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Volumn 17, Issue 4, 2017, Pages 357-375

Mechanisms of tubulin binding ligands to target cancer cells: Updates on their therapeutic potential and clinical trials

Author keywords

Anticancer; Combination therapy; Microtubule stabilizing agents; Tubulin binding ligands; Tubulin inhibitor; Tubulin polymerization depolymerization

Indexed keywords

6 METHOXY 2 METHYL 3 (3,4,5 TRIMETHOXYBENZOYL)BENZOFURAN 7 YL PHOSPHATE DISODIUM; ANETUMAB RAVTANSINE; COLCHICINE; COLTUXIMAB RAVTANSINE; COMBRETASTATIN A1 PHOSPHATE; COMBRETASTATIN A4 PHOSPHATE; LEXIBULIN; N [2 [(4 HYDROXYPHENYL)AMINO] 3 PYRIDINYL] 4 METHOXYBENZENESULFONAMIDE; OMBRABULIN; PLINABULIN; TRASTUZUMAB EMTANSINE; TUBULIN; VERUBULIN; VINBLASTINE; VINCRISTINE; LIGAND;

EID: 85020869828     PISSN: 15680096     EISSN: 18735576     Source Type: Journal    
DOI: 10.2174/1568009616666160928110818     Document Type: Review
Times cited : (66)

References (137)
  • 1
    • 0004028961 scopus 로고
    • Springer Verlag: Berlin, Heidelberg, New York
    • Dustin, P. Microtubules; Springer Verlag: Berlin, Heidelberg, New York, 1978, vol. 452.
    • (1978) Microtubules; , vol.452
    • Dustin, P.1
  • 2
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the a p tubulin dimer by electron crystallography
    • Nogales, E.; Wolf, S.G.; Downing, K.H. Structure of the a p tubulin dimer by electron crystallography. Nature, 1998, 391(6663), 199-203.
    • (1998) Nature , vol.391 , Issue.6663 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 3
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T.; Kirschner, M. Dynamic instability of microtubule growth. Nature, 1984, 312(5991), 237-242.
    • (1984) Nature , vol.312 , Issue.5991 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 4
    • 49649097047 scopus 로고    scopus 로고
    • The roles of β-tubulin mutations and isotype expression in acquired drug resistance
    • Huzil, J.T.; Chen, K.; Kurgan, L.; Tuszynski, J.A. The roles of β-tubulin mutations and isotype expression in acquired drug resistance. Cancer Inform., 2007, 3, 159-181.
    • (2007) Cancer Inform , vol.3 , pp. 159-181
    • Huzil, J.T.1    Chen, K.2    Kurgan, L.3    Tuszynski, J.A.4
  • 5
    • 0033594925 scopus 로고    scopus 로고
    • Phosphate release during microtubule assembly: What stabilizes growing microtubules?
    • Vandecandelaere, A.; Brune, M.; Webb, M.R.; Martin, S.R.; Bayley, P.M. Phosphate release during microtubule assembly: what stabilizes growing microtubules? Biochemistry, 1999, 38(25), 8179-8188.
    • (1999) Biochemistry , vol.38 , Issue.25 , pp. 8179-8188
    • Vandecandelaere, A.1    Brune, M.2    Webb, M.R.3    Martin, S.R.4    Bayley, P.M.5
  • 6
    • 0026538817 scopus 로고
    • γ-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation
    • Joshi, H.C.; Palacios, M.J.; McNamara, L.; Cleveland, D.W. γ-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation. Nature, 1992, 356(6364), 80-83.
    • (1992) Nature , vol.356 , Issue.6364 , pp. 80-83
    • Joshi, H.C.1    Palacios, M.J.2    McNamara, L.3    Cleveland, D.W.4
  • 7
    • 0035312819 scopus 로고    scopus 로고
    • γ-tubulin complexes and microtubule nucleation
    • Moritz, M.; Agard, D.A. γ-tubulin complexes and microtubule nucleation. Curr. Opin. Struct. Biol., 2001, 11(2), 174-181.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , Issue.2 , pp. 174-181
    • Moritz, M.1    Agard, D.A.2
  • 8
    • 0031867055 scopus 로고    scopus 로고
    • The UN13 gene is required for assembly of basal bodies of Chlamydomonas and encodes 8-tubulin, a new member of the tubulin superfamily
    • Dutcher, S.K.; Trabuco, E.C. The UN13 gene is required for assembly of basal bodies of Chlamydomonas and encodes 8-tubulin, a new member of the tubulin superfamily. Mol. Biol. Cell, 1998, 9(6), 1293-1308.
    • (1998) Mol. Biol. Cell , vol.9 , Issue.6 , pp. 1293-1308
    • Dutcher, S.K.1    Trabuco, E.C.2
  • 9
    • 0035125071 scopus 로고    scopus 로고
    • Structural models for the self-assembly and microtubule interactions of gamma-, delta- and epsilon-tubulin
    • Inclan, Y.F.; Nogales, E. Structural models for the self-assembly and microtubule interactions of gamma-, delta- and epsilon-tubulin. J. Cell Sci., 2001, 114(Pt 2), 413-422.
    • (2001) J. Cell Sci , vol.114 , pp. 413-422
    • Inclan, Y.F.1    Nogales, E.2
  • 10
    • 0033622320 scopus 로고    scopus 로고
    • γ-tubulin and epsilon-tubulin: Two new human centrosomal tubulins reveal new aspects of centrosome structure and function
    • Chang, P.; Stearns, T. γ-tubulin and epsilon-tubulin: two new human centrosomal tubulins reveal new aspects of centrosome structure and function. Nat. Cell Biol., 2000, 2(1), 30-35.
    • (2000) Nat. Cell Biol , vol.2 , Issue.1 , pp. 30-35
    • Chang, P.1    Stearns, T.2
  • 11
    • 84961583757 scopus 로고    scopus 로고
    • Recent developments on 1, 2, 4-triazole nucleus in anticancer compounds: A review
    • Kaur, R.; Dwivedi, A.R.; Kumar, B.; Kumar, V. Recent developments on 1, 2, 4-triazole nucleus in anticancer compounds: a review. Anticancer Agents Med. Chem., 2016, 16(4), 465-489.
    • (2016) Anticancer Agents Med. Chem , vol.16 , Issue.4 , pp. 465-489
    • Kaur, R.1    Dwivedi, A.R.2    Kumar, B.3    Kumar, V.4
  • 12
    • 84893931872 scopus 로고    scopus 로고
    • Recent progress with microtubule stabilizers: New compounds, binding modes and cellular activities
    • Rohena, C.C.; Mooberry, S.L. Recent progress with microtubule stabilizers: new compounds, binding modes and cellular activities. Nat. Prod. Rep., 2014, 31(3), 335-355.
    • (2014) Nat. Prod. Rep , vol.31 , Issue.3 , pp. 335-355
    • Rohena, C.C.1    Mooberry, S.L.2
  • 13
    • 64049097460 scopus 로고    scopus 로고
    • Microtubule dynamics as a target in oncology
    • Risinger, A.L.; Giles, F.J.; Mooberry, S.L. Microtubule dynamics as a target in oncology. Cancer Treat. Rev., 2009, 35(3), 255-261.
