메뉴 건너뛰기




Volumn 285, Issue 1, 1999, Pages 183-195

Macromolecular assemblage of aminoacyl-tRNA synthetases: Identification of protein-protein interactions and characterization of a core protein

Author keywords

Aminoacyl tRNA synthetase; Core protein; Macromolecular assemblage; Topology; Two hybrid system

Indexed keywords

AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; AMINOACYL TRANSFER RNA; COMPLEMENTARY DNA; CORE PROTEIN; MULTIENZYME COMPLEX; SYNAPTOPHYSIN;

EID: 0033534561     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2316     Document Type: Article
Times cited : (159)

References (54)
  • 1
    • 0031019325 scopus 로고    scopus 로고
    • Aspartyl-tRNA synthetase from rat. In vitro functional analysis of its assembly into the multisynthetase complex
    • Agou F., Mirande M. Aspartyl-tRNA synthetase from rat. In vitro functional analysis of its assembly into the multisynthetase complex. Eur. J. Biochem. 243:1997;259-267.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 259-267
    • Agou, F.1    Mirande, M.2
  • 2
    • 0029966920 scopus 로고    scopus 로고
    • Functional replacement of hamster lysyl-tRNA synthetase by the yeast enzyme requires cognate amino acid sequences for proper tRNA recognition
    • Agou F., Quevillon S., Kerjan P., Latreille M. T., Mirande M. Functional replacement of hamster lysyl-tRNA synthetase by the yeast enzyme requires cognate amino acid sequences for proper tRNA recognition. Biochemistry. 35:1996;15322-15331.
    • (1996) Biochemistry , vol.35 , pp. 15322-15331
    • Agou, F.1    Quevillon, S.2    Kerjan, P.3    Latreille, M.T.4    Mirande, M.5
  • 4
    • 0024840286 scopus 로고
    • Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1
    • Bec G., Kerjan P., Zha X. D., Waller J. P. Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1. J. Biol. Chem. 264:1989;21131-21137.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21131-21137
    • Bec, G.1    Kerjan, P.2    Zha, X.D.3    Waller, J.P.4
  • 5
    • 0028006545 scopus 로고
    • 2-terminal extension of valyl-tRNA synthetase and of the EF-1δ subunit in complex formation
    • 2-terminal extension of valyl-tRNA synthetase and of the EF-1δ subunit in complex formation. J. Biol. Chem. 269:1994;2086-2092.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2086-2092
    • Bec, G.1    Kerjan, P.2    Waller, J.P.3
  • 6
    • 0028783543 scopus 로고
    • Valyl-tRNA synthetase from Artemia. Purification and association with elongation factor
    • Brandsma M., Kerjan P., Dijk J., Janssen G. M. C., Möller W. Valyl-tRNA synthetase from Artemia. Purification and association with elongation factor. Eur. J. Biochem. 233:1995;277-282.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 277-282
    • Brandsma, M.1    Kerjan, P.2    Dijk, J.3    Janssen, G.M.C.4    Möller, W.5
  • 7
    • 0021674214 scopus 로고
    • A bacterial repressor protein or a yeast transcriptional terminator can block upstream activation of a yeast gene
    • Brent R., Ptashne M. A bacterial repressor protein or a yeast transcriptional terminator can block upstream activation of a yeast gene. Nature. 312:1984;612-615.
    • (1984) Nature , vol.312 , pp. 612-615
    • Brent, R.1    Ptashne, M.2
  • 8
    • 0015243237 scopus 로고
    • Modification of E. coli methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin modified enzyme
    • Cassio D., Waller J. P. Modification of E. coli methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin modified enzyme. Eur. J. Biochem. 20:1971;283-300.
    • (1971) Eur. J. Biochem. , vol.20 , pp. 283-300
    • Cassio, D.1    Waller, J.P.2
  • 9
    • 0025996404 scopus 로고
    • A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase
    • Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M. A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 10:1991;4267-4277.
    • (1991) EMBO J. , vol.10 , pp. 4267-4277
    • Cerini, C.1    Kerjan, P.2    Astier, M.3    Gratecos, D.4    Mirande, M.5    Semeriva, M.6
  • 10
    • 0024325490 scopus 로고
    • Blotting of proteins onto immobilon membranes
    • Choli T., Kapp U., Wittmann-Liebold B. Blotting of proteins onto immobilon membranes. J. Chromatog. 476:1989;59-72.
    • (1989) J. Chromatog. , vol.476 , pp. 59-72
    • Choli, T.1    Kapp, U.2    Wittmann-Liebold, B.3
