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Volumn 41, Issue 51, 2002, Pages 15342-15349

Extended conformation of mammalian translation elongation factor 1A in solution

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; PROTEINS; SPECIFIC HEAT; SYNTHESIS (CHEMICAL);

EID: 0347298819     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026495h     Document Type: Article
Times cited : (31)

References (58)
  • 1
    • 0031617024 scopus 로고    scopus 로고
    • Eukaryotic translation elongation factor 1α: Structure, expression, functions, and possible role in aminoacyl-tRNA channeling
    • Negrutskii, B. S., and El'skaya, A. V. (1998) Eukaryotic translation elongation factor 1α: Structure, expression, functions, and possible role in aminoacyl-tRNA channeling, Prog. Nucleic Acids Res. Mol. Biol. 60, 47-78.
    • (1998) Prog. Nucleic Acids Res. Mol. Biol. , vol.60 , pp. 47-78
    • Negrutskii, B.S.1    El'skaya, A.V.2
  • 2
    • 0023251561 scopus 로고
    • Development of structural organization of protein-synthesizing machinery from prokaryotes to eukaryotes
    • Ryazanov, A. G., Ovchinnikov, L. P., and Spirin, A. S. (1987) Development of structural organization of protein-synthesizing machinery from prokaryotes to eukaryotes, Biosystems 20, 275-288.
    • (1987) Biosystems , vol.20 , pp. 275-288
    • Ryazanov, A.G.1    Ovchinnikov, L.P.2    Spirin, A.S.3
  • 4
    • 0025876244 scopus 로고
    • Channeling of aminoacyl-tRNA for protein synthesis in vivo
    • Negrutskii, B. S., and Deutscher, M. P. (1991) Channeling of aminoacyl-tRNA for protein synthesis in vivo, Proc. Natl. Acad. Sci. U.S.A. 88, 4991-4995.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4991-4995
    • Negrutskii, B.S.1    Deutscher, M.P.2
  • 5
    • 0031582233 scopus 로고    scopus 로고
    • Evidence for the formation of an unusual ternary complex of rabbit liver tRNA with GDP and deacylated tRNA
    • Petrushenko, Z. M., Negrutskii, B. S., Ladokhin, A. S., Budkevich, T. V., Shalak, V. F., and El'skaya, A. V. (1997) Evidence for the formation of an unusual ternary complex of rabbit liver tRNA with GDP and deacylated tRNA, FEBS Lett. 407, 13-17.
    • (1997) FEBS Lett. , vol.407 , pp. 13-17
    • Petrushenko, Z.M.1    Negrutskii, B.S.2    Ladokhin, A.S.3    Budkevich, T.V.4    Shalak, V.F.5    El'skaya, A.V.6
  • 7
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard, M., Nissen, P., Thirup, S., and Nyborg, J. (1993) The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation, Structure 1, 35-50.
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 8
  • 9
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Echerichia coli EF-Tu:EF-Ts complex at 2.5 Å resolution
    • Kawashima, G., Berthet-Colominas, C., Wulff, M., Cussack, S., and Leberman, R. (1996) The structure of the Echerichia coli EF-Tu:EF-Ts complex at 2.5 Å resolution, Nature 379, 579-518.
    • (1996) Nature , vol.379 , pp. 579-518
    • Kawashima, G.1    Berthet-Colominas, C.2    Wulff, M.3    Cussack, S.4    Leberman, R.5
  • 11
    • 0033593370 scopus 로고    scopus 로고
    • Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 Å resolution
    • Song, H., Parsons, M. R., Rowsell, S., Leonard, G., and Phillips, S. E. (1999) Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 Å resolution, J. Mol. Biol. 285, 1245-1256.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1245-1256
    • Song, H.1    Parsons, M.R.2    Rowsell, S.3    Leonard, G.4    Phillips, S.E.5
  • 12
    • 0026553171 scopus 로고
    • Nucleotide sequence of rabbit elongation factor 1α cDNA
    • Cavallius, J., and Merrick, W. C. (1992) Nucleotide sequence of rabbit elongation factor 1α cDNA, Nucleic Acids Res. 20, 1422-1445.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1422-1445
    • Cavallius, J.1    Merrick, W.C.2
  • 13
    • 0026588965 scopus 로고
    • Refined structure of elongation factor EF-Tu from Escherichia coli
    • Kjeldgaard, M., and Nyborg, J. (1992) Refined structure of elongation factor EF-Tu from Escherichia coli, J. Mol. Biol. 223, 721-742.
