로고    scopus 로고
    • Potent topoisomerase I inhibitors and promising anticancer drugs
    • Bailly, C. Homocamptothecins: Potent topoisomerase I inhibitors and promising anticancer drugs. Crit. Rev. Oncol. Hematol., 2003, 45, 91-108.
    • (2003) Crit. Rev. Oncol. Hematol , vol.45 , pp. 91-108
    • Bailly, C.H.1
  • 59
    • 0035928802 scopus 로고    scopus 로고
    • A structural model for the ternary cleavable complex formed between human topoisomerase I, DNA, and camptothecin
    • Kerrigan, J.E.; Pilch, D.S. A structural model for the ternary cleavable complex formed between human topoisomerase I, DNA, and camptothecin. Biochemistry, 2001, 40, 9792-9798.
    • (2001) Biochemistry , vol.40 , pp. 9792-9798
    • Kerrigan, J.E.1    Pilch, D.S.2
  • 60
    • 0037022183 scopus 로고    scopus 로고
    • Human topoisomerase I inhibition: Docking camptothecin and derivatives into a structure-based active site model
    • Laco, G.S.; Collins, J.R.; Luke, B.T.; Kroth, H.; Sayer, J.M.; Jerina, D.M.; Pommier, Y. Human topoisomerase I inhibition: Docking camptothecin and derivatives into a structure-based active site model. Biochemistry, 2002, 41, 1428-1435.
    • (2002) Biochemistry , vol.41 , pp. 1428-1435
    • Laco, G.S.1    Collins, J.R.2    Luke, B.T.3    Kroth, H.4    Sayer, J.M.5    Jerina, D.M.6    Pommier, Y.7
  • 61
    • 0030249075 scopus 로고    scopus 로고
    • Irinotecan (CPT-11): Pharmacology and clinical applications
    • Bailly, C. Irinotecan (CPT-11): Pharmacology and clinical applications. Crit. Rev. Oncol. Hematol., 1996, 24, 3-26.
    • (1996) Crit. Rev. Oncol. Hematol , vol.24 , pp. 3-26
    • Bailly, C.1
  • 62
    • 0042346439 scopus 로고    scopus 로고
    • Catalytic topoisomerase II inhibitors in cancer therapy
    • Larsen, A.K.; Escargueil, A.E.; Skladanowski, A. Catalytic topoisomerase II inhibitors in cancer therapy. Pharmacol. Ther., 2003, 99, 167-181.
    • (2003) Pharmacol. Ther , vol.99 , pp. 167-181
    • Larsen, A.K.1    Escargueil, A.E.2    Skladanowski, A.3
  • 63
    • 0030836293 scopus 로고    scopus 로고
    • Differential poisoning of topoisomerases by menogaril and nogalamycin dictated by the minor groove-binding nogalose sugar
    • Sim, S.-P.; Gatto, B.; Yu, C.; Liu, A.A.; Li, T.-K.; Pilch, D.S.; LaVoie, E.J.; Liu, L.F. Differential poisoning of topoisomerases by menogaril and nogalamycin dictated by the minor groove-binding nogalose sugar. Biochemistry, 1997, 36, 13285-13291.
    • (1997) Biochemistry , vol.36 , pp. 13285-13291
    • Sim, S.-P.1    Gatto, B.2    Yu, C.3    Liu, A.A.4    Li, T.-K.5    Pilch, D.S.6    LaVoie, E.J.7    Liu, L.F.8
  • 64
    • 0014066067 scopus 로고
    • Daunomycin, an antitumor antibiotic in the treatment of neoplastic disease
    • Tan, C.; Tasaka, H.; Kou-Ping, Y. Daunomycin, an antitumor antibiotic in the treatment of neoplastic disease. Cancer, 1967, 20, 333-353.
    • (1967) Cancer , vol.20 , pp. 333-353
    • Tan, C.1    Tasaka, H.2    Kou-Ping, Y.3
  • 65
    • 0242329856 scopus 로고    scopus 로고
    • Ting, C.Y; Hsu, C.; Hsu, H.T.; Su, J.S.; Chen, J.Y.; Tarn, W.Y; Kuo, Y.H.; Whang-Peng, J.; Liu, L.F.; Hwang, J. Isodiospyrin as a novel human DNA topoisomerase I inhibitor. J. Biochem. Pharmacol., 2003, 66, 1981-1991.
