메뉴 건너뛰기




Volumn 135, Issue 4, 1996, Pages 953-963

F-actin sequesters elongation factor 1α from interaction with aminoacyl-tRNA in a pH-dependent reaction

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ELONGATION FACTOR; F ACTIN; TRANSFER RNA;

EID: 0029828821     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.4.953     Document Type: Article
Times cited : (116)

References (79)
  • 1
    • 0022319421 scopus 로고
    • Cytoplasmic pH and the regulation of the Dictyostelium cell cycle
    • Aerts, R.J., A.J. Durston, and W.H. Moolenaar 1985. Cytoplasmic pH and the regulation of the Dictyostelium cell cycle. Cell. 43:853-857.
    • (1985) Cell , vol.43 , pp. 853-857
    • Aerts, R.J.1    Durston, A.J.2    Moolenaar, W.H.3
  • 2
    • 0023658444 scopus 로고
    • Cyclic AMP induces a transient alkalization in Dictyostelium
    • Aerts, R.J., R.J. De Wit, and M.M. Van Lookeren Campagne. 1987. Cyclic AMP induces a transient alkalization in Dictyostelium. FEBS Lett. 220:366-370.
    • (1987) FEBS Lett. , vol.220 , pp. 366-370
    • Aerts, R.J.1    De Wit, R.J.2    Van Lookeren Campagne, M.M.3
  • 3
    • 0014687871 scopus 로고
    • Regulatory significance of transfer RNA charging levels: I. Measurements of charging levels in liver of chow-fed rats, fasting rats, and rats fed balanced or imbalanced mixtures of amino acids
    • Allen, R.E., P.L. Raines, and D.M. Regen. 1969. Regulatory significance of transfer RNA charging levels: I. Measurements of charging levels in liver of chow-fed rats, fasting rats, and rats fed balanced or imbalanced mixtures of amino acids. Biochim. Biophys. Acta. 190:323-336.
    • (1969) Biochim. Biophys. Acta , vol.190 , pp. 323-336
    • Allen, R.E.1    Raines, P.L.2    Regen, D.M.3
  • 4
    • 0027963350 scopus 로고
    • Single mRNAs visualized by ultrastructural in situ hybridization are principally localized at actin filament intersections in fibroblasts
    • Bassell, G.J., C.M. Powers, K.L. Taneja, and R.H. Singer. 1994. Single mRNAs visualized by ultrastructural in situ hybridization are principally localized at actin filament intersections in fibroblasts. J. Cell Biol. 126:863-876.
    • (1994) J. Cell Biol. , vol.126 , pp. 863-876
    • Bassell, G.J.1    Powers, C.M.2    Taneja, K.L.3    Singer, R.H.4
  • 5
    • 0028072134 scopus 로고
    • Interactions of eukaryotic elongation factor 2 with actin: A possible link between protein synthetic machinery and cytoskeleton
    • Bektas, M., R. Nurten, Z. Gürel, Z. Sayers, and E. Bermek. 1994. Interactions of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton. FEBS Lett. 356:89-93.
    • (1994) FEBS Lett. , vol.356 , pp. 89-93
    • Bektas, M.1    Nurten, R.2    Gürel, Z.3    Sayers, Z.4    Bermek, E.5
  • 8
    • 0014202530 scopus 로고
    • Studies on free membrane-bound ribosomes in rat liver: I. Distribution as related to total cellular RNA
    • Blobel, G., and V.R. Potter. 1967. Studies on free membrane-bound ribosomes in rat liver: I. Distribution as related to total cellular RNA. J. Mol. Biol. 26: 279-292.
    • (1967) J. Mol. Biol. , vol.26 , pp. 279-292
    • Blobel, G.1    Potter, V.R.2
  • 9
    • 0025764368 scopus 로고
    • Isolation of actin-binding proteins from Dictyostelium discoideum
    • Molecular Motors and the Cytoskeleton. (R.B. Vallee, editor). Academic Press, New York
    • Bresnick, A.R., and J. Condeelis. 1990. Isolation of actin-binding proteins from Dictyostelium discoideum. In Molecular Motors and the Cytoskeleton. Methods in Enzymology Vol. 96. (R.B. Vallee, editor). Academic Press, New York. 70-83.
