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Volumn 46, Issue 41, 2007, Pages 11514-11527

Enhanced microtubule binding and tubulin assembly properties of conformationally constrained paclitaxel derivatives

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BIOASSAY; CELLS; CONFORMATIONS; DERIVATIVES; POLYMERIZATION;

EID: 35348833682     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700753y     Document Type: Article
Times cited : (17)

References (68)
  • 2
    • 24644500678 scopus 로고    scopus 로고
    • Molecular mechanism of antitumor activity of taxanes in lung cancer
    • Zhao, J., Kim, J. E., Reed, E., and Li, Q. Q. (2005) Molecular mechanism of antitumor activity of taxanes in lung cancer, Int. J. Oncol. 27, 247-256.
    • (2005) Int. J. Oncol , vol.27 , pp. 247-256
    • Zhao, J.1    Kim, J.E.2    Reed, E.3    Li, Q.Q.4
  • 5
    • 0018387446 scopus 로고
    • Promotion of microtubule assembly in vitro by taxol
    • Schiff, P. B., Fant, J., and Horwitz, S. B. (1979) Promotion of microtubule assembly in vitro by taxol, Nature 277, 665-667.
    • (1979) Nature , vol.277 , pp. 665-667
    • Schiff, P.B.1    Fant, J.2    Horwitz, S.B.3
  • 6
    • 0019859353 scopus 로고
    • Taxol binds to polymerized tubulin in vitro
    • Parness, J., and Horwitz, S. B. (1981) Taxol binds to polymerized tubulin in vitro, J. Cell Biol. 91, 479-487.
    • (1981) J. Cell Biol , vol.91 , pp. 479-487
    • Parness, J.1    Horwitz, S.B.2
  • 7
    • 0028708677 scopus 로고
    • Taxol (paclitaxel): Mechanisms of action
    • Horwitz, S. B. (1994) Taxol (paclitaxel): mechanisms of action, Ann. Oncol. 5 (Suppl. 6), S3-S6.
    • (1994) Ann. Oncol , vol.5 , Issue.SUPPL. 6
    • Horwitz, S.B.1
  • 8
    • 0030020158 scopus 로고    scopus 로고
    • Mitotic block induced in HeLa cells by low concentrations of paclitaxel (Taxol) results in abnormal mitotic exit and apoptotic cell death
    • Jordan, M. A., Wendell, K., Gardiner, S., Deny, W. B., Copp, H., and Wilson, L. (1996) Mitotic block induced in HeLa cells by low concentrations of paclitaxel (Taxol) results in abnormal mitotic exit and apoptotic cell death, Cancer Res. 56, 816-825.
    • (1996) Cancer Res , vol.56 , pp. 816-825
    • Jordan, M.A.1    Wendell, K.2    Gardiner, S.3    Deny, W.B.4    Copp, H.5    Wilson, L.6
  • 11
    • 0028188080 scopus 로고
    • Paclitaxel: A new antimitotic chemotherapeutic agent
    • Gotaskie, G. E., and Andreassi, B. F. (1994) Paclitaxel: a new antimitotic chemotherapeutic agent, Cancer Pract. 2, 27-33.
    • (1994) Cancer Pract , vol.2 , pp. 27-33
    • Gotaskie, G.E.1    Andreassi, B.F.2
  • 12
    • 11244309692 scopus 로고    scopus 로고
    • New microtubule/tubulin-targeted anticancer drugs and novel chemotherapeutic strategies
    • Wilson, L., and Jordan, M. A. (2004) New microtubule/tubulin-targeted anticancer drugs and novel chemotherapeutic strategies, J. Chemother. 16 (Suppl. 4), 83-85.
    • (2004) J. Chemother , vol.16 , Issue.SUPPL. 4 , pp. 83-85
    • Wilson, L.1    Jordan, M.A.2
  • 13
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • Jordan, M. A., and Wilson, L. (2004) Microtubules as a target for anticancer drugs, Nat. Rev. Cancer 4, 253-265.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 14
    • 0035025093 scopus 로고    scopus 로고
    • Progress in the development of alternative pharmaceutical formulations of taxanes
    • Nuijen, B., Bouma, M., Schellens, J. H., and Beijnen, J. H. (2001) Progress in the development of alternative pharmaceutical formulations of taxanes, Invest. New Drugs 19, 143-153.