    • Ting, C.Y; Hsu, C.; Hsu, H.T.; Su, J.S.; Chen, J.Y.; Tarn, W.Y; Kuo, Y.H.; Whang-Peng, J.; Liu, L.F.; Hwang, J. Isodiospyrin as a novel human DNA topoisomerase I inhibitor. J. Biochem. Pharmacol., 2003, 66, 1981-1991.
  • 66
    • 0035885187 scopus 로고    scopus 로고
    • Meng, L.; Zhang, J.; Ding, J. Salvicine, a novel DNA topoisomerase II inhibitor, exerting its effects by trapping enzyme-DNA cleavage complexes. Biochem. Pharmacol., 2001, 62, 733-741.
    • Meng, L.; Zhang, J.; Ding, J. Salvicine, a novel DNA topoisomerase II inhibitor, exerting its effects by trapping enzyme-DNA cleavage complexes. Biochem. Pharmacol., 2001, 62, 733-741.
  • 67
    • 84965098356 scopus 로고    scopus 로고
    • Inhibition of DNA topoisomerase I and growth inhibition of human cancer cell lines by an oleanane from Junellia aspera (Verbenaceae)
    • Pungitore, C.R.; Padrón, J.M.; León, L.G.; García, C.; Ciuffo, G.M.; Martín, V.S.; Tonn, C.E. Inhibition of DNA topoisomerase I and growth inhibition of human cancer cell lines by an oleanane from Junellia aspera (Verbenaceae) Cell. Mol. Biol., 2007, 53, 13-17.
    • (2007) Cell. Mol. Biol , vol.53 , pp. 13-17
    • Pungitore, C.R.1    Padrón, J.M.2    León, L.G.3    García, C.4    Ciuffo, G.M.5    Martín, V.S.6    Tonn, C.E.7
  • 68
    • 0035684524 scopus 로고    scopus 로고
    • Screening of triterpenoids isolated from Phyllanthus flexuosus for DNA topoisomerase inhibitory activity
    • Wada, S.; Iida, A.; Tanaka, R. Screening of triterpenoids isolated from Phyllanthus flexuosus for DNA topoisomerase inhibitory activity. J. Nat. Prod., 2001, 64, 1545-1547.
    • (2001) J. Nat. Prod , vol.64 , pp. 1545-1547
    • Wada, S.1    Iida, A.2    Tanaka, R.3
  • 70
    • 0037294445 scopus 로고    scopus 로고
    • Rebeccamycin analogues as anti-cancer agents
    • Prudhomme, M. Rebeccamycin analogues as anti-cancer agents. Eur. J. Med. Chem., 2003, 38, 123-140.
    • (2003) Eur. J. Med. Chem , vol.38 , pp. 123-140
    • Prudhomme, M.1
  • 71
    • 0034691311 scopus 로고    scopus 로고
    • Human topoisomerase I poisoning by protoberberines: Potential roles for both drug-DNA and drug-enzyme interactions
    • Li, T.; Bathory, E.; LaVoie, E.J.; Srinivasan, A.R.; Olson, W.K.; Sauers, R.R.; Liu, L.F.; Pilch, D.S. Human topoisomerase I poisoning by protoberberines: Potential roles for both drug-DNA and drug-enzyme interactions. Biochemistry, 2000, 39, 7107-7116.
    • (2000) Biochemistry , vol.39 , pp. 7107-7116
    • Li, T.1    Bathory, E.2    LaVoie, E.J.3    Srinivasan, A.R.4    Olson, W.K.5    Sauers, R.R.6    Liu, L.F.7    Pilch, D.S.8
  • 73
    • 34447501906 scopus 로고    scopus 로고
    • Synthetic approach to condensed heterocyclic analogues from etoposide revisited. Synthesis of A-ring pyridazine etoposide
    • Bertounesque, E.; Meresse, P.; Monneret, C.; Florent J.-C. Synthetic approach to condensed heterocyclic analogues from etoposide revisited. Synthesis of A-ring pyridazine etoposide. Tetrahedron Lett., 2007, 48, 5781-5784.
