메뉴 건너뛰기




Volumn 6, Issue 10, 2006, Pages 1433-1447

Drug target interaction of tubulin-binding drugs in cancer therapy

Author keywords

Colchicine; Interaction parameters; Microtubules; Taxol; Tubulin; Vinca alkaloids

Indexed keywords

ANTINEOPLASTIC AGENT; BETA TUBULIN; COLCEMEID; COLCHICINE; COLCHICINOID DERIVATIVE; COMBRETASTATIN; COMBRETASTATIN A4; CYCLOSTREPTIN; CYTOTOXIC AGENT; DICTYOSTATIN; DISCODERMOLIDE; DOCETAXEL; ELEUTHEROBIN; EPOTHILONE A; EPOTHILONE B; EPOTHILONE DERIVATIVE; ESTRADIOL DERIVATIVE; ETOPOSIDE; NAVELBINE; NOCODAZOLE; PACLITAXEL; PODOPHYLLOTOXIN; SARCODICTYIN A; SARCODICTYIN B; SULFONAMIDE; TACCALONOLIDE DERIVATIVE; TAXOID; TUBULIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VINCA ALKALOID;

EID: 33750701126     PISSN: 14737140     EISSN: 17448328     Source Type: Journal    
DOI: 10.1586/14737140.6.10.1433     Document Type: Review
Times cited : (30)

References (124)
  • 1
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • Jordan MA, Wilson L. Microtubules as a target for anticancer drugs. Nat. Rev. Cancer 4, 253-265 (2004).
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 2
    • 0036083301 scopus 로고    scopus 로고
    • Mechanism of action of antitumor drugs that interact with microtubules and tubulin
    • Jordan MA. Mechanism of action of antitumor drugs 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
  • 3
    • 0032710681 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics by drugs: A paradigm for the actions of cell regulators
    • Wilson L, Panda D, Jordan MA. Modulation of microtubule dynamics by drugs: a paradigm for the actions of cell regulators. Cell Struct. Funct. 24, 329-335 (1999).
    • (1999) Cell Struct. Funct. , vol.24 , pp. 329-335
    • Wilson, L.1    Panda, D.2    Jordan, M.A.3
  • 5
    • 0035422780 scopus 로고    scopus 로고
    • Multiple microtubule alterations are associated with vinca alkaloid resistance in human leukemia cells
    • Kavallaris M, Tait AS, Walsh BJ et al. Multiple microtubule alterations are associated with vinca alkaloid resistance in human leukemia cells. Cancer Res. 61, 5803-5809 (2001)
    • (2001) Cancer Res. , vol.61 , pp. 5803-5809
    • Kavallaris, M.1    Tait, A.S.2    Walsh, B.J.3
  • 6
    • 0345688612 scopus 로고    scopus 로고
    • Mechanisms of taxol resistance related to microtubules
    • Orr GA, Verdier-Pinard P, McDaid H, Horwitz SB. Mechanisms of taxol resistance related to microtubules Oncogene 22, 7280-7295 (2003).
    • (2003) Oncogene , vol.22 , pp. 7280-7295
    • Orr, G.A.1    Verdier-Pinard, P.2    McDaid, H.3    Horwitz, S.B.4
  • 7
    • 23444443007 scopus 로고    scopus 로고
    • Alterations of β-tubulin isotypes in breast cancer cells resistant to docetaxel
    • Shalli K, Brown I, Heys SD, Schofield AC. Alterations of β-tubulin isotypes in breast cancer cells resistant to docetaxel. FASEB J. 19, 1299-12301 (2005).
    • (2005) FASEB J. , vol.19 , pp. 1299-12301
    • Shalli, K.1    Brown, I.2    Heys, S.D.3    Schofield, A.C.4
  • 8
    • 0028169689 scopus 로고
    • 3′-(p-azidobenzamido)taxol photolabels - The N-terminal 31 amino acids of β-tubulin
    • Rao S, Krauss NE, Heerding JM et al. 3′-(p-azidobenzamido)taxol photolabels - the N-terminal 31 amino acids of β-tubulin. J. Biol. Cbem. 269, 3132-3134 (1994).
    • (1994) J. Biol. Cbem. , vol.269 , pp. 3132-3134
    • Rao, S.1    Krauss, N.E.2    Heerding, J.M.3
  • 9
    • 0028123221 scopus 로고
    • Synthesis of a photoaffinity taxol analogue and its use in labeling tubulin
    • Dasgupta D, Park H, Harriman GCB, Georg GI, Himes RH. Synthesis of a photoaffinity taxol analogue and its use in labeling tubulin. J. Med. Chem. 37, 2976-2980 (1994).
    • (1994) J. Med. Chem. , vol.37 , pp. 2976-2980
    • Dasgupta, D.1    Park, H.2    Harriman, G.C.B.3    Georg, G.I.4    Himes, R.H.5
  • 10
    • 0028178514 scopus 로고
    • Goeldner M. Predominant labeling of β- over α-tubulin from porcine brain by a photoactivatable taxoid derivative
    • Combeau C, Commercon A, Miskowski C, Rousseau B, Aubert F. Goeldner M. Predominant labeling of β- over α-tubulin from porcine brain by a photoactivatable taxoid derivative. Biochemistry 33, 6676-6683 (1994)
    • (1994) Biochemistry , vol.33 , pp. 6676-6683
    • Combeau, C.1    Commercon, A.2    Miskowski, C.3    Rousseau, B.4    Aubert, F.5
  • 11
    • 0029063397 scopus 로고
    • Structure of tubulin at 6.5A and location of the taxol-binding site
    • Nogales E, Wolf SG, Khan IA, Luduena RF, Downing KA. Structure of tubulin at 6.5A and location of the taxol-binding site. Nature 375, 424-427 (1995).
    • (1995) Nature , vol.375 , pp. 424-427
    • Nogales, E.1    Wolf, S.G.2    Khan, I.A.3    Luduena, R.F.4    Downing, K.A.5
  • 12
    • 0035111779 scopus 로고    scopus 로고
    • Taxanes in combined modality therapy for solid tumors
    • Choy H. Taxanes in combined modality therapy for solid tumors. Crit. Rev. Oncol. hematol. 37, 237-247 (2001).
    • (2001) Crit. Rev. Oncol. Hematol. , vol.37 , pp. 237-247
    • Choy, H.1
  • 13
    • 0027936036 scopus 로고
    • How taxol modulates microtubule disassembly
    • Caplow M, Shanks J. Ruhlen R. How taxol modulates microtubule disassembly. J. Biol. Chem. 269, 23399-23402 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 23399-23402
    • Caplow, M.1    Shanks, J.2    Ruhlen, R.3
  • 14
    • 28844499921 scopus 로고    scopus 로고
    • Microtubule interactions with chemically diverse stabilizing agents: Thermodynamics of binding to the paclitaxel site predicts cytotoxicity
    • Buey RM, Barasoain I, Jackson E et al. Microtubule interactions with chemically diverse stabilizing agents: thermodynamics of binding to the paclitaxel site predicts cytotoxicity. Chem. Biol. 12, 1269-1279 (2005).
