메뉴 건너뛰기




Volumn 52, Issue 32, 2013, Pages 5345-5353

Different oligomeric properties and stability of highly homologous A1 and proto-oncogenic A2 variants of mammalian translation elongation factor eEF1

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; FUNCTIONAL PERFORMANCE; HOMOLOGOUS PROTEINS; LIPOPHILICITY; LOW RESISTANCE; SYNCHROTRON SMALL-ANGLE X-RAY SCATTERINGS; TRANSLATION ELONGATION; TRANSLATION FUNCTIONS;

EID: 84881635591     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400400r     Document Type: Article
Times cited : (20)

References (63)
  • 1
    • 77954377942 scopus 로고    scopus 로고
    • EEF1A: Thinking outside the ribosome
    • Mateyak, M. K. and Kinzy, T. G. (2010) eEF1A: Thinking outside the ribosome J. Biol. Chem. 285, 21209-21213
    • (2010) J. Biol. Chem. , vol.285 , pp. 21209-21213
    • Mateyak, M.K.1    Kinzy, T.G.2
  • 2
    • 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 Acid Res. Mol. Biol. 60, 47-78
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.60 , pp. 47-78
    • Negrutskii, B.S.1    El'Skaya, A.V.2
  • 3
    • 26844440904 scopus 로고    scopus 로고
    • Translation elongation factor eEF1A2 is a potential oncoprotein that is overexpressed in two-thirds of breast tumours
    • Tomlinson, V. A., Newbery, H. J., Wray, N. R., Jackson, J., Larionov, A., Miller, W. R., Dixon, J. M., and Abbott, C. M. (2005) Translation elongation factor eEF1A2 is a potential oncoprotein that is overexpressed in two-thirds of breast tumours BMC Cancer 5, 113
    • (2005) BMC Cancer , vol.5 , pp. 113
    • Tomlinson, V.A.1    Newbery, H.J.2    Wray, N.R.3    Jackson, J.4    Larionov, A.5    Miller, W.R.6    Dixon, J.M.7    Abbott, C.M.8
  • 4
    • 0032522219 scopus 로고    scopus 로고
    • The elongation factor 1 A-2 isoform from rabbit: Cloning of the cDNA and characterization of the protein
    • Kahns, S., Lund, A., Kristensen, P., Knudsen, C. R., Clark, B. F., Cavallius, J., and Merrick, W. C. (1998) The elongation factor 1 A-2 isoform from rabbit: Cloning of the cDNA and characterization of the protein Nucleic Acids Res. 26, 1884-1890
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1884-1890
    • Kahns, S.1    Lund, A.2    Kristensen, P.3    Knudsen, C.R.4    Clark, B.F.5    Cavallius, J.6    Merrick, W.C.7
  • 6
    • 0032515985 scopus 로고    scopus 로고
    • The lethal mutation of the mouse wasted (wst) is a deletion that abolishes expression of a tissue-specific isoform of translation elongation factor 1α, encoded by the Eef1a2 gene
    • Chambers, D. M., Peters, J., and Abbott, C. M. (1998) The lethal mutation of the mouse wasted (wst) is a deletion that abolishes expression of a tissue-specific isoform of translation elongation factor 1α, encoded by the Eef1a2 gene Proc. Natl. Acad. Sci. U.S.A. 95, 4463-4468
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 4463-4468
    • Chambers, D.M.1    Peters, J.2    Abbott, C.M.3
  • 8
    • 35348815574 scopus 로고    scopus 로고
    • Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes
    • Mishra, A. K., Gangwani, L., Davis, R. J., and Lambright, D. G. (2007) Structural insights into the interaction of the evolutionarily conserved ZPR1 domain tandem with eukaryotic EF1A, receptors, and SMN complexes Proc. Natl. Acad. Sci. U.S.A. 104, 13930-13935
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 13930-13935
    • Mishra, A.K.1    Gangwani, L.2    Davis, R.J.3    Lambright, D.G.4
  • 10
    • 4143091385 scopus 로고    scopus 로고
    • The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis: Review article
    • Lamberti, A., Caraglia, M., Longo, O., Marra, M., Abbruzzese, A., and Arcari, P. (2004) The translation elongation factor 1A in tumorigenesis, signal transduction and apoptosis: Review article Amino Acids 26, 443-448
    • (2004) Amino Acids , vol.26 , pp. 443-448
    • Lamberti, A.1    Caraglia, M.2    Longo, O.3    Marra, M.4    Abbruzzese, A.5    Arcari, P.6