    • (2001) Invest. New Drugs , vol.19 , pp. 143-153
    • Nuijen, B.1    Bouma, M.2    Schellens, J.H.3    Beijnen, J.H.4
  • 15
    • 0001892688 scopus 로고    scopus 로고
    • Enantiopure fluorine-containing taxoids: Potent anticancer agents and versatile probes for biomedical problems
    • Ojima, I., Inoue, T., and Chakravarty, S. (1999) Enantiopure fluorine-containing taxoids: potent anticancer agents and versatile probes for biomedical problems, J. Fluorine Chem. 97, 3-10.
    • (1999) J. Fluorine Chem , vol.97 , pp. 3-10
    • Ojima, I.1    Inoue, T.2    Chakravarty, S.3
  • 17
    • 0032508365 scopus 로고    scopus 로고
    • Identification of the domains of photoincorporation of the 3′- and 7-benzophenone analogues of taxol in the carboxyl-terminal half of murine mdr1b P-glycoprotein
    • Wu, Q., Bounaud, P. Y., Kuduk, S. D., Yang, C. P., Ojima, I., Horwitz, S. B., and Orr, G. A. (1998) Identification of the domains of photoincorporation of the 3′- and 7-benzophenone analogues of taxol in the carboxyl-terminal half of murine mdr1b P-glycoprotein, Biochemistry 37, 11272-11279.
    • (1998) Biochemistry , vol.37 , pp. 11272-11279
    • Wu, Q.1    Bounaud, P.Y.2    Kuduk, S.D.3    Yang, C.P.4    Ojima, I.5    Horwitz, S.B.6    Orr, G.A.7
  • 18
    • 0033621479 scopus 로고    scopus 로고
    • Characterization of the Taxol binding site on the microtubule. Identification of Arg(282) in beta-tubulin as the site of photoincorporation of a 7-benzophenone analogue of Taxol
    • Rao, S., He, L., Chakravarty, S., Ojima, I., Orr, G. A., and Horwitz, S. B. (1999) Characterization of the Taxol binding site on the microtubule. Identification of Arg(282) in beta-tubulin as the site of photoincorporation of a 7-benzophenone analogue of Taxol, J. Biol. Chem. 274, 37990-37994.
    • (1999) J. Biol. Chem , vol.274 , pp. 37990-37994
    • Rao, S.1    He, L.2    Chakravarty, S.3    Ojima, I.4    Orr, G.A.5    Horwitz, S.B.6
  • 19
    • 0028861177 scopus 로고
    • Characterization of the taxol binding site on the microtubule. 2-(m-Azidobenzoyl)taxol photolabels a peptide (amino acids 217-231) of beta-tubulin
    • Rao, S., Orr, G. A., Chaudhary, A. G., Kingston, D. G., and Horwitz, S. B. (1995) Characterization of the taxol binding site on the microtubule. 2-(m-Azidobenzoyl)taxol photolabels a peptide (amino acids 217-231) of beta-tubulin, J. Biol. Chem. 270, 20235-20238.
    • (1995) J. Biol. Chem , vol.270 , pp. 20235-20238
    • Rao, S.1    Orr, G.A.2    Chaudhary, A.G.3    Kingston, D.G.4    Horwitz, S.B.5
  • 20
    • 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., and 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
  • 21
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the α, β- tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S. G., and Downing, K. H. (1998) Structure of the α, β- tubulin dimer by electron crystallography, Nature 391, 199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 23
    • 0035942226 scopus 로고    scopus 로고
    • The binding conformation of Taxol in beta-tubulin: A model based on electron crystallographic density
    • Snyder, J. P., Nettles, J. H., Cornett, B., Downing, K. H., and Nogales, E. (2001) The binding conformation of Taxol in beta-tubulin: a model based on electron crystallographic density, Proc. Natl. Acad. Sci. U.S.A. 98, 5312-5316.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 5312-5316
    • Snyder, J.P.1    Nettles, J.H.2    Cornett, B.3    Downing, K.H.4    Nogales, E.5
  • 26
    • 0027383827 scopus 로고
    • Thermodynamics of ligand-induced assembly of tubulin
    • Diaz, J. F., Menendez, M., and Andreu, J. M. (1993) Thermodynamics of ligand-induced assembly of tubulin, Biochemistry 32, 10067-10077.
