메뉴 건너뛰기




Volumn 41, Issue 43, 2002, Pages 13029-13038

Perturbation of microtubule polymerization by quercetin through tubulin binding: A novel mechanism of its antiproliferative activity

Author keywords

[No Author keywords available]

Indexed keywords

MICROTUBULES;

EID: 0037195283     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi025952r     Document Type: Article
Times cited : (152)

References (63)
  • 3
    • 0022919318 scopus 로고
    • Beyond self-assembly: From microtubules to morphogenesis
    • Kirschner, M., and Mitchison, T. (1986) Beyond self-assembly: From microtubules to morphogenesis, Cell 45, 329-342.
    • (1986) Cell , vol.45 , pp. 329-342
    • Kirschner, M.1    Mitchison, T.2
  • 4
    • 0032710681 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics by drugs: A paradigm for the actions of cellular regulators
    • Wilson, L., Panda, D., and Jordan, M. A. (1999) Modulation of microtubule dynamics by drugs: A paradigm for the actions of cellular regulators. Cell Struct. Funct. 24, 329-335.
    • (1999) Cell Struct. Funct. , vol.24 , pp. 329-335
    • Wilson, L.1    Panda, D.2    Jordan, M.A.3
  • 5
    • 0036083301 scopus 로고    scopus 로고
    • Mechanism of action of antitumor drugs that interacts with microtubules and tubulin
    • Jordan, M. A. (2002) Mechanism of action of antitumor drugs that interacts with microtubules and tubulin, Curr. Med. Chem.-Anti-Cancer Agents 2, 1-17.
    • (2002) Curr. Med. Chem.-Anti-Cancer Agents , vol.2 , pp. 1-17
    • Jordan, M.A.1
  • 6
    • 0029965897 scopus 로고    scopus 로고
    • Antimitotic natural products and their interactions with tubulin
    • Hamel, E. (1996) Antimitotic natural products and their interactions with tubulin, Med. Res. Rev. 16, 207-231.
    • (1996) Med. Res. Rev. , vol.16 , pp. 207-231
    • Hamel, E.1
  • 7
    • 0030768517 scopus 로고    scopus 로고
    • Inhibition of mitosis and microtubule function through direct tubulin binding by a novel antiproliferative Naphthopyran LY290181
    • Wood, D. L., Panda, D., Wiernicki, T. R., Wilson, L., Jordan, M. A., and Singh, J. P. (1997) Inhibition of mitosis and microtubule function through direct tubulin binding by a novel antiproliferative Naphthopyran LY290181. Mol. Pharmacol. 52, 437-444.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 437-444
    • Wood, D.L.1    Panda, D.2    Wiernicki, T.R.3    Wilson, L.4    Jordan, M.A.5    Singh, J.P.6
  • 8
    • 0034844674 scopus 로고    scopus 로고
    • Physiochemical aspects of tubulin-interacting antimitotic drugs
    • Correia, J. J., and Lobert, S. (2001) Physiochemical aspects of tubulin-interacting antimitotic drugs, Curr. Pharm. Des. 7, 1213-1228.
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 1213-1228
    • Correia, J.J.1    Lobert, S.2
  • 10
    • 0029923972 scopus 로고    scopus 로고
    • Differential effects of vinblastine on polymerization and dynamics at opposite microtubule ends
    • Panda, D., Jordan, M. A., Chu, K. C., and Wilson, L. (1996) Differential effects of vinblastine on polymerization and dynamics at opposite microtubule ends, J. Biol. Chem. 271, 29807-29812.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29807-29812
    • Panda, D.1    Jordan, M.A.2    Chu, K.C.3    Wilson, L.4
  • 11
    • 0030886376 scopus 로고    scopus 로고
    • Stabilization of microtubule dynamics by estramustine by binding to a novel site in tubulin: A possible mechanistic basis of its antitumor action
    • Panda, D., Miller, H. P., Islam, K., and Wilson, L. (1997) Stabilization of microtubule dynamics by estramustine by binding to a novel site in tubulin: A possible mechanistic basis of its antitumor action, Proc. Natl. Acad. Sci. U.S.A. 94, 10560-10564.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10560-10564
    • Panda, D.1    Miller, H.P.2    Islam, K.3    Wilson, L.4
  • 12
    • 0030985027 scopus 로고    scopus 로고
    • Suppression of microtubule dynamics by LY290181: A potential mechanism for its antiproliferative action
    • Panda, D., Singh, J. P., and Wilson, L. (1997) Suppression of microtubule dynamics by LY290181: A potential mechanism for its antiproliferative action, J. Biol. Chem. 272, 7681-7687.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7681-7687
    • Panda, D.1    Singh, J.P.2    Wilson, L.3
  • 13
    • 0030721014 scopus 로고    scopus 로고
    • Mechanism of action of the unusually potent microtubule inhibitor, cryptophycin 1
    • Panda, D., Himes, R. H., Moore, R. E., Wilson, L., and Jordan, M. A. (1997) Mechanism of action of the unusually potent microtubule inhibitor, cryptophycin 1. Biochemistry 36, 12948-12953.