  • 12
    • 21344469230 scopus 로고    scopus 로고
    • Increased proteasome activity, ubiquitin-conjugating enzymes, and eEF1A translation factor detected in breast cancer tissue
    • Chen, L. and Madura, K. (2005) Increased proteasome activity, ubiquitin-conjugating enzymes, and eEF1A translation factor detected in breast cancer tissue Cancer Res. 65, 5599-5606
    • (2005) Cancer Res. , vol.65 , pp. 5599-5606
    • Chen, L.1    Madura, K.2
  • 13
    • 47049120759 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 1A2 cooperates with phosphatidylinositol-4 kinase IIIβ to stimulate production of filopodia through increased phosphatidylinositol-4,5 bisphosphate generation
    • Jeganathan, S., Morrow, A., Amiri, A., and Lee, J. M. (2008) Eukaryotic elongation factor 1A2 cooperates with phosphatidylinositol-4 kinase IIIβ to stimulate production of filopodia through increased phosphatidylinositol-4,5 bisphosphate generation Mol. Cell. Biol. 28, 4549-4561
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4549-4561
    • Jeganathan, S.1    Morrow, A.2    Amiri, A.3    Lee, J.M.4
  • 14
    • 0036683716 scopus 로고    scopus 로고
    • Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system
    • Mansilla, F., Friis, I., Jadidi, M., Nielsen, K. M., Clark, B. F., and Knudsen, C. R. (2002) Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system Biochem. J. 365, 669-676
    • (2002) Biochem. J. , vol.365 , pp. 669-676
    • Mansilla, F.1    Friis, I.2    Jadidi, M.3    Nielsen, K.M.4    Clark, B.F.5    Knudsen, C.R.6
  • 15
    • 35748970152 scopus 로고    scopus 로고
    • A2 isoform of mammalian translation factor eEF1A displays increased tyrosine phosphorylation and ability to interact with different signalling molecules
    • Panasyuk, G., Nemazanyy, I., Filonenko, V., Negrutskii, B., and El'skaya, A. V. (2008) A2 isoform of mammalian translation factor eEF1A displays increased tyrosine phosphorylation and ability to interact with different signalling molecules Int. J. Biochem. Cell Biol. 40, 63-71
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 63-71
    • Panasyuk, G.1    Nemazanyy, I.2    Filonenko, V.3    Negrutskii, B.4    El'Skaya, A.V.5
  • 16
    • 33846450656 scopus 로고    scopus 로고
    • Mouse translation elongation factor eEF1A-2 interacts with Prdx-I to protect cells against apoptotic death induced by oxidative stress
    • Chang, R. and Wang, E. (2007) Mouse translation elongation factor eEF1A-2 interacts with Prdx-I to protect cells against apoptotic death induced by oxidative stress J. Cell. Biochem. 100, 267-278
    • (2007) J. Cell. Biochem. , vol.100 , pp. 267-278
    • Chang, R.1    Wang, E.2
  • 19
    • 77956292558 scopus 로고    scopus 로고
    • Eef1a2 promotes cell growth, inhibits apoptosis and activates JAK/STAT and AKT signaling in mouse plasmacytomas
    • Li, Z., Qi, C. F., Shin, D. M., Zingone, A., Newbery, H. J., Kovalchuk, A. L., Abbott, C. M., and Morse, H. C., III (2010) Eef1a2 promotes cell growth, inhibits apoptosis and activates JAK/STAT and AKT signaling in mouse plasmacytomas PLoS One 5 (5) e10755
    • (2010) PLoS One , vol.5 , Issue.5 , pp. 10755
    • Li, Z.1    Qi, C.F.2    Shin, D.M.3    Zingone, A.4    Newbery, H.J.5    Kovalchuk, A.L.6    Abbott, C.M.7    Morse III, H.C.8
  • 21
    • 33646368154 scopus 로고    scopus 로고
    • Identification of putative oncogenes in lung adenocarcinoma by a comprehensive functional genomic approach
    • Li, R., Wang, H., Bekele, B. N., Yin, Z., Caraway, N. P., Katz, R. L., Stass, S. A., and Jiang, F. (2006) Identification of putative oncogenes in lung adenocarcinoma by a comprehensive functional genomic approach Oncogene 25, 2628-2635
    • (2006) Oncogene , vol.25 , pp. 2628-2635
    • Li, R.1    Wang, H.2    Bekele, B.N.3    Yin, Z.4    Caraway, N.P.5    Katz, R.L.6    Stass, S.A.7    Jiang, F.8
  • 23
    • 34248570992 scopus 로고    scopus 로고