    • (2009) Cancer Treat. Rev , vol.35 , Issue.3 , pp. 255-261
    • Risinger, A.L.1    Giles, F.J.2    Mooberry, S.L.3
  • 14
    • 44449152697 scopus 로고    scopus 로고
    • New tubulin targeting agents currently in clinical development
    • Carlson, R.O. New tubulin targeting agents currently in clinical development. Expert Opin. Investig. Drugs, 2008, 17(5), 707-722.
    • (2008) Expert Opin. Investig. Drugs , vol.17 , Issue.5 , pp. 707-722
    • Carlson, R.O.1
  • 15
    • 33947717002 scopus 로고    scopus 로고
    • Anticancer drugs from naturenatural products as a unique source of new microtubule-stabilizing agents
    • Altmann, K.-H.; Gertsch, J. Anticancer drugs from naturenatural products as a unique source of new microtubule-stabilizing agents. Nat. Prod. Rep., 2007, 24(2), 327-357.
    • (2007) Nat. Prod. Rep , vol.24 , Issue.2 , pp. 327-357
    • Altmann, K.-H.1    Gertsch, J.2
  • 16
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • Jordan, M.A.; Wilson, L. Microtubules as a target for anticancer drugs. Nat. Rev. Cancer, 2004, 4(4), 253-265.
    • (2004) Nat. Rev. Cancer , vol.4 , Issue.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 18
    • 34247391586 scopus 로고    scopus 로고
    • Peloruside A synergizes with other microtubule stabilizing agents in cultured cancer cell lines
    • Wilmes, A.; Bargh, K.; Kelly, C.; Northcote, P.T.; Miller, J.H. Peloruside A synergizes with other microtubule stabilizing agents in cultured cancer cell lines. Mot. Pharm., 2007, 4(2), 269-280.
    • (2007) Mot. Pharm , vol.4 , Issue.2 , pp. 269-280
    • Wilmes, A.1    Bargh, K.2    Kelly, C.3    Northcote, P.T.4    Miller, J.H.5
  • 19
    • 0037452096 scopus 로고    scopus 로고
    • Dynamics and mechanics of the microtubule plus end
    • Howard, J.; Hyman, A.A. Dynamics and mechanics of the microtubule plus end. Nature, 2003, 422(6933), 753-758.
    • (2003) Nature , vol.422 , Issue.6933 , pp. 753-758
    • Howard, J.1    Hyman, A.A.2
  • 20
    • 3843053396 scopus 로고    scopus 로고
    • The binding mode of epothilone A on a, beta-tubulin by electron crystallography
    • Nettles, J.H.; Li, H.; Cornett, B.; Krahn, J.M.; Snyder, J.P.; Downing, K.H. The binding mode of epothilone A on a, beta-tubulin by electron crystallography. Science, 2004, 305(5685), 866-869.
    • (2004) Science , vol.305 , Issue.5685 , pp. 866-869
    • Nettles, J.H.1    Li, H.2    Cornett, B.3    Krahn, J.M.4    Snyder, J.P.5    Downing, K.H.6
  • 21
    • 18444400213 scopus 로고    scopus 로고
    • The microtubule stabilizing agent laulimalide does not bind in the taxoid site, kills cells resistant to paclitaxel and epothilones, and may not require its epoxide moiety for activity
    • Pryor, D.E.; O’Brate, A.; Bilcer, G.; Diaz, J.F.; Wang, Y.; Wang, Y.; Kabaki, M.; Jung, M.K.; Andreu, J.M.; Ghosh, A.K.; Giannakakou, P.; Hamel, E. The microtubule stabilizing agent laulimalide does not bind in the taxoid site, kills cells resistant to paclitaxel and epothilones, and may not require its epoxide moiety for activity. Biochemistry, 2002, 41(29), 9109-9115.
    • (2002) Biochemistry , vol.41 , Issue.29 , pp. 9109-9115
    • Pryor, D.E.1    O’Brate, A.2    Bilcer, G.3    Diaz, J.F.4    Wang, Y.5    Wang, Y.6    Kabaki, M.7    Jung, M.K.8    Andreu, J.M.9    Ghosh, A.K.10    Giannakakou, P.11    Hamel, E.12
  • 22
    • 3442894416 scopus 로고    scopus 로고
    • Peloruside A does not bind to the taxoid site on β-tubulin and retains its activity in multidrug-resistant cell lines
    • Gaitanos, T.N.; Buey, R.M.; Diaz, J.F.; Northcote, P.T.; Teesdale Spittle, P.; Andreu, J.M.; Miller, J.H. Peloruside A does not bind to the taxoid site on β-tubulin and retains its activity in multidrug-resistant cell lines. Cancer Res., 2004, 64(15), 5063-5067.
    • (2004) Cancer Res , vol.64 , Issue.15 , pp. 5063-5067
    • Gaitanos, T.N.1    Buey, R.M.2    Diaz, J.F.3    Northcote, P.T.4    Teesdale Spittle, P.5    Andreu, J.M.6    Miller, J.H.7
  • 24
    • 0026558326 scopus 로고
    • Mechanism of inhibition of microtubule polymerization by colchicine: Inhibitory potencies of unliganded colchicine and tubulin-colchicine complexes
    • Skoufias, D.A.; Wilson, L. Mechanism of inhibition of microtubule polymerization by colchicine: inhibitory potencies of unliganded colchicine and tubulin-colchicine complexes. Biochemistry, 1992, 31(3), 738-746.
    • (1992) Biochemistry , vol.31 , Issue.3 , pp. 738-746
    • Skoufias, D.A.1    Wilson, L.2
  • 25
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S.; Weber, K. Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol., 2003, 4(12), 938-947.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , Issue.12 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 27
    • 84862580438 scopus 로고    scopus 로고
    • Tubulins as therapeutic targets in cancer: From bench to bedside
    • Katsetos, C.D.; Draber, P. Tubulins as therapeutic targets in cancer: from bench to bedside. Curr. Pharm. Des., 2012, 18(19), 2778-2792.
    • (2012) Curr. Pharm. Des , vol.18 , Issue.19 , pp. 2778-2792
    • Katsetos, C.D.1    Draber, P.2
  • 28
    • 0034895161 scopus 로고    scopus 로고
    • Mechanisms of taxotere-related drug resistance in pancreatic carcinoma
    • Liu, B.; Staren, E.D.; Iwamura, T.; Appert, H.E.; Howard, J.M. Mechanisms of taxotere-related drug resistance in pancreatic carcinoma. J. Surg. Res., 2001, 99(2), 179-186.
    • (2001) J. Surg. Res , vol.99 , Issue.2 , pp. 179-186
    • Liu, B.1    Staren, E.D.2    Iwamura, T.3    Appert, H.E.4    Howard, J.M.5
  • 29
    • 0037764082 scopus 로고    scopus 로고
    • Class III β-tubulin in human development and cancer
    • Katsetos, C.D.; Herman, M.M.; Mork, S.J. Class III β-tubulin in human development and cancer. Cell Motil. Cytoskelet., 2003, 55(2), 77-96.
    • (2003) Cell Motil. Cytoskelet , vol.55 , Issue.2 , pp. 77-96
    • Katsetos, C.D.1    Herman, M.M.2    Mork, S.J.3
  • 30
    • 23444443007 scopus 로고    scopus 로고
    • Alterations of β-tubulin isotypes in breast cancer cells resistant to docetaxel
    • Shalli, K.; Brown, I.; Heys, S.D.; Schofield, A.C. Alterations of β-tubulin isotypes in breast cancer cells resistant to docetaxel. FASEB J., 2005, 19(10), 1299-1301.
