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Volumn 35, Issue 4, 2009, Pages 805-812

A novel anti-tumor protein extracted from Meretrix meretrix Linnaeus induces cell death by increasing cell permeability and inhibiting tubulin polymerization

Author keywords

Anti tumor protein; Apoptosis; Cell cycle; Cell membrane permeability; Cytotoxicity; Meretrix meretrix Linnaeus; Tubulin polymerization

Indexed keywords

ALPHA TUBULIN; AMMONIUM SULFATE; ANTINEOPLASTIC AGENT; MERETRIX MERETRIX EXTRACT; TISSUE EXTRACT; UNCLASSIFIED DRUG;

EID: 70449448957     PISSN: 10196439     EISSN: 17912423     Source Type: Journal    
DOI: 10.3892/ijo_00000393     Document Type: Article
Times cited : (22)

References (53)
  • 1
    • 0029128645 scopus 로고
    • Fishing for drugs from the sea: Status and strategies
    • de Vries DJ and Beart PM: Fishing for drugs from the sea: status and strategies. Trends Pharmacol Sci 16: 275-279, 1995.
    • (1995) Trends Pharmacol Sci , vol.16 , pp. 275-279
    • De Vries, D.J.1    Beart, P.M.2
  • 2
    • 0031406964 scopus 로고    scopus 로고
    • Drugs from the sea: Harvesting the results of aeons of chemical evolution
    • Wallace RW: Drugs from the sea: harvesting the results of aeons of chemical evolution. Mol Med Today 3: 291-295, 1997.
    • (1997) Mol Med Today , vol.3 , pp. 291-295
    • Wallace, R.W.1
  • 3
    • 0030815582 scopus 로고    scopus 로고
    • New pharmaceuticals from marine organisms
    • Fenical W: New pharmaceuticals from marine organisms. Trends Biotechnol 15: 339-341, 1997.
    • (1997) Trends Biotechnol , vol.15 , pp. 339-341
    • Fenical, W.1
  • 4
    • 0036145807 scopus 로고    scopus 로고
    • Cytotoxic Cyplasin of the sea hare, Aplysia punctata, cDNA cloning, and expression of bioactive recombinants in insect cells
    • Petzelt C, Joswig G, Stammer H and Werner D: Cytotoxic Cyplasin of the sea hare, Aplysia punctata, cDNA cloning, and expression of bioactive recombinants in insect cells. Neoplasia 4: 49-59, 2002.
    • (2002) Neoplasia , vol.4 , pp. 49-59
    • Petzelt, C.1    Joswig, G.2    Stammer, H.3    Werner, D.4
  • 5
    • 0023568364 scopus 로고
    • Purification and characterization of aplysianin E, an antitumor factor from sea hare eggs
    • Kisugi J, Kamiya H and Yamazaki M: Purification and characterization of aplysianin E, an antitumor factor from sea hare eggs. Cancer Res 47: 5649-5653, 1987. (Pubitemid 18046761)
    • (1987) Cancer Research , vol.47 , Issue.21 , pp. 5649-5653
    • Kisugi, J.1    Kamiya, H.2    Yamazaki, M.3
  • 6
    • 0024382135 scopus 로고
    • Isolation and characterization of a novel cytolytic factor in purple fluid of the sea hare, Aplysia kurodai
    • Yamazaki M, Kimura K, Kisugi J, Muramoto K and Kamiya H: Isolation and characterization of a novel cytolytic factor in purple fluid of the sea hare, Aplysia kurodai. Cancer Res 49: 3834-3838, 1989. (Pubitemid 19197406)
    • (1989) Cancer Research , vol.49 , Issue.14 , pp. 3834-3838
    • Yamazaki, M.1    Kimura, K.2    Kisugi, J.3    Muramoto, K.4    Kamiya, H.5
  • 7
    • 0022469989 scopus 로고
    • Aplysianin-A, an antibacterial and antineoplastic glycoprotein in the albumen gland of a sea hare, Aplysia kurodai