    • Expression of eEF1A2 is associated with clear cell histology in ovarian carcinomas: Overexpression of the gene is not dependent on modifications at the EEF1A2 locus
    • Tomlinson, V. A., Newbery, H. J., Bergmann, J. H., Boyd, J., Scott, D., Wray, N. R., Sellar, G. C., Gabra, H., Graham, A., Williams, A. R., and Abbott, C. M. (2007) Expression of eEF1A2 is associated with clear cell histology in ovarian carcinomas: Overexpression of the gene is not dependent on modifications at the EEF1A2 locus Br. J. Cancer 96, 1613-1620
    • (2007) Br. J. Cancer , vol.96 , pp. 1613-1620
    • Tomlinson, V.A.1    Newbery, H.J.2    Bergmann, J.H.3    Boyd, J.4    Scott, D.5    Wray, N.R.6    Sellar, G.C.7    Gabra, H.8    Graham, A.9    Williams, A.R.10    Abbott, C.M.11
  • 27
    • 68149126140 scopus 로고    scopus 로고
    • Structural models of human eEF1A1 and eEF1A2 reveal two distinct surface clusters of sequence variation and potential differences in phosphorylation
    • Soares, D. C., Barlow, P. N., Newbery, H. J., Porteous, D. J., and Abbott, C. M. (2009) Structural models of human eEF1A1 and eEF1A2 reveal two distinct surface clusters of sequence variation and potential differences in phosphorylation PLoS One 4 (7) e6315
    • (2009) PLoS One , vol.4 , Issue.7 , pp. 6315
    • Soares, D.C.1    Barlow, P.N.2    Newbery, H.J.3    Porteous, D.J.4    Abbott, C.M.5
  • 28
    • 0343910574 scopus 로고
    • A simplified procedure for the preparation of "soluble" RNA from rat liver
    • Brungraber, E. F. (1962) A simplified procedure for the preparation of "soluble" RNA from rat liver Biochem. Biophys. Res. Commun. 8, 1-3
    • (1962) Biochem. Biophys. Res. Commun. , vol.8 , pp. 1-3
    • Brungraber, E.F.1
  • 29
  • 30
    • 0029249356 scopus 로고
    • Large-aperture TV detector with a beryllium-windowed image intensifier for X-ray diffraction
    • Amemiya, Y., Ito, K., Yagi, N., Asano, Y., Wakabayashi, K., Ueki, T., and Endo, T. (1995) Large-aperture TV detector with a beryllium-windowed image intensifier for X-ray diffraction Rev. Sci. Instrum. 66, 2290-2294
    • (1995) Rev. Sci. Instrum. , vol.66 , pp. 2290-2294
    • Amemiya, Y.1    Ito, K.2    Yagi, N.3    Asano, Y.4    Wakabayashi, K.5    Ueki, T.6    Endo, T.7
  • 31
    • 31544445519 scopus 로고    scopus 로고
    • Correction method and software for image distortion and nonuniform response in charge-coupled device-based X-ray detectors utilizing X-ray image intensifier
    • Ito, K., Kamikubo, H., Yagi, N., and Amemiya, Y. (2005) Correction method and software for image distortion and nonuniform response in charge-coupled device-based X-ray detectors utilizing X-ray image intensifier Jpn. J. Appl. Phys. 44, 8684-8691
    • (2005) Jpn. J. Appl. Phys. , vol.44 , pp. 8684-8691
    • Ito, K.1    Kamikubo, H.2    Yagi, N.3    Amemiya, Y.4
  • 32
    • 0029185933 scopus 로고
    • CRYSOL: A program to evaluate the X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D. I., Barberato, C., and Koch, M. H. C. (1995) CRYSOL: A program to evaluate the 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.I.1    Barberato, C.2    Koch, M.H.C.3
  • 33
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 35
    • 80052470762 scopus 로고    scopus 로고
    • Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models
    • Ortega, A., Amoros, D., and Garcia de la Torre, J. (2011) Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models Biophys. J. 101, 892-898
    • (2011) Biophys. J. , vol.101 , pp. 892-898
    • Ortega, A.1    Amoros, D.2    Garcia De La Torre, J.3
  • 36
    • 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
    • 0027241662 scopus 로고
    • Surface hydrophobicity of a low molecular weight basic trypsin subtilisin inhibitor from marine turtle eggwhite
    • Chaudhuri, T. K., Das, K. P., and Sinha, N. K. (1993) Surface hydrophobicity of a low molecular weight basic trypsin subtilisin inhibitor from marine turtle eggwhite J. Biochem. 113, 729-733