    • (1992) J. Mol. Biol. , vol.223 , pp. 721-742
    • Kjeldgaard, M.1    Nyborg, J.2
  • 14
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C., and Koch, M. H. J. (1995) CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates, J. Appl. Crystallogr. 28, 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 15
    • 0028110316 scopus 로고
    • The triple isotopic substitution method in small angle neutron scattering. Application to the study of the ternary complex EF-Tu·GTP·aminoacyl-tRNA
    • Serdyuk, I. N., Pavlov, M. Yu., Rublevskaya, I. N., Zaccai, G., and Leberman, R. (1994) The triple isotopic substitution method in small angle neutron scattering. Application to the study of the ternary complex EF-Tu·GTP·aminoacyl-tRNA, Biophys. Chem. 53, 123-130.
    • (1994) Biophys. Chem. , vol.53 , pp. 123-130
    • Serdyuk, I.N.1    Pavlov, M.Yu.2    Rublevskaya, I.N.3    Zaccai, G.4    Leberman, R.5
  • 16
    • 0017392697 scopus 로고
    • Structural fluctuation of the polypeptide-chain elongation factor Tu
    • Ohta, S., Nakanishi, M., Tsuboi, M., Arai, K., and Kaziro, Y. (1977) Structural fluctuation of the polypeptide-chain elongation factor Tu, Eur. J. Biochem. 78, 599-608.
    • (1977) Eur. J. Biochem. , vol.78 , pp. 599-608
    • Ohta, S.1    Nakanishi, M.2    Tsuboi, M.3    Arai, K.4    Kaziro, Y.5
  • 17
    • 0023873851 scopus 로고
    • Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8
    • Kushiro, M., Shimizu, M., and Tomita, K. (1987) Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8, Eur. J. Biochem. 170, 93-98.
    • (1987) Eur. J. Biochem. , vol.170 , pp. 93-98
    • Kushiro, M.1    Shimizu, M.2    Tomita, K.3
  • 18
    • 0026632982 scopus 로고
    • Sequence of the tufa gene encoding elongation factor EF-Tu from Thermus aquaticus and overproduction of the protein in Escherichia coli
    • Voss, R. H., Hartmann, R. K., Lippmann, C., Alexander, C., Jahn, O., and Erdmann, V. (1992) Sequence of the tufa gene encoding elongation factor EF-Tu from Thermus aquaticus and overproduction of the protein in Escherichia coli, Eur. J. Biochem. 207, 839-846.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 839-846
    • Voss, R.H.1    Hartmann, R.K.2    Lippmann, C.3    Alexander, C.4    Jahn, O.5    Erdmann, V.6
  • 20
    • 0035477797 scopus 로고    scopus 로고
    • The crystal structure of Sulfolobus solfataricus elongation factor 1α in complex with GDP reveals novel feature in nucleotide binding and exchange
    • Vitagliano, L., Masullo, M., Sica, F., Zagari, A., and Bocchini, V. (2001) The crystal structure of Sulfolobus solfataricus elongation factor 1α in complex with GDP reveals novel feature in nucleotide binding and exchange, EMBO J. 20, 5305-5311.
    • (2001) EMBO J. , vol.20 , pp. 5305-5311
    • Vitagliano, L.1    Masullo, M.2    Sica, F.3    Zagari, A.4    Bocchini, V.5
  • 21
    • 0033638335 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Ba
    • Andersen, G. R., Pedersen, L., Valente, L., Chatterjee, I., Kinzy, T. G., Kjeldgaard, M., and Nyborg, J. (2000) Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Ba, Mol. Cell 6, 1261-1266.
    • (2000) Mol. Cell , vol.6 , pp. 1261-1266
    • Andersen, G.R.1    Pedersen, L.2    Valente, L.3    Chatterjee, I.4    Kinzy, T.G.5    Kjeldgaard, M.6    Nyborg, J.7
  • 22
    • 0031083225 scopus 로고    scopus 로고
    • A fast and effective method for purification of elongation factor 1α from rabbit liver
    • Shalak, V. F., Budkevich, T. V., Negrutskii, B. S., and El'skaya, A. V. (1997) A fast and effective method for purification of elongation factor 1α from rabbit liver, Ukr. Biokhim. Zh. 69, 104-109.