    • Kamiya H, Muramoto K and Yamazaki M: Aplysianin A, an antibacterial and antineoplastic glycoprotein in the albumen gland of a sea hare, Aplysia kurodai. Experientia 42: 1065-1067, 1986. (Pubitemid 16030690)
    • (1986) Experientia , vol.42 , Issue.9 , pp. 1065-1067
    • Kamiya, H.1    Muramoto, K.2    Yamazaki, M.3
  • 8
    • 0024891110 scopus 로고
    • Purification and characterization of an antibacterial and antineoplastic protein secretion of a sea hare, Aplysia juliana
    • DOI 10.1016/0041-0101(89)90058-5
    • Kamiya H, Muramoto K, Goto R, Sakai M, Endo Y and Yamazaki M: Purification and characterization of an antibacterial and antineoplastic protein secretion of a sea hare, Aplysia Juliana. Toxicon 27: 1269-1277, 1989. (Pubitemid 20096660)
    • (1989) Toxicon , vol.27 , Issue.12 , pp. 1269-1277
    • Kamiya, H.1    Muramoto, K.2    Goto, R.3    Sakai, M.4    Endo, Y.5    Yamazaki, M.6
  • 9
    • 85011804640 scopus 로고
    • Characterization of an antibacterial and antineoplastic glycoprotein in a sea hare, Aplysia Juliana
    • Kamiya H, Muramoto K, Goto R and Yamazaki M: Characterization of an antibacterial and antineoplastic glycoprotein in a sea hare, Aplysia Juliana. Nippon Suisan Gakkaishi 54: 773-777, 1989.
    • (1989) Nippon Suisan Gakkaishi , vol.54 , pp. 773-777
    • Kamiya, H.1    Muramoto, K.2    Goto, R.3    Yamazaki, M.4
  • 10
    • 0024447989 scopus 로고
    • Purification and characterization of a cytolytic protein from purple fluid of the sea hare, Dolabella auricularia
    • Yamazaki M, Tansho S, Kisugi J, Muramoto K and Kamiya H: Purification and characterization of a cytolytic protein from purple fluid of the sea hare, Dolabella auricularia. Chem Pharm Bull 37: 2179-2182, 1989. (Pubitemid 19226536)
    • (1989) Chemical and Pharmaceutical Bulletin , vol.37 , Issue.8 , pp. 2179-2182
    • Yamazaki, M.1    Tansho, S.2    Kisugi, J.3    Muramoto, K.4    Kamiya, H.5
  • 11
    • 0000430008 scopus 로고
    • Purification of a novel cytolytic protein from albumen gland of the sea hare, Dolabella auricularia
    • Kisugi J, Yamazaki M, Tansho S, Muramoto K and Kamiya H: Purification of a novel cytolytic protein from albumen gland of the sea hare, Dolabella auricularia. Chem Pharm Bull 37: 2773-2781, 1989.
    • (1989) Chem Pharm Bull , vol.37 , pp. 2773-2781
    • Kisugi, J.1    Yamazaki, M.2    Tansho, S.3    Muramoto, K.4    Kamiya, H.5
  • 12
    • 0024406063 scopus 로고
    • Purification of dolabellanin-C an antineoplastic glycoprotein in the body fluid of a sea hare, Dolabella auricularia
    • DOI 10.1016/0145-305X(89)90010-4
    • Kisugi J, Kamiya H and Yamazaki M: Purification of dolabellanin-C, an antineoplastic glycoprotein in the body fluid of a sea hare, Dolabella auricularia. Dev Comp Immunol 13: 3-15, 1989. (Pubitemid 19198855)
    • (1989) Developmental and Comparative Immunology , vol.13 , Issue.1 , pp. 3-8
    • Kisugi, J.1    Kamiya, H.2    Yamazaki, M.3
  • 13
    • 0027194250 scopus 로고
    • Antitumor and antimicrobial glycoproteins from sea hares
    • Yamazaki M: Antitumor and antimicrobial glycoproteins from sea hares. Comp Biochem Physiol 105C: 141-146, 1993.