    • (1997) Biochemistry , vol.36 , pp. 12948-12953
    • Panda, D.1    Himes, R.H.2    Moore, R.E.3    Wilson, L.4    Jordan, M.A.5
  • 14
    • 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, M. A., and Wilson, L. (1998) Antiproliferative mechanism of action of cryptophycin-52: Kinetic stabilization of microtubule dynamics by high-affinity binding to microtubule ends, Proc. Natl. Acad. Sci. U.S.A. 95, 9313-9318.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9313-9318
    • Panda, D.1    DeLuca, K.2    Williams, D.3    Jordan, M.A.4    Wilson, L.5
  • 15
    • 0032535634 scopus 로고    scopus 로고
    • Suppression of Microtubule dynamics by binding of Cemadotin to a novel site in tubulin: A possible mechanism for its antitumor action
    • Jordan, M. A., Walker, D., de Arruda, M. D., Barlozzari, T., and Panda, D. (1998) Suppression of Microtubule dynamics by binding of Cemadotin to a novel site in tubulin: A possible mechanism for its antitumor action. Biochemistry 37, 17571-17578.
    • (1998) Biochemistry , vol.37 , pp. 17571-17578
    • Jordan, M.A.1    Walker, D.2    De Arruda, M.D.3    Barlozzari, T.4    Panda, D.5
  • 16
    • 0037053409 scopus 로고    scopus 로고
    • Minor alteration of microtubule dynamics causes loss of tension across kinetochore pairs and activates the spindle check-point
    • Zhou, J., Panda, D., Landen, J. W., Wilson, L., and Joshi, H. C. (2002) Minor alteration of microtubule dynamics causes loss of tension across kinetochore pairs and activates the spindle check-point, J. Biol. Chem. 277, 17200-17208.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17200-17208
    • Zhou, J.1    Panda, D.2    Landen, J.W.3    Wilson, L.4    Joshi, H.C.5
  • 17
    • 0023904579 scopus 로고
    • Natural products as antitumor agents: Direct versus indirect mechanisms of activity of flavonoids
    • Wiltrout, R. H., and Hornung, R. L. (1988) Natural products as antitumor agents: Direct versus indirect mechanisms of activity of flavonoids, J. Natl. Cancer. Inst. 80, 220-222.
    • (1988) J. Natl. Cancer. Inst. , vol.80 , pp. 220-222
    • Wiltrout, R.H.1    Hornung, R.L.2
  • 19
    • 0029610477 scopus 로고
    • Review of the biology of quercetin and related bioflavonoids
    • Formica, J. V., and Regelson, W. (1995) Review of the biology of quercetin and related bioflavonoids, Food Chem. Toxic. 33, 1061-1080.
    • (1995) Food Chem. Toxic. , vol.33 , pp. 1061-1080
    • Formica, J.V.1    Regelson, W.2
  • 20
    • 0030593485 scopus 로고    scopus 로고
    • Comparative effects of flavonoids on the growth, viability and metabolism of a colonic adenocarcinoma cell line (HT29 cells)
    • Agullo, G., Gamet-Payrastre, L., Fernandez, Y., Anciaux, N., Demigne, C., and Remesy, C. (1996) Comparative effects of flavonoids on the growth, viability and metabolism of a colonic adenocarcinoma cell line (HT29 cells), Cancer Lett. 105, 61-70.