    • (1997) Ukr. Biokhim. Zh. , vol.69 , pp. 104-109
    • Shalak, V.F.1    Budkevich, T.V.2    Negrutskii, B.S.3    El'skaya, A.V.4
  • 23
    • 0021703254 scopus 로고
    • Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes
    • Carvalho, M. D., Carvalho, J. F., and Merrick, W. C. (1984) Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes, Arch. Biochem. Biophys. 234, 603-611.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 603-611
    • Carvalho, M.D.1    Carvalho, J.F.2    Merrick, W.C.3
  • 24
    • 0030845290 scopus 로고    scopus 로고
    • Three tRNA binding sites in rabbit liver ribosomes and role of the intrinsic ATPase in 80S ribosomes from higher eukaryotes
    • El'skaya, A. V., Ovcharenko, G. V., Pal'chevskii, S. S., Petrushenko, Z. M., Triana-Alonso, F. J., and Nierhaus, K. H. (1997) Three tRNA binding sites in rabbit liver ribosomes and role of the intrinsic ATPase in 80S ribosomes from higher eukaryotes, Biochemistry 36, 10492-10497.
    • (1997) Biochemistry , vol.36 , pp. 10492-10497
    • El'skaya, A.V.1    Ovcharenko, G.V.2    Pal'chevskii, S.S.3    Petrushenko, Z.M.4    Triana-Alonso, F.J.5    Nierhaus, K.H.6
  • 25
    • 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
  • 26
    • 0023157157 scopus 로고
    • The interaction between biologically inactive tRNA conformers and leucyl-tRNA synthetase from rabbit liver
    • El'skaya, A. V., and Negrutskii, B. S. (1987) The interaction between biologically inactive tRNA conformers and leucyl-tRNA synthetase from rabbit liver, Eur. J. Biochem. 164, 65-69.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 65-69
    • El'skaya, A.V.1    Negrutskii, B.S.2
  • 27
    • 0018064450 scopus 로고
    • Studies on polypeptide-chain-elongation factors from an extreme thermophil, Thermus thermophilus HB8
    • Arai, O., Ota, Y., Arai, N., Nakamura, S., Henneke, C., Oshima, T., and Kaziro, Y. (1978) Studies on polypeptide-chain-elongation factors from an extreme thermophile, Thermus thermophilus HB8, Eur. J. Biochem. 92, 509-519.
    • (1978) Eur. J. Biochem. , vol.92 , pp. 509-519
    • Arai, O.1    Ota, Y.2    Arai, N.3    Nakamura, S.4    Henneke, C.5    Oshima, T.6    Kaziro, Y.7
  • 28
    • 0026509493 scopus 로고
    • Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR
    • Limmer, S., Reiser, C. O. A., Schirmer, N. K., Grillenbeck, N. W., and Sprinzl, M. (1992) Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR, Biochemistry 31, 2970-2977.
    • (1992) Biochemistry , vol.31 , pp. 2970-2977
    • Limmer, S.1    Reiser, C.O.A.2    Schirmer, N.K.3    Grillenbeck, N.W.4    Sprinzl, M.5
  • 30
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov, P. L., and Potekhin, S. A. (1986) Scanning microcalorimetry in studying temperature-induced changes in proteins, Methods Enzymol. 131, 1-51.
    • (1986) Methods Enzymol. , vol.131 , pp. 1-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 31
    • 0036399322 scopus 로고    scopus 로고
    • Novel complexes of mammalian translation elongation factor eEF1A·GDP with uncharged tRNA and aminoacyl-tRNA synthetase. Implications for tRNA channeling
    • Petrushenko, Z. M., Budkevich, T. V., Shalak, V. F., Negrutskii, B. S., and El'skaya A. V. (2002) Novel complexes of mammalian translation elongation factor eEF1A·GDP with uncharged tRNA and aminoacyl-tRNA synthetase. Implications for tRNA channeling, Eur. J. Biochem. 269, 4811-4818.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4811-4818
    • Petrushenko, Z.M.1    Budkevich, T.V.2    Shalak, V.F.3    Negrutskii, B.S.4    El'skaya, A.V.5
  • 32
    • 0642362001 scopus 로고
    • The in situ structure of the L3 and L4 proteins of the large subunit of E. coli ribosomes as determined by nuclear-spin contrast variation
    • Zhao, J., and Stuhrmann, H. B. (1993) The in situ structure of the L3 and L4 proteins of the large subunit of E. coli ribosomes as determined by nuclear-spin contrast variation, J. Phys. 3, 233-236.
