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Volumn 55, Issue 2, 2007, Pages 236-245

Classical ligands interact with native and recombinant tubulin from Onchocerca volvulus with similar rank order of magnitude

Author keywords

Binding capacity and binding affinity; Classical ligands; Onchocerca volvulus; Recombinant and native tubulin; Tubulin expression

Indexed keywords

COMPLEMENTARY DNA; LIGAND; PRIMER DNA; RECOMBINANT PROTEIN; TUBULIN;

EID: 34548405166     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.04.011     Document Type: Article
Times cited : (9)

References (32)
  • 1
    • 0021152816 scopus 로고
    • Comparison of the interaction of anthelmintic benzimidazole with tubulin isolated from mammalian tissue and the parasite nematode Ascaridia galli
    • Dawson P.J., Gutteridge W.E., and Gull K.A. Comparison of the interaction of anthelmintic benzimidazole with tubulin isolated from mammalian tissue and the parasite nematode Ascaridia galli. Biochem. Pharmacol. 33 (1983) 1069-1074
    • (1983) Biochem. Pharmacol. , vol.33 , pp. 1069-1074
    • Dawson, P.J.1    Gutteridge, W.E.2    Gull, K.A.3
  • 2
    • 0024273591 scopus 로고
    • The role of the cytoskeleton protein, tubulin, in the mode of action and mechanism of drug resistance to benzimidazole
    • Lacey E. The role of the cytoskeleton protein, tubulin, in the mode of action and mechanism of drug resistance to benzimidazole. Int. J. Parasitol. 18 (1988) 885-936
    • (1988) Int. J. Parasitol. , vol.18 , pp. 885-936
    • Lacey, E.1
  • 3
    • 4344572092 scopus 로고    scopus 로고
    • Microtubule structure and its stabilization
    • Amos L.A. Microtubule structure and its stabilization. Org. Biomol. Chem. 2 (2004) 2153-2160
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 2153-2160
    • Amos, L.A.1
  • 4
    • 0142150279 scopus 로고    scopus 로고
    • Antimicrotubular drugs binding to vinca domain of tubulin
    • Gupta S., and Bhattacharyya B. Antimicrotubular drugs binding to vinca domain of tubulin. Mol. Cell Biochem. 253 (2003) 41-47
    • (2003) Mol. Cell Biochem. , vol.253 , pp. 41-47
    • Gupta, S.1    Bhattacharyya, B.2
  • 5
    • 2942538660 scopus 로고    scopus 로고
    • A high-throughput model for screening anti-tumor agents capable of promoting polymerization of tubulin in vitro
    • HU W., Dong H., LI Y.-z., HU X.-t., HAN G.-j., and QU Y.-b. A high-throughput model for screening anti-tumor agents capable of promoting polymerization of tubulin in vitro. Acta Pharmacol. Sin. 6 (2004) 775-782
    • (2004) Acta Pharmacol. Sin. , vol.6 , pp. 775-782
    • HU, W.1    Dong, H.2    LI, Y.-z.3    HU, X.-t.4    HAN, G.-j.5    QU, Y.-b.6
  • 6
    • 0006775899 scopus 로고
    • Biochemistry of tubulin
    • Roberts K., and Hyams J.S. (Eds), Academic Press, London
    • Luduena R.F. Biochemistry of tubulin. In: Roberts K., and Hyams J.S. (Eds). Microtubules (1986), Academic Press, London 65-116
    • (1986) Microtubules , pp. 65-116
    • Luduena, R.F.1
  • 8
    • 34548414016 scopus 로고    scopus 로고
    • WHO Expert Committee on Onchocerciasis. Third report, World Health Organ. Tech. Rep. Ser. 752 (1987) 1-167.
  • 9
    • 0018887074 scopus 로고
    • Tubulin characterization during embryogenesis of Ascaris suum
    • Friedman P.A., Platzer E.G., and Carroll E.L. Tubulin characterization during embryogenesis of Ascaris suum. Dev. Biol. 76 (1980) 47-57
    • (1980) Dev. Biol. , vol.76 , pp. 47-57
    • Friedman, P.A.1    Platzer, E.G.2    Carroll, E.L.3