    • (1996) Cancer Lett. , vol.105 , pp. 61-70
    • Agullo, G.1    Gamet-Payrastre, L.2    Fernandez, Y.3    Anciaux, N.4    Demigne, C.5    Remesy, C.6
  • 21
    • 0030872689 scopus 로고    scopus 로고
    • Effect of antiproliferative flavonoids on ascorbic acid accumulation in human colon adenocarcinoma cells
    • Kuo, S. M., Morehouse, H. F., and Lin, C. P. (1997) Effect of antiproliferative flavonoids on ascorbic acid accumulation in human colon adenocarcinoma cells, Cancer Lett. 116, 131-137.
    • (1997) Cancer Lett. , vol.116 , pp. 131-137
    • Kuo, S.M.1    Morehouse, H.F.2    Lin, C.P.3
  • 22
    • 0030945675 scopus 로고    scopus 로고
    • Molecular mechanisms in the antiproliferative action of quercetin
    • Csokay, B., Prajda, N., Weber, G., and Olah, E. (1997) Molecular mechanisms in the antiproliferative action of quercetin, Life Sci. 60, 2157-2163.
    • (1997) Life Sci. , vol.60 , pp. 2157-2163
    • Csokay, B.1    Prajda, N.2    Weber, G.3    Olah, E.4
  • 24
    • 0032411871 scopus 로고    scopus 로고
    • Quercetin, a flavonol, promotes disassembly of microtubules in prostate cancer cells: Possible mechanism of its antitumor activity
    • Takagi, T., Takekoshi, S., Okabe, T., and Nagata, H. (1998) Quercetin, a flavonol, promotes disassembly of microtubules in prostate cancer cells: Possible mechanism of its antitumor activity, Acta Histochem. Cytochem. 31, 435-445.
    • (1998) Acta Histochem. Cytochem. , vol.31 , pp. 435-445
    • Takagi, T.1    Takekoshi, S.2    Okabe, T.3    Nagata, H.4
  • 25
    • 0032697363 scopus 로고    scopus 로고
    • Antioxidants in cancer therapy; their actions and interactions with oncologic therapies
    • Lamson, D. W., and Brignall, M. S. (1999) Antioxidants in cancer therapy; their actions and interactions with oncologic therapies, Altern. Med. Rev. 4, 304-329.
    • (1999) Altern. Med. Rev. , vol.4 , pp. 304-329
    • Lamson, D.W.1    Brignall, M.S.2
  • 26
    • 0034202211 scopus 로고    scopus 로고
    • Antioxidants and cancer, part 3: Quercetin
    • Lamson, D. W., and Brignall, M. S. (2000) Antioxidants and cancer, part 3: Quercetin, Altern. Med. Rev. 5, 196-208.
    • (2000) Altern. Med. Rev. , vol.5 , pp. 196-208
    • Lamson, D.W.1    Brignall, M.S.2
  • 27
    • 0037039712 scopus 로고    scopus 로고
    • Effect of flavonoids on cell cycle progression in prostate cancer cells
    • Kobayashi, T., Nakata, T., and Kuzumaki, T. (2002) Effect of flavonoids on cell cycle progression in prostate cancer cells, Cancer Lett. 176, 17-23.
    • (2002) Cancer Lett. , vol.176 , pp. 17-23
    • Kobayashi, T.1    Nakata, T.2    Kuzumaki, T.3
  • 28
    • 18244403795 scopus 로고    scopus 로고
    • Inhibition of P-glycoprotein by flavonoid derivatives in adriamycin-resistant human myelogenous leukemia (K562/ADM) cells
    • Ikegawa, T., Ohtani, H., Koyabu, N., Juichi, M., Iwase, Y., Ito, C., Furukawa, H., Naito, M., Tsuruo, T., and Sawada, Y. (2002) Inhibition of P-glycoprotein by flavonoid derivatives in adriamycin-resistant human myelogenous leukemia (K562/ADM) cells, Cancer Lett. 177, 89-93.
    • (2002) Cancer Lett. , vol.177 , pp. 89-93
    • Ikegawa, T.1    Ohtani, H.2    Koyabu, N.3    Juichi, M.4    Iwase, Y.5    Ito, C.6    Furukawa, H.7    Naito, M.8    Tsuruo, T.9    Sawada, Y.10
  • 30
    • 0023897154 scopus 로고
    • Differential effects of flavonoids as inhibitors of tyrosine protein kinases and serine/threonine protein kinases
    • Hagiwara, M., Inoue, S., Tanaka, T., Nunoki, K., Ito, M., and Hidaka, H. (1988) Differential effects of flavonoids as inhibitors of tyrosine protein kinases and serine/threonine protein kinases, Biochem. Pharmacol. 37, 2987-2992.