    • (1990) Methods in Enzymology , vol.96 , pp. 70-83
    • Bresnick, A.R.1    Condeelis, J.2
  • 10
    • 0025293017 scopus 로고
    • Identification of a short sequence essential for actin binding by Dictyostelium ABP-120
    • Bresnick, A.R., V. Warren, and J. Condeelis. 1990. Identification of a short sequence essential for actin binding by Dictyostelium ABP-120. J. Biol. Chem. 265:9236-9240.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9236-9240
    • Bresnick, A.R.1    Warren, V.2    Condeelis, J.3
  • 12
    • 0014434371 scopus 로고
    • The distribution of RNA and ribosomes in reticulocytes
    • Burka, E.R. 1968. The distribution of RNA and ribosomes in reticulocytes. Biochim. Biophys. Acta. 166:672-680.
    • (1968) Biochim. Biophys. Acta , vol.166 , pp. 672-680
    • Burka, E.R.1
  • 13
    • 0020683694 scopus 로고
    • Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue
    • Capon, D.J., E.Y. Chen, A.D. Levinson, P.H. Seeburg, and D.V. Geoddel. 1983. Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue. Nature (Lond.). 302:33-37.
    • (1983) Nature (Lond.) , vol.302 , pp. 33-37
    • Capon, D.J.1    Chen, E.Y.2    Levinson, A.D.3    Seeburg, P.H.4    Geoddel, D.V.5
  • 14
    • 0022481384 scopus 로고
    • Intracellular pH controls growth factor-induced ribosomal protein S6 phosphorylation and protein synthesis in the G0-G1 transition of fibroblasts
    • Chambard, J.C., and J. Pouyssegur. 1986. Intracellular pH controls growth factor-induced ribosomal protein S6 phosphorylation and protein synthesis in the G0-G1 transition of fibroblasts. Exp. Cell Res. 164:282-294.
    • (1986) Exp. Cell Res. , vol.164 , pp. 282-294
    • Chambard, J.C.1    Pouyssegur, J.2
  • 15
    • 0025161475 scopus 로고
    • Structural determination of the functional sites of E. coli elongation factor Tu
    • Clark, B.F.C., M. Kjeldgaard, T. la Cour, S. Thirup, and J. Nyborg. 1990. Structural determination of the functional sites of E. coli elongation factor Tu. Biochim. Biophys. Acta. 1050:203-208.
    • (1990) Biochim. Biophys. Acta , vol.1050 , pp. 203-208
    • Clark, B.F.C.1    Kjeldgaard, M.2    La Cour, T.3    Thirup, S.4    Nyborg, J.5
  • 16
    • 0028988998 scopus 로고
    • Elongation factor 1α, translation and the cytoskeleton
    • Condeelis, J. 1995. Elongation factor 1α, translation and the cytoskeleton. Trends Biochem. Sci. 20:169-170.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 169-170
    • Condeelis, J.1
  • 17
    • 0022916176 scopus 로고
    • Characterization of the elongation factors from calf brain. 3. Properties of the GTPase activity of EF-1α and mode of action of kirromysin
    • Crechet, J.B., and A. Parmeggiani. 1986. Characterization of the elongation factors from calf brain. 3. Properties of the GTPase activity of EF-1α and mode of action of kirromysin. Eur. J. Biochem. 161:655-660.
    • (1986) Eur. J. Biochem. , vol.161 , pp. 655-660
    • Crechet, J.B.1    Parmeggiani, A.2
  • 18
    • 0025002846 scopus 로고
    • Isolation of an abundant 50,000 dalton actin filament bundling protein from Dictyostelium amoebae
    • Demma, M., V. Warren, R. Hock, S. Dharmawardhane, and J. Condeelis. 1990. Isolation of an abundant 50,000 dalton actin filament bundling protein from Dictyostelium amoebae. J. Biol. Chem. 265:2286-2291.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2286-2291
    • Demma, M.1    Warren, V.2    Hock, R.3    Dharmawardhane, S.4    Condeelis, J.5
  • 19
    • 0026320055 scopus 로고
    • Compartmentalization and actin binding properties of ABP-50: The elongation factor-1α of Dictyostelium
    • Dharmawardhane, S., M. Demma, F. Yang, and J. Condeelis. 1991. Compartmentalization and actin binding properties of ABP-50: the elongation factor-1α of Dictyostelium. Cell Motil. Cytoskel. 20:279-288.