  • 11
    • 0021934231 scopus 로고
    • Leucyl-tRNA and lysyl-tRNA synthetases, derived from the high-Mr complex of sheep liver, are hydrophobic proteins
    • Cirakoglu B., Waller J. P. Leucyl-tRNA and lysyl-tRNA synthetases, derived from the high-Mr complex of sheep liver, are hydrophobic proteins. Eur. J. Biochem. 151:1985;101-110.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 101-110
    • Cirakoglu, B.1    Waller, J.P.2
  • 12
    • 0027674975 scopus 로고
    • The aminoacyl-tRNA synthetase family. Modules at work
    • Delarue M., Moras D. The aminoacyl-tRNA synthetase family. Modules at work. BioEssays. 15:1993;675-687.
    • (1993) BioEssays , vol.15 , pp. 675-687
    • Delarue, M.1    Moras, D.2
  • 13
    • 0029092610 scopus 로고
    • Correlation of two-hybrid affinity data with in vitro measurements
    • Estojak J., Brent R., Golemis E. A. Correlation of two-hybrid affinity data with in vitro measurements. Mol. Cell. Biol. 15:1995;5820-5829.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5820-5829
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3
  • 14
    • 0028264012 scopus 로고
    • Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro
    • Filonenko V. V., Deutscher M. P. Evidence for similar structural organization of the multienzyme aminoacyl-tRNA synthetase complex in vivo and in vitro. J. Biol. Chem. 269:1994;17375-17378.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17375-17378
    • Filonenko, V.V.1    Deutscher, M.P.2
  • 15
    • 0029131892 scopus 로고
    • A novel yeast gene product, G4p1, with a specific affinity for quadruplex nucleic acids
    • Frantz J. D., Gilbert W. A novel yeast gene product, G4p1, with a specific affinity for quadruplex nucleic acids. J. Biol. Chem. 270:1995;20692-20697.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20692-20697
    • Frantz, J.D.1    Gilbert, W.2
  • 16
    • 0027437850 scopus 로고
    • Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2
    • Gyuris J., Golemis E., Chertkov H., Brent R. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell. 75:1993;791-803.
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.2    Chertkov, H.3    Brent, R.4
  • 17
    • 0023132250 scopus 로고
    • Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloning
    • Han J. H., Stratowa C., Rutter W. J. Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloning. Biochemistry. 26:1987;1617-1625.
    • (1987) Biochemistry , vol.26 , pp. 1617-1625
    • Han, J.H.1    Stratowa, C.2    Rutter, W.J.3
  • 18
    • 0025818017 scopus 로고
    • Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase
    • Hsieh S. L., Campbell R. D. Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase. Biochem. J. 278:1991;809-816.
    • (1991) Biochem. J. , vol.278 , pp. 809-816
    • Hsieh, S.L.1    Campbell, R.D.2
  • 19
    • 0019406741 scopus 로고
    • Stoichiometry and composition of an aminoacyl-tRNA synthetase complex from rat liver
    • Johnson D. L., Yang D. C. H. Stoichiometry and composition of an aminoacyl-tRNA synthetase complex from rat liver. Proc. Natl Acad. Sci. USA. 78:1981;4059-4062.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 4059-4062
    • Johnson, D.L.1    Yang, D.C.H.2
  • 20
    • 0019321118 scopus 로고
    • Purification and characterization of lysyl-tRNA synthetase after dissociation of the particulate aminoacyl-tRNA synthetases from rat liver
    • Johnson D. L., Dang C. V., Yang D. C. H. Purification and characterization of lysyl-tRNA synthetase after dissociation of the particulate aminoacyl-tRNA synthetases from rat liver. J. Biol. Chem. 255:1980;4362-4366.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4362-4366
    • Johnson, D.L.1    Dang, C.V.2    Yang, D.C.H.3
  • 21
    • 0027958169 scopus 로고
    • The human EPRS locus (formerly the QARS locus) - A gene encoding a class I and a class II aminoacyl-tRNA synthetase
    • Kaiser E., Hu B., Becher S., Eberhard D., Schray B., Baack M., Hameister H., Knippers R. The human EPRS locus (formerly the QARS locus) - A gene encoding a class I and a class II aminoacyl-tRNA synthetase. Genomics. 19:1994;280-290.
    • (1994) Genomics , vol.19 , pp. 280-290
    • Kaiser, E.1    Hu, B.2    Becher, S.3    Eberhard, D.4    Schray, B.5    Baack, M.6    Hameister, H.7    Knippers, R.8
  • 22