    • (1988) Biochem. Pharmacol , vol.37 , pp. 2987-2992
    • Hagiwara, M.1    Inoue, S.2    Tanaka, T.3    Nunoki, K.4    Ito, M.5    Hidaka, H.6
  • 31
    • 0019513433 scopus 로고
    • Glutamate-induced polymerization of tubulin: Characteristics of the reaction and application to the large-scale purification of tubulin
    • Hamel, E., and Lin, C. M. (1981) Glutamate-induced polymerization of tubulin: Characteristics of the reaction and application to the large-scale purification of tubulin, Arch. Biochem. Biophys. 209, 29-40.
    • (1981) Arch. Biochem. Biophys. , vol.209 , pp. 29-40
    • Hamel, E.1    Lin, C.M.2
  • 32
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0016344556 scopus 로고
    • Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules
    • Gaskin, F., Cantor, C. R., and Shelanski, M. L. (1974) Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules, J. Mol. Biol. 89, 737-755.
    • (1974) J. Mol. Biol. , vol.89 , pp. 737-755
    • Gaskin, F.1    Cantor, C.R.2    Shelanski, M.L.3
  • 35
    • 0017593250 scopus 로고
    • Optical Studies of the interaction of 4′-6′-diamidino-2-phenylindole with DNA and metaphase chromosomes
    • Lin, M. S., Comings, D. E., and Alfi, O. S. (1977) Optical Studies of the interaction of 4′-6′-diamidino-2-phenylindole with DNA and metaphase chromosomes, Chromosoma 60, 15-25.
    • (1977) Chromosoma , vol.60 , pp. 15-25
    • Lin, M.S.1    Comings, D.E.2    Alfi, O.S.3
  • 36
    • 0021950830 scopus 로고
    • 4′, 6-Diamidino-2-phenylindole, a fluorescent probe for tubulin and microtubules
    • Bonne, D., Heusele, C., Simon, C., and Pantaloni, D. (1985) 4′, 6-Diamidino-2-phenylindole, a fluorescent probe for tubulin and microtubules. J. Biol. Chem. 260, 2819-2825.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2819-2825
    • Bonne, D.1    Heusele, C.2    Simon, C.3    Pantaloni, D.4
  • 38
    • 0015217218 scopus 로고
    • Fluorescent probes for conformational states of proteins - The pepsinogen - Pepsin conversion
    • Wang, J. L., and Edelman, G. M. (1971) Fluorescent probes for conformational states of proteins - The pepsinogen - Pepsin conversion. J. Biol. Chem. 246, 1185-1191.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1185-1191
    • Wang, J.L.1    Edelman, G.M.2
  • 39
    • 0022291011 scopus 로고
    • Measurement of ligand binding to proteins by fluorescence spectroscopy
    • Ward, L. D. (1985) Measurement of ligand binding to proteins by fluorescence spectroscopy, Methods Enzymol. 117, 509-525.
    • (1985) Methods Enzymol. , vol.117 , pp. 509-525
    • Ward, L.D.1
  • 40
    • 0020440236 scopus 로고
    • Determination of binding stoichiometry by the continuous variation method: The Job plot
    • Huang C. Y. (1982) Determination of binding stoichiometry by the continuous variation method: The Job plot, Methods Enzymol. 87, 509-525.
    • (1982) Methods Enzymol. , vol.87 , pp. 509-525
    • Huang, C.Y.1
  • 41
    • 0008891824 scopus 로고
    • Promotion of fluorescence upon binding of colchicine to tubulin
    • Bhattacharyya, B., and Wolff, J. (1974) Promotion of fluorescence upon binding of colchicine to tubulin. Proc. Natl. Acad. Sci. U.S.A. 71, 2627-2631.
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 2627-2631
    • Bhattacharyya, B.1    Wolff, J.2
  • 42
    • 0026328348 scopus 로고
    • Interactions of colchicine with tubulin
    • Hastie, S. B. (1991) Interactions of colchicine with tubulin, Pharmacol. Ther. 512, 377-401.