    • (1991) Cell Motil. Cytoskel. , vol.20 , pp. 279-288
    • Dharmawardhane, S.1    Demma, M.2    Yang, F.3    Condeelis, J.4
  • 20
    • 0028445306 scopus 로고
    • A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1α
    • Durso, N.A., and R.J. Cyr. 1994a. A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1α. Plant Cell. 6:893-905.
    • (1994) Plant Cell , vol.6 , pp. 893-905
    • Durso, N.A.1    Cyr, R.J.2
  • 21
    • 0027951751 scopus 로고
    • Beyond translation: Elongation factor-1α and the cytoskeleton
    • Durso, N.A., and R.J. Cyr. 1994b. Beyond translation: elongation factor-1α and the cytoskeleton. Protoplasma. 180:99-105.
    • (1994) Protoplasma , vol.180 , pp. 99-105
    • Durso, N.A.1    Cyr, R.J.2
  • 22
    • 0027158424 scopus 로고
    • ABP50: An actin-binding elongation factor 1α from Dictyostelium discoideum
    • Edmonds, B.T. 1993. ABP50: an actin-binding elongation factor 1α from Dictyostelium discoideum. J. Cell. Biochem. 52:134-139.
    • (1993) J. Cell. Biochem. , vol.52 , pp. 134-139
    • Edmonds, B.T.1
  • 23
    • 0029020353 scopus 로고
    • pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1α
    • Edmonds, B.T., J. Murray, and J. Condeelis. 1995. pH regulation of the F-actin binding properties of Dictyostelium elongation factor 1α. J. Biol. Chem. 270: 15222-15230.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15222-15230
    • Edmonds, B.T.1    Murray, J.2    Condeelis, J.3
  • 26
    • 0024225944 scopus 로고
    • Measurement of the cytoplasmic pH of Dictyostelium discoideum using a low light level microspectrofluorometer
    • Furukawa, R., J.E. Wampler, and M. Fecheimer. 1988. Measurement of the cytoplasmic pH of Dictyostelium discoideum using a low light level microspectrofluorometer. J. Cell Biol. 107:2541-2549.
    • (1988) J. Cell Biol. , vol.107 , pp. 2541-2549
    • Furukawa, R.1    Wampler, J.E.2    Fecheimer, M.3
  • 27
    • 0025314492 scopus 로고
    • Cytoplasmic pH of Dictyostelium discoideum amebae during early development: Identification of two cell subpopulation before the aggregation stage
    • Furukawa, R., J.E. Wampler, and M. Fecheimer. 1990. Cytoplasmic pH of Dictyostelium discoideum amebae during early development: identification of two cell subpopulation before the aggregation stage. J. Cell Biol. 110:1947-1954.
    • (1990) J. Cell Biol. , vol.110 , pp. 1947-1954
    • Furukawa, R.1    Wampler, J.E.2    Fecheimer, M.3
  • 28
    • 79953271731 scopus 로고
    • Quantitation of DNA and RNA with absorption and fluorescence spectroscopy
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, and K. Struhl, editors. John Wiley & Sons Inc., New York
    • Gallagher, S.R. 1994. Quantitation of DNA and RNA with absorption and fluorescence spectroscopy. In Current Protocols in Molecular Biology. F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, and K. Struhl, editors. John Wiley & Sons Inc., New York. A3.D.1-A3.D.5.
    • (1994) Current Protocols in Molecular Biology
    • Gallagher, S.R.1
  • 30
    • 0019335828 scopus 로고
    • Polypeptide elongation and tRNA cycling in Escherichia coli: A dynamic approach
    • Gouy, M., and R. Granthan. 1980. Polypeptide elongation and tRNA cycling in Escherichia coli: a dynamic approach. FEBS Lett. 115:151-155.
    • (1980) FEBS Lett. , vol.115 , pp. 151-155
    • Gouy, M.1    Granthan, R.2
  • 31
    • 0024529464 scopus 로고
    • + exchange and growth factor-induced cytosolic pH changes. Role in cellular proliferation
    • + exchange and growth factor-induced cytosolic pH changes. Role in cellular proliferation. Biochim. Biophy. Acta. 988:73-97.