    • (2005) Chem. Biol. , vol.12 , pp. 1269-1279
    • Buey, R.M.1    Barasoain, I.2    Jackson, E.3
  • 15
    • 0029123511 scopus 로고
    • Interaction of a fluorescent paclitaxel analogue with tubulin
    • Sengupta S, Boge TC, Georg GI, Himes RH. Interaction of a fluorescent paclitaxel analogue with tubulin. Biochemistry 34, 11889-11894 (1995).
    • (1995) Biochemistry , vol.34 , pp. 11889-11894
    • Sengupta, S.1    Boge, T.C.2    Georg, G.I.3    Himes, R.H.4
  • 16
    • 0020532762 scopus 로고
    • Taxol effect on tubulin polymerization and associated guanosine 5′-triphosphate hydrolysis
    • Carlier MF, Pantaloni D. Taxol effect on tubulin polymerization and associated guanosine 5′-triphosphate hydrolysis. Biochemistry 22, 4814-4822 (1983).
    • (1983) Biochemistry , vol.22 , pp. 4814-4822
    • Carlier, M.F.1    Pantaloni, D.2
  • 17
    • 10544253844 scopus 로고    scopus 로고
    • Interaction of a fluorescent derivative of paclitaxel (Taxol) with microtubules and tubulin-colchicine
    • Han Y. Chaudhary AG, Chordia MD et al. Interaction of a fluorescent derivative of paclitaxel (Taxol) with microtubules and tubulin-colchicine. Biochemistry 35, 14173-14183 (1996).
    • (1996) Biochemistry , vol.35 , pp. 14173-14183
    • Han, Y.1    Chaudhary, A.G.2    Chordia, M.D.3
  • 18
    • 0030955486 scopus 로고    scopus 로고
    • Probing the environment of tubulin-bound paclitaxel using fluorescent paclitaxel analogs
    • Sengupta S, Boge TC, Liu Y, Hepperle M, Georg GI, Himes RH. Probing the environment of tubulin-bound paclitaxel using fluorescent paclitaxel analogs. Biochemistry 36, 5179-5184 (1997).
    • (1997) Biochemistry , vol.36 , pp. 5179-5184
    • Sengupta, S.1    Boge, T.C.2    Liu, Y.3    Hepperle, M.4    Georg, G.I.5    Himes, R.H.6
  • 19
    • 0028348005 scopus 로고
    • Schotten-Baumann acylation of N-debenzoyltaxol: An efficient route to -acyl taxol analogs and their biological evaluation
    • Georg GI, Boge TC, Cheruvallath ZS et al. Schotten-Baumann acylation of N-debenzoyltaxol: an efficient route to -acyl taxol analogs and their biological evaluation. Bioorg. Med, Chem. Lett. 4, 335-338 (1994).
    • (1994) Bioorg. Med. Chem. Lett. , vol.4 , pp. 335-338
    • Georg, G.I.1    Boge, T.C.2    Cheruvallath, Z.S.3
  • 21
    • 17744396665 scopus 로고    scopus 로고
    • Docetaxel in patients with anthracycline-resistant advanced breast cancer
    • Vici P, Belli F, Lauro LD et al. Docetaxel in patients with anthracycline-resistant advanced breast cancer. Oncology 60, 60-65 (2001).
    • (2001) Oncology , vol.60 , pp. 60-65
    • Vici, P.1    Belli, F.2    Lauro, L.D.3
  • 22
    • 0029049468 scopus 로고
    • Epothilones, a new class of microtubule-stabilizing agents with a taxol-like mechanism of action
    • Bollag DM, McQueney PA, Zhu J et al. Epothilones, a new class of microtubule-stabilizing agents with a taxol-like mechanism of action. Cancer Res. 55, 2325-2333 (1995).
    • (1995) Cancer Res. , vol.55 , pp. 2325-2333
    • Bollag, D.M.1    McQueney, P.A.2    Zhu, J.3
  • 23
    • 1542380040 scopus 로고    scopus 로고
    • Interaction of epothilone analogs with the paclitaxel binding site: Relationship between binding affinity, microtubule stabilization, and cytotoxicity
    • Buey RM, Diaz JF, Andreu JM et al. Interaction of epothilone analogs with the paclitaxel binding site: relationship between binding affinity, microtubule stabilization, and cytotoxicity. Chem. Biol. 11, 225-236 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 225-236
    • Buey, R.M.1    Diaz, J.F.2    Andreu, J.M.3
  • 24
    • 0030039669 scopus 로고    scopus 로고
    • Discodermolicle, a cytotoxic marine agent that stabilizes microtubules more potently than taxol
    • ter Haar E, Kowaiski RJ, Hamel E et al. Discodermolicle, a cytotoxic marine agent that stabilizes microtubules more potently than taxol. Biochemistry 35, 243-250 (1996).
    • (1996) Biochemistry , vol.35 , pp. 243-250
    • ter Haar, E.1    Kowaiski, R.J.2    Hamel, E.3
  • 25
    • 0037832515 scopus 로고    scopus 로고
    • Synthesis and high content cell-based profiling of simplified analogs of the microtubule stabilizer (+)-discodermolide
    • Minguez JM, Giuliano KA, Balachandran R, Madiraju C, Curran DR, Day BW. Synthesis and high content cell-based profiling of simplified analogs of the microtubule stabilizer (+)-discodermolide. Mol. Cancer Therapeutics 1. 1305-1313 (2002).
    • (2002) Mol. Cancer Therapeutics , vol.1 , pp. 1305-1313
    • Minguez, J.M.1    Giuliano, K.A.2    Balachandran, R.3    Madiraju, C.4    Curran, D.R.5    Day, B.W.6
  • 27
    • 0016223474 scopus 로고
    • A controlled trial of colchicine in preventing attacks of familial mediterranean fever
    • Zemer D, Revach M, Pras M, Modan B, Schor S, Sohar E. A controlled trial of colchicine in preventing attacks of familial mediterranean fever. N. Engl. J. Med. 291, 932-934 (1974).
    • (1974) N. Engl. J. Med. , vol.291 , pp. 932-934
    • Zemer, D.1    Revach, M.2    Pras, M.3    Modan, B.4    Schor, S.5    Sohar, E.6
  • 29
    • 14644386838 scopus 로고    scopus 로고
    • -NH-dansyl isocolchicine exhibits a significantly improved tubulin-binding affinity and microtubule inhibition in comparison to isocolchicine by binding tubulin through its A and B rings
    • Das L, Datta AB, Cupta S et al, -NH-dansyl isocolchicine exhibits a significantly improved tubulin-binding affinity and microtubule inhibition in comparison to isocolchicine by binding tubulin through its A and B rings. Biochemisty 44, 3249-3258 (2005).
    • (2005) Biochemisty , vol.44 , pp. 3249-3258
    • Das, L.1    Datta, A.B.2    Cupta, S.3
  • 30
    • 34547205120 scopus 로고
    • Brossi A, (Ed.). Academic Press, New York, USA
    • Capraro HG, Brossi A. The Alkaloids. Brossi A, (Ed.). Academic Press, New York, USA, 1-70 (1984).
    • (1984) The Alkaloids , pp. 1-70
    • Capraro, H.G.1    Brossi, A.2
  • 31
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin like domain
    • Ravelli RBG, Cigant B, Curmi PA et al. Insight into tubulin regulation from a complex with colchicine and a stathmin like domain. Nature 428, 198-202 (2004).