    • (1991) Pharmacol. Ther. , vol.512 , pp. 377-401
    • Hastie, S.B.1
  • 43
    • 0025759015 scopus 로고
    • Kinetics of dissociation of the tubulin-colchicine complex. Complete reaction scheme and comparison to thermodynamic measurements
    • Fernando Diaz, J., and Andreu, J. M. (1991) Kinetics of dissociation of the tubulin-colchicine complex. Complete reaction scheme and comparison to thermodynamic measurements, J. Biol. Chem. 266, 2890-2896.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2890-2896
    • Fernando Diaz, J.1    Andreu, J.M.2
  • 44
    • 0025369731 scopus 로고
    • The carboxy terminus of the alpha subunit of tubulin regulates its interaction with colchicine
    • Mukhopadhyay, K., Parrack, P. K., and Bhattacharyya, B. (1990) The carboxy terminus of the alpha subunit of tubulin regulates its interaction with colchicine, Biochemistry 29, 6845-6850.
    • (1990) Biochemistry , vol.29 , pp. 6845-6850
    • Mukhopadhyay, K.1    Parrack, P.K.2    Bhattacharyya, B.3
  • 45
  • 46
    • 0017387874 scopus 로고
    • Role of tubulin-SH groups in polymerization to microtubules. Functional-SH groups in tubulin for polymerization
    • Kuriyama, R., and Sakai, H. (1974) Role of tubulin-SH groups in polymerization to microtubules. Functional-SH groups in tubulin for polymerization, J. Biochem. (Tokyo) 81, 1115-1125.
    • (1974) J. Biochem. (Tokyo) , vol.81 , pp. 1115-1125
    • Kuriyama, R.1    Sakai, H.2
  • 47
    • 0025976944 scopus 로고
    • Tubulin sulfhydryl groups as probes and targets for antimitotic and antimicrotubule agents
    • Luduena, R. F., and Roach, M. C. (1991) Tubulin sulfhydryl groups as probes and targets for antimitotic and antimicrotubule agents, Pharmacol. Ther. 49, 133-152.
    • (1991) Pharmacol. Ther. , vol.49 , pp. 133-152
    • Luduena, R.F.1    Roach, M.C.2
  • 49
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., and Candia, O. A. (1979) An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100, 95-97.
    • (1979) Anal. Biochem. , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 50
    • 0018186529 scopus 로고
    • Kinetics and mechanism of colchicine binding to tubulin: Evidence for ligand-induced conformational change
    • Garland, D. L. (1978) Kinetics and mechanism of colchicine binding to tubulin: Evidence for ligand-induced conformational change, Biochemistry 17, 4266-4272.
    • (1978) Biochemistry , vol.17 , pp. 4266-4272
    • Garland, D.L.1
  • 51
    • 0021682113 scopus 로고
    • Bis(1,8-anilinonaphthalenesulfonate) a novel and potent inhibitor of microtubule assembly
    • Horowitz, P., Prasad, V., and Luduena, R. F. (1984) Bis(1,8-anilinonaphthalenesulfonate) a novel and potent inhibitor of microtubule assembly, J. Biol. Chem. 259, 14647-14650.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14647-14650
    • Horowitz, P.1    Prasad, V.2    Luduena, R.F.3
  • 52
    • 0028032820 scopus 로고
    • Cooperative multiple binding of bisANS and daunomycin to tubulin
    • Ward, L. D., and Timasheff, S. N. (1994) Cooperative multiple binding of bisANS and daunomycin to tubulin, Biochemistry 33, 11891-11899.
    • (1994) Biochemistry , vol.33 , pp. 11891-11899
    • Ward, L.D.1    Timasheff, S.N.2
  • 53
    • 0022449008 scopus 로고
    • Bis(8-anilinonaphthalene-1-sulfonate) as a probe for tubulin decay
    • Prasad, A. R. S., Luduena, R. F., and Horowitz, P. M. (1986) Bis(8-anilinonaphthalene-1-sulfonate) as a probe for tubulin decay, Biochemistry 25, 739-742.
    • (1986) Biochemistry , vol.25 , pp. 739-742
    • Prasad, A.R.S.1    Luduena, R.F.2    Horowitz, P.M.3
  • 54
    • 0014937571 scopus 로고
    • Properties of colchicine binding protein from chick embryo brain. Interactions with Vinca Alkaloids and podophyllotoxin
    • Wilson, L. (1970) Properties of colchicine binding protein from chick embryo brain. Interactions with Vinca Alkaloids and podophyllotoxin, Biochemistry 9, 4999-5007.