    • (1989) Biochim. Biophy. Acta , vol.988 , pp. 73-97
    • Grinstein, S.1    Rotin, D.2    Mason, M.J.3
  • 32
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion protein with glutathione S-transferase
    • Guan, K., and J.K. Dixon. 1991. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion protein with glutathione S-transferase. Anal. Biochem. 192:262-267.
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.1    Dixon, J.K.2
  • 33
    • 0027960357 scopus 로고
    • Polyribosome targeting to microtubules: Enrichment of specific mRNAs in a reconstituted microtubule preparation from sea urchin embryos
    • Hamill, D., J. Davis, J. Drawbridge, and K.A. Suprenant. 1994. Polyribosome targeting to microtubules: enrichment of specific mRNAs in a reconstituted microtubule preparation from sea urchin embryos. J. Cell Biol. 127:973-984.
    • (1994) J. Cell Biol. , vol.127 , pp. 973-984
    • Hamill, D.1    Davis, J.2    Drawbridge, J.3    Suprenant, K.A.4
  • 34
    • 0026092845 scopus 로고
    • Immunohistochemical evidence for an association of ribosome with microfilaments in 3T3 fibroblasts
    • Hesketh, J.E., Z. Home, and G.P. Campbell. 1991. Immunohistochemical evidence for an association of ribosome with microfilaments in 3T3 fibroblasts. Cell Biol. Int. Rep. 15:141-150.
    • (1991) Cell Biol. Int. Rep. , vol.15 , pp. 141-150
    • Hesketh, J.E.1    Home, Z.2    Campbell, G.P.3
  • 35
    • 0021227920 scopus 로고
    • Translational initiation factor and ribosome association with the cytoskeletal framework fraction from HeLa cells
    • Howe, J.G., and J.W. Hershey. 1984. Translational initiation factor and ribosome association with the cytoskeletal framework fraction from HeLa cells. Cell. 37:85-93.
    • (1984) Cell , vol.37 , pp. 85-93
    • Howe, J.G.1    Hershey, J.W.2
  • 36
    • 0022394955 scopus 로고
    • Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins
    • Jurnak, F. 1985. Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Science (Wash. DC). 230: 32-36.
    • (1985) Science (Wash. DC) , vol.230 , pp. 32-36
    • Jurnak, F.1
  • 37
    • 0027933535 scopus 로고
    • Protein translation elongation factor-1α from Trypanosome brucei binds calmodulin
    • Kaur, K.J., and L. Ruben. 1994. Protein translation elongation factor-1α from Trypanosome 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
  • 38
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu·EF-Ts complex at 2.5 Å resolution
    • Kawashima, T., C. Berthet-Colominas, M. Wulff, S. Cusack, and R. Leberman. 1996. The structure of the Escherichia coli EF-Tu·EF-Ts complex at 2.5 Å resolution. Nature (Lond.). 379:511-518.
    • (1996) Nature (Lond.) , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 39
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard, M., P. Nissen, S. Thirup, and J. Nyborg. 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
  • 40
    • 0026515440 scopus 로고
    • L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • Kocks, C., E. Gouin, M. Tabouret, P. Berche, H. Ohayon, and P. Cossart. 1992. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell. 68:521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, E.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., M.W. MacArthur, D.S. Moss, and J.M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26:283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 44
    • 0024592014 scopus 로고
    • The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1 alpha) mRNA
    • Lu, X., and D. Werner. 1989. The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1 alpha) mRNA. Nucleic Acid Res. 17:442.
    • (1989) Nucleic Acid Res. , vol.17 , pp. 442
    • Lu, X.1    Werner, D.2
  • 45
    • 0019255897 scopus 로고
    • Regulation of development in Dictyostelium discoideum. IV. Effects of ions on the rate of differentiation and cellular response to cyclic AMP
    • Marin, F.T., and F.G. Rothman. 1980. Regulation of development in Dictyostelium discoideum. IV. Effects of ions on the rate of differentiation and cellular response to cyclic AMP. J. Cell Biol. 87:823-827.
    • (1980) J. Cell Biol. , vol.87 , pp. 823-827
    • Marin, F.T.1    Rothman, F.G.2
  • 46
    • 0018400571 scopus 로고
    • Assays for eukaryotic protein synthesis
    • K. Moldave and L. Grossman, editors. Academic Press, New York
    • Merrick, W.C. 1979. Assays for eukaryotic protein synthesis. In Methods in Enzymology. Vol. 60. K. Moldave and L. Grossman, editors. Academic Press, New York. 108-123.