    • (2004) Nature , vol.428 , pp. 198-202
    • Ravelli, R.B.G.1    Cigant, B.2    Curmi, P.A.3
  • 33
    • 0019426065 scopus 로고
    • Biological effects or modified colchicines. Improved preparation of 2-demethylcolchicine, 3-demethylcolchicine, and (+)-colchicine and reassignment of the position of the double bond in dehydro-7-deacetamidocolchicines
    • Rosner M, Capraro HG, Jacobson AE et al. Biological effects or modified colchicines. Improved preparation of 2-demethylcolchicine, 3-demethylcolchicine, and (+)-colchicine and reassignment of the position of the double bond in dehydro-7-deacetamidocolchicines. J. Med. Chem. 24, 257-261 (1981).
    • (1981) J. Med. Chem. , vol.24 , pp. 257-261
    • Rosner, M.1    Capraro, H.G.2    Jacobson, A.E.3
  • 35
    • 0019487051 scopus 로고
    • Role of B-ring of colchicine in its binding to tubulin
    • Ray K, Bhattacharyya B, Biswas BB. Role of B-ring of colchicine in its binding to tubulin. J. Biol. Chem. 256, 6241-6244 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 6241-6244
    • Ray, K.1    Bhattacharyya, B.2    Biswas, B.B.3
  • 36
    • 0030050334 scopus 로고    scopus 로고
    • Thermodynamics of colchicinoids-tubulin interactions, role of B-ring and C-7 substituent
    • Chakrabarti G, Sengupta S, Bhattacharyya B. Thermodynamics of colchicinoids-tubulin interactions, role of B-ring and C-7 substituent. J. Biol. Chem. 271, 2897-2901 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 2897-2901
    • Chakrabarti, G.1    Sengupta, S.2    Bhattacharyya, B.3
  • 37
    • 0025759015 scopus 로고
    • Kinetics of dissociation of the tubulin-colchicine complex
    • Diaz JF, Andreu JM. Kinetics of dissociation of the tubulin-colchicine complex. J. Biol. Chem. 266, 2883-2889 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 2883-2889
    • Diaz, J.F.1    Andreu, J.M.2
  • 38
    • 0021235143 scopus 로고
    • Binding to tubulin of the colchicine analog 2-methoxy-5-(2′,3′,4′-trimethoxyphenyl)tropone: Thermodynamic and kinetic aspects
    • Bane S, Puett D, MacDonald TL, Williams RC Jr. Binding to tubulin of the colchicine analog 2-methoxy-5-(2′,3′,4′-trimethoxyphenyl)tropone: thermodynamic and kinetic aspects. J. Biol. Chem. 259, 7391-7398 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 7391-7398
    • Bane, S.1    Puett, D.2    MacDonald, T.L.3    Williams Jr., R.C.4
  • 40
    • 0018186529 scopus 로고
    • Kinetics and mechanism of colchicine binding to tubulin: Evidence for ligand-induced conformational change
    • Garland DL. Kinetics and mechanism of colchicine binding to tubulin: evidence for ligand-induced conformational change. Biochemistry 17, 4266-4272 (1978).
    • (1978) Biochemistry , vol.17 , pp. 4266-4272
    • Garland, D.L.1
  • 41
    • 0019856315 scopus 로고
    • Changes in the circular dichroic spectrum of colchicine associated with its binding to tubulin
    • Detrich HW III, Williams RC Jr, Macdonald TL, Wilson L, Puett D. Changes in the circular dichroic spectrum of colchicine associated with its binding to tubulin. Biochemistry 20, 5999-6005 (1981).
    • (1981) Biochemistry , vol.20 , pp. 5999-6005
    • Detrich III, H.W.1    Williams Jr., R.C.2    Macdonald, T.L.3    Wilson, L.4    Puett, D.5
  • 42
    • 0020422990 scopus 로고
    • Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin
    • Andreu JM, Timasheff SN. Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin. Biochemistry 21, 6465-6476 (1982).
    • (1982) Biochemistry , vol.21 , pp. 6465-6476
    • Andreu, J.M.1    Timasheff, S.N.2
  • 43
    • 0008891824 scopus 로고
    • Promotion of Fluorescence upon binding of colchicine to tubulin
    • Bhatacharyya B, Wolff J. Promotion of Fluorescence upon binding of colchicine to tubulin. Proc. Natl Acad. Sci. USA 71, 2627-2631 (1974).
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 2627-2631
    • Bhatacharyya, B.1    Wolff, J.2
  • 44
    • 0026645572 scopus 로고
    • Kinetics of colchicine binding to purified β-tubulin isotypes from bovine brain
    • Banerjee A, Luduena RF. Kinetics of colchicine binding to purified β-tubulin isotypes from bovine brain. J. Biol. Chem. 267, 13335-13339 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 13335-13339
    • Banerjee, A.1    Luduena, R.F.2
  • 45
    • 0028290817 scopus 로고
    • Interaction of desacetamido-colchicine, a fast binding analogue of colchicine with isotypically pure tubulin dimers α β II, a β III, and 2a β IV
    • Banerjee A, D'Hoore A, Enjelborghs Y. Interaction of desacetamido-colchicine, a fast binding analogue of colchicine with isotypically pure tubulin dimers α β II, a β III, and 2a β IV. J. Biol. Chem. 269, 10324-10329 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 10324-10329
    • Banerjee, A.1    D'Hoore, A.2    Enjelborghs, Y.3
  • 46
    • 0024502909 scopus 로고
    • The binding of isocolchicine to tubulin. Mechanisms of ligand association with tubulin
    • Hastie SB, Puett D, Mcdonald TL, Williams RC Jr. The binding of isocolchicine to tubulin. Mechanisms of ligand association with tubulin J. Biol. Chem. 264, 6682-6688 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 6682-6688
    • Hastie, S.B.1    Puett, D.2    Mcdonald, T.L.3    Williams Jr., R.C.4
  • 47
    • 0034054690 scopus 로고    scopus 로고
    • NBD-isocolcemid-tubulin interaction: A novel one-step reaction involving no conformational adjustment of reactants
    • Sengupta S, Banerjee S, Chakrabarti G, Mahapatra PK, Roy S, Bhattacharya B. NBD-isocolcemid-tubulin interaction: a novel one-step reaction involving no conformational adjustment of reactants. Biochemistry 39, 2227-2234 (2000)
    • (2000) Biochemistry , vol.39 , pp. 2227-2234
    • Sengupta, S.1    Banerjee, S.2    Chakrabarti, G.3    Mahapatra, P.K.4    Roy, S.5    Bhattacharya, B.6
  • 49
    • 0442309863 scopus 로고    scopus 로고
    • Cytotoxicity of in vitro produced podophyllotoxin from Podophyllum bexandrum on human cancer cell line
    • Chattopadhyay S, Bisaria VS, Panda AK, Srivastava AK. Cytotoxicity of in vitro produced podophyllotoxin from Podophyllum bexandrum on human cancer cell line. Nat. Prod. Res. 18, 51-57 (2004).