  • 10
    • 0019892225 scopus 로고
    • Intestinal tubulin as possible target for chemotherapeutic action of mebendazole in parasitic nematodes
    • Kohler P., and Bachmann R. Intestinal tubulin as possible target for chemotherapeutic action of mebendazole in parasitic nematodes. Mol. Biochem. Parasitol. 4 (1981) 325-336
    • (1981) Mol. Biochem. Parasitol. , vol.4 , pp. 325-336
    • Kohler, P.1    Bachmann, R.2
  • 11
    • 0024023219 scopus 로고
    • Characterization of tubulin from Nippostrongylus brasiliensis, and comparison with mammalian brain tubulin
    • Tang L., and Prichard R.K. Characterization of tubulin from Nippostrongylus brasiliensis, and comparison with mammalian brain tubulin. Mol. Biochem. Parasitol. 29 (1988) 133-140
    • (1988) Mol. Biochem. Parasitol. , vol.29 , pp. 133-140
    • Tang, L.1    Prichard, R.K.2
  • 12
    • 0025732566 scopus 로고
    • Beta tubulin and benzimidazole resistance in sheep nematode Haemonchus contortus
    • Lubega G.W., and Prichard R.K. Beta tubulin and benzimidazole resistance in sheep nematode Haemonchus contortus. Mol. Biochem. Parasitol. 47 (1991) 129-138
    • (1991) Mol. Biochem. Parasitol. , vol.47 , pp. 129-138
    • Lubega, G.W.1    Prichard, R.K.2
  • 13
    • 0024273447 scopus 로고    scopus 로고
    • Diagnosis and expiration of nodules in human Onchocerciasis
    • Albeiz E.J., Buttner D.W., and Duke B.O.L. Diagnosis and expiration of nodules in human Onchocerciasis. Trop. Med. Parasitol. 39 (1998) 331-346
    • (1998) Trop. Med. Parasitol. , vol.39 , pp. 331-346
    • Albeiz, E.J.1    Buttner, D.W.2    Duke, B.O.L.3
  • 14
    • 0031957678 scopus 로고    scopus 로고
    • Cloning and characterization of cDNA encoding beta tubulins from Dirofilaria immitis and Onchocerca volvulus
    • Geary T.G., Nulf S.C., Alexander-Bowman S.J., Mahmoud B.M., Prichard R.K., and Klein R.D. Cloning and characterization of cDNA encoding beta tubulins from Dirofilaria immitis and Onchocerca volvulus. J. Parasitol. 2 (1998) 356-360
    • (1998) J. Parasitol. , vol.2 , pp. 356-360
    • Geary, T.G.1    Nulf, S.C.2    Alexander-Bowman, S.J.3    Mahmoud, B.M.4    Prichard, R.K.5    Klein, R.D.6
  • 15
    • 0024606953 scopus 로고
    • Enhancement of heterologous polypeptide expression by alterations in the ribosome-binding-site sequence
    • Olsen M.K., Rockenbach S.K., Curry K.A., and Tomich C.C. Enhancement of heterologous polypeptide expression by alterations in the ribosome-binding-site sequence. J. Biotechnol. 9 (1989) 179-190
    • (1989) J. Biotechnol. , vol.9 , pp. 179-190
    • Olsen, M.K.1    Rockenbach, S.K.2    Curry, K.A.3    Tomich, C.C.4
  • 17
    • 0027787461 scopus 로고
    • Expression of cloned β-tubulin genes of Haemonchus contortus in E. coli: interaction of recombinant β-tubulin with native tubulin and mebendazole
    • Lubega G.W., Geary T.G., Klein R.D., and Prichard R.K. Expression of cloned β-tubulin genes of Haemonchus contortus in E. coli: interaction of recombinant β-tubulin with native tubulin and mebendazole. Mol. Biochem. Parasitol. 62 (1993) 281-292
    • (1993) Mol. Biochem. Parasitol. , vol.62 , pp. 281-292
    • Lubega, G.W.1    Geary, T.G.2    Klein, R.D.3    Prichard, R.K.4
  • 19
    • 0034957287 scopus 로고    scopus 로고
    • Individual expression of recombinant α- and β-tubulin from Heamonchus contortus. Polymerization and drug effects
    • Oxberry M.E., Geary T.G., Winterrowd C.A., and Prichard R. Individual expression of recombinant α- and β-tubulin from Heamonchus contortus. Polymerization and drug effects. Protein Expr. Purif. 21 (2001) 30-39