    • (1993) Comp Biochem Physiol , vol.105 C , pp. 141-146
    • Yamazaki, M.1
  • 15
    • 13844293531 scopus 로고
    • The anticancer research of extraction from Mercenaria
    • in Chinese
    • Chen HY, Cong XQ, Zhang A and Zhu JM: The anticancer research of extraction from Mercenaria. Cancer Res Prev Treat (in Chinese) 4: 3-7, 1980.
    • (1980) Cancer Res Prev Treat , vol.4 , pp. 3-7
    • Chen, H.Y.1    Cong, X.Q.2    Zhang, A.3    Zhu, J.M.4
  • 16
    • 13844270083 scopus 로고
    • Studies on anti-cancer activity of Meretrix Meretrix nucleic acid
    • in Chinese
    • Zhang JX and Xing YP: Studies on anti-cancer activity of Meretrix Meretrix nucleic acid. Oceanol Et Limnol (in Chinese) 21: 88-91, 1990.
    • (1990) Oceanol et Limnol , vol.21 , pp. 88-91
    • Zhang, J.X.1    Xing, Y.P.2
  • 17
    • 13844251382 scopus 로고    scopus 로고
    • An experimental study on the effects of Meretrix polysaccharide
    • in Chinese
    • Dou CH, Huang F, Huang LS, Li PZ and Xiao WD: An experimental study on the effects of Meretrix polysaccharide. J Marine Drugs (in Chinese) 2: 15-19, 1999.
    • (1999) J Marine Drugs , vol.2 , pp. 15-19
    • Dou, C.H.1    Huang, F.2    Huang, L.S.3    Li, P.Z.4    Xiao, W.D.5
  • 18
    • 13844261177 scopus 로고    scopus 로고
    • Inhibitory effects of anticancer peptide from Mercenaria on the BGC-823 cells and several enzymes
    • Leng B, Liu XD and Chen QX: Inhibitory effects of anticancer peptide from Mercenaria on the BGC-823 cells and several enzymes. FEBS Lett 579: 1187-1190, 2005.
    • (2005) FEBS Lett , vol.579 , pp. 1187-1190
    • Leng, B.1    Liu, X.D.2    Chen, Q.X.3
  • 19
    • 33744797374 scopus 로고    scopus 로고
    • Isolation and characterization of glycopeptide MGP0405 from Meretrix meretrix
    • in Chinese
    • Zhang B and Wu JL: Isolation and characterization of glycopeptide MGP0405 from Meretrix meretrix. Chin J Nat Med (in Chinese) 4: 230-233, 2006.
    • (2006) Chin J Nat Med , vol.4 , pp. 230-233
    • Zhang, B.1    Wu, J.L.2
  • 20
    • 70449418288 scopus 로고    scopus 로고
    • The antitumor activity of glycopeptide (MGP0501) from Meretrix meretrix in vitro
    • in Chinese
    • Wu JL, Zhang B, Huang CH, Zhu XC and Wu WT: The antitumor activity of glycopeptide (MGP0501) from Meretrix meretrix in vitro. Pharm Biotech (in Chinese) 13: 260-264, 2006.
    • (2006) Pharm Biotech , vol.13 , pp. 260-264
    • Wu, J.L.1    Zhang, B.2    Huang, C.H.3    Zhu, X.C.4    Wu, W.T.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the bacteriophage T4. Nature 227: 680-688, 1970.