    • (2004) Nat. Prod. Res. , vol.18 , pp. 51-57
    • Chattopadhyay, S.1    Bisaria, V.S.2    Panda, A.K.3    Srivastava, A.K.4
  • 50
    • 0017344821 scopus 로고
    • Poclophyllotoxin as a probe for the colchicine binding site of tubulin
    • Cortese F, Bhattacharyya B, Wolff J. Poclophyllotoxin as a probe for the colchicine binding site of tubulin. J. BioI. Chem. 252, 1134-1140 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 1134-1140
    • Cortese, F.1    Bhattacharyya, B.2    Wolff, J.3
  • 51
    • 33646856607 scopus 로고    scopus 로고
    • Oxalone and lactone moieties of poclophyllotoxin exhibit properties of both the B and C rings of colchicine in its binding with tubulin
    • Gupta S, Das L, Datta AB, Poddar A, Janik ME, Bhattacharyya B. Oxalone and lactone moieties of poclophyllotoxin exhibit properties of both the B and C rings of colchicine in its binding with tubulin. Biochemistry 45, 6467-6475 (2006).
    • (2006) Biochemistry , vol.45 , pp. 6467-6475
    • Gupta, S.1    Das, L.2    Datta, A.B.3    Poddar, A.4    Janik, M.E.5    Bhattacharyya, B.6
  • 52
    • 0026744399 scopus 로고
    • Preparation and antitumor activity of 2″-O-, 3″ O- and 2″,3″ -di-O- substituted derivatives of etoposide
    • Ohnuma T, Obata R, Nishiyama Y et al. Preparation and antitumor activity of 2″-O-, 3″ O- and 2″,3″ -di-O- substituted derivatives of etoposide. Chem. Pharm. Bull. 40, 1783-1788 (1992).
    • (1992) Chem. Pharm. Bull. , vol.40 , pp. 1783-1788
    • Ohnuma, T.1    Obata, R.2    Nishiyama, Y.3
  • 54
    • 31544436860 scopus 로고    scopus 로고
    • Efficacy of vincristine and etoposide with escalating cyclophosphamide in poor-prognosis pediatric brain tumors
    • Ziegler DS, Cohn RJ, McCowage G et al. Efficacy of vincristine and etoposide with escalating cyclophosphamide in poor-prognosis pediatric brain tumors. Neuro-oncology 8, 53-59 (2006).
    • (2006) Neuro-oncology , vol.8 , pp. 53-59
    • Ziegler, D.S.1    Cohn, R.J.2    McCowage, G.3
  • 55
    • 0024339336 scopus 로고
    • Podophyllotoxin analogs: Effects on DNA topoisomerase II, tubulin polymerization, human tumor KB cells, and their VP-16-resistant variants
    • Liu SY, Hwang BD, Haruna M, Imakura Y, Lee KH, Cheng YC. Podophyllotoxin analogs: effects on DNA topoisomerase II, tubulin polymerization, human tumor KB cells, and their VP-16-resistant variants. Mol. Pbarmacol. 36, 78-82 (1989).
    • (1989) Mol. Pbarmacol. , vol.36 , pp. 78-82
    • Liu, S.Y.1    Hwang, B.D.2    Haruna, M.3    Imakura, Y.4    Lee, K.H.5    Cheng, Y.C.6
  • 56
    • 0031552141 scopus 로고    scopus 로고
    • Antitumor agents 177. Design, synthesis, and biological evaluation of novel etoposide analogs bearing pyrrolecarboxamidino group as DNA topoisomerase II inhibitors
    • Ji Z, Wang HK, Bastow KF et al. Antitumor agents 177. Design, synthesis, and biological evaluation of novel etoposide analogs bearing pyrrolecarboxamidino group as DNA topoisomerase II inhibitors. Bioorg. Med. Chem. Lett. 7, 607-612 (1997).
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 607-612
    • Ji, Z.1    Wang, H.K.2    Bastow, K.F.3
  • 57
    • 0017276478 scopus 로고
    • The effects of methyl (5-(2-thienylcarbonyl)-1H-benzimidazol-2-yl) carbamate, (R 17934; NSC 238159), a new synthetic antitumoral drug interfering with microtubutes, on mammalian cells cultured in vitro
    • DeBrabander M, Van de Veine R, Aerts F, Geuens G, Borgers M, Janssen PAJ. The effects of methyl (5-(2-thienylcarbonyl)-1H-benzimidazol-2-yl) carbamate, (R 17934; NSC 238159), a new synthetic antitumoral drug interfering with microtubutes, on mammalian cells cultured in vitro. Cancer Res. 36, 905-916 (1976).
    • (1976) Cancer Res. , vol.36 , pp. 905-916
    • DeBrabander, M.1    Van de Veine, R.2    Aerts, F.3    Geuens, G.4    Borgers, M.5    Janssen, P.A.J.6
  • 58
    • 0022214871 scopus 로고
    • Equilibrium and rapid kinetic studies on nocodazole-tubulin interaction
    • Head J, Lee LL, Field DJ, Lee JC. Equilibrium and rapid kinetic studies on nocodazole-tubulin interaction. J. Biol. Chem. 260, 11060-11066 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 11060-11066
    • Head, J.1    Lee, L.L.2    Field, D.J.3    Lee, J.C.4
  • 59
    • 0018162381 scopus 로고
    • Interaction of antihelminthic benzimidazole and benzimidazole derivatives with bovine brain tubulin
    • Friedman PA, Platzer EG. Interaction of antihelminthic benzimidazole and benzimidazole derivatives with bovine brain tubulin. Biochim. Biophys. Acta 554, 605-614 (1978).
    • (1978) Biochim. Biophys. Acta , vol.554 , pp. 605-614
    • Friedman, P.A.1    Platzer, E.G.2
  • 60
    • 0036240628 scopus 로고    scopus 로고
    • Interaction of nocodazole with tubulin isotypes
    • Xu K, Schwarz PM, Ludueña RF. Interaction of nocodazole with tubulin isotypes. Drug Dev. Res. 55, 91-96 (2002).
    • (2002) Drug Dev. Res. , vol.55 , pp. 91-96
    • Xu, K.1    Schwarz, P.M.2    Ludueña, R.F.3
  • 61
    • 0019833086 scopus 로고
    • Effects of inhibitors of tubulin polymerization on GTP hydrolysis
    • Lin CM, Hamel E. Effects of inhibitors of tubulin polymerization on GTP hydrolysis. J. Biol. Chem. 256, 9242-9246 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 9242-9246
    • Lin, C.M.1    Hamel, E.2
  • 62
    • 0019276123 scopus 로고
    • Effects of nocodazole on structures of calf brain tubulin
    • Lee JC, Field DJ, Lee LLY. Effects of nocodazole on structures of calf brain tubulin. Biochemistry 19, 6209-6215 (1980).