    • (2007) Tetrahedron Lett , vol.48 , pp. 5781-5784
    • Bertounesque, E.1    Meresse, P.2    Monneret, C.3    Florent, J.-C.4
  • 74
    • 34248221211 scopus 로고    scopus 로고
    • Podophyllotoxin: Current perspectives
    • Liu, Y.-Q.; Yang, L.; Tian, X. Podophyllotoxin: Current perspectives. Curr. Bioact. Comp., 2007, 3, 37-66.
    • (2007) Curr. Bioact. Comp , vol.3 , pp. 37-66
    • Liu, Y.-Q.1    Yang, L.2    Tian, X.3
  • 76
    • 15944415851 scopus 로고    scopus 로고
    • Inhibitory activities against topoisomerase I and II by isoaurostatin derivatives and their structure-activity relationships
    • Suzuki, K.; Okawara, T.; Higashijima, T.; Yokomizo, K.; Mizushima, T.; Otsuka, M. Inhibitory activities against topoisomerase I and II by isoaurostatin derivatives and their structure-activity relationships. Bioorg. Med. Chem. Lett., 2005, 15, 2065-2068.
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 2065-2068
    • Suzuki, K.1    Okawara, T.2    Higashijima, T.3    Yokomizo, K.4    Mizushima, T.5    Otsuka, M.6
  • 77
    • 0042196252 scopus 로고    scopus 로고
    • Inhibition of DNA topoisomerases I and II, and growth inhibition of human cancer cell lines by a marine microalgal polysaccharide
    • Umemura, K.; Yanase, K.; Suzuki, M.; Okutani, K.; Yamori, T.; Andoh, T. Inhibition of DNA topoisomerases I and II, and growth inhibition of human cancer cell lines by a marine microalgal polysaccharide. Biochem. Pharmacol., 2003, 66, 481-487.
    • (2003) Biochem. Pharmacol , vol.66 , pp. 481-487
    • Umemura, K.1    Yanase, K.2    Suzuki, M.3    Okutani, K.4    Yamori, T.5    Andoh, T.6
  • 78
    • 0030720062 scopus 로고    scopus 로고
    • Rebeccamycin analogues as anti-cancer agents. Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A
    • Walsh, A.H.; Cheng, A.; Honkanen, R.E. Rebeccamycin analogues as anti-cancer agents. Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A. FEBS Lett., 1997, 416, 230-234.
    • (1997) FEBS Lett , vol.416 , pp. 230-234
    • Walsh, A.H.1    Cheng, A.2    Honkanen, R.E.3
  • 79
    • 33646029119 scopus 로고    scopus 로고
    • Abietane diterpenoid dimers from the roots of Salvia prionitis
    • Xu, J.; Chang, J.; Zhao, M.; Zhang, J.-S. Abietane diterpenoid dimers from the roots of Salvia prionitis. Phytochemistry, 2006, 67, 795-799.
    • (2006) Phytochemistry , vol.67 , pp. 795-799
    • Xu, J.1    Chang, J.2    Zhao, M.3    Zhang, J.-S.4
  • 80
    • 65649091506 scopus 로고    scopus 로고
    • Protein Data Bank, access code: 1S1X.
    • Protein Data Bank, access code: 1S1X.
  • 81
    • 0028932883 scopus 로고
    • Structures of DNA and RNA polymerases and their interactions with nucleic acid substrates
    • Arnold, E.; Ding, J.; Hughes, S.H.; Hostomsky, Z. Structures of DNA and RNA polymerases and their interactions with nucleic acid substrates. Curr. Opin. Struct. Biol., 1995, 5, 27-38.
    • (1995) Curr. Opin. Struct. Biol , vol.5 , pp. 27-38
    • Arnold, E.1    Ding, J.2    Hughes, S.H.3    Hostomsky, Z.4
  • 83
    • 0026659363 scopus 로고
    • Development of inhibitors of reverse transcriptase and protease as therapeutics against HIV infection
    • l-8
    • Mitsuya, H.; Development of inhibitors of reverse transcriptase and protease as therapeutics against HIV infection. J. Enzyme Inhib., 1992, 6, l-8.