    • (2005) FASEB J , vol.19 , Issue.10 , pp. 1299-1301
    • Shalli, K.1    Brown, I.2    Heys, S.D.3    Schofield, A.C.4
  • 32
    • 77953750777 scopus 로고    scopus 로고
    • betaIII-tubulin is a multifunctional protein involved in drug sensitivity and tumorigenesis in non-small cell lung cancer
    • McCarroll, J.A.; Gan, P.P.; Liu, M.; Kavallaris, M. betaIII-tubulin is a multifunctional protein involved in drug sensitivity and tumorigenesis in non-small cell lung cancer. Cancer Res., 2010, 70(12), 4995-5003.
    • (2010) Cancer Res , vol.70 , Issue.12 , pp. 4995-5003
    • McCarroll, J.A.1    Gan, P.P.2    Liu, M.3    Kavallaris, M.4
  • 33
    • 77649191871 scopus 로고    scopus 로고
    • Microtubules and resistance to tubulin-binding agents
    • Kavallaris, M. Microtubules and resistance to tubulin-binding agents. Nat. Rev. Cancer, 2010, 10(3), 194-204.
    • (2010) Nat. Rev. Cancer , vol.10 , Issue.3 , pp. 194-204
    • Kavallaris, M.1
  • 35
    • 35148854099 scopus 로고    scopus 로고
    • Class III β-tubulin mediates sensitivity to chemotherapeutic drugs in non small cell lung cancer
    • Gan, P.P.; Pasquier, E.; Kavallaris, M. Class III β-tubulin mediates sensitivity to chemotherapeutic drugs in non small cell lung cancer. Cancer Res., 2007, 67(19), 9356-9363.
    • (2007) Cancer Res , vol.67 , Issue.19 , pp. 9356-9363
    • Gan, P.P.1    Pasquier, E.2    Kavallaris, M.3
  • 37
    • 18244364381 scopus 로고    scopus 로고
    • Resistance to the tubulin-binding agents in renal cell carcinoma: No mutations in the class I β-tubulin gene but changes in tubulin isotype protein expression
    • Ferguson, R.E.; Taylor, C.; Stanley, A.; Butler, E.; Joyce, A.; Harnden, P.; Patel, P.M.; Selby, P.J.; Banks, R.E. Resistance to the tubulin-binding agents in renal cell carcinoma: no mutations in the class I β-tubulin gene but changes in tubulin isotype protein expression. Clin. Cancer Res., 2005, 77(9), 3439-3445.
    • (2005) Clin. Cancer Res , vol.77 , Issue.9 , pp. 3439-3445
    • Ferguson, R.E.1    Taylor, C.2    Stanley, A.3    Butler, E.4    Joyce, A.5    Harnden, P.6    Patel, P.M.7    Selby, P.J.8    Banks, R.E.9
  • 39
    • 2142744812 scopus 로고    scopus 로고
    • Mutations in α- and β-tubulin that stabilize microtubules and confer resistance to colcemid and vinblastine
    • Hari, M.; Wang, Y.; Veeraraghavan, S.; Cabral, F. Mutations in α- and β-tubulin that stabilize microtubules and confer resistance to colcemid and vinblastine. Mol. Cancer Ther., 2003, 2(7), 597-605.
    • (2003) Mol. Cancer Ther , vol.2 , Issue.7 , pp. 597-605
    • Hari, M.1    Wang, Y.2    Veeraraghavan, S.3    Cabral, F.4
  • 40
    • 0035422780 scopus 로고    scopus 로고
    • Multiple microtubule alterations are associated with Vinca alkaloid resistance in human leukemia cells
    • Kavallaris, M.; Tait, A.S.; Walsh, B.J.; He, L.; Horwitz, S.B.; Norris, M.D.; Haber, M. Multiple microtubule alterations are associated with Vinca alkaloid resistance in human leukemia cells. Cancer Res., 2001, 67(15), 5803-5809.
    • (2001) Cancer Res , vol.67 , Issue.15 , pp. 5803-5809
    • Kavallaris, M.1    Tait, A.S.2    Walsh, B.J.3    He, L.4    Horwitz, S.B.5    Norris, M.D.6    Haber, M.7
  • 41
    • 0018387446 scopus 로고
    • Promotion of microtubule assembly in vitro by taxol
    • Schiff, P.B.; Fant, J.; Horwitz, S.B. Promotion of microtubule assembly in vitro by taxol. Nature, 1979, 277(5698), 665-667.
    • (1979) Nature , vol.277 , Issue.5698 , pp. 665-667
    • Schiff, P.B.1    Fant, J.2    Horwitz, S.B.3
  • 42
    • 0027383827 scopus 로고
    • Thermodynamics of ligand-induced assembly of tubulin
    • Díaz, J.F.; Menéndez, M.; Andreu, J.M. Thermodynamics of ligand-induced assembly of tubulin. Biochemistry, 1993, 52(38), 10067-10077.
    • (1993) Biochemistry , vol.52 , Issue.38 , pp. 10067-10077
    • Díaz, J.F.1    Menéndez, M.2    Andreu, J.M.3
  • 43
    • 80051985188 scopus 로고    scopus 로고
    • Insights into the interaction of discodermolide and docetaxel with tubulin. Mapping the binding sites of microtubule-stabilizing agents by using an integrated NMR and computational approach
    • Canales, A.; Rodríguez-Salarichs, J.; Trigili, C.; Nieto, L.; Coderch, C.; Andreu, J.M.; Paterson, I.; Jiménez-Barbero, J.; Díaz, J.F. Insights into the interaction of discodermolide and docetaxel with tubulin. Mapping the binding sites of microtubule-stabilizing agents by using an integrated NMR and computational approach. ACS Chem. Biol., 2011, 6(8), 789-799.
    • (2011) ACS Chem. Biol , vol.6 , Issue.8 , pp. 789-799
    • Canales, A.1    Rodríguez-Salarichs, J.2    Trigili, C.3    Nieto, L.4    Coderch, C.5    Andreu, J.M.6    Paterson, I.7    Jiménez-Barbero, J.8    Díaz, J.F.9
  • 46
    • 77955478732 scopus 로고    scopus 로고
    • Structural basis of interprotofilament interaction and lateral deformation of microtubules
    • Sui, H.; Downing, K.H. Structural basis of interprotofilament interaction and lateral deformation of microtubules. Structure, 2010, 78(8), 1022-1031.
    • (2010) Structure , vol.78 , Issue.8 , pp. 1022-1031
    • Sui, H.1    Downing, K.H.2
  • 49
    • 55949090064 scopus 로고    scopus 로고
    • Taxol allosterically alters the dynamics of the tubulin dimer and increases the flexibility of microtubules
    • Mitra, A.; Sept, D. Taxol allosterically alters the dynamics of the tubulin dimer and increases the flexibility of microtubules. Biophys. J., 2008, 95(7), 3252-3258.
    • (2008) Biophys. J , vol.95 , Issue.7 , pp. 3252-3258
    • Mitra, A.1    Sept, D.2
  • 52
    • 0031027531 scopus 로고    scopus 로고
    • Activities of the microtubule-stabilizing agents epothilones A and B with purified tubulin and in cells resistant to paclitaxel (Taxol(R))
    • Kowalski, R.J.; Giannakakou, P.; Hamel, E. Activities of the microtubule-stabilizing agents epothilones A and B with purified tubulin and in cells resistant to paclitaxel (Taxol(R)). J. Biol. Chem., 1997, 272(4), 2534-2541.