    • (1980) Biochemistry , vol.19 , pp. 6209-6215
    • Lee, J.C.1    Field, D.J.2    Lee, L.L.Y.3
  • 64
    • 0030756156 scopus 로고    scopus 로고
    • Mechanism of action of E7010, an orally active sulfonamide antitumor agent: Inhibition of mitosis by binding to the colchicine site of tubulin
    • Yoshimatsu K, Yamaguchi A, Yoshino H, Koyanagi N, Kitoh K. Mechanism of action of E7010, an orally active sulfonamide antitumor agent: inhibition of mitosis by binding to the colchicine site of tubulin. Cancer Res. 57, 3208-3213 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 3208-3213
    • Yoshimatsu, K.1    Yamaguchi, A.2    Yoshino, H.3    Koyanagi, N.4    Kitoh, K.5
  • 65
    • 13044294012 scopus 로고    scopus 로고
    • Selective, covalent modification of β-tubulin residue Cys-239 by T138067, an antitumor agent with in vivo efficacy against multidrug-resistant tumors
    • Shan B, Medina JC, Santha E et al. Selective, covalent modification of β-tubulin residue Cys-239 by T138067, an antitumor agent with in vivo efficacy against multidrug-resistant tumors. Proc. Natl Acad. Sei. USA 92, 5686-5691 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5686-5691
    • Shan, B.1    Medina, J.C.2    Santha, E.3
  • 67
    • 20944447321 scopus 로고    scopus 로고
    • Phase 2 study of T138067-sodium in patients with malignant glioma: Trial of the National Cancer Institute of the Canada clinical trials group
    • Kirby S, Gertler SZ, Mason W et al. Phase 2 study of T138067-sodium in patients with malignant glioma: trial of the National Cancer Institute of the Canada clinical trials group. Neuro-oncology 7, 183-188 (2005).
    • (2005) Neuro-oncology , vol.7 , pp. 183-188
    • Kirby, S.1    Gertler, S.Z.2    Mason, W.3
  • 68
    • 12344326693 scopus 로고    scopus 로고
    • Sulfonamide drugs binding to the colchicine site of tubulin: Thermodynamic analysis of the drug-tubutin interactions by isothermal titration calorimetry
    • Banerjee M, Poddar A, Mitra G, Surolia A, Owa T, Bhattacharyya B. Sulfonamide drugs binding to the colchicine site of tubulin: thermodynamic analysis of the drug-tubutin interactions by isothermal titration calorimetry. J. Med. Chem. 48, 547-555 (2005).
    • (2005) J. Med. Chem. , vol.48 , pp. 547-555
    • Banerjee, M.1    Poddar, A.2    Mitra, G.3    Surolia, A.4    Owa, T.5    Bhattacharyya, B.6
  • 69
    • 0024427745 scopus 로고
    • Antimitotic natural products combretastatin A-4 and combretastatin A-2: Studies on the mechanism of their inhibition of the binding of colchicine to tubulin
    • Lin CM, Ho HH, Pettit GR, Hamel E. Antimitotic natural products combretastatin A-4 and combretastatin A-2: studies on the mechanism of their inhibition of the binding of colchicine to tubulin. Biochemistry 28, 6984-6991 (1989).
    • (1989) Biochemistry , vol.28 , pp. 6984-6991
    • Lin, C.M.1    Ho, H.H.2    Pettit, G.R.3    Hamel, E.4
  • 70
    • 0346433524 scopus 로고    scopus 로고
    • Combrelastatins: From natural products to drug discovery
    • Cirla A, Mann J. Combrelastatins: from natural products to drug discovery Nat. Prod. Rep. 20, 558-564 (2003).
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 558-564
    • Cirla, A.1    Mann, J.2
  • 71
    • 0031980124 scopus 로고    scopus 로고
    • Antineoplastic agents 389. New syntheses of the combretastatin A-4 prodrug
    • Pettit GR, Rhodes MR. Antineoplastic agents 389. New syntheses of the combretastatin A-4 prodrug. Anticancer Drug Des. 13, 183-191 (1998).
    • (1998) Anticancer Drug Des. , vol.13 , pp. 183-191
    • Pettit, G.R.1    Rhodes, M.R.2
  • 72
    • 0033065833 scopus 로고    scopus 로고
    • Positron emission tomography of murine liver metastases and the effects of treatment by combretastatin A-4
    • Zhao S, Moore JV, Waller ML et al. Positron emission tomography of murine liver metastases and the effects of treatment by combretastatin A-4. Eur. J. Nuclear Med. 26, 231-238 (1999).
    • (1999) Eur. J. Nuclear Med. , vol.26 , pp. 231-238
    • Zhao, S.1    Moore, J.V.2    Waller, M.L.3
  • 73
    • 0035262598 scopus 로고    scopus 로고
    • Targeting tumour vasculature: The development of combretastatin A4
    • Griggs J, Metcalfe JC, Hesketh R. Targeting tumour vasculature: the development of combretastatin A4. Lancet Oncol. 2, 82-87 (2001).
    • (2001) Lancet Oncol. , vol.2 , pp. 82-87
    • Griggs, J.1    Metcalfe, J.C.2    Hesketh, R.3
  • 74
    • 0034594647 scopus 로고    scopus 로고
    • Indanocine, a microtubule-binding Indanone and a selective inducer Of apoptosis in multidrug-resistant cancer cells
    • Leoni LM, Hamel E, Genini D et al. Indanocine, a microtubule-binding Indanone and a selective inducer Of apoptosis in multidrug-resistant cancer cells. J. Natl Cancer Inst. 92, 217-220 (2000).
    • (2000) J. Natl Cancer Inst. , vol.92 , pp. 217-220
    • Leoni, L.M.1    Hamel, E.2    Genini, D.3
  • 75
    • 0036606778 scopus 로고    scopus 로고
    • 2-aroylindoles, a novel class of potent, orally active small molecule tubulin inhibitors
    • Beckers T, Reissmann T, Schmidt M et al. 2-aroylindoles, a novel class of potent, orally active small molecule tubulin inhibitors. Cancer Res. 62, 3113-3119 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 3113-3119
    • Beckers, T.1    Reissmann, T.2    Schmidt, M.3
  • 76
    • 0028295948 scopus 로고
    • Antitumour agents 150. 2′3′4′5′5 6 7-substituted 2-phenyl-4quinolones and related compounds: Their synthesis, cytotoxicity and inhibition of tubulin polymerisation
    • Li L, Wang HK, Kuo SC et al. Antitumour agents 150. 2′3′4′5′5 6 7-substituted 2-phenyl-4quinolones and related compounds: their synthesis, cytotoxicity and inhibition of tubulin polymerisation. J. Med. Cbem. 37, 1126-1135 (1994).
    • (1994) J. Med. Cbem. , vol.37 , pp. 1126-1135
    • Li, L.1    Wang, H.K.2    Kuo, S.C.3
  • 78
    • 30544450012 scopus 로고    scopus 로고
    • 4-Amino-5-benzoyl-2-(4-methoxyphenylamino)thiazole (DATl): A cytotoxic agent towards cancer cells and a probe for tubulin-microtubule system
    • Sengupta S, Smitha SL, Nisha ET et al. 4-Amino-5-benzoyl-2-(4-methoxyphenylamino)thiazole (DATl): a cytotoxic agent towards cancer cells and a probe for tubulin-microtubule system. Br. J. Pharmacol. 145, 1076-1083 (2005).
    • (2005) Br. J. Pharmacol. , vol.145 , pp. 1076-1083
    • Sengupta, S.1    Smitha, S.L.2    Nisha, E.T.3
  • 79
    • 10744223288 scopus 로고    scopus 로고
    • Oral vinorelbine in combination with cisplatin: A novel active regimen in advanced non-small-cell lung cancer
    • Jassem J, Kosmidis P, Ramlau R et al. Oral vinorelbine in combination with cisplatin: a novel active regimen in advanced non-small-cell lung cancer. Ann. Oncol. 14, 1634-1639 (2003).