    • (1970) Nature , vol.227 , pp. 680-688
    • Laemmli, U.K.1
  • 22
    • 29244447127 scopus 로고    scopus 로고
    • Contragestazol (DL111-IT) inhibits proliferation of human androgen-independent prostate cancer cell line PC3 in vitro and in vivo
    • DOI 10.1111/j.1745-7262.2005.00072.x
    • He QJ, Yang B, Lou YJ and Fang RY: Contragestazol (DL111-IT) inhibits proliferation of human androgen-independent prostate cancer cell line PC3 in vitro and in vivo. Asian J Androl 7: 389-393, 2005. (Pubitemid 41819353)
    • (2005) Asian Journal of Andrology , vol.7 , Issue.4 , pp. 389-393
    • He, Q.-J.1    Yang, B.2    Lou, Y.-J.3    Fang, R.-Y.4
  • 23
    • 0030746525 scopus 로고    scopus 로고
    • Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells
    • DOI 10.1016/S0304-4165(97)00024-X, PII S030441659700024X
    • Chen HM, Wang W, Smith D and Chan SC: Effects of the anti-bacterial peptide cecropin B and its analogs, cecropinsB-1 and B-2, on liposomes, bacteria and cancer cells. Biochim Biophys Acta 1336: 171-179, 1997. (Pubitemid 27364170)
    • (1997) Biochimica et Biophysica Acta - General Subjects , vol.1336 , Issue.2 , pp. 171-179
    • Chen, H.M.1    Wang, W.2    Smith, D.3    Chan, S.C.4
  • 24
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms and partial cDNA sequence of a precursor
    • Zasloff M: Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA 84: 5449-5453, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 25
    • 0027166016 scopus 로고
    • Anticancer efficacy of Magainin2 and analogue peptides
    • Baker MA, Maloy WL, Zasloff M and Jacob LS: Anticancer efficacy of Magainin2 and analogue peptides. Cancer Res 53: 3052-3057, 1993. (Pubitemid 23210311)
    • (1993) Cancer Research , vol.53 , Issue.13 , pp. 3052-3057
    • Baker, M.A.1    Maloy, W.L.2    Zasloff, M.3    Jacob, L.S.4
  • 27
    • 33744933929 scopus 로고    scopus 로고
    • Antitumor Activity of the Antimicrobial Peptide Magainin II against Bladder Cancer Cell Lines
    • DOI 10.1016/j.eururo.2005.12.043, PII S0302283805008687
    • Lehmann J, Retz M, Sidhu SS, Suttmann H, Sell M, Paulsen F, Harder J, Unteregger G and Stockle M: Antitumor activity of the antimicrobial peptide Magainin II against bladder cancer cell lines. Eur Urol 50: 141-147, 2006. (Pubitemid 43850110)
    • (2006) European Urology , vol.50 , Issue.1 , pp. 141-147
    • Lehmann, J.1    Retz, M.2    Sidhu, S.S.3    Suttmann, H.4    Sell, M.5    Paulsen, F.6    Harder, J.7    Unteregger, G.8    Stockle, M.9
  • 29
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • DOI 10.1038/292246a0
    • Steiner H, Hultmark D, Engström A, Bennich H and Boman HG: Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292: 246-248, 1981. (Pubitemid 11001840)
    • (1981) Nature , vol.292 , Issue.5820 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3
  • 30
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
    • DOI 10.1016/0005-2736(88)90069-7
    • Steiner H, Andreu D and Merrifield RB: Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim Biophys Acta 939: 60-66, 1988. (Pubitemid 18088775)
    • (1988) Biochimica et Biophysica Acta - Biomembranes , vol.939 , Issue.2 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 31
    • 0023712129 scopus 로고
    • The solution conformation of the antibacterial peptide cecropin A: A nuclear magnetic resonance and dynamical simulated annealing study
    • DOI 10.1021/bi00420a008
    • Holak TA, Engström A, Kraulis PJ, Lindeberg G, Bennich H, Jones TA, Gronenborn AM and Clore GM: The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27: 7620-7629, 1988. (Pubitemid 18247513)
    • (1988) Biochemistry , vol.27 , Issue.20 , pp. 7620-7629
    • Holak, T.A.1    Engstrom, A.2    Kraulis, P.J.3    Lindeberg, G.4    Bennich, H.5    Jones, T.A.6    Gronenborn, A.M.7    Clore, G.M.8
  • 32
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen B, Fink J, Merrifield RB and Mauzerall D: Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc Natl Acad Sci USA 85: 5072-5076, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 33
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger B: Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J Membr Biol 156: 197-211, 1997.
    • (1997) J Membr Biol , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 34
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman HG: Antibacterial peptides: basic facts and emerging concepts. J Intern Med 254: 197-215, 2003.