    • (1997) J. Biol. Chem , vol.272 , Issue.4 , pp. 2534-2541
    • Kowalski, R.J.1    Giannakakou, P.2    Hamel, E.3
  • 53
    • 84971373107 scopus 로고    scopus 로고
    • Epothilones suppress neointimal thickening in the rat carotid balloon-injury model by inducing vascular smooth muscle cell apoptosis through p53-dependent signaling pathway
    • Son, D.J.; Jung, J.C.; Hong, J.T. Epothilones suppress neointimal thickening in the rat carotid balloon-injury model by inducing vascular smooth muscle cell apoptosis through p53-dependent signaling pathway. PLoS One, 2016, 77(5), e0155859.
    • (2016) PLoS One , vol.77 , Issue.5 , pp. 155859
    • Son, D.J.1    Jung, J.C.2    Hong, J.T.3
  • 54
    • 71249103102 scopus 로고    scopus 로고
    • Novel microtubule-targeting agents - the epothilones
    • Cheng, K.L.; Bradley, T.; Budman, D.R. Novel microtubule-targeting agents - the epothilones. Biologics, 2008, 2(4), 789-811.
    • (2008) Biologics , vol.2 , Issue.4 , pp. 789-811
    • Cheng, K.L.1    Bradley, T.2    Budman, D.R.3
  • 55
    • 3042701597 scopus 로고    scopus 로고
    • Epothilones: Mechanism of action and biologic activity
    • Goodin, S.; Kane, M.P.; Rubin, E.H. Epothilones: mechanism of action and biologic activity. J. Clin. Oncol., 2004, 22(10), 2015-2025.
    • (2004) J. Clin. Oncol , vol.22 , Issue.10 , pp. 2015-2025
    • Goodin, S.1    Kane, M.P.2    Rubin, E.H.3
  • 56
    • 3042584537 scopus 로고    scopus 로고
    • Laulimalide and paclitaxel: A comparison of their effects on tubulin assembly and their synergistic action when present simultaneously
    • Gapud, E.J.; Bai, R.; Ghosh, A.K.; Hamel, E. Laulimalide and paclitaxel: a comparison of their effects on tubulin assembly and their synergistic action when present simultaneously. Mol. Pharmacol, 2004, 66(1), 113-121.
    • (2004) Mol. Pharmacol , vol.66 , Issue.1 , pp. 113-121
    • Gapud, E.J.1    Bai, R.2    Ghosh, A.K.3    Hamel, E.4
  • 57
    • 4444315009 scopus 로고    scopus 로고
    • Computational comparison of microtubule-stabilising agents laulimalide and peloruside with taxol and colchicine
    • Pineda, O.; Farras, J.; Maccari, L.; Manetti, F.; Botta, M.; Vilarrasa, J. Computational comparison of microtubule-stabilising agents laulimalide and peloruside with taxol and colchicine. Bioorg. Med. Chem. Lett., 2004, 74(19), 4825-4829.
    • (2004) Bioorg. Med. Chem. Lett , vol.74 , Issue.19 , pp. 4825-4829
    • Pineda, O.1    Farras, J.2    Maccari, L.3    Manetti, F.4    Botta, M.5    Vilarrasa, J.6
  • 62
    • 79953232399 scopus 로고    scopus 로고
    • Hallmarks of molecular action of microtubule stabilizing agents: Effects of epothilone B, ixabepilone, peloruside A, and laulimalide on microtubule conformation
    • Khrapunovich-Baine, M.; Menon, V.; Yang, C.-P.; Northcote, P.T.; Miller, J.H.; Angeletti, R.H.; Fiser, A.; Horwitz, S.B.; Xiao, H. Hallmarks of molecular action of microtubule stabilizing agents: effects of epothilone B, ixabepilone, peloruside A, and laulimalide on microtubule conformation. J. Biol. Chem., 2011, 286(13), 11765-11778.
    • (2011) J. Biol. Chem , vol.286 , Issue.13 , pp. 11765-11778
    • Khrapunovich-Baine, M.1    Menon, V.2    Yang, C.-P.3    Northcote, P.T.4    Miller, J.H.5    Angeletti, R.H.6    Fiser, A.7    Horwitz, S.B.8    Xiao, H.9
  • 63
    • 0031040149 scopus 로고    scopus 로고
    • The development and clinical utility of the taxane class of antimicrotubule chemotherapy agents
    • Rowinsky, E.K.; Eric, K. The development and clinical utility of the taxane class of antimicrotubule chemotherapy agents. Ann. Rev Med., 1997, 48(1), 353-374.
    • (1997) Ann. Rev Med , vol.48 , Issue.1 , pp. 353-374
    • Rowinsky, E.K.1    Eric, K.2
  • 64
    • 0027935479 scopus 로고
    • Synthesis and structure-activity relationships of new antitumor taxoids. Effects of cyclohexyl substitution at the C-3 and/or C-2 of taxotere (docetaxel)
    • Ojima, I.; Duclos, O.; Zucco, M.; Bissery, M.-C.; Combeau, C.; Vrignaud, P.; Riou, J.F.; Lavelle, F. Synthesis and structure-activity relationships of new antitumor taxoids. Effects of cyclohexyl substitution at the C-3 and/or C-2 of taxotere (docetaxel). J. Med. Chem., 1994, 37(16), 2602-2608.
    • (1994) J. Med. Chem , vol.37 , Issue.16 , pp. 2602-2608
    • Ojima, I.1    Duclos, O.2    Zucco, M.3    Bissery, M.-C.4    Combeau, C.5    Vrignaud, P.6    Riou, J.F.7    Lavelle, F.8
  • 65
    • 84905644195 scopus 로고    scopus 로고
    • Antiproliferative mechanism of action of the novel taxane cabazitaxel as compared with the parent compound docetaxel in MCF7 breast cancer cells
    • Azarenko, O.; Smiyun, G.; Mah, J.; Wilson, L.; Jordan, M.A. Antiproliferative mechanism of action of the novel taxane cabazitaxel as compared with the parent compound docetaxel in MCF7 breast cancer cells. Mol. Cancer Ther., 2014, 73(8), 2092-2103.
    • (2014) Mol. Cancer Ther , vol.73 , Issue.8 , pp. 2092-2103
    • Azarenko, O.1    Smiyun, G.2    Mah, J.3    Wilson, L.4    Jordan, M.A.5
  • 66
    • 82455162574 scopus 로고    scopus 로고
    • Tesetaxel, a new oral taxane, in combination with capecitabine: A phase I, dose-escalation study in patients with advanced solid tumors
    • Saif, M.W.; Sarantopoulos, J.; Patnaik, A.; Tolcher, A.W.; Takimoto, C.; Beeram, M. Tesetaxel, a new oral taxane, in combination with capecitabine: a phase I, dose-escalation study in patients with advanced solid tumors. Cancer Chemother. Pharmacol., 2011, 68(6), 1565-1573.