    • (1970) Biochemistry , vol.9 , pp. 4999-5007
    • Wilson, L.1
  • 55
    • 0031745659 scopus 로고    scopus 로고
    • Tubulin stability and decay: Mediation by two distinct classes of IKP104-binding sites
    • Chaudhuri, A. R., Tomita, I., Mizuhashi, F., Murata, K., and Luduena, R. F. (1998) Tubulin stability and decay: Mediation by two distinct classes of IKP104-binding sites, J. Protein Chem. 17, 303-309.
    • (1998) J. Protein Chem. , vol.17 , pp. 303-309
    • Chaudhuri, A.R.1    Tomita, I.2    Mizuhashi, F.3    Murata, K.4    Luduena, R.F.5
  • 57
    • 0018570883 scopus 로고
    • Effect of antimitotic drugs on tubulin GTPase activity and self-assembly
    • David-Pfeuty, T., Simon, C., and Pantaloni, D. (1979) Effect of antimitotic drugs on tubulin GTPase activity and self-assembly, J. Biol. Chem. 254, 11696-11702.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11696-11702
    • David-Pfeuty, T.1    Simon, C.2    Pantaloni, D.3
  • 58
    • 0019821342 scopus 로고
    • The ligand- and microtubule assembly-induced GTPase activity of purified calf brain tubulin
    • Andreu, J. M., and Timasheff, S. N. (1981) The ligand- and microtubule assembly-induced GTPase activity of purified calf brain tubulin, Arch. Biochem. Biophys. 211, 151-157.
    • (1981) Arch. Biochem. Biophys. , vol.211 , pp. 151-157
    • Andreu, J.M.1    Timasheff, S.N.2
  • 59
    • 0020422990 scopus 로고
    • Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin
    • Andreu, J. M., and Timasheff, S. N. (1982) Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin, Biochemistry, 21, 6465-6476.
    • (1982) Biochemistry , vol.21 , pp. 6465-6476
    • Andreu, J.M.1    Timasheff, S.N.2
  • 60
    • 0021759710 scopus 로고
    • Immobilization-dependent fluorescence of colchicine
    • Bhattacharyya, B., and Wolff, J. (1984) Immobilization-dependent fluorescence of colchicine, J. Biol. Chem. 259, 11836-11843.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11836-11843
    • Bhattacharyya, B.1    Wolff, J.2
  • 61
    • 0034704077 scopus 로고    scopus 로고
    • Mapping the binding site of colchicinoids on beta-tubulin: 2-Chloroacetyl-2 demethylthio colchicine covalently reacts predominantly with cysteine 239 and secondarily with cysteine 354
    • Bai, R., Covell, D. G., Pei, X. F., Ewell, J. B., Nguyen, N. Y., Brossi, A., and Hamel, E. (2000) Mapping the binding site of colchicinoids on beta-tubulin: 2-Chloroacetyl-2 demethylthio colchicine covalently reacts predominantly with cysteine 239 and secondarily with cysteine 354, J. Biol. Chem. 275, 40443-40452.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40443-40452
    • Bai, R.1    Covell, D.G.2    Pei, X.F.3    Ewell, J.B.4    Nguyen, N.Y.5    Brossi, A.6    Hamel, E.7
  • 62
    • 0018622376 scopus 로고
    • Colchicine inhibition of microtubule assembly via copolymer formation
    • Sternlicht, H., and Ringel, I. (1979) Colchicine inhibition of microtubule assembly via copolymer formation. J. Biol. Chem. 254, 10540-50.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10540-10550
    • Sternlicht, H.1    Ringel, I.2
  • 63
    • 0029155318 scopus 로고
    • Kinetic stabilization of microtubule dynamics at steady state in vitro by substoichiometric concentration of tubulin-colchicine complex
    • Panda, D., Daijo, J., Jordan, M. A., and Wilson, L. (1995) Kinetic stabilization of microtubule dynamics at steady state in vitro by substoichiometric concentration of tubulin-colchicine complex, Biochemistry 34, 9921-9929.
    • (1995) Biochemistry , vol.34 , pp. 9921-9929
    • Panda, D.1    Daijo, J.2    Jordan, M.A.3    Wilson, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.