    • 0020491186 scopus 로고
    • Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. I. Species specificity of the polypeptide composition
    • Kellermann O., Tonetti H., Brevet A., Mirande M., Pailliez J. P., Waller J. P. Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. I. Species specificity of the polypeptide composition. J. Biol. Chem. 257:1982;11041-11048.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11041-11048
    • Kellermann, O.1    Tonetti, H.2    Brevet, A.3    Mirande, M.4    Pailliez, J.P.5    Waller, J.P.6
  • 23
    • 0026504411 scopus 로고
    • Mammalian prolyl-tRNA synthetase corresponds to the 150 kDa subunit of the high-Mr aminoacyl-tRNA synthetase complex
    • Kerjan P., Triconnet M., Waller J. P. Mammalian prolyl-tRNA synthetase corresponds to the 150 kDa subunit of the high-Mr aminoacyl-tRNA synthetase complex. Biochimie. 74:1992;195-205.
    • (1992) Biochimie , vol.74 , pp. 195-205
    • Kerjan, P.1    Triconnet, M.2    Waller, J.P.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of Bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0030608370 scopus 로고    scopus 로고
    • Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase
    • Lage H., Dietel M. Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. Gene. 178:1996;187-189.
    • (1996) Gene , vol.178 , pp. 187-189
    • Lage, H.1    Dietel, M.2
  • 26
    • 0027992228 scopus 로고
    • Evolution of the Glx-tRNA synthetase family: The glutaminyl enzyme as a case of horizontal gene transfer
    • Lamour V., Quevillon S., Diriong S., Nguyen V. C., Lipinski M., Mirande M. Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc. Natl Acad. Sci. USA. 91:1994;8670-8674.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8670-8674
    • Lamour, V.1    Quevillon, S.2    Diriong, S.3    Nguyen, V.C.4    Lipinski, M.5    Mirande, M.6
  • 27
    • 0027423060 scopus 로고
    • Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension
    • Lazard M., Mirande M. Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension. Gene. 132:1993;237-245.
    • (1993) Gene , vol.132 , pp. 237-245
    • Lazard, M.1    Mirande, M.2
  • 28
    • 0022001124 scopus 로고
    • Purification and characterization of the isoleucyl-tRNA synthetase component from the high molecular weight complex of sheep liver: A hydrophobic metalloprotein
    • Lazard M., Mirande M., Waller J. P. Purification and characterization of the isoleucyl-tRNA synthetase component from the high molecular weight complex of sheep liver: a hydrophobic metalloprotein. Biochemistry. 24:1985;5099-5106.
    • (1985) Biochemistry , vol.24 , pp. 5099-5106
    • Lazard, M.1    Mirande, M.2    Waller, J.P.3
  • 29
    • 0030464497 scopus 로고    scopus 로고
    • Competitive interaction of component enzymes with the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Kinetic analysis using surface plasmon resonance detection
    • Lessard I. A., Fuller C., Perham R. N. Competitive interaction of component enzymes with the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: kinetic analysis using surface plasmon resonance detection. Biochemistry. 35:1996;16863-16870.
    • (1996) Biochemistry , vol.35 , pp. 16863-16870
    • Lessard, I.A.1    Fuller, C.2    Perham, R.N.3
  • 30
    • 0023649184 scopus 로고
    • A new class of yeast transcriptional activators
    • Ma J., Ptashne M. A new class of yeast transcriptional activators. Cell. 51:1987;113-119.
    • (1987) Cell , vol.51 , pp. 113-119
    • Ma, J.1    Ptashne, M.2
  • 31
    • 0025930249 scopus 로고
    • Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: Structural domains and their implications
    • Mirande M. Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications. Prog. Nucl. Acid Res. Mol. Biol. 40:1991;95-142.
    • (1991) Prog. Nucl. Acid Res. Mol. Biol. , vol.40 , pp. 95-142
    • Mirande, M.1
  • 32
    • 0024531905 scopus 로고
    • Molecular cloning and primary structure of cDNA encoding the catalytic domain of rat liver aspartyl-tRNA synthetase
    • Mirande M., Waller J. P. Molecular cloning and primary structure of cDNA encoding the catalytic domain of rat liver aspartyl-tRNA synthetase. J. Biol. Chem. 264:1989;842-847.
    • (1989) J. Biol. Chem. , vol.264 , pp. 842-847
    • Mirande, M.1    Waller, J.P.2
  • 33
    • 0020341115 scopus 로고