    • (2011) Cancer Chemother. Pharmacol , vol.68 , Issue.6 , pp. 1565-1573
    • Saif, M.W.1    Sarantopoulos, J.2    Patnaik, A.3    Tolcher, A.W.4    Takimoto, C.5    Beeram, M.6
  • 67
    • 46249085475 scopus 로고    scopus 로고
    • Phase II multicenter study of larotaxel (XRP9881), a novel taxoid, in patients with metastatic breast cancer who previously received taxane-based therapy
    • Diéras, V.; Limentani, S.; Romieu, G.; Tubiana-Hulin, M.; Lortholary, A.; Kaufman, P.; Girre, V.; Besenval, M.; Valero, V. Phase II multicenter study of larotaxel (XRP9881), a novel taxoid, in patients with metastatic breast cancer who previously received taxane-based therapy. Ann. Oncol., 2008, 79(7), 1255-1260.
    • (2008) Ann. Oncol , vol.79 , Issue.7 , pp. 1255-1260
    • Diéras, V.1    Limentani, S.2    Romieu, G.3    Tubiana-Hulin, M.4    Lortholary, A.5    Kaufman, P.6    Girre, V.7    Besenval, M.8    Valero, V.9
  • 68
    • 58149140537 scopus 로고    scopus 로고
    • Randomized multicenter phase II study of larotaxel (XRP9881) in combination with cisplatin or gemcitabine as first line chemotherapy in nonirradiable stage IIIB or stage IV nonsmall cell lung cancer
    • Zatloukal, P.; Gervais, R.; Vansteenkiste, J.; Bosquee, L.; Sessa, C.; Brain, E.; Dansin, E.; Urban, T.; Dohollou, N.; Besenval, M.; Quoix, E. Randomized multicenter phase II study of larotaxel (XRP9881) in combination with cisplatin or gemcitabine as first line chemotherapy in nonirradiable stage IIIB or stage IV nonsmall cell lung cancer. J. Thorac. Oncol., 2008, 3(8), 894-901.
    • (2008) J. Thorac. Oncol , vol.3 , Issue.8 , pp. 894-901
    • Zatloukal, P.1    Gervais, R.2    Vansteenkiste, J.3    Bosquee, L.4    Sessa, C.5    Brain, E.6    Dansin, E.7    Urban, T.8    Dohollou, N.9    Besenval, M.10    Quoix, E.11
  • 70
    • 84905722883 scopus 로고    scopus 로고
    • Zampanolide and dactylolide: Cytotoxic tubulin-assembly agents and promising anticancer leads
    • Chen, Q-H.; Kingston, D.G. Zampanolide and dactylolide: cytotoxic tubulin-assembly agents and promising anticancer leads. Nat Prod. Rep., 2014, 37(9), 1202-1226.
    • (2014) Nat Prod. Rep , vol.37 , Issue.9 , pp. 1202-1226
    • Chen, Q.-H.1    Kingston, D.G.2
  • 71
    • 0036565885 scopus 로고    scopus 로고
    • Ectopic overexpression of second mitochondria-derived activator of caspases (Smac/DIABLO) or cotreatment with N-terminus of Smac/DIABLO peptide potentiates epothilone B derivative-(BMS 247550) and Apo-2L/TRAIL-induced apoptosis
    • Guo, F.; Nimmanapalli, R.; Paranawithana, S.; Wittman, S.; Griffin, D.; Bali, P.; O’Bryan, E.; Fumero, C.; Wang, H.G.; Bhalla, K. Ectopic overexpression of second mitochondria-derived activator of caspases (Smac/DIABLO) or cotreatment with N-terminus of Smac/DIABLO peptide potentiates epothilone B derivative-(BMS 247550) and Apo-2L/TRAIL-induced apoptosis. Blood, 2002, 99(9), 3419-3426.
    • (2002) Blood , vol.99 , Issue.9 , pp. 3419-3426
    • Guo, F.1    Nimmanapalli, R.2    Paranawithana, S.3    Wittman, S.4    Griffin, D.5    Bali, P.6    O’Bryan, E.7    Fumero, C.8    Wang, H.G.9    Bhalla, K.10
  • 72
    • 45349106522 scopus 로고    scopus 로고
    • Activity of patupilone for the treatment of recurrent or progressive brain metastases in patients (pts) with non-small cell lung cancer (NSCLC): An open-label, multicenter, phase II study
    • Abstract No. 18058
    • Abrey, L.; Wen, P.; Govindan, R.; Reimers, H.; Rigas, J.; Robins, H.; de Bedout, S.; O’Connell, C.; Li, X.; Johri, A. Activity of patupilone for the treatment of recurrent or progressive brain metastases in patients (pts) with non-small cell lung cancer (NSCLC): an open-label, multicenter, phase II study. J. Clin. Oncol., 2007, 25(18), Abstract No. 18058.
    • (2007) J. Clin. Oncol , vol.25 , Issue.18
    • Abrey, L.1    Wen, P.2    Govindan, R.3    Reimers, H.4    Rigas, J.5    Robins, H.6    de Bedout, S.7    O’Connell, C.8    Li, X.9    Johri, A.10
  • 76
    • 85020896450 scopus 로고    scopus 로고
    • Taccalonolides: Novel microtubule stabilizers with clinical potential
    • Risinger, A.L.; Mooberry, S.L. Taccalonolides: Novel microtubule stabilizers with clinical potential. Cancer Lett., 2010, 297(1), 1419.
    • (2010) Cancer Lett , vol.297 , Issue.1 , pp. 1419
    • Risinger, A.L.1    Mooberry, S.L.2
  • 79
    • 84892518213 scopus 로고    scopus 로고
    • Resistance to peloruside A and laulimalide: Functional significance of acquired βI-tubulin mutations at sites important for drugtubulin binding
    • Kanakkanthara, A.; Eras, J.; Northcote, P.T.; Cabral, F.; Miller, J.H. Resistance to peloruside A and laulimalide: functional significance of acquired βI-tubulin mutations at sites important for drugtubulin binding. Curr. Cancer Drug Targets, 2014, 74(1), 79-90.
    • (2014) Curr. Cancer Drug Targets , vol.74 , Issue.1 , pp. 79-90
    • Kanakkanthara, A.1    Eras, J.2    Northcote, P.T.3    Cabral, F.4    Miller, J.H.5
  • 80
    • 0037096807 scopus 로고    scopus 로고
    • Peloruside A, a novel antimitotic agent with paclitaxel-like microtubule-stabilizing activity
    • Hood, K.A.; West, L.M.; Rouwé, B.; Northcote, P.T.; Berridge, M.V.; Wakefield, S.J.; Miller, J.H. Peloruside A, a novel antimitotic agent with paclitaxel-like microtubule-stabilizing activity. Cancer Res., 2002, 62(12), 3356-3360.
    • (2002) Cancer Res , vol.62 , Issue.12 , pp. 3356-3360
    • Hood, K.A.1    West, L.M.2    Rouwé, B.3    Northcote, P.T.4    Berridge, M.V.5    Wakefield, S.J.6    Miller, J.H.7
  • 81
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli, R.B.; Gigant, B.; Curmi, P.A.; Jourdain, I.; Lachkar, S.; Sobel, A.; Knossow, M. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature, 2004, 428(6979), 198-202.
    • (2004) Nature , vol.428 , Issue.6979 , pp. 198-202
    • Ravelli, R.B.1    Gigant, B.2    Curmi, P.A.3    Jourdain, I.4    Lachkar, S.5    Sobel, A.6    Knossow, M.7
  • 82
    • 0020422990 scopus 로고
    • Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin
    • Andreu, J.M.; Timasheff, S.N. Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin. Biochemistry, 1982, 27(25), 6465-6476.