    • (1993) J. Phys. , vol.3 , pp. 233-236
    • Zhao, J.1    Stuhrmann, H.B.2
  • 33
    • 0037193194 scopus 로고    scopus 로고
    • Microcalorimetric study of elongation factor Tu from Thermus thermophilus in nucleotide-free, GDP and GTP forms and in the presence of elongation factor Ts
    • Seldak, E., Sprinzl, M., Grillenbeck, N., and Antalik M. (2002) Microcalorimetric study of elongation factor Tu from Thermus thermophilus in nucleotide-free, GDP and GTP forms and in the presence of elongation factor Ts, Biochim. Biophys. Acta 1596, 357-365.
    • (2002) Biochim. Biophys. Acta , vol.1596 , pp. 357-365
    • Seldak, E.1    Sprinzl, M.2    Grillenbeck, N.3    Antalik, M.4
  • 35
    • 0021195067 scopus 로고
    • Amino acid, peptide and protein volume in solution
    • Zamyatnin, A. A. (1984) Amino acid, peptide and protein volume in solution, Annu. Rev. Biophys. Bioeng. 13, 145-165.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatnin, A.A.1
  • 37
  • 38
    • 0030850322 scopus 로고    scopus 로고
    • Solution scattering structural analysis of the 70S Escherichia coli ribosome by contrast variation. II. A model of the ribosome and its RNA at 3.5 nm resolution
    • Svergun, D. I., Burkhardt, N., Pedersen, J. S., Koch, M. H. J., Volkov, V. V., Kozin, M. B., Meerwinck, W., Stuhrmann, H. B., Diedrich, G., and Nierhaus, K. H. (1997b) Solution scattering structural analysis of the 70S Escherichia coli ribosome by contrast variation. II. A model of the ribosome and its RNA at 3.5 nm resolution, J. Mol. Biol. 271, 602-618.
    • (1997) J. Mol. Biol. , vol.271 , pp. 602-618
    • Svergun, D.I.1    Burkhardt, N.2    Pedersen, J.S.3    Koch, M.H.J.4    Volkov, V.V.5    Kozin, M.B.6    Meerwinck, W.7    Stuhrmann, H.B.8    Diedrich, G.9    Nierhaus, K.H.10
  • 40
    • 0018146188 scopus 로고
    • Studies on the structure of protein L7/L12 from Escherichia coli ribosomes
    • Gudkov, A. T., and Khechinashvili, N. N. (1978) Studies on the structure of protein L7/L12 from Escherichia coli ribosomes, Eur. J. Biochem. 90, 313-318.
    • (1978) Eur. J. Biochem. , vol.90 , pp. 313-318
    • Gudkov, A.T.1    Khechinashvili, N.N.2
  • 41
    • 0017231488 scopus 로고
    • Interaction of the low molecular weight form of elongation factor 1 with guanine nucleotides and aminoacyl-tRNA
    • Nagata, S., Iwasaki, K., and Kaziro, Y. (1976) Interaction of the low molecular weight form of elongation factor 1 with guanine nucleotides and aminoacyl-tRNA, Arch. Biochem. Biophys. 172, 168-177.
    • (1976) Arch. Biochem. Biophys. , vol.172 , pp. 168-177
    • Nagata, S.1    Iwasaki, K.2    Kaziro, Y.3
  • 42
    • 0025348355 scopus 로고
    • How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?
    • Ehrenberg, M., Rojas, A. M., Weiser, J., and Kurland, C. G. (1990) How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?, J. Mol. Biol. 211, 739-749.
    • (1990) J. Mol. Biol. , vol.211 , pp. 739-749
    • Ehrenberg, M.1    Rojas, A.M.2    Weiser, J.3    Kurland, C.G.4
  • 43
    • 0028941626 scopus 로고
    • GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs
    • Rodnina, M. V., and Wintermeyer, W. (1995) GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs, Proc. Natl. Acad. Sci. U.S.A. 92, 1945-1949.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1945-1949
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 44
    • 0025937461 scopus 로고
    • How many EF-Tu molecules participate in aminoacyl-tRNA binding?
    • Bensch, K., Pieper, U., Ott, G., Schirmer, N., Sprinzl, M., and Pingoud, A. (1991) How many EF-Tu molecules participate in aminoacyl-tRNA binding?, Biochimie 73, 1045-1050.