    • (1993) Biochemistry , vol.32 , pp. 10067-10077
    • Diaz, J.F.1    Menendez, M.2    Andreu, J.M.3
  • 27
    • 0034714203 scopus 로고    scopus 로고
    • Molecular recognition of taxol by microtubules. Kinetics and thermodynamics of binding of fluorescent taxol derivatives to an exposed site
    • Diaz, J. F., Strobe, R., Engelborghs, Y., Souto, A. A., and Andreu, J. M. (2000) Molecular recognition of taxol by microtubules. Kinetics and thermodynamics of binding of fluorescent taxol derivatives to an exposed site, J. Biol. Chem. 275, 26265-26276.
    • (2000) J. Biol. Chem , vol.275 , pp. 26265-26276
    • Diaz, J.F.1    Strobe, R.2    Engelborghs, Y.3    Souto, A.A.4    Andreu, J.M.5
  • 28
    • 0020009818 scopus 로고
    • Preparation of tubulin from brain
    • Williams, R. C., Jr., and Lee, J. C. (1982) Preparation of tubulin from brain, Methods Enzymol. 85 (Part B), 376-385.
    • (1982) Methods Enzymol , vol.85 , Issue.PART B , pp. 376-385
    • Williams Jr., R.C.1    Lee, J.C.2
  • 29
    • 0018337981 scopus 로고
    • Preparation of nucleotide-depleted F1 and binding of adenine nucleotides and analogs to the depleted enzyme
    • Penefsky, H. S. (1979) Preparation of nucleotide-depleted F1 and binding of adenine nucleotides and analogs to the depleted enzyme, Methods Enzymol. 55, 377-380.
    • (1979) Methods Enzymol , vol.55 , pp. 377-380
    • Penefsky, H.S.1
  • 30
    • 0018170308 scopus 로고
    • Reversible dissociation of the α, β dimer of tubulin from bovine brain
    • Detrich, H. W., 3rd, and Williams, R. C. (1978) Reversible dissociation of the α, β dimer of tubulin from bovine brain, Biochemistry 17, 3900-3907.
    • (1978) Biochemistry , vol.17 , pp. 3900-3907
    • Detrich 3rd, H.W.1    Williams, R.C.2
  • 31
    • 0031048573 scopus 로고    scopus 로고
    • Thermodynamic and structural analysis of microtubule assembly: The role of GTP hydrolysis
    • Vulevic, B., and Correia, J. J. (1997) Thermodynamic and structural analysis of microtubule assembly: the role of GTP hydrolysis, Biophys. J. 72, 1357-1375.
    • (1997) Biophys. J , vol.72 , pp. 1357-1375
    • Vulevic, B.1    Correia, J.J.2
  • 32
    • 0034711725 scopus 로고    scopus 로고
    • Equilibrium studies of a fluorescent paclitaxel derivative binding to microtubules
    • Li, Y., Edsall, R., Jr., Jagtap, P. G., Kingston, D. G., and Bane, S. (2000) Equilibrium studies of a fluorescent paclitaxel derivative binding to microtubules, Biochemistry 39, 616-623.
    • (2000) Biochemistry , vol.39 , pp. 616-623
    • Li, Y.1    Edsall Jr., R.2    Jagtap, P.G.3    Kingston, D.G.4    Bane, S.5
  • 33
    • 0025308218 scopus 로고
    • Interactions of tubulin with guanylyl-(beta-gamma-methylene)diphosphonate. Formation and assembly of a stoichiometric complex
    • Seckler, R., Wu, G. M., and Timasheff, S. N. (1990) Interactions of tubulin with guanylyl-(beta-gamma-methylene)diphosphonate. Formation and assembly of a stoichiometric complex, J. Biol. Chem. 265, 7655-7661.
