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Volumn 42, Issue 9, 1998, Pages 2279-2283

Identification of elongation factor 2 as the essential protein targeted by sordarins in Candida albicans

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFUNGAL AGENT; ELONGATION FACTOR 2; FUNGAL PROTEIN; SORDARIN; UNCLASSIFIED DRUG;

EID: 0040837015     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.42.9.2279     Document Type: Article
Times cited : (105)

References (33)
  • 2
    • 0029049427 scopus 로고
    • Translation elongation factor-3 (EF-3): An evolving eukaryotic ribosomal-protein?
    • Belfield, G. P., N. J. Ross-Smith, and M. F. Tuite. 1995. Translation elongation factor-3 (EF-3): an evolving eukaryotic ribosomal-protein? J. Mol. Evol. 41:376-387.
    • (1995) J. Mol. Evol. , vol.41 , pp. 376-387
    • Belfield, G.P.1    Ross-Smith, N.J.2    Tuite, M.F.3
  • 3
    • 0021161567 scopus 로고
    • Diphthamide in elongation factor 2: ADP-ribosylation, purification and properties
    • Bodley, J. W., P. C. Dunlop, and B. G. van Ness. 1984. Diphthamide in elongation factor 2: ADP-ribosylation, purification and properties. Methods Enzymol. 106:378-387.
    • (1984) Methods Enzymol. , vol.106 , pp. 378-387
    • Bodley, J.W.1    Dunlop, P.C.2    Van Ness, B.G.3
  • 4
    • 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
  • 7
    • 0028108977 scopus 로고
    • Multiformity of clongation factor eEF-2 isolated from rat liver cells
    • Gajko, A., W. Galasinski, and A. Gindzienski. 1994. Multiformity of clongation factor eEF-2 isolated from rat liver cells. Biochem. Biophys. Res. Commun. 202:844-849.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 844-849
    • Gajko, A.1    Galasinski, W.2    Gindzienski, A.3
  • 8
    • 0030007107 scopus 로고    scopus 로고
    • Eukaryotic polypeptide elongation system and its sensitivity to the inhibitory substances of plant origin
    • Galasinski, W. 1996. Eukaryotic polypeptide elongation system and its sensitivity to the inhibitory substances of plant origin. Proc. Soc. Exp. Biol. Med. 212:24-37.
    • (1996) Proc. Soc. Exp. Biol. Med. , vol.212 , pp. 24-37
    • Galasinski, W.1
  • 9
    • 0023245517 scopus 로고
    • Purification of elongation factor 2 from human placenta and evidence of its fragmentation patterns in various eukaryotic sources
    • Giovane, A., L. Servillo, L. Quagliuolo, and C. Balestieri. 1987. Purification of elongation factor 2 from human placenta and evidence of its fragmentation patterns in various eukaryotic sources. Biochem. J. 244:337-344.
    • (1987) Biochem. J. , vol.244 , pp. 337-344
    • Giovane, A.1    Servillo, L.2    Quagliuolo, L.3    Balestieri, C.4
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0017637023 scopus 로고
    • Cleavage at aspartyl-prolyl bonds
    • Landon, M. 1977. Cleavage at aspartyl-prolyl bonds. Methods Enzymol. 47: 145-149.
    • (1977) Methods Enzymol. , vol.47 , pp. 145-149
    • Landon, M.1
  • 14
    • 25344436732 scopus 로고
    • Ribosomes
    • A. H. Rose and J. S. Harrison. (ed.), Academic Press, Inc., San Diego, Calif.
    • Lee, J. C. 1991. Ribosomes, p. 489-540. In A. H. Rose and J. S. Harrison. (ed.), The yeasts, vol. 4. Yeast organelles. Academic Press, Inc., San Diego, Calif.
    • (1991) The Yeasts, Vol. 4. Yeast Organelles , vol.4 , pp. 489-540
    • Lee, J.C.1
  • 15
    • 0026326231 scopus 로고
    • Comparative biochemistry and biophysics of ribosomal proteins
    • Liljas, A. 1991. Comparative biochemistry and biophysics of ribosomal proteins. Int. Rev. Cytol. 124:103-136.
    • (1991) Int. Rev. Cytol. , vol.124 , pp. 103-136
    • Liljas, A.1
  • 16
    • 0026718508 scopus 로고
    • Mechanism and regulation of eukaryotic protein synthesis
    • Merrick, W. C. 1992. Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 56:291-315.
    • (1992) Microbiol. Rev. , vol.56 , pp. 291-315
    • Merrick, W.C.1
  • 17
    • 0021891865 scopus 로고
    • Eukaryotic protein synthesis
    • Moldave, K. 1985. Eukaryotic protein synthesis. Annu. Rev. Biochem. 54: 1109-1149.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1109-1149
    • Moldave, K.1
  • 18
    • 0030574576 scopus 로고    scopus 로고
    • An elongation factor turn-on
    • Nierhaus, K. H. 1996. An elongation factor turn-on. Nature 379:491-492.
    • (1996) Nature , vol.379 , pp. 491-492
    • Nierhaus, K.H.1
  • 19
    • 0022425951 scopus 로고
    • Localization of the sites of ADP-ribosylation and GTP binding in the eukaryotic elongation factor EF-2
    • Nilsson, L., and O. Nygard. 1985. Localization of the sites of ADP-ribosylation and GTP binding in the eukaryotic elongation factor EF-2. Eur. J. Biochem. 148:299-304.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 299-304
    • Nilsson, L.1    Nygard, O.2
  • 20
    • 0024514137 scopus 로고
    • Characterization of the ribosomal properties required for formation of a GTPase active complex with the eukaryotic elongation factor 2