    • (1982) Biochemistry , vol.27 , Issue.25 , pp. 6465-6476
    • Andreu, J.M.1    Timasheff, S.N.2
  • 84
    • 0035224509 scopus 로고    scopus 로고
    • Apoptosis in caspase-inhibited neurons
    • Volbracht, C.; Leist, M.; Kolb, S.A.; Nicotera, P. Apoptosis in caspase-inhibited neurons. Mol. Med., 2001, 7(1), 36-48.
    • (2001) Mol. Med , vol.7 , Issue.1 , pp. 36-48
    • Volbracht, C.1    Leist, M.2    Kolb, S.A.3    Nicotera, P.4
  • 85
    • 0027330403 scopus 로고
    • Podophyllotoxin, steganacin and combretastatin: Natural products that bind at the colchicine site of tubulin
    • Sackett, D.L. Podophyllotoxin, steganacin and combretastatin: natural products that bind at the colchicine site of tubulin. Pharmacol. Ther., 1993, 59(2), 163-228.
    • (1993) Pharmacol. Ther , vol.59 , Issue.2 , pp. 163-228
    • Sackett, D.L.1
  • 86
    • 0024353869 scopus 로고
    • The effect of podophyl-lotoxin on microtubule dynamics
    • Schilstra, M.J.; Martin, S.R.; Bayley, P.M. The effect of podophyl-lotoxin on microtubule dynamics. J. Biol. Chem., 1989, 264(15), 8827-8834.
    • (1989) J. Biol. Chem , vol.264 , Issue.15 , pp. 8827-8834
    • Schilstra, M.J.1    Martin, S.R.2    Bayley, P.M.3
  • 87
    • 0036282385 scopus 로고    scopus 로고
    • The biology of the combretastatins as tumour vascular targeting agents
    • Tozer, G.M.; Kanthou, C.; Parkins, C.S.; Hill, S.A. The biology of the combretastatins as tumour vascular targeting agents. Int. J. Exp. Pathol, 2002, 83(1), 21-38.
    • (2002) Int. J. Exp. Pathol , vol.83 , Issue.1 , pp. 21-38
    • Tozer, G.M.1    Kanthou, C.2    Parkins, C.S.3    Hill, S.A.4
  • 88
    • 33845286942 scopus 로고    scopus 로고
    • III Vascular disrupting agents
    • Lippert, J.W., III Vascular disrupting agents. Bioorg. Med. Chem., 2007, 75(2), 605-615.
    • (2007) Bioorg. Med. Chem , vol.75 , Issue.2 , pp. 605-615
    • Lippert, J.W.1
  • 89
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K.; Wennerberg, K. Rho and Rac take center stage. Cell, 2004, 776(2), 167-179.
    • (2004) Cell , vol.776 , Issue.2 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 90
    • 84857727692 scopus 로고    scopus 로고
    • Tubulin-based structure-affinity relationships for antimitotic Vinca alkaloids
    • Coderch, C.; Morreale, A.; Gago, F. Tubulin-based structure-affinity relationships for antimitotic Vinca alkaloids. Anti-Cancer Agent. Med. Chem., 2012, 72(3), 219-225.
    • (2012) Anti-Cancer Agent. Med. Chem , vol.72 , Issue.3 , pp. 219-225
    • Coderch, C.1    Morreale, A.2    Gago, F.3
  • 94
    • 0036909567 scopus 로고    scopus 로고
    • Small molecules, big impact: A history of chemical inhibitors and the cytoskeleton
    • Peterson, J.R.; Mitchison, T.J. Small molecules, big impact: a history of chemical inhibitors and the cytoskeleton. Chem. Biol., 2002, 9(12), 1275-1285.
    • (2002) Chem. Biol , vol.9 , Issue.12 , pp. 1275-1285
    • Peterson, J.R.1    Mitchison, T.J.2
  • 95
    • 84867889521 scopus 로고    scopus 로고
    • An overview of tubulin inhibitors that interact with the colchicine binding site
    • Lu, Y.; Chen, J.; Xiao, M.; Li, W.; Miller, D.D. An overview of tubulin inhibitors that interact with the colchicine binding site. Pharm. Res., 2012, 29(11), 2943-2971.
    • (2012) Pharm. Res , vol.29 , Issue.11 , pp. 2943-2971
    • Lu, Y.1    Chen, J.2    Xiao, M.3    Li, W.4    Miller, D.D.5
  • 96
    • 0141518578 scopus 로고    scopus 로고
    • Structural requirements for the interaction of combretastatins with tubulin: How important is the trimethoxy unit?
    • Gaukroger, K.; Hadfield, J.A.; Lawrence, N.J.; Nolan, S.; McGown, A.T. Structural requirements for the interaction of combretastatins with tubulin: how important is the trimethoxy unit? Org. Biomol. Chem., 2003, 7(17), 3033-3037.
    • (2003) Org. Biomol. Chem , vol.7 , Issue.17 , pp. 3033-3037
    • Gaukroger, K.1    Hadfield, J.A.2    Lawrence, N.J.3    Nolan, S.4    McGown, A.T.5
  • 100
    • 84876279820 scopus 로고    scopus 로고
    • Combretazet-3 a novel synthetic cis-stable combretastatin A-4-azetidinone hybrid with enhanced stability and therapeutic efficacy in colon cancer
    • Greene, L.M.; Wang, S.; O’Boyle, N.M.; Bright, S.A.; Reid, J.E.; Kelly, P.; Meegan, M.J.; Zisterer, D.M. Combretazet-3 a novel synthetic cis-stable combretastatin A-4-azetidinone hybrid with enhanced stability and therapeutic efficacy in colon cancer. Oncol. Rep., 2013, 29(6), 2451-2458.
    • (2013) Oncol. Rep , vol.29 , Issue.6 , pp. 2451-2458
    • Greene, L.M.1    Wang, S.2    O’Boyle, N.M.3    Bright, S.A.4    Reid, J.E.5    Kelly, P.6    Meegan, M.J.7    Zisterer, D.M.8
  • 101
    • 84978137663 scopus 로고    scopus 로고
    • Abstract A08: Investigating tumor vasculature development and the effects of OXi4503 by non-invasive photoacoustic imaging
    • Johnson, S.P.; Ogunlade, O.; Zhang, E.; Lythgoe, M.; Beard, P.; Pedley, R.B. Abstract A08: Investigating tumor vasculature development and the effects of OXi4503 by non-invasive photoacoustic imaging. Cancer Res., 2015, 75(Suppl. 1), A08-A08.
    • (2015) Cancer Res , vol.75 , pp. A08-A08
    • Johnson, S.P.1    Ogunlade, O.2    Zhang, E.3    Lythgoe, M.4    Beard, P.5    Pedley, R.B.6
  • 105
    • 78049454954 scopus 로고    scopus 로고
    • Phase II study of docetaxel with or without plinabulin (NPI-2358) in patients with non-small cell lung cancer (NSCLC)
    • Abstract No. 7592
    • Mita, A.; Heist, R.; Aren, O.; Mainwaring, P.; Bazhenova, L.; Gadgeel, S.; Blum, R.; Polikoff, J.; Biswas, J.; Spear, M. Phase II study of docetaxel with or without plinabulin (NPI-2358) in patients with non-small cell lung cancer (NSCLC). J. Clin. Oncol., 2010, 28(15), Abstract No. 7592.