    • (1990) J. Biol. Chem , vol.265 , pp. 7655-7661
    • Seckler, R.1    Wu, G.M.2    Timasheff, S.N.3
  • 34
    • 0032584067 scopus 로고    scopus 로고
    • Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (α, β) methylenediphosphonate
    • Muller-Reichert, T., Chretien, D., Severin, F., and Hyman, A. A. (1998) Structural changes at microtubule ends accompanying GTP hydrolysis: information from a slowly hydrolyzable analogue of GTP, guanylyl (α, β) methylenediphosphonate, Proc. Natl. Acad. Sci. U.S.A. 95, 3661-3666.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 3661-3666
    • Muller-Reichert, T.1    Chretien, D.2    Severin, F.3    Hyman, A.A.4
  • 35
    • 0027075124 scopus 로고
    • Role of GTP hydrolysis in microtubule dynamics: Information from a slowly hydrolyzable analogue, GMPCPP
    • Hyman, A. A., Salser, S., Drechsel, D. N., Unwin, N., and Mitchison, T. J. (1992) Role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP, Mol. Biol. Cell 3, 1155-1167.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1155-1167
    • Hyman, A.A.1    Salser, S.2    Drechsel, D.N.3    Unwin, N.4    Mitchison, T.J.5
  • 36
    • 0017334810 scopus 로고
    • In vitro reconstitution of calf brain microtubules: Effects of solution variables
    • Lee, J. C., and Timasheff, S. N. (1977) In vitro reconstitution of calf brain microtubules: effects of solution variables, Biochemistry 16, 1754-1764.
    • (1977) Biochemistry , vol.16 , pp. 1754-1764
    • Lee, J.C.1    Timasheff, S.N.2
  • 37
    • 0027467778 scopus 로고
    • Assembly of purified GDP-tubulin into microtubules induced by taxol and taxotere: Reversibility, ligand stoichiometry, and competition
    • Diaz, J. F., and Andreu, J. M. (1993) Assembly of purified GDP-tubulin into microtubules induced by taxol and taxotere: reversibility, ligand stoichiometry, and competition, Biochemistry 32, 2747-2755.
    • (1993) Biochemistry , vol.32 , pp. 2747-2755
    • Diaz, J.F.1    Andreu, J.M.2
  • 38
    • 0035849572 scopus 로고    scopus 로고
    • Baccatin III induces assembly of purified tubulin into long microtubules
    • Chatterjee, S. K., Barron, D. M., Vos, S., and Bane, S. (2001) Baccatin III induces assembly of purified tubulin into long microtubules, Biochemistry 40, 6964-6970.
    • (2001) Biochemistry , vol.40 , pp. 6964-6970
    • Chatterjee, S.K.1    Barron, D.M.2    Vos, S.3    Bane, S.4
  • 39
    • 0001061464 scopus 로고    scopus 로고
    • Merck molecular force field .4. Conformational energies and geometries for MMFF94
    • Halgren, T. A., and Nachbar, R. B. (1996) Merck molecular force field .4. Conformational energies and geometries for MMFF94, J. Comput. Chem. 17, 587-615.
    • (1996) J. Comput. Chem , vol.17 , pp. 587-615
    • Halgren, T.A.1    Nachbar, R.B.2
  • 40
    • 0001242234 scopus 로고    scopus 로고
    • MMFF VII. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular-interaction energies and geometries
    • Halgren, T. A. (1999) MMFF VII. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular-interaction energies and geometries, J. Comput. Chem. 20, 730-748.
    • (1999) J. Comput. Chem , vol.20 , pp. 730-748
    • Halgren, T.A.1
  • 41
    • 35348922314 scopus 로고    scopus 로고
    • Maestro, version 7.5 (2006) Schrodinger, LLC, New York
    • Maestro, version 7.5 (2006) Schrodinger, LLC, New York.
  • 42
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of α, β-tubulin at 3.5 A resolution
    • Lowe, J., Li, H., Downing, K. H., and Nogales, E. (2001) Refined structure of α, β-tubulin at 3.5 A resolution, J. Mol. Biol. 313, 1045-1057.
    • (2001) J. Mol. Biol , vol.313 , pp. 1045-1057
    • Lowe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 43
    • 35348906755 scopus 로고    scopus 로고
    • Glide, version 4.0 (2005) Schrodinger, LLC, New York
    • Glide, version 4.0 (2005) Schrodinger, LLC, New York. http://www. schrodinger.com.
