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Volumn 75, Issue 6, 2010, Pages 541-550

Computational design and biological testing of highly cytotoxic colchicine ring a modifications

Author keywords

Colchicine; Cytotoxicity; Docking; Molecular modeling; Rational drug design

Indexed keywords

BETA TUBULIN; COLCHICINE; COLCHICINE DERIVATIVE; ISOPROTEIN; PACLITAXEL;

EID: 77951973915     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2010.00970.x     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 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
    • DOI 10.1016/0006-2952(90)90613-P
    • Bai R., Pettit G.R., Hamel E. (1990) 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. (Pubitemid 20187330)
    • (1990) Biochemical Pharmacology , vol.39 , Issue.12 , pp. 1941-1949
    • Bai, R.1    Pettit, G.R.2    Hamel, E.3
  • 2
    • 0018387446 scopus 로고
    • Promotion of microtubule assembly in vitro by taxol
    • Schiff P.B., Fant J., Horwitz S.B. (1979) Promotion of microtubule assembly in vitro by taxol. Nature 277 : 665 667. (Pubitemid 9114288)
    • (1979) Nature , vol.277 , Issue.5698 , pp. 665-667
    • Schiff, P.B.1    Fant, J.2    Horwitz, S.B.3
  • 3
  • 5
    • 0028012344 scopus 로고
    • In vitro analysis of microtubule assembly of isotypically pure tubulin dimers: Intrinsic differences in the assembly properties of αβII, αβIII, and αβIV tubulin dimers in the absence of microtubule-associated proteins
    • Lu Q., Luduena R.F. (1994) In vitro analysis of microtubule assembly of isotypically pure tubulin dimers. Intrinsic differences in the assembly properties of alpha beta II, alpha beta III, and alpha beta IV tubulin dimers in the absence of microtubule-associated proteins. J Biol Chem 269 : 2041 2047. (Pubitemid 24978467)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.3 , pp. 2041-2047
    • Lu, Q.1    Luduena, R.F.2
  • 6
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: Different gene products and covalent modifications
    • Luduena R.F. (1998) Multiple forms of tubulin: different gene products and covalent modifications. Int Rev Cytol 178 : 207 275.
    • (1998) Int Rev Cytol , vol.178 , pp. 207-275
    • Luduena, R.F.1
  • 7
    • 0031978187 scopus 로고    scopus 로고
    • Preparation of a monoclonal antibody specific for the class I isotype of β-tubulin: The β isotypes of tubulin differ in their cellular distributions within human tissues
    • DOI 10.1002/(SICI)1097-0169(1998)39:4<273::AID-CM3>3.0.CO;2-4
    • Roach M.C., Boucher V.L., Walss C., Ravdin P.M., Luduena R.F. (1998) Preparation of a monoclonal antibody specific for the class I isotype of beta-tubulin: the beta isotypes of tubulin differ in their cellular distributions within human tissues. Cell Motil Cytoskeleton 39 : 273 285. (Pubitemid 28153231)
    • (1998) Cell Motility and the Cytoskeleton , vol.39 , Issue.4 , pp. 273-285
    • Roach, M.C.1    Boucher, V.L.2    Walss, C.3    Ravdin, P.M.4    Luduena, R.F.5
  • 8
    • 0038353464 scopus 로고    scopus 로고
    • Different effects of vinblastine on the polymerization of isotypically purified tubulins from bovine brain
    • Khan I.A., Luduena R.F. (2003) Different effects of vinblastine on the polymerization of isotypically purified tubulins from bovine brain. Invest New Drugs 21 : 3 13.
    • (2003) Invest New Drugs , vol.21 , pp. 3-13
    • Khan, I.A.1    Luduena, R.F.2
  • 9
    • 0026645572 scopus 로고
    • Kinetics of colchicine binding to purified beta-tubulin isotypes from bovine brain
    • Banerjee A., Luduena R.F. (1992) Kinetics of colchicine binding to purified beta-tubulin isotypes from bovine brain. J Biol Chem 267 : 13335 13339.
    • (1992) J Biol Chem , vol.267 , pp. 13335-13339
    • Banerjee, A.1    Luduena, R.F.2
  • 10
    • 0036240628 scopus 로고    scopus 로고
    • Interaction of nocodazole with tubulin isotypes
    • Schwarz P.M., Luduena R.F. (2002) Interaction of nocodazole with tubulin isotypes. Drug Dev Res 55 : 91 96.
    • (2002) Drug Dev Res , vol.55 , pp. 91-96
    • Schwarz, P.M.1    Luduena, R.F.2
  • 11