    • (2003) Ann. Oncol. , vol.14 , pp. 1634-1639
    • Jassem, J.1    Kosmidis, P.2    Ramlau, R.3
  • 80
    • 12444269637 scopus 로고    scopus 로고
    • Single agent vinorelbine as first-line chemotherapy in elderly patients with advanced breast cancer
    • Rossi A, Gridelli C, Gebbia V et al. Single agent vinorelbine as first-line chemotherapy in elderly patients with advanced breast cancer. Anticancer Res. 23, 1657-1664 (2003).
    • (2003) Anticancer Res. , vol.23 , pp. 1657-1664
    • Rossi, A.1    Gridelli, C.2    Gebbia, V.3
  • 82
    • 0036021714 scopus 로고    scopus 로고
    • Vinorelbine plus cisplatin versus cisplatin plus vindesine and mitomycin C in stage IIIB-IV non-small cell lung carcinoma: A prospective randomized study
    • Gebbia V, Galletta D, Riccardi F et al. Vinorelbine plus cisplatin versus cisplatin plus vindesine and mitomycin C in stage IIIB-IV non-small cell lung carcinoma: a prospective randomized study. Lung Cancer 37, 179-187 (2002).
    • (2002) Lung Cancer , vol.37 , pp. 179-187
    • Gebbia, V.1    Galletta, D.2    Riccardi, F.3
  • 83
    • 19544393159 scopus 로고    scopus 로고
    • Structural basis for the regulation of tubulin by vinblastine
    • Gigant B, Wang C, Ravelli RBG et al. Structural basis for the regulation of tubulin by vinblastine. Nature 435, 519-522 (2005).
    • (2005) Nature , vol.435 , pp. 519-522
    • Gigant, B.1    Wang, C.2    Ravelli, R.B.G.3
  • 84
    • 17544366715 scopus 로고    scopus 로고
    • Localization of the vinblastine-binding site on β-tubulin
    • Rai SS, Wolff J. Localization of the vinblastine-binding site on β-tubulin. J. Biol. Chem. 271, 14707-14711 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 14707-14711
    • Rai, S.S.1    Wolff, J.2
  • 85
    • 0017164513 scopus 로고
    • Tubulin aggregation and disaggregation: Mediation by two distinct vinblastine-binding sites
    • Bhattacharyya B, Wolff J. Tubulin aggregation and disaggregation: mediation by two distinct vinblastine-binding sites. Proc. Natl Acad. Sci. USA 73, 2375-2378 (1976)
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2375-2378
    • Bhattacharyya, B.1    Wolff, J.2
  • 86
    • 0018197941 scopus 로고
    • H-labeled vinblastine binding to vinblastine-tubulin crystals
    • H-labeled vinblastine binding to vinblastine-tubulin crystals. J. Mol. Biol. 121, 255-264 (1978).
    • (1978) J. Mol. Biol. , vol.121 , pp. 255-264
    • Wilson, L.1    Morse, A.N.C.2
  • 87
    • 0014937571 scopus 로고
    • Properties of colchicine binding protein from chick embryo brain. Interactions with vinca alkaloids and podophyllotoxin
    • Wilson L. Properties of colchicine binding protein from chick embryo brain. Interactions with vinca alkaloids and podophyllotoxin. Biochemistry 9, 4999-5007 (1970).
    • (1970) Biochemistry , vol.9 , pp. 4999-5007
    • Wilson, L.1
  • 88
    • 0020404591 scopus 로고
    • In vitro vinblastine-induced tubulin paracrystals
    • Na GC, Timasheff SN. In vitro vinblastine-induced tubulin paracrystals. J. Biol. Chem. 257, 10387-10391 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 10387-10391
    • Na, G.C.1    Timasheff, S.N.2
  • 89
    • 0034601812 scopus 로고    scopus 로고
    • Vinca alkaloid-induced tubulin spiral formation correlates with cytotoxicity in the leukemic L1210 cell line
    • Lobert S, Fahy J, Hill BT Duflos S, Etievant C, Correia JJ. Vinca alkaloid-induced tubulin spiral formation correlates with cytotoxicity in the leukemic L1210 cell line. Biochemistry 39, 12053-12062 (2000).
    • (2000) Biochemistry , vol.39 , pp. 12053-12062
    • Lobert, S.1    Fahy, J.2    Hill, B.T.3    Duflos, S.4    Etievant, C.5    Correia, J.J.6
  • 90
    • 0030008570 scopus 로고    scopus 로고
    • Interaction of vinca alkaloids with tubulin: A comparison of vinblastine, vincristine, and vinorelbine
    • Lobert S, Vulevic B, Correia JJ. Interaction of vinca alkaloids with tubulin: a comparison of vinblastine, vincristine, and vinorelbine. Biochemistry 35, 6806-6814 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6806-6814
    • Lobert, S.1    Vulevic, B.2    Correia, J.J.3
  • 91
    • 0029020164 scopus 로고
    • Binding of vinblastine to phosphocellulose-purified and α β-class III tubulin: The role of nucleotides and β-tubulin isotypes
    • Lobert S, Frankfurter A, Correia JJ. Binding of vinblastine to phosphocellulose-purified and α β-class III tubulin: the role of nucleotides and β-tubulin isotypes. Biochemistry 34, 8050-8060 (1995).
    • (1995) Biochemistry , vol.34 , pp. 8050-8060
    • Lobert, S.1    Frankfurter, A.2    Correia, J.J.3
  • 93
    • 0022453641 scopus 로고
    • Identification of a distinct class of vinblastine binding sites on microtubules
    • Jordan MA, Margoli RL, Himes RH, Wilson L. Identification of a distinct class of vinblastine binding sites on microtubules. J. Mol. Biol. 187, 61-73 (1986).
    • (1986) J. Mol. Biol. , vol.187 , pp. 61-73
    • Jordan, M.A.1    Margoli, R.L.2    Himes, R.H.3    Wilson, L.4
  • 94
    • 0025352537 scopus 로고
    • Dolastatin 10, a powerful cytostatic peptide derived from a marine animal. Inhibition of tubulin polymerization mediated through the vinca alkaloid binding domain
    • Bai RL, Pettit GR, Hamel E. Dolastatin 10, a powerful cytostatic peptide derived from a marine animal. Inhibition of tubulin polymerization mediated through the vinca alkaloid binding domain. Biochem. Pharmacol. 39, 1941-1949 (1990).
    • (1990) Biochem. Pharmacol. , vol.39 , pp. 1941-1949
    • Bai, R.L.1    Pettit, G.R.2    Hamel, E.3
  • 95
    • 0642272506 scopus 로고    scopus 로고
    • Biological activity of A-289099: An orally active tubulin-binding indolyloxazoline derivative
    • Tahir SK, Nukkala MA, Mozny NAZ et al. Biological activity of A-289099: an orally active tubulin-binding indolyloxazoline derivative. Mol. Cancer Therapeutics 2, 227-233 (2003).