  • 44
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., Hess, B., and Spoel, D. v. d. (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis, J. Mol. Model. 7, 306-317.
    • (2001) J. Mol. Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Spoel, D.V.D.3
  • 45
  • 46
    • 35348859567 scopus 로고    scopus 로고
    • At
    • At http://davapc1.bioch.dundee.ac.uk/cgi-bin/prodrg_beta.
  • 48
  • 50
    • 33846823909 scopus 로고
    • Particle Mesh Ewald - an N.Log(N) Method for Ewald Sums in Large Systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle Mesh Ewald - an N.Log(N) Method for Ewald Sums in Large Systems, J. Chem. Phys. 98, 10089-10092.
    • (1993) J. Chem. Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 53
    • 0024538551 scopus 로고
    • A synchrotron X-ray scattering characterization of purified tubulin and of its expansion induced by mild detergent binding
    • Andreu, J. M., Garcia de Ancos, J., Starling, D., Hodgkinson, J. L., and Bordas, J. (1989) A synchrotron X-ray scattering characterization of purified tubulin and of its expansion induced by mild detergent binding, Biochemistry 28, 4036-4040.
    • (1989) Biochemistry , vol.28 , pp. 4036-4040
    • Andreu, J.M.1    Garcia de Ancos, J.2    Starling, D.3    Hodgkinson, J.L.4    Bordas, J.5
  • 54
    • 0037375622 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of C-3′NH/C-10 and C-2/C-10 modified paclitaxel analogues
    • Baloglu, E., Hoch, J. M., Chatterjee, S. K., Ravindra, R., Bane, S., and Kingston, D. G. (2003) Synthesis and biological evaluation of C-3′NH/C-10 and C-2/C-10 modified paclitaxel analogues, Bioorg. Med. Chem. 11, 1557-1568.
    • (2003) Bioorg. Med. Chem , vol.11 , pp. 1557-1568
    • Baloglu, E.1    Hoch, J.M.2    Chatterjee, S.K.3    Ravindra, R.4    Bane, S.5    Kingston, D.G.6
  • 56
    • 0028916505 scopus 로고
    • Differential effects of paclitaxel (Taxol) analogs modified at positions C-2, C-7, and C-3′ on tubulin polymerization and polymer stabilization: Identification of a hyperactive paclitaxel derivative
    • Grover, S., Rimoldi, J. M., Molinero, A. A., Chaudhary, A. G., Kingston, D. G., and Hamel, E. (1995) Differential effects of paclitaxel (Taxol) analogs modified at positions C-2, C-7, and C-3′ on tubulin polymerization and polymer stabilization: identification of a hyperactive paclitaxel derivative, Biochemistry 34, 3927-3934.
    • (1995) Biochemistry , vol.34 , pp. 3927-3934
    • Grover, S.1    Rimoldi, J.M.2    Molinero, A.A.3    Chaudhary, A.G.4    Kingston, D.G.5    Hamel, E.6
  • 57
    • 0030580283 scopus 로고    scopus 로고
    • The multiple origins of cooperativity in binding to multi-site lattices
    • Sackett, D. L., and Saroff, H. A. (1996) The multiple origins of cooperativity in binding to multi-site lattices, FEBS Lett. 397, 1-6.
    • (1996) FEBS Lett , vol.397 , pp. 1-6
    • Sackett, D.L.1    Saroff, H.A.2
  • 58
    • 24944590338 scopus 로고    scopus 로고
    • The taxol pharmacophore and the T-taxol bridging principle
    • Kingston, D. G., Bane, S., and Snyder, J. P. (2005) The taxol pharmacophore and the T-taxol bridging principle, Cell Cycle 4, 279-289.
    • (2005) Cell Cycle , vol.4 , pp. 279-289
    • Kingston, D.G.1    Bane, S.2    Snyder, J.P.3
  • 59
    • 0036086206 scopus 로고    scopus 로고
    • The solid state, solution and tubulin-bound conformations of agents that promote microtubule stabilization
    • Jimenez-Barbero, J., Amat-Guerri, F., and Snyder, J. P. (2002) The solid state, solution and tubulin-bound conformations of agents that promote microtubule stabilization, Curr. Med. Chem.: AntiCancer Agents 2, 91-122.