    • 0345874561 scopus 로고    scopus 로고
    • Class III β-tubulin isotype: A key cytoskeletal protein at the crossroads of developmental neurobiology and tumor neuropathology
    • Katsetos C.D., Legido A., Perentes E., Mork S.J. (2003) Class III beta-tubulin isotype: a key cytoskeletal protein at the crossroads of developmental neurobiology and tumor neuropathology. J Child Neurol 18 : 851 866. (Pubitemid 38088739)
    • (2003) Journal of Child Neurology , vol.18 , Issue.12 , pp. 851-866
    • Katsetos, C.D.1    Legido, A.2    Perentes, E.3    Mork, S.J.4
  • 14
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • DOI 10.1038/nature02393
    • Ravelli R.B., Gigant B., Curmi P.A., Jourdain I., Lachkar S., Sobel A., Knossow M. (2004) Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428 : 198 202. (Pubitemid 38374318)
    • (2004) Nature , vol.428 , Issue.6979 , pp. 198-202
    • Ravelli, R.B.G.1    Gigant, B.2    Curmi, P.A.3    Jourdain, I.4    Lachkar, S.5    Sobel, A.6    Knossow, M.7
  • 16
    • 0029063397 scopus 로고
    • Structure of tubulin at 6.5 A and location of the taxol-binding site
    • Nogales E., Wolf S.G., Khan I.A., Luduena R.F., Downing K.H. (1995) Structure of tubulin at 6.5 A and location of the taxol-binding site. Nature 375 : 424 427.
    • (1995) Nature , vol.375 , pp. 424-427
    • Nogales, E.1    Wolf, S.G.2    Khan, I.A.3    Luduena, R.F.4    Downing, K.H.5
  • 17
    • 31944439260 scopus 로고    scopus 로고
    • Comparative modelling of human β tubulin isotypes and implications for drug binding
    • DOI 10.1088/0957-4484/17/4/014, PII S0957448406048835
    • Huzil J.T., Luduena R.F., Tuszynski J. (2006) Comparative modelling of human beta-tubulin isotypes and implications for drug binding. Nanotechnology 17 : S90 S100. (Pubitemid 43190484)
    • (2006) Nanotechnology , vol.17 , Issue.4
    • Huzil, J.T.1    Luduena, R.F.2    Tuszynski, J.3
  • 19
    • 0033920430 scopus 로고    scopus 로고
    • Rapid colchicine competition-binding scintillation proximity assay using biotin-labeled tubulin
    • Tahir S.K., Kovar P., Rosenberg S.H., Ng S.C. (2000) Rapid colchicine competition-binding scintillation proximity assay using biotin-labeled tubulin. BioTechniques 29 : 156 160. (Pubitemid 30439429)
    • (2000) BioTechniques , vol.29 , Issue.1 , pp. 156-160
    • Tahir, S.K.1    Kovar, P.2    Rosenberg, S.H.3    Ng, S.-C.4
  • 20
    • 0029414976 scopus 로고
    • 3H]mebendazole binding to tubulin by structurally diverse microtubule inhibitors which interact at the colchicine binding site
    • Russell G.J., Lacey E. (1995) Inhibition of [3H]mebendazole binding to tubulin by structurally diverse microtubule inhibitors which interact at the colchicine binding site. Biochem Mol Biol Int 35 : 1153 1159. (Pubitemid 26174736)
    • (1995) Biochemistry and Molecular Biology International , vol.35 , Issue.6 , pp. 1153-1159
    • Russell, G.J.1    Lacey, E.2
  • 21
    • 0017227021 scopus 로고
    • Interaction of oncodazole (R
    • 17934), a new antitumoral drug, with rat brain tubulin
    • Hoebeke J., Van Nijen G., De Brabander M. (1976) Interaction of oncodazole (R 17934), a new antitumoral drug, with rat brain tubulin. Biochem Biophys Res Commun 69 : 319 324.
    • (1976) Biochem Biophys Res Commun , vol.69 , pp. 319-324
    • Hoebeke, J.1    Van Nijen, G.2    De Brabander, M.3
  • 22
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • DOI 10.1007/S008940100045
    • Lindahl E., Hess B., van der Spoel D. (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Model 7 : 306 317. (Pubitemid 36153547)
    • (2001) Journal of Molecular Modeling , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 24
    • 0041781898 scopus 로고    scopus 로고
    • Detailed analysis of grid-based molecular docking: A case study of CDOCKER-A CHARMm-based MD docking algorithm
    • Wu G., Robertson D.H., Brooks C.L., Vieth M. (2003) Detailed analysis of grid-based molecular docking: a case study of CDOCKER-A CHARMm-based MD docking algorithm. J Comput Chem 24 : 1549 1562.
    • (2003) J Comput Chem , vol.24 , pp. 1549-1562
