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Volumn 47, Issue 7, 2003, Pages 2273-2282

Molecular basis for fungal selectivity of novel antimitotic compounds

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTIMITOTIC AGENT; BENOMYL; BETA TUBULIN; CERULENIN; COLCHICINE; CYCLOHEXIMIDE; FLUCONAZOLE; MC 05905; MC 05991; MC 06011; MC 06285; MC 06307; MC 06341; MC 06380; MC 226728; MC 239300; MC 247136; MC 253166; MC 253637; MC 291734; MC 305904; NOCODAZOLE; TIABENDAZOLE; TUBULIN; UNCLASSIFIED DRUG;

EID: 0037636479     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.47.7.2273-2282.2003     Document Type: Article
Times cited : (7)

References (26)
  • 2
    • 0033102385 scopus 로고    scopus 로고
    • How Taxol stabilises microtubule structure
    • Amos, L. A., and J. Lowe. 1999. How Taxol stabilises microtubule structure. Chem. Biol. 6:R65-R69.
    • (1999) Chem. Biol. , vol.6
    • Amos, L.A.1    Lowe, J.2
  • 3
    • 0034704077 scopus 로고    scopus 로고
    • Mapping the binding site of colchicinoids on beta-tubulin. 2-Chloroacetyl-2-demethylthiocolchicine covalently reacts predominantly with cysteine 239 and secondarily with cysteine 354
    • Bai, R., D. G. Covell, X. F. Pei, J. B. Ewell, N. Y. Nguyen, A. Brossi, and E. Hamel. 2000. Mapping the binding site of colchicinoids on beta-tubulin. 2-Chloroacetyl-2-demethylthiocolchicine 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
  • 4
    • 0027056174 scopus 로고
    • Yeast proteins associated with microtubules in vitro and in vivo
    • Barnes, G., K. A. Louie, and D. Botstein. 1992. Yeast proteins associated with microtubules in vitro and in vivo. Mol. Biol. Cell 3:29-47.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 29-47
    • Barnes, G.1    Louie, K.A.2    Botstein, D.3
  • 5
    • 0037177229 scopus 로고    scopus 로고
    • Epothilone and paclitaxel: Unexpected differences in promoting the assembly and stabilization of yeast microtubules
    • Bode, C. J., M. L. Gupta, Jr., E. A. Reiff, K. A. Suprenant, G. I. Georg, and R. H. Himes. 2002. Epothilone and paclitaxel: unexpected differences in promoting the assembly and stabilization of yeast microtubules. Biochemistry 41:3870-3874.
    • (2002) Biochemistry , vol.41 , pp. 3870-3874
    • Bode, C.J.1    Gupta M.L., Jr.2    Reiff, E.A.3    Suprenant, K.A.4    Georg, G.I.5    Himes, R.H.6
  • 6
    • 0027248960 scopus 로고
    • Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae
    • Davis, A., C. R. Sage, L. Wilson, and K. W. Farrell. 1993. Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae. Biochemistry 32:8823-8835.
    • (1993) Biochemistry , vol.32 , pp. 8823-8835
    • Davis, A.1    Sage, C.R.2    Wilson, L.3    Farrell, K.W.4
  • 7
    • 0027192868 scopus 로고
    • Isogenic strain construction and gene mapping in Candida albicans
    • Fonzi, W. A., and M. Y. Imin. 1993. Isogenic strain construction and gene mapping in Candida albicans. Genetics 134:717-728.
    • (1993) Genetics , vol.134 , pp. 717-728
    • Fonzi, W.A.1    Imin, M.Y.2
  • 8
    • 0026559290 scopus 로고
    • A single amino-acid substitution in the beta-tubulin gene of Neurospora confers both carbendazim resistance and diethofencarb sensitivity
    • Fujimura, M., K. Oeda, H. Inoue, and T. Kato. 1992. A single amino-acid substitution in the beta-tubulin gene of Neurospora confers both carbendazim resistance and diethofencarb sensitivity. Curr. Genet. 21:399-404.
    • (1992) Curr. Genet , vol.21 , pp. 399-404
    • Fujimura, M.1    Oeda, K.2    Inoue, H.3    Kato, T.4
  • 9
    • 0034177962 scopus 로고    scopus 로고
    • Dissecting cellular processes using small molecules: Identification of colchicine-like, taxol-like and other small molecules that perturb mitosis
    • Haggarty, S. J., T. U. Mayer, D. T. Miyamoto, R. Fathi, R. W. King, T. J. Mitchison, and S. L. Schreiber. 2000. Dissecting cellular processes using small molecules: identification of colchicine-like, taxol-like and other small molecules that perturb mitosis. Chem. Biol. 7:275-286.
    • (2000) Chem. Biol. , vol.7 , pp. 275-286
    • Haggarty, S.J.1    Mayer, T.U.2    Miyamoto, D.T.3    Fathi, R.4    King, R.W.5    Mitchison, T.J.6    Schreiber, S.L.7
  • 10
    • 0025066572 scopus 로고
    • Identification of an amino acid substitution in the benA, beta-tubulin gene of Aspergillus nidulans that confers thiabendazole resistance and benomyl supersensitivity
    • Jung, M. K., and B. R. Oakley. 1990. Identification of an amino acid substitution in the benA, beta-tubulin gene of Aspergillus nidulans that confers thiabendazole resistance and benomyl supersensitivity. Cell Motil. Cytoskeleton 17:87-94.