    • (2003) J Intern Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 35
    • 0028504387 scopus 로고
    • Preliminary experimental anticancer activity of cecropins
    • Moore AJ, Devine DA and Bibby MC: Preliminary experimental anticancer activity of cecropins. Pept Res 7: 265-269, 1994.
    • (1994) Pept Res , vol.7 , pp. 265-269
    • Moore, A.J.1    Devine, D.A.2    Bibby, M.C.3
  • 36
    • 0000378555 scopus 로고    scopus 로고
    • Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides
    • Shin SY, Lee MK, Kim KL and Hahm KS: Structure-antitumor and hemolytic activity relationships of synthetic peptides derived from cecropin A-magainin 2 and cecropin A-melittin hybrid peptides. J Pept Res 50: 279-285, 1997. (Pubitemid 27440877)
    • (1997) Journal of Peptide Research , vol.50 , Issue.4 , pp. 279-285
    • Shin, S.Y.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.-S.4
  • 37
    • 0032436788 scopus 로고    scopus 로고
    • Enhancement of the cytolytic effect of anti-bacterial cecropin by the microvilli of cancer cells
    • Chan SC, Hui L and Chen HM: Enhancement of the cytolytic effect of anti-bacterial cecropin by the microvilli of cancer cells. Anticancer Res 18: 4467-4474, 1998. (Pubitemid 29043678)
    • (1998) Anticancer Research , vol.18 , Issue.6 A , pp. 4467-4474
    • Chan, S.-C.1    Hui, L.2    Chen, H.M.3
  • 39
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y: Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim Biophys Acta 1462: 55-70, 1999.
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 40
    • 18544366816 scopus 로고    scopus 로고
    • Host defense peptides as new weapons in cancer treatment
    • DOI 10.1007/s00018-005-4560-2
    • Papo N and Shai Y: Host defense peptides as new weapons in cancer treatment. Cell Mol Life Sci 62: 784-790, 2005. (Pubitemid 40655628)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.7-8 , pp. 784-790
    • Papo, N.1    Shai, Y.2
  • 41
    • 0028818140 scopus 로고
    • Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers
    • Matsuzaki K, Murase O and Miyajima K: Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers. Biochemistry 34: 12553-12559, 1995.
    • (1995) Biochemistry , vol.34 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 43
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein G and Lecar H: Electrically gated ionic channels in lipid bilayers. Q Rev Biophys 10: 1-34, 1977. (Pubitemid 8065109)
    • (1977) Quarterly Reviews of Biophysics , vol.10 , Issue.1 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 44
    • 0021097003 scopus 로고
    • The orientation of melittin in lipid membranes: A polarized infrared spectroscopy study
    • Vogel H, Jahnig F, Hoffmann V and Stumpel J: The orientation of melittin in lipid membranes: a polarized infrared spectroscopy study. Biochim Biophys Acta 733: 201-209, 1983.
    • (1983) Biochim Biophys Acta , vol.733 , pp. 201-209
    • Vogel, H.1    Jahnig, F.2    Hoffmann, V.3    Stumpel, J.4
  • 45
    • 0036083301 scopus 로고    scopus 로고
    • Mechanism of action of antitumor drug that interact with microtubules and tubulin
    • Jordan MA: Mechanism of action of antitumor drug that interact with microtubules and tubulin. Curr Med Chem Anticancer Agents 2: 1-17, 2002.
