메뉴 건너뛰기




Volumn 29, Issue 1, 2000, Pages 156-160

Rapid colchicine competition-binding scintillation proximity assay using biotin-labeled tubulin

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; COLCHICINE; TUBULIN;

EID: 0033920430     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/00291rr02     Document Type: Article
Times cited : (62)

References (29)
  • 1
    • 0016648839 scopus 로고
    • Fluorometric assay of tubulin-colchicine complex
    • Arai, T. and T. Okuyama. 1975. Fluorometric assay of tubulin-colchicine complex. Anal. Biochem. 69:443-450.
    • (1975) Anal. Biochem. , vol.69 , pp. 443-450
    • Arai, T.1    Okuyama, T.2
  • 2
    • 0031671581 scopus 로고    scopus 로고
    • Microtubule-damaging drugs triggered bc12 phosphorylation-requirement of phosphorylation on both serine-70 and serine-87 residues of bc12 protein
    • Basu, A. and S. Haldar. 1998. Microtubule-damaging drugs triggered bc12 phosphorylation-requirement of phosphorylation on both serine-70 and serine-87 residues of bc12 protein. Int. J. Oncol. 13:659-664.
    • (1998) Int. J. Oncol. , vol.13 , pp. 659-664
    • Basu, A.1    Haldar, S.2
  • 5
    • 0015442186 scopus 로고
    • A rapid method for quantitative determination of microtubule protein using DEAE-cellulose filters
    • Borisy, G.G. 1972. A rapid method for quantitative determination of microtubule protein using DEAE-cellulose filters. Anal. Biochem. 50:373-385.
    • (1972) Anal. Biochem. , vol.50 , pp. 373-385
    • Borisy, G.G.1
  • 7
    • 0032950870 scopus 로고    scopus 로고
    • Anti-vascular approaches to solid tumour therapy: Evaluation of combretastatin A4 phosphate
    • Chaplin, D.J., G.R. Pettit and S.A. Hill. 1999. Anti-vascular approaches to solid tumour therapy: evaluation of combretastatin A4 phosphate. Anticancer Res. 19:189-195.
    • (1999) Anticancer Res. , vol.19 , pp. 189-195
    • Chaplin, D.J.1    Pettit, G.R.2    Hill, S.A.3
  • 9
    • 0004028961 scopus 로고
    • Springer-Verlag, Berlin
    • Dustin, P. 1984. Microtubules. Springer-Verlag, Berlin.
    • (1984) Microtubules
    • Dustin, P.1
  • 10
    • 0018186529 scopus 로고
    • Kinetics and mechanism of colchicine binding to tubulin. Evidence for ligand-induced conformational change
    • Garland, D. 1978. Kinetics and mechanism of colchicine binding to tubulin. Evidence for ligand-induced conformational change. Biochemistry 17:4266-4271.
    • (1978) Biochemistry , vol.17 , pp. 4266-4271
    • Garland, D.1
  • 11
    • 0029965897 scopus 로고    scopus 로고
    • Antimitotic natural products and their interactions with tubulin
    • Hamel, E. 1996. Antimitotic natural products and their interactions with tubulin. Biochemistry 16:207-231.
    • (1996) Biochemistry , vol.16 , pp. 207-231
    • Hamel, E.1
  • 13
    • 0031872051 scopus 로고    scopus 로고
    • Tubulin as a target for anticancer drugs: Agents which interact with the mitotic spindle
    • Jordan, M.A., J.A. Hadfield, N.J. Lawrence and A.T. McGown. 1998. Tubulin as a target for anticancer drugs: agents which interact with the mitotic spindle. Med. Res. Rev. 18:259-296.
    • (1998) Med. Res. Rev. , vol.18 , pp. 259-296
    • Jordan, M.A.1    Hadfield, J.A.2    Lawrence, N.J.3    McGown, A.T.4
  • 14
    • 0032006059 scopus 로고    scopus 로고
    • Microtubules and actin filaments: Dynamic targets for cancer chemotherapy
    • Jordan, M.A. and L. Wilson. 1998. Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr. Opin. Cell Biol. 10:123-130.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 123-130
    • Jordan, M.A.1    Wilson, L.2
  • 15
    • 0031610542 scopus 로고    scopus 로고
    • Use of drugs to study role of microtubule assembly dynamics in living cells
    • Jordan, M.A. and L. Wilson. 1998. Use of drugs to study role of microtubule assembly dynamics in living cells. Methods Enzymol. 298:252-276.
    • (1998) Methods Enzymol. , vol.298 , pp. 252-276
    • Jordan, M.A.1    Wilson, L.2
  • 16
    • 0017601419 scopus 로고
    • Tubulin binding affinities of podophyllotoxin and colchicine analogues
    • Kelleher, J.K. 1977. Tubulin binding affinities of podophyllotoxin and colchicine analogues. Mol. Pharmacol. 13:232-241.
    • (1977) Mol. Pharmacol. , vol.13 , pp. 232-241
    • Kelleher, J.K.1
  • 17
    • 0019047985 scopus 로고
    • A quantitative analysis of tubulin-colchicine binding to microtubules
    • Lambier, A. and Y. Engelborghs. A quantitative analysis of tubulin-colchicine binding to microtubules. 1980. Eur. J. Biochem. 109:619-624.
    • (1980) Eur. J. Biochem. , vol.109 , pp. 619-624