    • (2003) Mol. Cancer Therapeutics , vol.2 , pp. 227-233
    • Tahir, S.K.1    Nukkala, M.A.2    Mozny, N.A.Z.3
  • 96
    • 0032482920 scopus 로고    scopus 로고
    • Antiproliferative mechanism of action of cryptophycin-52: Kinetic stabilization of microtubule dynamics by high-affinity binding to microtubule ends
    • Panda D, DeLuca K, Williams D, Jordan MA, Wilson L. Antiproliferative mechanism of action of cryptophycin-52: kinetic stabilization of microtubule dynamics by high-affinity binding to microtubule ends. Proc. Natl Acad. Sci. USA 95, 9313-9318 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9313-9318
    • Panda, D.1    DeLuca, K.2    Williams, D.3    Jordan, M.A.4    Wilson, L.5
  • 97
    • 33750736164 scopus 로고    scopus 로고
    • Phase II trial of weekly docetaxel (D) and complete androgen blockade (CAB) prior to radical prostatectomy (RP) in high-risk localized prostate cancer (PC) patients (pts)
    • Mellado B, Font A, Aparicio LA et al. Phase II trial of weekly docetaxel (D) and complete androgen blockade (CAB) prior to radical prostatectomy (RP) in high-risk localized prostate cancer (PC) patients (pts). J. Clin. Oncol. 24, 14515 (2006).
    • (2006) J. Clin. Oncol. , vol.24 , pp. 14515
    • Mellado, B.1    Font, A.2    Aparicio, L.A.3
  • 98
    • 33645352797 scopus 로고    scopus 로고
    • A multicenter Phase II study of the cryptophycin analog LY355703 in patients with platinum- resistant ovarian cancer
    • D'Agostino G, del Campo J, Mellado B et al. A multicenter Phase II study of the cryptophycin analog LY355703 in patients with platinum- resistant ovarian cancer. Int. J. Gynecol. Cancer. 16, 71-76 (2006).
    • (2006) Int. J. Gynecol. Cancer. , vol.16 , pp. 71-76
    • D'Agostino, G.1    del Campo, J.2    Mellado, B.3
  • 99
    • 0032195190 scopus 로고    scopus 로고
    • Cell cycle control and cancer
    • Wagner HP. Cell cycle control and cancer. Indian J. Pediatr. 65, 805-814 (1998).
    • (1998) Indian J. Pediatr. , vol.65 , pp. 805-814
    • Wagner, H.P.1
  • 100
    • 0028141462 scopus 로고
    • Cryptophycin: A new antimicrotubule agent active against drug-resistant cells
    • Smith CD, Zhang X, Mooberry SL, Patterson GM, Moore RE. Cryptophycin: a new antimicrotubule agent active against drug-resistant cells. Cancer Res. 54, 3779-3784 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 3779-3784
    • Smith, C.D.1    Zhang, X.2    Mooberry, S.L.3    Patterson, G.M.4    Moore, R.E.5
  • 101
    • 0029874514 scopus 로고    scopus 로고
    • Mechanism of action cryptophycin. Interaction with the vinca alkaloid domain of tubulin
    • Smith CD, Zhang X. Mechanism of action cryptophycin. Interaction with the vinca alkaloid domain of tubulin. J. Biol. Chem. 271, 6192-6198 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 6192-6198
    • Smith, C.D.1    Zhang, X.2
  • 102
    • 0041537280 scopus 로고
    • Structure determination, conformational-analysis, chemical-stability studies, and antitumor evaluation of the cryptophycins - Isolation of 18 new analogs from nostoc sp strain gsv-224
    • Trimurtulu G, Ogino J, Heltzel CE et al. Structure determination, conformational-analysis, chemical-stability studies, and antitumor evaluation of the cryptophycins - isolation of 18 new analogs from nostoc sp strain gsv-224. J. Am. Chem. Soc. 117, 12030-12049 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12030-12049
    • Trimurtulu, G.1    Ogino, J.2    Heltzel, C.E.3
  • 105
    • 33645500289 scopus 로고    scopus 로고
    • Antibody-maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing
    • Erikson HK, Park PU, Widdison WC et al. Antibody-maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing Cancer Res. 66, 4426-4433 (2006)
    • (2006) Cancer Res. , vol.66 , pp. 4426-4433
    • Erikson, H.K.1    Park, P.U.2    Widdison, W.C.3
  • 106
    • 0031872051 scopus 로고    scopus 로고
    • Tubulin as a target for anticancer drugs: Agents which interact with the mitotic spindle
    • Jordan A, Hadfield JA, Lawrence NJ, McGown Al Tubulin as a target for anticancer drugs: agents which interact with the mitotic spindle. Med. Res. Rev. 18, 259-296 (1998).
    • (1998) Med. Res. Rev. , vol.18 , pp. 259-296
    • Jordan, A.1    Hadfield, J.A.2    Lawrence, N.J.3    McGown, A.T.4
  • 107
    • 0023133165 scopus 로고
    • Studies on macrocyclic lactone antibiotics. XI. Anti-mitotic and anti-tubulin activity of new antitumor antibiotics, rhizoxin and its homologues
    • Takahashi M, Iwasaki S, Kobayashi H et al. Studies on macrocyclic lactone antibiotics. XI. Anti-mitotic and anti-tubulin activity of new antitumor antibiotics, rhizoxin and its homologues J. Antibiot. (Tokyo) 40, 66-72 (1987).
    • (1987) J. Antibiot. (Tokyo) , vol.40 , pp. 66-72
    • Takahashi, M.1    Iwasaki, S.2    Kobayashi, H.3
  • 108
    • 0026557243 scopus 로고
    • Interaction of phomopsin A with porcine brain tubulin. Inhibition of tubulin polymerization and binding at a rhizoxin binding site
    • Li Y, Kobayashi H, Tokiwa Y, Hashimoto Y, Iwasaki S. Interaction of phomopsin A with porcine brain tubulin. Inhibition of tubulin polymerization and binding at a rhizoxin binding site. Biochem. Pharmacol. 43, 219-224 (1992).
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 219-224
    • Li, Y.1    Kobayashi, H.2    Tokiwa, Y.3    Hashimoto, Y.4    Iwasaki, S.5
  • 109
    • 53249119478 scopus 로고    scopus 로고
    • Interaction of phomopsin A with normal and subtilisin-treated bovine brain tubulin
    • Chaudhuri AR, Luduena RF. Interaction of phomopsin A with normal and subtilisin-treated bovine brain tubulin. J. Protein Chem. 16, 99-105 (1997).
    • (1997) J. Protein Chem. , vol.16 , pp. 99-105
    • Chaudhuri, A.R.1    Luduena, R.F.2
  • 110
    • 0033607202 scopus 로고    scopus 로고
    • Interactions of the sponge-derived antimitotic tripeptide hemiasterlin with tubulin: Comparison with dolastatin 10 and cryptophycin 1
    • Bai R, Durso NA, Sackett DL, Hamel E Interactions of the sponge-derived antimitotic tripeptide hemiasterlin with tubulin: comparison with dolastatin 10 and cryptophycin 1. Biochemistry 38, 14302-14310 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14302-14310
    • Bai, R.1    Durso, N.A.2    Sackett, D.L.3    Hamel, E.4
  • 112
    • 0031060389 scopus 로고    scopus 로고
    • Cytotoxic peptides hemiasterlin, hermasterlin A and hemiasterlin B induce mitotic arrest and abnormal spindle formation
    • Anderson HJ, Coleman JE, Andersen RJ, Roberge M. Cytotoxic peptides hemiasterlin, hermasterlin A and hemiasterlin B induce mitotic arrest and abnormal spindle formation. Cancer Chemother. Pharmacol. 39, 223-226 (1997).