    • (2010) J. Clin. Oncol , vol.28 , Issue.15
    • Mita, A.1    Heist, R.2    Aren, O.3    Mainwaring, P.4    Bazhenova, L.5    Gadgeel, S.6    Blum, R.7    Polikoff, J.8    Biswas, J.9    Spear, M.10
  • 106
    • 78650450212 scopus 로고    scopus 로고
    • Phase I clinical trial of MPC-6827 (Azixa), a microtubule destabilizing agent, in patients with advanced cancer
    • Breuleux, M.; Bachmann, F.; Pohlmann, J.; Mathews, S.; Burger, K.; Kellenberger, L.; Lane, H. Phase I clinical trial of MPC-6827 (Azixa), a microtubule destabilizing agent, in patients with advanced cancer. Mol. Cancer Ther., 2010, 9(12), 3410-3419.
    • (2010) Mol. Cancer Ther , vol.9 , Issue.12 , pp. 3410-3419
    • Breuleux, M.1    Bachmann, F.2    Pohlmann, J.3    Mathews, S.4    Burger, K.5    Kellenberger, L.6    Lane, H.7
  • 109
    • 84925317054 scopus 로고    scopus 로고
    • Microtubule-targeting agents are clinically successful due to both mitotic and interphase impairment of microtubule function
    • Field, J.J.; Kanakkanthara, A.; Miller, J.H. Microtubule-targeting agents are clinically successful due to both mitotic and interphase impairment of microtubule function. Bioorg. Med. Chem., 2014, 22(18), 5050-5059.
    • (2014) Bioorg. Med. Chem , vol.22 , Issue.18 , pp. 5050-5059
    • Field, J.J.1    Kanakkanthara, A.2    Miller, J.H.3
  • 110
    • 84930638256 scopus 로고    scopus 로고
    • Vinflunine in routine clinical practice for the treatment of advanced or metastatic urothelial cell carcinoma data from a prospective, multicenter experience
    • Retz, M.; de Geeter, P.; Goebell, P.J.; Matz, U.; de Schultz, W.; Hegele, A. Vinflunine in routine clinical practice for the treatment of advanced or metastatic urothelial cell carcinoma data from a prospective, multicenter experience. BMC Cancer, 2015, 75(1), 455.
    • (2015) BMC Cancer , vol.75 , Issue.1 , pp. 455
    • Retz, M.1    de Geeter, P.2    Goebell, P.J.3    Matz, U.4    de Schultz, W.5    Hegele, A.6
  • 111
    • 84897043920 scopus 로고    scopus 로고
    • Phase II study of treatment of advanced ovarian cancer with folate-receptor-targeted therapeutic (vintafolide) and companion SPECT-based imaging agent (99mTc-etarfolatide)
    • Morris, R.T.; Joyrich, R.N.; Naumann, R.W.; Shah, N.P.; Maurer, A.H.; Strauss, H.W.; Uszler, J.M.; Symanowski, J.T.; Ellis, P.R.; Harb, W.A. Phase II study of treatment of advanced ovarian cancer with folate-receptor-targeted therapeutic (vintafolide) and companion SPECT-based imaging agent (99mTc-etarfolatide). Ann. Oncol., 2014, 25(4), 852-858.
    • (2014) Ann. Oncol , vol.25 , Issue.4 , pp. 852-858
    • Morris, R.T.1    Joyrich, R.N.2    Naumann, R.W.3    Shah, N.P.4    Maurer, A.H.5    Strauss, H.W.6    Uszler, J.M.7    Symanowski, J.T.8    Ellis, P.R.9    Harb, W.A.10
  • 112
    • 77957374075 scopus 로고    scopus 로고
    • Microtubule-binding agents: A dynamic field of cancer therapeutics
    • Dumontet, C.; Jordan, M.A. Microtubule-binding agents: a dynamic field of cancer therapeutics. Nat. Rev. Drug Discov., 2010, 9(10), 790-803.
    • (2010) Nat. Rev. Drug Discov , vol.9 , Issue.10 , pp. 790-803
    • Dumontet, C.1    Jordan, M.A.2
  • 120
    • 77958043944 scopus 로고    scopus 로고
    • Maytansine and cellular metabolites of antibody-maytansinoid conjugates strongly suppress microtubule dynamics by binding to microtubules
    • Lopus, M.; Oroudjev, E.; Wilson, L.; Wilhelm, S.; Widdison, W.; Chari, R.; Jordan, M.A. Maytansine and cellular metabolites of antibody-maytansinoid conjugates strongly suppress microtubule dynamics by binding to microtubules. Mol. Cancer Ther., 2010, 9(10), 2689-2699.
    • (2010) Mol. Cancer Ther , vol.9 , Issue.10 , pp. 2689-2699
    • Lopus, M.1    Oroudjev, E.2    Wilson, L.3    Wilhelm, S.4    Widdison, W.5    Chari, R.6    Jordan, M.A.7
  • 121
    • 0024378608 scopus 로고
    • Binding of vinblastine to stabilized microtubules
    • Singer, W.D.; Jordan, M.A.; Wilson, L.; Himes, R.H. Binding of vinblastine to stabilized microtubules. Mol. Pharmacol., 1989, 56(3), 366-370.
    • (1989) Mol. Pharmacol , vol.56 , Issue.3 , pp. 366-370
    • Singer, W.D.1    Jordan, M.A.2    Wilson, L.3    Himes, R.H.4
  • 122
    • 0021148483 scopus 로고
    • Different effects of tubulin ligands on the intrachain cross-linking of beta 1-tubulin
    • Roach, M.C.; Ludueña, R.F. Different effects of tubulin ligands on the intrachain cross-linking of beta 1-tubulin. J. Biol. Chem., 1984, 259(19), 12063-12071.
    • (1984) J. Biol. Chem , vol.259 , Issue.19 , pp. 12063-12071
    • Roach, M.C.1    Ludueña, R.F.2
  • 124
    • 84943585191 scopus 로고    scopus 로고
    • Evaluation of targets for maytansinoid ADC therapy using a novel radiochemical Assay
    • Lai, K.C.; Deckert, J.; Setiady, Y.Y.; Shah, P.; Wang, L.; Chari, R.; Lambert, J.M. Evaluation of targets for maytansinoid ADC therapy using a novel radiochemical Assay. Pharm. Res., 2015, 32(11), 3593-3603.
    • (2015) Pharm. Res , vol.32 , Issue.11 , pp. 3593-3603
    • Lai, K.C.1    Deckert, J.2    Setiady, Y.Y.3    Shah, P.4    Wang, L.5    Chari, R.6    Lambert, J.M.7
  • 125
    • 80054121479 scopus 로고    scopus 로고
    • Phase I/II study of the anti-CD19 maytansinoid immuno conjugate SAR3419 administered weekly to patients (pts) with relapsed/refractory B-cell non-Hodgkin lymphoma (NHL)
    • Abstract No. 8017
    • Coiffier, B.; Ribrag, V.; Dupuis, J.; Tilly, H.; Haioun, C.; Morschhauser, F.; Lamy, T.; Copie-Bergman, C.; Brehar, O.; Houot, R. Phase I/II study of the anti-CD19 maytansinoid immuno conjugate SAR3419 administered weekly to patients (pts) with relapsed/refractory B-cell non-Hodgkin lymphoma (NHL). J. Clin. Oncol., 2011, 29(15), Abstract No. 8017.