    • (1990) Cell Motil. Cytoskeleton , vol.17 , pp. 87-94
    • Jung, M.K.1    Oakley, B.R.2
  • 11
    • 0026708525 scopus 로고
    • Amino acid alterations in the benA (beta-tubulin) gene of Aspergillus nidulans that confer benomyl resistance
    • Jung, M. K., I. B. Wilder, and B. R. Oakley. 1992. Amino acid alterations in the benA (beta-tubulin) gene of Aspergillus nidulans that confer benomyl resistance. Cell Motil. Cytoskeleton 22:170-174.
    • (1992) Cell Motil. Cytoskeleton , vol.22 , pp. 170-174
    • Jung, M.K.1    Wilder, I.B.2    Oakley, B.R.3
  • 12
    • 0019876086 scopus 로고
    • Purification of yeast tubulin by self-assembly in vitro
    • Kilmartin, J. V. 1981. Purification of yeast tubulin by self-assembly in vitro. Biochemistry 20:3629-3633.
    • (1981) Biochemistry , vol.20 , pp. 3629-3633
    • Kilmartin, J.V.1
  • 13
    • 0029889945 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Saccharomyces cerevisiae beta-tubulin: Interaction between residue 167 and benzimidazole compounds
    • Li, J., S. K. Katiyar, and T. D. Edlind. 1996. Site-directed mutagenesis of Saccharomyces cerevisiae beta-tubulin: interaction between residue 167 and benzimidazole compounds, FEBS Lett. 385:7-10.
    • (1996) FEBS Lett. , vol.385 , pp. 7-10
    • Li, J.1    Katiyar, S.K.2    Edlind, T.D.3
  • 14
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 A resolution
    • Lowe, J., H. Li, K. H. Downing, and E. Nogales. 2001. Refined structure of alpha beta-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
  • 15
    • 0029113209 scopus 로고
    • Microtubule stability in budding yeast: Characterization and dosage suppression of a benomyl-dependent tubulin mutant
    • Machin, N. A., J. M. Lee, and G. Barnes. 1995. Microtubule stability in budding yeast: characterization and dosage suppression of a benomyl-dependent tubulin mutant. Mol. Biol. Cell 6:1241-1259.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1241-1259
    • Machin, N.A.1    Lee, J.M.2    Barnes, G.3
  • 16
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer, T. U., T. M. Kapoor, S. J. Haggarty, R. W. King, S. L. Schreiber, and T. J. Mitchison. 1999. Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 286:971-974.
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1    Kapoor, T.M.2    Haggarty, S.J.3    King, R.W.4    Schreiber, S.L.5    Mitchison, T.J.6
  • 17
    • 0029063397 scopus 로고
    • Structure of tubulin at 6.5 A and location of the taxol-binding site
    • Nogales, E., S. G. Wolf, I. A. Khan, R. F. Luduena, and K. H. Downing. 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
  • 18
    • 0026752669 scopus 로고
    • Identification of novel antimitotic agents acting at the tubulin level by computer-assisted evaluation of differential cytotoxicity data
    • Paull, K. D., C. M. Lin, L. Malspeis, and E. Hamel. 1992. Identification of novel antimitotic agents acting at the tubulin level by computer-assisted evaluation of differential cytotoxicity data. Cancer Res. 52:3892-3900.
    • (1992) Cancer Res. , vol.52 , pp. 3892-3900
    • Paull, K.D.1    Lin, C.M.2    Malspeis, L.3    Hamel, E.4
  • 19
    • 0035450813 scopus 로고    scopus 로고
    • Genetic variability following selection of Haemonchus contortus with anthelmintics
    • Prichard, R. 2001. Genetic variability following selection of Haemonchus contortus with anthelmintics. Trends Parasitol. 17:445-453.
    • (2001) Trends Parasitol. , vol.17 , pp. 445-453
    • Prichard, R.1
  • 20
    • 17544366715 scopus 로고    scopus 로고
    • Localization of the vinblastine-binding site on beta-tubulin
    • Rai, S. S., and J. Wolff. 1996. Localization of the vinblastine-binding site on beta-tubulin. J. Biol. Chem. 271:14707-14711.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14707-14711
    • Rai, S.S.1    Wolff, J.2
  • 21
    • 0028123401 scopus 로고
    • Systematic mutational analysis of the yeast beta-tubulin gene
    • Reijo, R. A., E. M. Cooper, G. J. Beagle, and T. C. Huffaker. 1994. Systematic mutational analysis of the yeast beta-tubulin gene. Mol. Biol. Cell 5:29-43.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 29-43
    • Reijo, R.A.1    Cooper, E.M.2    Beagle, G.J.3    Huffaker, T.C.4
  • 23
    • 0025317502 scopus 로고
    • Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming
    • Sali, A., and T. L. Blundell. 1990. Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. J. Mol. Biol. 212:403-428.
    • (1990) J. Mol. Biol. , vol.212 , pp. 403-428
    • Sali, A.1    Blundell, T.L.2
  • 26
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.