    • (1991) Biochimie , vol.73 , pp. 1045-1050
    • Bensch, K.1    Pieper, U.2    Ott, G.3    Schirmer, N.4    Sprinzl, M.5    Pingoud, A.6
  • 45
    • 0029091802 scopus 로고
    • A channeled tRNA cycle during mammalian protein synthesis
    • Stapulionis, R., and Deutscher, M. P. (1995) A channeled tRNA cycle during mammalian protein synthesis, Proc. Natl. Acad. Sci. U.S.A. 92, 7158-7161.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7158-7161
    • Stapulionis, R.1    Deutscher, M.P.2
  • 46
    • 0035818529 scopus 로고    scopus 로고
    • Identification of sites for exponential translation in living dendrites
    • Job, C., and Eberwine, J. (2001) Identification of sites for exponential translation in living dendrites, Proc. Natl. Acad. Sci. U.S.A. 98, 13037-13042.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13037-13042
    • Job, C.1    Eberwine, J.2
  • 47
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: reassessing the protein structure-function paradigm, J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 48
    • 0033597729 scopus 로고    scopus 로고
    • The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1
    • Hershey, P. E., McWhirter, S. M., Gross, J. D., Wagner, G., Alber, T., and Sachs, A. B. (1999) The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1, J. Biol. Chem. 274, 21297-21304.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21297-21304
    • Hershey, P.E.1    McWhirter, S.M.2    Gross, J.D.3    Wagner, G.4    Alber, T.5    Sachs, A.B.6
  • 50
    • 0029828821 scopus 로고    scopus 로고
    • F-actin sequesters elongation factor 1α from interaction with aminoacyl-tRNA in a pH-dependent reaction
    • Liu, G., Tang, J., Edmonds, B. T., Murray, J., Levin, S., and Condeelis, J. (1996) F-actin sequesters elongation factor 1α from interaction with aminoacyl-tRNA in a pH-dependent reaction, J. Cell Biol. 135, 953-963.
    • (1996) J. Cell Biol. , vol.135 , pp. 953-963
    • Liu, G.1    Tang, J.2    Edmonds, B.T.3    Murray, J.4    Levin, S.5    Condeelis, J.6
  • 51
    • 0034031362 scopus 로고    scopus 로고
    • Association between elongation factor-1α and microtubules in vivo is domain dependent and conditional
    • Moore, R. C., and Cyr, R. J. (2000) Association between elongation factor-1α and microtubules in vivo is domain dependent and conditional, Cell Motil. Cytoskeleton 45, 279-292.
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 279-292
    • Moore, R.C.1    Cyr, R.J.2
  • 52
    • 0027933535 scopus 로고
    • Protein translation elongation factor-1α from Trypanosoma brucei binds calmodulin
    • Kaur, K. J., and Ruben, L. (1994) Protein translation elongation factor-1α from Trypanosoma brucei binds calmodulin, J. Biol. Chem. 269, 23045-23050.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23045-23050
    • Kaur, K.J.1    Ruben, L.2
  • 53
    • 0033597292 scopus 로고    scopus 로고
    • Interaction of plant chimeric calcium/calmodulin-dependent protein kinase with a homolog of eukaryotic elongation factor-1α
    • Wang, W., and Poovaiah, B. W. (1999) Interaction of plant chimeric calcium/calmodulin-dependent protein kinase with a homolog of eukaryotic elongation factor-1α, J. Biol. Chem. 274, 12001-12008.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12001-12008
    • Wang, W.1    Poovaiah, B.W.2
  • 54
    • 0032517763 scopus 로고    scopus 로고
    • Interaction of ZPR1 with translation elongation factor-1α in proliferating cells
    • Gangwani, L., Mikrut, M., Galcheva-Gargova, Z., and Davis, R. J. (1998) Interaction of ZPR1 with translation elongation factor-1α in proliferating cells, J. Cell Biol. 143, 1471-1484.
    • (1998) J. Cell Biol. , vol.143 , pp. 1471-1484
    • Gangwani, L.1    Mikrut, M.2    Galcheva-Gargova, Z.3    Davis, R.J.4
  • 57
    • 0030761459 scopus 로고    scopus 로고
    • Translation elongation factor-1α interacts with the 3′ stem-loop region of West Nile virus genomic RNA
    • Blackwell, J. L., and Brinton, M. A. (1997) Translation elongation factor-1α interacts with the 3′ stem-loop region of West Nile virus genomic RNA, J. Virol. 71, 6433-6444.
    • (1997) J. Virol. , vol.71 , pp. 6433-6444
    • Blackwell, J.L.1    Brinton, M.A.2
  • 58
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins, Curr. Opin. Struct. Biol. 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2


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