    • (2011) J. Clin. Oncol , vol.29 , Issue.15
    • Coiffier, B.1    Ribrag, V.2    Dupuis, J.3    Tilly, H.4    Haioun, C.5    Morschhauser, F.6    Lamy, T.7    Copie-Bergman, C.8    Brehar, O.9    Houot, R.10
  • 126
    • 84891930782 scopus 로고    scopus 로고
    • Preclinical evaluation of IMGN853, an anti-FOLR1 antibody-maytansinoid conjugate, as a potential therapeutic for ovarian cancer
    • Whiteman, K.R.; Johnson, H.A.; Xu, S.; Carrigan, C.N.; Ab, O.; Pinkas, J. Preclinical evaluation of IMGN853, an anti-FOLR1 antibody-maytansinoid conjugate, as a potential therapeutic for ovarian cancer. Cancer Res., 2011, 71(Suppl. 8), 1760-1760.
    • (2011) Cancer Res , vol.71 , pp. 1760
    • Whiteman, K.R.1    Johnson, H.A.2    Xu, S.3    Carrigan, C.N.4    Ab, O.5    Pinkas, J.6
  • 127
    • 84947980546 scopus 로고    scopus 로고
    • Phase 1 study of IMGN853, a folate receptor alpha (FR {alpha})-targeting antibody-drug conjugate (ADC) in patients (Pts) with epithelial ovarian cancer (EOC) and other FRA-positive solid tumors
    • Abstract No. 5558
    • Borghaei, H.; O’Malley, D.M.; Seward, S.M.; Bauer, T.M.; Perez, R.P.; Oza, A.M.; Jeong, W.; Michenzie, M.F.; Kirby, M.W.; Chandorkar, G. Phase 1 study of IMGN853, a folate receptor alpha (FR {alpha})-targeting antibody-drug conjugate (ADC) in patients (Pts) with epithelial ovarian cancer (EOC) and other FRA-positive solid tumors. J. Clin. Oncol., 2015, 33, Abstract No. 5558.
    • (2015) J. Clin. Oncol , vol.33
    • Borghaei, H.1    O’Malley, D.M.2    Seward, S.M.3    Bauer, T.M.4    Perez, R.P.5    Oza, A.M.6    Jeong, W.7    Michenzie, M.F.8    Kirby, M.W.9    Chandorkar, G.10
  • 128
    • 0025183762 scopus 로고
    • Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites
    • Bai, R.L.; Pettit, G.R.; Hamel, E. Binding of dolastatin 10 to tubulin at a distinct site for peptide antimitotic agents near the exchangeable nucleotide and vinca alkaloid sites. J. Biol. Chem., 1990, 265(28), 17141-17149.
    • (1990) J. Biol. Chem , vol.265 , Issue.28 , pp. 17141-17149
    • Bai, R.L.1    Pettit, G.R.2    Hamel, E.3
  • 130
    • 0029133540 scopus 로고
    • The spongistatins, potently cytotoxic inhibitors of tubulin polymerization, bind in a distinct region of the vinca domain
    • Bai, R.; Taylor, G.F.; Cichacz, Z.A.; Herald, C.L.; Kepler, J.A.; Pettit, G.R.; Hamel, E. The spongistatins, potently cytotoxic inhibitors of tubulin polymerization, bind in a distinct region of the vinca domain. Biochemistry, 1995, 34(30), 9714-9721.
    • (1995) Biochemistry , vol.34 , Issue.30 , pp. 9714-9721
    • Bai, R.1    Taylor, G.F.2    Cichacz, Z.A.3    Herald, C.L.4    Kepler, J.A.5    Pettit, G.R.6    Hamel, E.7
  • 131
    • 0028240449 scopus 로고
    • Pironetin, a novel plant growth regulator produced by Streptomyces sp. NK10958. I. Taxonomy, production, isolation and preliminary characterization
    • Kobayashi, S.; Tsuchiya, K.; Harada, T.; Nishide, M.; Kurokawa, T.; Nakagawa, T.; Shimada, N.; Kobayashi, K. Pironetin, a novel plant growth regulator produced by Streptomyces sp. NK10958. I. Taxonomy, production, isolation and preliminary characterization. J. Antibiot., 1994, 47(6), 697-702.
    • (1994) J. Antibiot , vol.47 , Issue.6 , pp. 697-702
    • Kobayashi, S.1    Tsuchiya, K.2    Harada, T.3    Nishide, M.4    Kurokawa, T.5    Nakagawa, T.6    Shimada, N.7    Kobayashi, K.8
  • 133
    • 0033152543 scopus 로고    scopus 로고
    • Apoptosis induction via microtubule disassembly by an antitumour compound, pironetin
    • Kondoh, M.; Usui, T.; Nishikiori, T.; Mayumi, T.; Osada, H. Apoptosis induction via microtubule disassembly by an antitumour compound, pironetin. Biochem. J., 1999, 340(Pt 2), 411-416.
    • (1999) Biochem. J , vol.340 , pp. 411-416
    • Kondoh, M.1    Usui, T.2    Nishikiori, T.3    Mayumi, T.4    Osada, H.5
  • 135
    • 84978886681 scopus 로고    scopus 로고
    • Pironetin binds covalently to aCys316 and perturbs a major loop and helix of a-tubulin to inhibit microtubule formation
    • Prota, A.E.; Setter, J.; Waight, A.B.; Bargsten, K.; Murga, J.; Diaz, J.F.; Steinmetz, M.O. Pironetin binds covalently to aCys316 and perturbs a major loop and helix of a-tubulin to inhibit microtubule formation. J. Mol. Biol., 2016, 428(15), 2981-2988.
    • (2016) J. Mol. Biol , vol.428 , Issue.15 , pp. 2981-2988
    • Prota, A.E.1    Setter, J.2    Waight, A.B.3    Bargsten, K.4    Murga, J.5    Diaz, J.F.6    Steinmetz, M.O.7
  • 136
    • 34247112846 scopus 로고    scopus 로고
    • Antiproliferating activity of the mitotic inhibitor pironetin against vindesine and paclitaxel-resistant human small cell lung cancer H69 cells
    • Yoshida, M.; Matsui, Y.; Ikarashi, Y.; Usui, T.; Osada, H.; Wakasugi, H. Antiproliferating activity of the mitotic inhibitor pironetin against vindesine and paclitaxel-resistant human small cell lung cancer H69 cells. Anticancer Res., 2007, 27(2), 729-736.
    • (2007) Anticancer Res , vol.27 , Issue.2 , pp. 729-736
    • Yoshida, M.1    Matsui, Y.2    Ikarashi, Y.3    Usui, T.4    Osada, H.5    Wakasugi, H.6
  • 137
    • 84948710970 scopus 로고    scopus 로고
    • Radiation resistance: Cancer stem cells (CSCs) and their enigmatic prosurvival signaling
    • Skvortsova, I.; Debbage, P.; Kumar, V.; Skvortsov, S. Radiation resistance: cancer stem cells (CSCs) and their enigmatic prosurvival signaling. Semin. Cancer Biol., 2015, 35, 39-44.
    • (2015) Semin. Cancer Biol , vol.35 , pp. 39-44
    • Skvortsova, I.1    Debbage, P.2    Kumar, V.3    Skvortsov, S.4


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