    • (1979) Methods in Enzymology , vol.60 , pp. 108-123
    • Merrick, W.C.1
  • 47
    • 0025930249 scopus 로고
    • Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: Structural domains and their implications
    • Mirande, M. 1991. Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications. Prog. Nucleic Acid Res. Mol. Biol. 40:95-142.
    • (1991) Prog. Nucleic Acid Res. Mol. Biol. , vol.40 , pp. 95-142
    • Mirande, M.1
  • 48
    • 0015505265 scopus 로고
    • Interaction of brain transferase I with guanine nucleotides and aminoacyl-tRNA
    • Moon, H.M., and H. Weissbach. 1972. Interaction of brain transferase I with guanine nucleotides and aminoacyl-tRNA. Biochem. Biophys. Res. Commun. 46:254-262.
    • (1972) Biochem. Biophys. Res. Commun. , vol.46 , pp. 254-262
    • Moon, H.M.1    Weissbach, H.2
  • 49
    • 10544255629 scopus 로고    scopus 로고
    • Elongation factor 1 alpha alters the initial rates and final extent of actin polymerization and depolymerization
    • In press
    • Murray, J., B.T. Edmonds, G. Liu, and J. Condeelis. 1996. Elongation factor 1 alpha alters the initial rates and final extent of actin polymerization and depolymerization. J. Cell Biol. In press.
    • (1996) J. Cell Biol.
    • Murray, J.1    Edmonds, B.T.2    Liu, G.3    Condeelis, J.4
  • 50
    • 0017231488 scopus 로고
    • Interaction of the low molecular weight form of elongation factor 1 with guanine nucleotides and aminoacyl-tRNA
    • Nagata, S., K. Iwasaki, and Y. Kaziro. 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
  • 51
    • 0025876244 scopus 로고
    • Channeling of aminoacyl-tRNA for protein synthesis in viva
    • Negrutskii, B.S., and M.P. Deutscher. 1991. Channeling of aminoacyl-tRNA for protein synthesis in viva. Proc. Natl. Acad. Sci. 88:4991-4995.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 4991-4995
    • Negrutskii, B.S.1    Deutscher, M.P.2
  • 52
    • 0020531374 scopus 로고
    • The role of the cytoskeleton in eukaryotic protein synthesis
    • Nielsen, P., S. Goelz, and H. Trachsel. 1983. The role of the cytoskeleton in eukaryotic protein synthesis. Cell Biol. Int. Rep. 7:245-254.
    • (1983) Cell Biol. Int. Rep. , vol.7 , pp. 245-254
    • Nielsen, P.1    Goelz, S.2    Trachsel, H.3
  • 54
    • 0018794774 scopus 로고
    • Control of proteins synthesis in mammalian cells by aminoacylation of transfer ribonucleic acid
    • Ogilvie, A., U. Huschka, and W. Kersten. 1979. Control of proteins synthesis in mammalian cells by aminoacylation of transfer ribonucleic acid. Biochim. Biophys. Acta. 565:293-304.
    • (1979) Biochim. Biophys. Acta , vol.565 , pp. 293-304
    • Ogilvie, A.1    Huschka, U.2    Kersten, W.3
  • 55
    • 0028860154 scopus 로고
    • Differential association of three actin-bundling proteins with microfilaments in Dictyostelium amoebae
    • Okazaki, K., and S. Yumura. 1995. Differential association of three actin-bundling proteins with microfilaments in Dictyostelium amoebae. Eur. J. Cell Biol. 66:75-81.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 75-81
    • Okazaki, K.1    Yumura, S.2
  • 56
    • 0026974889 scopus 로고
    • Actin crosslinking protein EF-1α of Dictyostelium discoideum has a unique bonding rule that allows square packed bundles
    • Owen, C., D. DeRosier, and J. Condeelis. 1992. Actin crosslinking protein EF-1α of Dictyostelium discoideum has a unique bonding rule that allows square packed bundles. J. Struct. Biol. 109:248-254.