    • (2002) Curr. Med. Chem.: AntiCancer Agents , vol.2 , pp. 91-122
    • Jimenez-Barbero, J.1    Amat-Guerri, F.2    Snyder, J.P.3
  • 61
    • 0033102385 scopus 로고    scopus 로고
    • How Taxol stabilises microtubule structure
    • Amos, L. A., and Lowe, J. (1999) How Taxol stabilises microtubule structure, Chem. Biol. 6, R65-R69.
    • (1999) Chem. Biol , vol.6
    • Amos, L.A.1    Lowe, J.2
  • 62
    • 0028116602 scopus 로고
    • Solution structure of taxotere-induced microtubules to 3-nm resolution. The change in protofilament number is linked to the binding of the taxol side chain
    • Andreu, J. M., Diaz, J. F., Gil, R., de Pereda, J. M., Garcia, de Lacobal, M., Peyrot, M., Briand, C., Towns-Andrewsll, E., and Bordas, J. (1994) Solution structure of taxotere-induced microtubules to 3-nm resolution. The change in protofilament number is linked to the binding of the taxol side chain, J. Biol. Chem. 269, 31785-31792.
    • (1994) J. Biol. Chem , vol.269 , pp. 31785-31792
    • Andreu, J.M.1    Diaz, J.F.2    Gil, R.3    de Pereda, J.M.4    Garcia5    de Lacobal, M.6    Peyrot, M.7    Briand, C.8    Towns-Andrewsll, E.9    Bordas, J.10
  • 63
    • 0029347192 scopus 로고
    • How does taxol stabilize microtubules
    • Arnal, I., and Wade, R. H. (1995) How does taxol stabilize microtubules, Curr. Biol. 5, 900-908.
    • (1995) Curr. Biol , vol.5 , pp. 900-908
    • Arnal, I.1    Wade, R.H.2
  • 64
    • 0035838406 scopus 로고    scopus 로고
    • Microtubule structure at improved resolution
    • Meurer-Grob, P, Kasparian, J, Wade, RH. (2001) Microtubule structure at improved resolution, Biochemistry 40, 8000-8008.
    • (2001) Biochemistry , vol.40 , pp. 8000-8008
    • Meurer-Grob, P.1    Kasparian, J.2    Wade, R.H.3
  • 65
    • 0032509226 scopus 로고    scopus 로고
    • Changes in microtubule protofilament number induced by Taxol binding to an easily accessible site. Internal microtubule dynamics
    • Diaz, J. F., Valpuesta, J. M., Chacon, P., Diakun, G., and Andreu, J. M. (1998) Changes in microtubule protofilament number induced by Taxol binding to an easily accessible site. Internal microtubule dynamics, J. Biol. Chem. 273, 33803-33810.
    • (1998) J. Biol. Chem , vol.273 , pp. 33803-33810
    • Diaz, J.F.1    Valpuesta, J.M.2    Chacon, P.3    Diakun, G.4    Andreu, J.M.5
  • 66
    • 0001843250 scopus 로고
    • Taxane anticancer agents: Basic science and current status
    • Georg, G. I, Chen, T. T, Ojima, I, and Vyas, D. M, Eds., American Chemical Society, Washington, DC
    • Georg, G. I., Chen, T. T., Ojima, I., and Vyas, D. M., Eds.(1995) Taxane anticancer agents: Basic science and current status, ACS Symposium Series 583, pp 1-353, American Chemical Society, Washington, DC.
    • (1995) ACS Symposium Series , vol.583 , pp. 1-353
  • 67
    • 0029878720 scopus 로고    scopus 로고
    • VMD-Visual Molecular Dynamics
    • Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD-Visual Molecular Dynamics, J. Mol. Graphics, 14, 33-38; http://www.ks.uiuc.edu/Research/ vmd/.
    • (1996) J. Mol. Graphics , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 68
    • 35348865573 scopus 로고    scopus 로고
    • DeLano Scientific, Palo Alto, CA;
    • DeLano, W. L. (2002) The PyMOL Molecular Graphics System, DeLano Scientific, Palo Alto, CA; http://www.pymol.org.
    • (2002)
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.