    • Wu, G.1    Robertson, D.H.2    Brooks, C.L.3    Vieth, M.4
  • 25
    • 0023220088 scopus 로고
    • A novel synthesis of colchicide and analogues from thiocolchicine and congeners: Reevaluation of colchicide as a potential antitumor agent
    • DOI 10.1021/jm00387a028
    • Dumont R., Brossi A., Chignell C.F., Quinn F.R., Suffness M. (1987) A novel synthesis of colchicide and analogues from thiocolchicine and congeners: reevaluation of colchicide as a potential antitumor agent. J Med Chem 30 : 732 735. (Pubitemid 17065215)
    • (1987) Journal of Medicinal Chemistry , vol.30 , Issue.4 , pp. 732-735
    • Dumont, R.1    Brossi, A.2    Chignell, C.F.3
  • 26
    • 70350570376 scopus 로고    scopus 로고
    • The efficacy of new colchicine derivatives and viability of the T-Lymphoblastoid cells in three-dimensional culture using 19F MRI and HPLC-UV ex vivo
    • Bartusik D., Tomanek B., Lattova E., Perreault H., Tuszynski J., Fallone G. (2009) The efficacy of new colchicine derivatives and viability of the T-Lymphoblastoid cells in three-dimensional culture using 19F MRI and HPLC-UV ex vivo. Bioorg Chem 37 : 193 201.
    • (2009) Bioorg Chem , vol.37 , pp. 193-201
    • Bartusik, D.1    Tomanek, B.2    Lattova, E.3    Perreault, H.4    Tuszynski, J.5    Fallone, G.6
  • 27
    • 0017646208 scopus 로고
    • Microtubule assembly in vitro. Purification of assembly-promoting factors
    • DOI 10.1111/j.1432-1033.1977.tb11726.x
    • Fellous A., Francon J., Lennon A.M., Nunez J. (1977) Microtubule assembly in vitro. Purification of assembly-promoting factors. Eur J Biochem 78 : 167 174. (Pubitemid 8164734)
    • (1977) European Journal of Biochemistry , vol.78 , Issue.1 , pp. 167-174
    • Fellous, A.1    Francon, J.2    Lennon, A.M.3    Nunez, J.4
  • 28
  • 29
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of αβ-tubulin at 3.5 Å resolution
    • DOI 10.1006/jmbi.2001.5077
    • Lowe J., Li H., Downing K.H., Nogales E. (2001) Refined structure of alpha beta-tubulin at 3.5 A resolution. J Mol Biol 313 : 1045 1057. (Pubitemid 33081900)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.5 , pp. 1045-1057
    • Lowe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 31
    • 0027192087 scopus 로고
    • Antitumor agents. 141. Synthesis and biological evaluation of novel thiocolchicine analogs: N-acyl-, N-aroyl-, and N-(substituted benzyl)deacetylthiocolchicines as potent cytotoxic and antimitotic compounds
    • DOI 10.1021/jm00062a021
    • Sun L., Hamel E., Lin C.M., Hastie S.B., Pyluck A., Lee K.H. (1993) Antitumor agents. 141. Synthesis and biological evaluation of novel thiocolchicine analogs: N-acyl-, N-aroyl-, and N-(substituted benzyl)deacetylthiocolchicines as potent cytotoxic and antimitotic compounds. J Med Chem 36 : 1474 1479. (Pubitemid 23164505)
    • (1993) Journal of Medicinal Chemistry , vol.36 , Issue.10 , pp. 1474-1479
    • Sun, L.1    Hamel, E.2    Lin, C.M.3    Hastie, S.B.4    Pyluck, A.5    Lee, K.-H.6
  • 32
    • 35348864558 scopus 로고    scopus 로고
    • Validation of an automated procedure for the prediction of relative free energies of binding on a set of aldose reductase inhibitors
    • DOI 10.1016/j.bmc.2007.08.019, PII S0968089607006931
    • Ferrari A.M., Degliesposti G., Sgobba M., Rastelli G. (2007) Validation of an automated procedure for the prediction of relative free energies of binding on a set of aldose reductase inhibitors. Bioorg Med Chem 15 : 7865 7877. (Pubitemid 47575902)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.24 , pp. 7865-7877
    • Ferrari, A.M.1    Degliesposti, G.2    Sgobba, M.3    Rastelli, G.4
  • 36
    • 0036290799 scopus 로고    scopus 로고
    • IV-tubulin isotypes in paclitaxel-resistant MCF-7 breast cancer cells
    • DOI 10.1016/S0006-291X(02)00269-3, PII S0006291X02002693
    • Banerjee A. (2002) Increased levels of tyrosinated alpha-, beta(III)-, and beta(IV)-tubulin isotypes in paclitaxel-resistant MCF-7 breast cancer cells. Biochem Biophys Res Commun 293 : 598 601. (Pubitemid 34694251)