    • Lambier, A.1    Engelborghs, Y.2
  • 18
    • 0029020378 scopus 로고
    • Characterization of tubulin-alkaloid interactions by enzyme-linked immunosorbent assay
    • Liliom, K., A. Lehotzky, A. Molnar and J. Ovadi. 1995. Characterization of tubulin-alkaloid interactions by enzyme-linked immunosorbent assay. Anal. Biochem. 228:18-26.
    • (1995) Anal. Biochem. , vol.228 , pp. 18-26
    • Liliom, K.1    Lehotzky, A.2    Molnar, A.3    Ovadi, J.4
  • 19
    • 0024427745 scopus 로고
    • Antimitotic natural products combretastatin A-4 and Combretastatin A-2: Studies on the mechanism of their inhibition of the binding of colchicine to tubulin
    • Lin, C.M., H.H. Ho, G.R. Pettit and E. Hamel. 1989. Antimitotic natural products combretastatin A-4 and Combretastatin A-2: studies on the mechanism of their inhibition of the binding of colchicine to tubulin. Biochemistry 28:6984-6991.
    • (1989) Biochemistry , vol.28 , pp. 6984-6991
    • Lin, C.M.1    Ho, H.H.2    Pettit, G.R.3    Hamel, E.4
  • 20
    • 0021721647 scopus 로고
    • Binding of colchicine to beef brain tubulin: Influence of methodology on binding constants
    • Luyckx, M., C. Brunet and M. Cazin. 1984. Binding of colchicine to beef brain tubulin: influence of methodology on binding constants. Methods Find. Exp. Clin. Pharmacol. 6:679-684.
    • (1984) Methods Find. Exp. Clin. Pharmacol. , vol.6 , pp. 679-684
    • Luyckx, M.1    Brunet, C.2    Cazin, M.3
  • 21
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales, E., S.G. Wolf and K.H. Dowing. 1998. Structure of the αβ tubulin dimer by electron crystallography. Nature 391:199-202.
    • (1998) Nature , vol.391 , pp. 199-202
    • Nogales, E.1    Wolf, S.G.2    Dowing, K.H.3
  • 22
    • 0019487051 scopus 로고
    • Role of B-ring of colchicine in its binding to tubulin
    • Ray, K., B. Bhattacharyya and B.B. Biswas. 1981. Role of B-ring of colchicine in its binding to tubulin. J. Bio. Chem. 256:6241-6244.
    • (1981) J. Bio. Chem. , vol.256 , pp. 6241-6244
    • Ray, K.1    Bhattacharyya, B.2    Biswas, B.B.3
  • 23
    • 0026611714 scopus 로고
    • 3H|benzimidazole carbamates to mammalian brain tubulin and the mechanism of selective toxicity of the benzimidazole anthelmintics
    • 3H|benzimidazole carbamates to mammalian brain tubulin and the mechanism of selective toxicity of the benzimidazole anthelmintics. Biochem. Pharmacol. 43:1095-1100.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1095-1100
    • Russell, G.1    Gill, J.H.2    Lacey, E.3
  • 24
    • 0016358529 scopus 로고
    • A new colchicine binding assay for tubulin
    • Sherline, P., C.K. Bodwin and D.M. Kipnis. 1974. A new colchicine binding assay for tubulin. Anal. Biochem. 62:400-407.
    • (1974) Anal. Biochem. , vol.62 , pp. 400-407
    • Sherline, P.1    Bodwin, C.K.2    Kipnis, D.M.3
  • 26
    • 0343135608 scopus 로고
    • Biochemical studies of the kinetochore/centromere of mammalian chromosomes
    • G.G. Borisy, D.W. Cleveland and D.B. Murphy (Eds.), CSH Laboratory Press, Cold Spring Harbor, New York
    • Valdivia, M. and B.R. Brinkley. 1984. Biochemical studies of the kinetochore/centromere of mammalian chromosomes, p. 79-86. In G.G. Borisy, D.W. Cleveland and D.B. Murphy (Eds.), Molecular Biology of the Cytoskeleton. CSH Laboratory Press, Cold Spring Harbor, New York.
    • (1984) Molecular Biology of the Cytoskeleton , pp. 79-86
    • Valdivia, M.1    Brinkley, B.R.2
  • 27
    • 0022557217 scopus 로고
    • Kinetics and steady state dynamics of tubulin addition and loss at opposite microtubule ends:The mechanism of action of colchicine
    • Wilson, L. and K.W. Farrell. 1986. Kinetics and steady state dynamics of tubulin addition and loss at opposite microtubule ends:the mechanism of action of colchicine. Ann. NY Acad. Sci. 466:690-708.
    • (1986) Ann. NY Acad. Sci. , vol.466 , pp. 690-708
    • Wilson, L.1    Farrell, K.W.2
  • 29
    • 0030756156 scopus 로고    scopus 로고
    • Mechanism of action of E7010, an orally active sulfonamide antitumor agent: Inhibition of mitosis by binding to the colchicine site of tubulin
    • Yoshimatsu, K., A. Yamaguchi, H. Yoshino, N. Koyanagi and K. Kitoh. 1997. Mechanism of action of E7010, an orally active sulfonamide antitumor agent: inhibition of mitosis by binding to the colchicine site of tubulin. Cancer Res. 57:3208-3213.
    • (1997) Cancer Res. , vol.57 , pp. 3208-3213
    • Yoshimatsu, K.1    Yamaguchi, A.2    Yoshino, H.3    Koyanagi, N.4    Kitoh, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.