    • (1997) Cancer Chemother. Pharmacol. , vol.39 , pp. 223-226
    • Anderson, H.J.1    Coleman, J.E.2    Andersen, R.J.3    Roberge, M.4
  • 113
    • 20944436156 scopus 로고    scopus 로고
    • Two photoaffinity analogues of the tripeptide, hemiasterlin, exclusively label α-tubulin
    • Nunes M, Kaplan J, Wooters J et al. Two photoaffinity analogues of the tripeptide, hemiasterlin, exclusively label α-tubulin. Biochemistry 44, 6844-6857 (2005).
    • (2005) Biochemistry , vol.44 , pp. 6844-6857
    • Nunes, M.1    Kaplan, J.2    Wooters, J.3
  • 114
    • 0038102301 scopus 로고    scopus 로고
    • Diazonamide A and a synthetic structural analogue. Disruptive effects on mitosis and cellular microtubules and analysis of their interactions with tubulin
    • Cruz-Monserrate Z, Vervoort HC, Bai R et al. Diazonamide A and a synthetic structural analogue. Disruptive effects on mitosis and cellular microtubules and analysis of their interactions with tubulin. Mol. Pharmacol. 63, 1273-1280 (2003).
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1273-1280
    • Cruz-Monserrate, Z.1    Vervoort, H.C.2    Bai, R.3
  • 115
    • 0033002547 scopus 로고    scopus 로고
    • Phase I trial of dolastatin-10 (NSC 376128) in patients with advanced solid tumors
    • Pitor HC, McElroy EA Jr, Reid JM et al. Phase I trial of dolastatin-10 (NSC 376128) in patients with advanced solid tumors. Clin. Cancer Res. 5, 525-531 (1999).
    • (1999) Clin. Cancer Res. , vol.5 , pp. 525-531
    • Pitor, H.C.1    McElroy Jr., E.A.2    Reid, J.M.3
  • 116
    • 0033739893 scopus 로고    scopus 로고
    • Phase II study of dolastatin-10 in patients with hormone-refractory metastatic prostate adenocarcinoma
    • Vaishampayan U, Glode M, Du W et al. Phase II study of dolastatin-10 in patients with hormone-refractory metastatic prostate adenocarcinoma. Clin. Cancer Res. 6, 4205-4208 (2000).
    • (2000) Clin. Cancer Res. , vol.6 , pp. 4205-4208
    • Vaishampayan, U.1    Glode, M.2    Du, W.3
  • 117
    • 0029039801 scopus 로고
    • Interaction of dolastatin 10 with tubulin: Induction of aggregation and binding and dissociation reactions
    • Bai R, Taylor GF, Schmidt JM et al. 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
  • 118
    • 0026069885 scopus 로고
    • Halichondrin B and homohalichondrin B, marine natural products binding in the vinca domain of tubulin. Discovery of tubulin-based mechanism of action by analysis of differential cytotoxicity data
    • Bai RL, Paull KD, Herald CL, Malspeis L, Pettit GR, Hamel E. Halichondrin B and homohalichondrin B, marine natural products binding in the vinca domain of tubulin. Discovery of tubulin-based mechanism of action by analysis of differential cytotoxicity data. J. Biol. Chem. 266, 15882-15889 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 15882-15889
    • Bai, R.L.1    Paull, K.D.2    Herald, C.L.3    Malspeis, L.4    Pettit, G.R.5    Hamel, E.6
  • 119
    • 17344374835 scopus 로고    scopus 로고
    • Comparative antiturnour activities of halichondrins and vinblastine against human tumour xenografts
    • Fodstad O, Breistol K, Pettit GR, Shoemaker RH, Boyd MR. Comparative antiturnour activities of halichondrins and vinblastine against human tumour xenografts. J. Exp. Ther. Oncol. 1, 119-125 (1996).
    • (1996) J. Exp. Ther. Oncol. , vol.1 , pp. 119-125
    • Fodstad, O.1    Breistol, K.2    Pettit, G.R.3    Shoemaker, R.H.4    Boyd, M.R.5
  • 120
    • 23144433687 scopus 로고    scopus 로고
    • The primary antimitotic mechanism of action of the synthetic halichondrin E7389 is suppression of microtubule growth
    • Jordan MA, Kamath K, Manna T et al. The primary antimitotic mechanism of action of the synthetic halichondrin E7389 is suppression of microtubule growth. Mol. Cancer Ther. 4, 1086-1095 (2005).
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1086-1095
    • Jordan, M.A.1    Kamath, K.2    Manna, T.3
  • 121
    • 0027482896 scopus 로고
    • A highly cytotoxic, sponge-derived, marine natural product that inhibits mitosis, microtubule assembly, and the binding of vinblastine to tubulin
    • Bai R, Cichacz ZA, Herald CL, Pettit GR, Hamel E, Spongistatin I. a highly cytotoxic, sponge-derived, marine natural product that inhibits mitosis, microtubule assembly, and the binding of vinblastine to tubulin. Mol. Pharm, 44, 757-766 (1993).
    • (1993) Mol. Pharm. , vol.44 , pp. 757-766
    • Bai, R.1    Cichacz, Z.A.2    Herald, C.L.3    Pettit, G.R.4    Hamel, E.5    Spongistatin, I.6
  • 122
    • 0029133540 scopus 로고
    • The spongistatins, potently cytotoxic inhibitors of tubulin polymerization, bind in a distinct region of the vincadomain
    • Bai R, Taylor GF, Cichacz ZA et al. The spongistatins, potently cytotoxic inhibitors of tubulin polymerization, bind in a distinct region of the vincadomain. Biochemistry 34, 9714-9721 (1995).
    • (1995) Biochemistry , vol.34 , pp. 9714-9721
    • Bai, R.1    Taylor, G.F.2    Cichacz, Z.A.3
  • 123
    • 0027155835 scopus 로고
    • Isolation and structure of spongistatin 1
    • Pettit GR, Cichacz ZA, Gao F et al. Isolation and structure of spongistatin 1. J. Org. Chem. 58, 1302-1304 (1993).
    • (1993) J. Org. Chem. , vol.58 , pp. 1302-1304
    • Pettit, G.R.1    Cichacz, Z.A.2    Gao, F.3
  • 124
    • 0027243738 scopus 로고
    • A potent anti-tumor macrolide from the Okinawan marine sponge Hyrtios altum
    • Kobayashi M, Aoki S, Sakai H et al. A potent anti-tumor macrolide from the Okinawan marine sponge Hyrtios altum. Tetrahedron Lett. 34, 2795-2798 (1993).
    • (1993) Tetrahedron Lett. , vol.34 , pp. 2795-2798
    • Kobayashi, M.1    Aoki, S.2    Sakai, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.