    • (2002) Biochemical and Biophysical Research Communications , vol.293 , Issue.1 , pp. 598-601
    • Banerjee, A.1
  • 37
    • 0030940117 scopus 로고    scopus 로고
    • Taxol differentially modulates the dynamics of microtubules assembled from unfractionated and purified β-tubulin isotypes
    • DOI 10.1021/bi962724m
    • Derry W.B., Wilson L., Khan I.A., Luduena R.F., Jordan M.A. (1997) Taxol differentially modulates the dynamics of microtubules assembled from unfractionated and purified beta-tubulin isotypes. Biochemistry 36 : 3554 3562. (Pubitemid 27143509)
    • (1997) Biochemistry , vol.36 , Issue.12 , pp. 3554-3562
    • Derry, W.B.1    Wilson, L.2    Khan, I.A.3    Luduena, R.F.4    Jordan, M.A.5
  • 41
    • 0028805270 scopus 로고
    • Interaction of bovine brain tubulin with the 4(1H)-pyrizinone derivative IKP104, an antimitotic drug with a complex set of effects on the conformational stability of the tubulin molecule
    • Luduena R.F., Roach M.C., Prasad V., Chaudhuri A.R., Tomita I., Mizuhashi F., Murata K. (1995) Interaction of bovine brain tubulin with the 4(1H)-pyrizinone derivative IKP104, an antimitotic drug with a complex set of effects on the conformational stability of the tubulin molecule. Biochemistry 34 : 15751 15759.
    • (1995) Biochemistry , vol.34 , pp. 15751-15759
    • Luduena, R.F.1    Roach, M.C.2    Prasad, V.3    Chaudhuri, A.R.4    Tomita, I.5    Mizuhashi, F.6    Murata, K.7
  • 42
    • 0032584298 scopus 로고    scopus 로고
    • Beta-tubulin isotypes purified from bovine brain have different relative stabilities
    • Schwarz P.M., Liggins J.R., Luduena R.F. (1998) Beta-tubulin isotypes purified from bovine brain have different relative stabilities. Biochemistry 37 : 4687 4692.
    • (1998) Biochemistry , vol.37 , pp. 4687-4692
    • Schwarz, P.M.1    Liggins, J.R.2    Luduena, R.F.3
  • 43
    • 0031745659 scopus 로고    scopus 로고
    • Tubulin stability and decay: Mediation by two distinct classes of IKP104-binding sites
    • DOI 10.1023/A:1022579930546
    • Chaudhuri A.R., Tomita I., Mizuhashi F., Murata K., Luduena R.F. (1998) Tubulin stability and decay: mediation by two distinct classes of IKP104-binding sites. J Protein Chem 17 : 303 309. (Pubitemid 28242300)
    • (1998) Journal of Protein Chemistry , vol.17 , Issue.4 , pp. 303-309
    • Chaudhuri, A.R.1    Tomita, I.2    Mizuhashi, F.3    Murata, K.4    Luduena, R.F.5
  • 44
    • 0034634366 scopus 로고    scopus 로고
    • The interaction of the B-ring of colchicine with alpha-tubulin: A novel footprinting approach
    • Chaudhuri A.R., Seetharamalu P., Schwarz P.M., Hausheer F.H., Luduena R.F. (2000) The interaction of the B-ring of colchicine with alpha-tubulin: a novel footprinting approach. J Mol Biol 303 : 679 692.
    • (2000) J Mol Biol , vol.303 , pp. 679-692
    • Chaudhuri, A.R.1    Seetharamalu, P.2    Schwarz, P.M.3    Hausheer, F.H.4    Luduena, R.F.5
  • 47
    • 35148854099 scopus 로고    scopus 로고
    • Class III β-tubulin mediates sensitivity to chemotherapeutic drugs in non-small cell lung cancer
    • DOI 10.1158/0008-5472.CAN-07-0509
    • Gan P.P., Pasquier E., Kavallaris M. (2007) Class III beta-tubulin mediates sensitivity to chemotherapeutic drugs in non small cell lung cancer. Cancer Res 67 : 9356 9363. (Pubitemid 47535925)
    • (2007) Cancer Research , vol.67 , Issue.19 , pp. 9356-9363
    • Pei, P.G.1    Pasquier, E.2    Kavallaris, M.3
  • 48
    • 0029973041 scopus 로고    scopus 로고
    • Increase of β(III)- and β(IVa)-tubulin isotypes in human prostate carcinoma cells as a result of estramustine resistance
    • Ranganathan S., Dexter D.W., Benetatos C.A., Chapman A.E., Tew K.D., Hudes G.R. (1996) Increase of beta(III)- and beta(IVa)-tubulin isotopes in human prostate carcinoma cells as a result of estramustine resistance. Cancer Res 56 : 2584 2589. (Pubitemid 26170695)
    • (1996) Cancer Research , vol.56 , Issue.11 , pp. 2584-2589
    • Ranganathan, S.1    Dexter, D.W.2    Benetatos, C.A.3    Chapman, A.E.4    Tew, K.D.5    Hudes, G.R.6


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