    • (1993) J. Biochem. , vol.113 , pp. 729-733
    • Chaudhuri, T.K.1    Das, K.P.2    Sinha, N.K.3
  • 38
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato, A. and Nakai, S. (1980) Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins Biochim. Biophys. Acta 624, 13-20
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 39
    • 0021114559 scopus 로고
    • The accuracy of poly(U) translation by different eukaryotic tRNAs
    • El'skaya, A. V. and Soldatkin, A. P. (1983) The accuracy of poly(U) translation by different eukaryotic tRNAs FEBS Lett. 164, 93-96
    • (1983) FEBS Lett. , vol.164 , pp. 93-96
    • El'Skaya, A.V.1    Soldatkin, A.P.2
  • 41
    • 41149102857 scopus 로고    scopus 로고
    • Roles of three domains of Tetrahymena eEF1A in bundling F-actin
    • Morita, K., Bunai, F., and Numata, O. (2008) Roles of three domains of Tetrahymena eEF1A in bundling F-actin Zool. Sci. 25, 22-29
    • (2008) Zool. Sci. , vol.25 , pp. 22-29
    • Morita, K.1    Bunai, F.2    Numata, O.3
  • 42
    • 33750695976 scopus 로고    scopus 로고
    • Tetrahymena eukaryotic translation elongation factor 1A (eEF1A) bundles filamentous actin through dimer formation
    • Bunai, F., Ando, K., Ueno, H., and Numata, O. (2006) Tetrahymena eukaryotic translation elongation factor 1A (eEF1A) bundles filamentous actin through dimer formation J. Biochem. 140, 393-399
    • (2006) J. Biochem. , vol.140 , pp. 393-399
    • Bunai, F.1    Ando, K.2    Ueno, H.3    Numata, O.4
  • 47
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25, 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 48
    • 67649852558 scopus 로고    scopus 로고
    • Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins
    • Pechmann, S., Levy, E. D., Tartaglia, G. G., and Vendruscolo, M. (2009) Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins Proc. Natl. Acad. Sci. U.S.A. 106, 10159-10164
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 10159-10164
    • Pechmann, S.1    Levy, E.D.2    Tartaglia, G.G.3    Vendruscolo, M.4
  • 49
    • 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
  • 50
    • 0031582233 scopus 로고    scopus 로고
    • Evidence for the formation of an unusual ternary complex of rabbit liver EF-1α 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 EF-1α 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
  • 52
    • 84856589270 scopus 로고    scopus 로고
    • From global phosphoproteomics to individual proteins: The case of translation elongation factor eEF1A
    • Negrutskii, B., Vlasenko, D., and El'skaya, A. (2012) From global phosphoproteomics to individual proteins: The case of translation elongation factor eEF1A Expert Rev. Proteomics 9 (1) 71-83
    • (2012) Expert Rev. Proteomics , vol.9 , Issue.1 , pp. 71-83
    • Negrutskii, B.1    Vlasenko, D.2    El'Skaya, A.3
  • 53
    • 0035005341 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:EEF1Bα
    • Andersen, G. R., Valente, L., Pedersen, L., Kinzy, T. G., and Nyborg, J. (2001) Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Bα Nat. Struct. Biol. 8, 531-534
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 531-534
    • Andersen, G.R.1    Valente, L.2    Pedersen, L.3    Kinzy, T.G.4    Nyborg, J.5
  • 55
    • 34547499110 scopus 로고    scopus 로고
    • The design and characterization of two proteins with 88% sequence identity but different structure and function
    • Alexander, P. A., He, Y., Chen, Y., Orban, J., and Bryan, P. N. (2007) The design and characterization of two proteins with 88% sequence identity but different structure and function Proc. Natl. Acad. Sci. U.S.A. 104, 11963-11968
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 11963-11968
    • Alexander, P.A.1    He, Y.2    Chen, Y.3    Orban, J.4    Bryan, P.N.5
  • 56
    • 0024341194 scopus 로고
    • Location of seven post-translational modifications in rabbit elongation factor 1α including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine
    • Dever, T. E., Costello, C. E., Owens, C. L., Rosenberry, T. L., and Merrick, W. C. (1989) Location of seven post-translational modifications in rabbit elongation factor 1α including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine J. Biol. Chem. 264, 20518-20525
    • (1989) J. Biol. Chem. , vol.264 , pp. 20518-20525
    • Dever, T.E.1    Costello, C.E.2    Owens, C.L.3    Rosenberry, T.L.4    Merrick, W.C.5
  • 57
    • 84878770165 scopus 로고    scopus 로고
    • Protein kinase CK2 regulates the dimerization of histone deacetylase (HDAC) 1 and HDAC2 during mitosis
    • Khan, D. H., He, S., Yu, J., Winter, S., Cao, W., Seiser, C., and Davie, J. R. (2013) Protein kinase CK2 regulates the dimerization of histone deacetylase (HDAC) 1 and HDAC2 during mitosis J. Biol. Chem. 288, 16518-16528
    • (2013) J. Biol. Chem. , vol.288 , pp. 16518-16528
    • Khan, D.H.1    He, S.2    Yu, J.3    Winter, S.4    Cao, W.5    Seiser, C.6    Davie, J.R.7
  • 58
    • 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 (4) 739-749
    • (1990) J. Mol. Biol. , vol.211 , Issue.4 , pp. 739-749
    • Ehrenberg, M.1    Rojas, A.M.2    Weiser, J.3    Kurland, C.G.4
  • 59
    • 0038548437 scopus 로고    scopus 로고
    • Changes in protein levels of elongation factors, eEF1A-1 and eEF1A-2/S1, in long-term denervated rat muscle
    • Khalyfa, A., Carlson, B. M., Dedkov, E. I., and Wang, E. (2003) Changes in protein levels of elongation factors, eEF1A-1 and eEF1A-2/S1, in long-term denervated rat muscle Restor. Neurol. Neurosci. 21, 47-53
    • (2003) Restor. Neurol. Neurosci. , vol.21 , pp. 47-53
    • Khalyfa, A.1    Carlson, B.M.2    Dedkov, E.I.3    Wang, E.4
  • 60
    • 35848957488 scopus 로고    scopus 로고
    • Overexpression of the elongation factor 1A1 relates to muscle proteolysis and proapoptotic p66(ShcA) gene transcription in hypercatabolic trauma patients
    • Bosutti, A., Scaggiante, B., Grassi, G., Guarnieri, G., and Biolo, G. (2007) Overexpression of the elongation factor 1A1 relates to muscle proteolysis and proapoptotic p66(ShcA) gene transcription in hypercatabolic trauma patients Metabolism 56, 1629-1634
    • (2007) Metabolism , vol.56 , pp. 1629-1634
    • Bosutti, A.1    Scaggiante, B.2    Grassi, G.3    Guarnieri, G.4    Biolo, G.5
  • 61
    • 42349096996 scopus 로고    scopus 로고
    • MGluR-dependent long-term depression is associated with increased phosphorylation of S6 and synthesis of elongation factor 1A but remains expressed in S6K-deficient mice
    • Antion, M. D., Hou, L., Wong, H., Hoeffer, C. A., and Klann, E. (2008) mGluR-dependent long-term depression is associated with increased phosphorylation of S6 and synthesis of elongation factor 1A but remains expressed in S6K-deficient mice Mol. Cell. Biol. 28, 2996-3007
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2996-3007
    • Antion, M.D.1    Hou, L.2    Wong, H.3    Hoeffer, C.A.4    Klann, E.5
  • 62
    • 23444445375 scopus 로고    scopus 로고
    • The mRNA for elongation factor 1α is localized in dendrites and translated in response to treatments that induce long-term depression
    • Huang, F., Chotiner, J. K., and Steward, O. (2005) The mRNA for elongation factor 1α is localized in dendrites and translated in response to treatments that induce long-term depression J. Neurosci. 25, 7199-7209
    • (2005) J. Neurosci. , vol.25 , pp. 7199-7209
    • Huang, F.1    Chotiner, J.K.2    Steward, O.3
  • 63
    • 79952285928 scopus 로고    scopus 로고
    • Neurite outgrowth mediated by translation elongation factor eEF1A1: A target for antiplatelet agent cilostazol
    • Hashimoto, K. and Ishima, T. (2011) Neurite outgrowth mediated by translation elongation factor eEF1A1: A target for antiplatelet agent cilostazol PLoS One 6 (3) e17431
    • (2011) PLoS One , vol.6 , Issue.3 , pp. 17431
    • Hashimoto, K.1    Ishima, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.