    • (2002) Curr Med Chem Anticancer Agents , vol.2 , pp. 1-17
    • Jordan, M.A.1
  • 46
    • 0028018509 scopus 로고
    • Interaction of marine toxin dolastatin 10 with porcine brain tubulin: Competitive inhibition of rhizoxin and phomopsin a binding
    • DOI 10.1016/0009-2797(94)90018-3
    • Li Y, Kobayaski H, Hashimoto Y, Shirai R, Hirata A, Hayashi K, Hamada Y, Shiori T and Iwasaki S: Interaction of the marine toxin dolastatin 10 with porcine brain tubulin: competitive inhibition of rhizoxin and phomopsin A binding. Chem Biol Interact 93: 175-183, 1994. (Pubitemid 24290238)
    • (1994) Chemico-Biological Interactions , vol.93 , Issue.3 , pp. 175-183
    • Li, Y.1    Kobayashi, H.2    Hashimoto, Y.3    Shirai, R.4    Hirata, A.5    Hayashi, K.6    Hamada, Y.7    Shioiri, T.8    Iwasaki, S.9
  • 47
    • 0029039801 scopus 로고
    • Interaction of dolastatin 10 with tubulin: Induction of aggregation and binding and dissociation reactions
    • Bai R, Taylor GF, Schmidt JM, Williams MD, Kepler JA, Pettit GR and Hamel E: Interaction of dolastatin 10 with tubulin: induction of aggregation and binding and dissociation reactions. Mol Pharmacol 47: 965-976, 1995.
    • (1995) Mol Pharmacol , vol.47 , pp. 965-976
    • Bai, R.1    Taylor, G.F.2    Schmidt, J.M.3    Williams, M.D.4    Kepler, J.A.5    Pettit, G.R.6    Hamel, E.7
  • 48
    • 0031960723 scopus 로고    scopus 로고
    • Treatment of human prostate cancer cells with dolastatin 10, a peptide isolated from a marine shell-less mollusc
    • DOI 10.1002/(SICI)1097-0045(19980215)34:3<175::AID-PROS4>3.0.CO;2-H
    • Turner T, Jackson WH, Pettit GR, Wells A and Kraft AS: Treatment of human prostate cancer cells with Dolastatin 10, a peptide isolated from a marine shell-less mollusk. Prostate 34: 175-181, 1998. (Pubitemid 28156607)
    • (1998) Prostate , vol.34 , Issue.3 , pp. 175-181
    • Turner, T.1    Jackson, W.H.2    Pettit, G.R.3    Wells, A.4    Kraft, A.S.5
  • 49
    • 0029874514 scopus 로고    scopus 로고
    • Mechanism of action of cryptophycin
    • Smith CD and Zhang XQ: Mechanism of action of cryptophycin. J Biol Chem 271: 6192-6198, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 6192-6198
    • Smith, C.D.1    Zhang, X.Q.2
  • 50
    • 0028838082 scopus 로고
    • Current position of vinorelbine in cancer chemotherapy
    • Sorensen JB: Current position of vinorelbine in cancer chemotherapy. Ann Oncol 6: 105-107, 1995.
    • (1995) Ann Oncol , vol.6 , pp. 105-107
    • Sorensen, J.B.1
  • 51
    • 37249020371 scopus 로고    scopus 로고
    • Anti-mitotic activity of colchicine and the structural basis for its interaction with tubulin
    • DOI 10.1002/med.20097
    • Bhattacharyya B, Panda D, Gupta S and Banerjee M: Anti-mitotic activity of colchicine and the structural basis for its interaction with tubulin. Med Res Rev 28: 155-183, 2008. (Pubitemid 350274963)
    • (2008) Medicinal Research Reviews , vol.28 , Issue.1 , pp. 155-183
    • Bhattacharyya, B.1    Panda, D.2    Gupta, S.3    Banerjee, M.4
  • 52
    • 0025247903 scopus 로고
    • Apoptosis: The role of the endonuclease
    • Arends MJ, Morris RG and Wyllie AH: Apoptosis: the role of the endonuclease. Am J Pathol 136: 593-608, 1990.
    • (1990) Am J Pathol , vol.136 , pp. 593-608
    • Arends, M.J.1    Morris, R.G.2    Wyllie, A.H.3
  • 53
    • 0026761580 scopus 로고
    • A biochemical hallmark of apoptosis: Internucleosomal degradation of the genome
    • Compton MM: A biochemical hallmark of apoptosis: internucleosomal degradation of the genome. Cancer Metastasis Rev 11: 105-119, 1992.
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 105-119
    • Compton, M.M.1


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