    • (1992) J. Struct. Biol. , vol.109 , pp. 248-254
    • Owen, C.1    DeRosier, D.2    Condeelis, J.3
  • 57
    • 0021100471 scopus 로고
    • The elongation factor Tu from Escherichia coli, aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is hound by programmed ribosomes
    • Pingoud, A., F.-U. Gast, W. Block, and F. Peters. 19S3. The elongation factor Tu from Escherichia coli, aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is hound by programmed ribosomes. J. Biol. Chem. 258:14200-14205.
    • (1953) J. Biol. Chem. , vol.258 , pp. 14200-14205
    • Pingoud, A.1    Gast, F.-U.2    Block, W.3    Peters, F.4
  • 58
    • 0029067095 scopus 로고
    • Protein synthesis increases after fertilization of sea urchin eggs in the absence of an increase in intracellular pH
    • Rees, B.B., C. Patton, J.L. Grainger, and D. Epel. 1995. Protein synthesis increases after fertilization of sea urchin eggs in the absence of an increase in intracellular pH. Dev. Biol. 169:683-698.
    • (1995) Dev. Biol. , vol.169 , pp. 683-698
    • Rees, B.B.1    Patton, C.2    Grainger, J.L.3    Epel, D.4
  • 60
    • 0029065026 scopus 로고
    • The intracellular localization of messenger RNAs
    • St Johnston, D. 1995. The intracellular localization of messenger RNAs. Cell. 81:161-170.
    • (1995) Cell , vol.81 , pp. 161-170
    • St Johnston, D.1
  • 61
    • 0024713175 scopus 로고
    • 31P-NMR probe for intracellular pH measurements in Dictyostelium amoebae
    • 31P-NMR probe for intracellular pH measurements in Dictyostelium amoebae. Biochimie (Paris). 71:941-948.
    • (1986) Biochimie (Paris) , vol.71 , pp. 941-948
    • Satre, M.1    Martin, J.B.2    Klein, G.3
  • 62
    • 0017701040 scopus 로고
    • Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors
    • Schreier, M.H., B. Erni, and T. Staehelin. 1977. Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors. J. Mol. Biol. 116:727-753.
    • (1977) J. Mol. Biol. , vol.116 , pp. 727-753
    • Schreier, M.H.1    Erni, B.2    Staehelin, T.3
  • 64
    • 0027158423 scopus 로고
    • Spatial organisation of mRNA within cells
    • Singer, R.H. 1993. Spatial organisation of mRNA within cells. J. Cell. Biochem. 52:125-126.
    • (1993) J. Cell. Biochem. , vol.52 , pp. 125-126
    • Singer, R.H.1
  • 65
    • 0019062683 scopus 로고
    • The roleof eukaryotic elongation factor Tu in protein synthesis: The measurement of the elongation factor Tu content of rabbit reticulocytes and other mammalian cells by a sensitive radioimmunoassay
    • Slohin, L.I. 1980. The roleof eukaryotic elongation factor Tu in protein synthesis: the measurement of the elongation factor Tu content of rabbit reticulocytes and other mammalian cells by a sensitive radioimmunoassay. Eur. J. Biochem. 110:555-563.
    • (1980) Eur. J. Biochem. , vol.110 , pp. 555-563
    • Slohin, L.I.1
  • 66
    • 0017090164 scopus 로고
    • Characterization of developmentally regulated forms of elongation factor 1 in Artimia salina
    • Slobin, L.I., and W. Möller. 1976. Characterization of developmentally regulated forms of elongation factor 1 in Artimia salina. Eur. J. Biochem. 69:367-375.
    • (1976) Eur. J. Biochem. , vol.69 , pp. 367-375
    • Slobin, L.I.1    Möller, W.2
  • 67
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B., and K.S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 68
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 69
    • 0029091802 scopus 로고
    • A channeled tRNA cycle during mammalian protein synthesis
    • Stapulionis, R., and M.P. Deutscher. 1995. A channeled tRNA cycle during mammalian protein synthesis. Proc. Natl. Acad. Sci. USA. 92:7158-7161.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7158-7161
    • Stapulionis, R.1    Deutscher, M.P.2
  • 70
    • 0024544872 scopus 로고
    • 2-terminal segment of depactin participates in interaction with actin
    • 2-terminal segment of depactin participates in interaction with actin. Biochemistry. 28:102-106.