    • (1992) J. Enzyme Inhib , vol.6
    • Mitsuya, H.1
  • 84
    • 0026771249 scopus 로고
    • Correlations between the in vitro and in vivo activity of anti-HIV agents: Implications for future drug development
    • Yarchoan, R.; Broker, S. Correlations between the in vitro and in vivo activity of anti-HIV agents: Implications for future drug development. J. Enzyme Inhib., 1992, 6, 99-111.
    • (1992) J. Enzyme Inhib , vol.6 , pp. 99-111
    • Yarchoan, R.1    Broker, S.2
  • 85
    • 0030836055 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus (anti-HIV) natural products with special emphasis on HIV reverse transcriptase inhibitors
    • Ng, T.B.; Huang, B.; Fong, W.P.; Yeung, H.W. Anti-human immunodeficiency virus (anti-HIV) natural products with special emphasis on HIV reverse transcriptase inhibitors. Life Sci., 1997, 61, 933-949.
    • (1997) Life Sci , vol.61 , pp. 933-949
    • Ng, T.B.1    Huang, B.2    Fong, W.P.3    Yeung, H.W.4
  • 86
    • 0031903267 scopus 로고    scopus 로고
    • The inhibition of the reverse transcriptase of HIV-1 by the natural sulfoglycolipids from cyanobacteria: Contribution of different moieties to their high potency
    • Loya, S.; Reshef, V.; Mizrachi, E.; Silberstein, C.; Rachamim, Y.; Carmeli, S.; Hizi, A. The inhibition of the reverse transcriptase of HIV-1 by the natural sulfoglycolipids from cyanobacteria: Contribution of different moieties to their high potency. J. Nat. Prod., 1998, 61, 891-895.
    • (1998) J. Nat. Prod , vol.61 , pp. 891-895
    • Loya, S.1    Reshef, V.2    Mizrachi, E.3    Silberstein, C.4    Rachamim, Y.5    Carmeli, S.6    Hizi, A.7
  • 87
    • 33845936572 scopus 로고    scopus 로고
    • Antiangiogenic activity of Andrographis paniculata extract and andrographolide
    • Sheeja, K.; Guruvayoorappan, C.; Kuttan, G. Antiangiogenic activity of Andrographis paniculata extract and andrographolide. Int. Immunopharmacol., 2007, 7, 211-221.
    • (2007) Int. Immunopharmacol , vol.7 , pp. 211-221
    • Sheeja, K.1    Guruvayoorappan, C.2    Kuttan, G.3
  • 89
    • 0032078830 scopus 로고    scopus 로고
    • Antiamoebic and phytochemical screening of some Congolese medicinal plants
    • Tona, L.; Kambu, K.; Ngimbi, N.; Cimanga, K.; Vlietinck, A.J. Antiamoebic and phytochemical screening of some Congolese medicinal plants. J. Ethnopharmacol., 1998, 61, 57-65.
    • (1998) J. Ethnopharmacol , vol.61 , pp. 57-65
    • Tona, L.1    Kambu, K.2    Ngimbi, N.3    Cimanga, K.4    Vlietinck, A.J.5
  • 90
    • 48949105133 scopus 로고    scopus 로고
    • Screening of anti-HIV-1 inophyllums by HPLC-DAD of Calophyllum inophyllum leaf extracts from French Polynesia Islands
    • Laure, F.; Raharivelomanana, P.; Butaud, J.-F.; Bianchini, J.-P.; Gaydou, E. Screening of anti-HIV-1 inophyllums by HPLC-DAD of Calophyllum inophyllum leaf extracts from French Polynesia Islands. Anal. Chim. Acta, 2008, 624, 147-153.
    • (2008) Anal. Chim. Acta , vol.624 , pp. 147-153
    • Laure, F.1    Raharivelomanana, P.2    Butaud, J.-F.3    Bianchini, J.-P.4    Gaydou, E.5
  • 91
    • 3343003028 scopus 로고    scopus 로고
    • Lack of altitudinal trends in phytochemical constituents of Swertia franchetiana (Gentianaceae)
    • Yang, H.; Duan, Y.; Hu, F.; Liu, J. Lack of altitudinal trends in phytochemical constituents of Swertia franchetiana (Gentianaceae). Biochem. Syst. Ecol., 2004, 32, 861-866.
    • (2004) Biochem. Syst. Ecol , vol.32 , pp. 861-866
    • Yang, H.1    Duan, Y.2    Hu, F.3    Liu, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.