    • (2001) Protein Expr. Purif. , vol.21 , pp. 30-39
    • Oxberry, M.E.1    Geary, T.G.2    Winterrowd, C.A.3    Prichard, R.4
  • 20
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0023214812 scopus 로고
    • Interaction of Phormopsin and related compounds with purified sheep brain tubulin
    • Lacey E., John E., Claude C.J., and Culvenor C.C. Interaction of Phormopsin and related compounds with purified sheep brain tubulin. Biochem. Pharmacol. 36 (1987) 2133-2138
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 2133-2138
    • Lacey, E.1    John, E.2    Claude, C.J.3    Culvenor, C.C.4
  • 23
    • 0022497174 scopus 로고
    • Interaction of benzimidazoles (BZ) with tubulin from BZ-sensitive and BZ-resistant isolates of Haemonchus contortus
    • Lacey E., and Prichard R.K. Interaction of benzimidazoles (BZ) with tubulin from BZ-sensitive and BZ-resistant isolates of Haemonchus contortus. Mol Biochem. Parasitol. 19 (1986) 171-181
    • (1986) Mol Biochem. Parasitol. , vol.19 , pp. 171-181
    • Lacey, E.1    Prichard, R.K.2
  • 24
    • 0025267185 scopus 로고
    • Mode of action of benzimidazoles
    • Lacey E. Mode of action of benzimidazoles. Parasitol. Today 6 (1986) 112-115
    • (1986) Parasitol. Today , vol.6 , pp. 112-115
    • Lacey, E.1
  • 25
    • 0026667315 scopus 로고
    • Differential stability of the BZ-tubulin complex in BZ-resistant and BZ-susceptible isolates of Heamonchus contortus and Trichostrongylus columbriformis
    • Russell G.J., and Lacey E. Differential stability of the BZ-tubulin complex in BZ-resistant and BZ-susceptible isolates of Heamonchus contortus and Trichostrongylus columbriformis. Int. J. Parasitol. 22 (1992) 399-402
    • (1992) Int. J. Parasitol. , vol.22 , pp. 399-402
    • Russell, G.J.1    Lacey, E.2
  • 26
    • 0034958718 scopus 로고    scopus 로고
    • Assessment of benzimidazole binding to individual recombinant tubulin isotypes from Heamonchus contortus
    • Oxberry M.E., Geary T.G., and Prichard R.K. Assessment of benzimidazole binding to individual recombinant tubulin isotypes from Heamonchus contortus. Parasitology 122 (2000) 683-687
    • (2000) Parasitology , vol.122 , pp. 683-687
    • Oxberry, M.E.1    Geary, T.G.2    Prichard, R.K.3
  • 28
    • 0036293071 scopus 로고    scopus 로고
    • Classical ligands bind tubulin of trypanosomes and inhibit their growth in vitro
    • Ochola D.O.K., Prichard R.K., and Lubega G.W. Classical ligands bind tubulin of trypanosomes and inhibit their growth in vitro. J. Parasitol. 88 (2002) 600-604
    • (2002) J. Parasitol. , vol.88 , pp. 600-604
    • Ochola, D.O.K.1    Prichard, R.K.2    Lubega, G.W.3
  • 30
    • 0020490025 scopus 로고
    • Number of receptor sites from Scatchad graphs. Facts an Fantasies
    • Kloitz I.M. Number of receptor sites from Scatchad graphs. Facts an Fantasies. Science 217 (1982) 1247-1249
    • (1982) Science , vol.217 , pp. 1247-1249
    • Kloitz, I.M.1
  • 32
    • 0035901501 scopus 로고    scopus 로고
    • Properties of microtubules assembled from mammalian tubulin synthesized in Escherichia coli
    • Shah C., Xu C.Z., Vickers J., and Williams R. Properties of microtubules assembled from mammalian tubulin synthesized in Escherichia coli. Biochemistry 40 (2001) 4844-4852
    • (2001) Biochemistry , vol.40 , pp. 4844-4852
    • Shah, C.1    Xu, C.Z.2    Vickers, J.3    Williams, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.