    • Nygard, O., and L. Nilsson. 1989. Characterization of the ribosomal properties required for formation of a GTPase active complex with the eukaryotic elongation factor 2. Eur. J. Biochem. 179:603-608.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 603-608
    • Nygard, O.1    Nilsson, L.2
  • 21
    • 0026531732 scopus 로고
    • Protein toxin inhibitors of protein synthesis
    • Perenthesis, J. P., S. P. Miller, and J. W. Bodley. 1992. Protein toxin inhibitors of protein synthesis. BioFactors 3:173-184.
    • (1992) BioFactors , vol.3 , pp. 173-184
    • Perenthesis, J.P.1    Miller, S.P.2    Bodley, J.W.3
  • 22
    • 0026565694 scopus 로고
    • Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression and G-domain modeling
    • Perenthesis, J. P., L. D. Phan, W. R. Gleason, D. C. LaPorte, D. M. Livingston, and J. W. Bodley. 1992. Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression and G-domain modeling. J. Biol. Chem. 267:1190-1197.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1190-1197
    • Perenthesis, J.P.1    Phan, L.D.2    Gleason, W.R.3    LaPorte, D.C.4    Livingston, D.M.5    Bodley, J.W.6
  • 23
    • 0014940086 scopus 로고
    • Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations
    • Piszkiewicz, D., M. Landon, and E. L. Smith. 1970. Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations. Biochem. Biophys. Res. Commun. 40:1173-1178.
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 1173-1178
    • Piszkiewicz, D.1    Landon, M.2    Smith, E.L.3
  • 24
    • 0028432912 scopus 로고
    • Peptide-chain elongation in eukaryotes
    • Proud, C. G. 1994. Peptide-chain elongation in eukaryotes. Mol. Biol. Rep. 19:161-170.
    • (1994) Mol. Biol. Rep. , vol.19 , pp. 161-170
    • Proud, C.G.1
  • 25
    • 0027273725 scopus 로고
    • Regulation of elongation factor-2 by multisite phosphorylation
    • Redpath, N. T., N. T. Price, K. V. Severinov, and C. G. Proud. 1993. Regulation of elongation factor-2 by multisite phosphorylation. Eur. J. Biochem. 213:689-699.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 689-699
    • Redpath, N.T.1    Price, N.T.2    Severinov, K.V.3    Proud, C.G.4
  • 27
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina, M. V., A. Savelsbergh, V. I. Katunin, and W. Wintermeyer. 1997. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385:37-41.
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 28
    • 0025182923 scopus 로고
    • Protein synthesis in yeast. Structural and functional analysis of the gene encoding elongation factor 3
    • Sandbaken, M. G., J. A. Lupisella, B. Di Domenico, and K. Chakraburtty. 1990. Protein synthesis in yeast. Structural and functional analysis of the gene encoding elongation factor 3. J. Biol. Chem. 265:15838-15844.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15838-15844
    • Sandbaken, M.G.1    Lupisella, J.A.2    Di Domenico, B.3    Chakraburtty, K.4
  • 29
    • 0024202617 scopus 로고
    • Evidence of a yeast proteinase specific for elongation factor 2
    • Servillo, L., L. Quagliuolo, C. Balestrieri, and A. Giovane. 1988. Evidence of a yeast proteinase specific for elongation factor 2. FEBS Lett. 241:257-260.
    • (1988) FEBS Lett. , vol.241 , pp. 257-260
    • Servillo, L.1    Quagliuolo, L.2    Balestrieri, C.3    Giovane, A.4
  • 30
    • 0018338668 scopus 로고
    • Separation and characterization of yeast elongation factors
    • Skogerson, L. 1979. Separation and characterization of yeast elongation factors. Methods Enzymol. 40:676-685.
    • (1979) Methods Enzymol. , vol.40 , pp. 676-685
    • Skogerson, L.1
  • 31
    • 0344135964 scopus 로고
    • A ribosome-dependent GTPase from yeast distinct from elongation factor 2
    • Skogerson, L., and E. Wakatama. 1976. A ribosome-dependent GTPase from yeast distinct from elongation factor 2. Proc. Natl. Acad. Sci. USA 73: 73-76.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 73-76
    • Skogerson, L.1    Wakatama, E.2
  • 32
    • 0002477677 scopus 로고
    • Isolation and analysis of ribosomes from prokaryotes, eukaryotes, and organelles
    • G. Spedding (ed.), IRL Press, Oxford, United Kingdom
    • Spedding, G. 1990. Isolation and analysis of ribosomes from prokaryotes, eukaryotes, and organelles, p. 1-29. In G. Spedding (ed.), Ribosomes and protein synthesis: a practical approach. IRL Press, Oxford, United Kingdom.
    • (1990) Ribosomes and Protein Synthesis: A Practical Approach , pp. 1-29
    • Spedding, G.1
  • 33
    • 0023971594 scopus 로고
    • Characterization of the ATPase and GTPase activities of elongation factor 3 (EF-3) purified from yeasts
    • Uritani, M., and M. Miyazaki. 1988. Characterization of the ATPase and GTPase activities of elongation factor 3 (EF-3) purified from yeasts. J. Biochem. 103:522-530.
    • (1988) J. Biochem. , vol.103 , pp. 522-530
    • Uritani, M.1    Miyazaki, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.