    • (1989) Biochemistry , vol.28 , pp. 102-106
    • Sutoh, K.1    Mabuchi, J.2
  • 71
    • 0018885271 scopus 로고
    • Vegetative Dictyostelium cells containing 17 actin genes express a single major actin
    • Vandekerckhove, J., and K. Weber. 1980. Vegetative Dictyostelium cells containing 17 actin genes express a single major actin. Nature (Lond.). 284:475-477.
    • (1980) Nature (Lond.) , vol.284 , pp. 475-477
    • Vandekerckhove, J.1    Weber, K.2
  • 73
    • 0015853674 scopus 로고
    • Control of initiation of protein synthesis in human cells: Evidence for a role of uncharged transfer ribonucleic acid
    • Vaughan, M.H., and B.S. Hansen. 1973. Control of initiation of protein synthesis in human cells: evidence for a role of uncharged transfer ribonucleic acid. J. Biol. Chem. 248:7087-7096.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7087-7096
    • Vaughan, M.H.1    Hansen, B.S.2
  • 74
    • 0026632982 scopus 로고
    • Sequence of the tufA gene encoding elongation factor EF-Tu from Thermits aquaticus and over-production of the protein in Escherichia coli
    • Voss, R.H., R.K. Hartmann, C. Lippman, C. Alexander, O. Jahn, and V.A. Erdmann. 1992. Sequence of the tufA gene encoding elongation factor EF-Tu from Thermits aquaticus and over-production 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    Lippman, C.3    Alexander, C.4    Jahn, O.5    Erdmann, V.A.6
  • 75
    • 0019161074 scopus 로고
    • Dual ionic controls for the activation of protein synthesis at fertilization
    • Winkler, M.M., R.A. Steinhardt, J.L. Grainger, and L. Minning. 1980. Dual ionic controls for the activation of protein synthesis at fertilization. Nature (Lond.). 287:558-560.
    • (1980) Nature (Lond.) , vol.287 , pp. 558-560
    • Winkler, M.M.1    Steinhardt, R.A.2    Grainger, J.L.3    Minning, L.4
  • 76
    • 0024342546 scopus 로고
    • Homologies in the structure of G-binding proteins: An analysis based on elongation factor EF-Tu
    • Woolley, P., and B.F.C. Clark. 1989. Homologies in the structure of G-binding proteins: an analysis based on elongation factor EF-Tu. Biotechnology. 7: 913-920.
    • (1989) Biotechnology , vol.7 , pp. 913-920
    • Woolley, P.1    Clark, B.F.C.2
  • 77
    • 0025000290 scopus 로고
    • Identification of an actin-binding protein from Dictyostelium as elongation factor 1α
    • Yang, F., M. Demma, V. Warren, S. Dharmawardhane, and J. Condeelis. 1990. Identification of an actin-binding protein from Dictyostelium as elongation factor 1α. Nature (Lond.). 347:494-496.
    • (1990) Nature (Lond.) , vol.347 , pp. 494-496
    • Yang, F.1    Demma, M.2    Warren, V.3    Dharmawardhane, S.4    Condeelis, J.5
  • 78
    • 0027463634 scopus 로고
    • Purification and characterization of a phosphatidylinositol-4-kinase activator in carrot cells
    • Yang, W., W. Burkhart, J. Cavallius, W.C. Merrick, and W.F. Boss. 1993. Purification and characterization of a phosphatidylinositol-4-kinase activator in carrot cells. J. Biol. Chem. 268:392-398.
    • (1993) J. Biol. Chem. , vol.268 , pp. 392-398
    • Yang, W.1    Burkhart, W.2    Cavallius, J.3    Merrick, W.C.4    Boss, W.F.5
  • 79
    • 0025649192 scopus 로고
    • Differential association of membrane-bound and non-membrane-bound polysomes with the cytoskeleton
    • Zambelli, G., L. Wilming, E.G. Fey, S. Penman, J. Stein, and G. Stein. 1990. Differential association of membrane-bound and non-membrane-bound polysomes with the cytoskeleton. Exp. Cell Res. 191:246-255.
    • (1990) Exp. Cell Res. , vol.191 , pp. 246-255
    • Zambelli, G.1    Wilming, L.2    Fey, E.G.3    Penman, S.4    Stein, J.5    Stein, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.