    • Seven mammalian aminoacyl-tRNA synthetases co-purified as high molecular weight entities are associated within the same complex
    • Mirande M., Gache Y., Le Corre D., Waller J. P. Seven mammalian aminoacyl-tRNA synthetases co-purified as high molecular weight entities are associated within the same complex. EMBO J. 1:1982;733-736.
    • (1982) EMBO J. , vol.1 , pp. 733-736
    • Mirande, M.1    Gache, Y.2    Le Corre, D.3    Waller, J.P.4
  • 34
    • 0022033589 scopus 로고
    • A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases
    • Mirande M., Le Corre D., Waller J. P. A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Eur. J. Biochem. 147:1985;281-289.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 281-289
    • Mirande, M.1    Le Corre, D.2    Waller, J.P.3
  • 35
    • 0026058878 scopus 로고
    • Purification and the properties of a high-molecular mass complex between valyl-tRNA synthetase and the heavy form of elongation factor 1 from mammalian cells
    • Motorin Y. A., Wolfson A. D., Lohr D., Orlovsky A. F., Gladilin K. L. Purification and the properties of a high-molecular mass complex between valyl-tRNA synthetase and the heavy form of elongation factor 1 from mammalian cells. Eur. J. Biochem. 201:1991;325-331.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 325-331
    • Motorin, Y.A.1    Wolfson, A.D.2    Lohr, D.3    Orlovsky, A.F.4    Gladilin, K.L.5
  • 36
    • 0029100814 scopus 로고
    • Analysis of the 5′ region of PMS2 reveals heterogeneous transcripts and a novel overlapping gene
    • Nicolaides N. C., Kinzler K. W., Vogelstein B. Analysis of the 5′ region of PMS2 reveals heterogeneous transcripts and a novel overlapping gene. Genomics. 29:1995;329-334.
    • (1995) Genomics , vol.29 , pp. 329-334
    • Nicolaides, N.C.1    Kinzler, K.W.2    Vogelstein, B.3
  • 37
    • 0024419067 scopus 로고
    • Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells
    • Norcum M. T. Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells. J. Biol. Chem. 264:1989;15043-15050.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15043-15050
    • Norcum, M.T.1
  • 38
    • 0025883651 scopus 로고
    • Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex: Effects of neutral salts and detergents
    • Norcum M. T. Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex: effects of neutral salts and detergents. J. Biol. Chem. 266:1991;15398-15405.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15398-15405
    • Norcum, M.T.1
  • 39
    • 0031939704 scopus 로고    scopus 로고
    • Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: A three-domain model based on reversible chemical crosslinking
    • Norcum M. T., Warrington J. A. Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: a three-domain model based on reversible chemical crosslinking. Protein Sci. 7:1998;79-87.
    • (1998) Protein Sci. , vol.7 , pp. 79-87
    • Norcum, M.T.1    Warrington, J.A.2
  • 40
    • 0030583549 scopus 로고    scopus 로고
    • The p18 component of the multisynthetase complex shares a protein motif with the β and γ subunits of eukaryotic elongation factor 1
    • Quevillon S., Mirande M. The p18 component of the multisynthetase complex shares a protein motif with the β and γ subunits of eukaryotic elongation factor 1. FEBS Letters. 395:1996;63-67.
    • (1996) FEBS Letters , vol.395 , pp. 63-67
    • Quevillon, S.1    Mirande, M.2
  • 41
    • 0031464187 scopus 로고    scopus 로고
    • The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine
    • Quevillon S., Agou F., Robinson J. C., Mirande M. The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine. J. Biol. Chem. 272:1997;32573-32579.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32573-32579
    • Quevillon, S.1    Agou, F.2    Robinson, J.C.3    Mirande, M.4
  • 42
    • 0000983324 scopus 로고    scopus 로고
    • Interaction between human tRNA synthetases involves repeated sequence elements
    • Rho S. B., Lee K. H., Kim J. W., Shiba K., Jo Y. J., Kim S. Interaction between human tRNA synthetases involves repeated sequence elements. Proc. Natl Acad. Sci. USA. 93:1996;10128-10133.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10128-10133
    • Rho, S.B.1    Lee, K.H.2    Kim, J.W.3    Shiba, K.4    Jo, Y.J.5    Kim, S.6
  • 43
    • 0000781162 scopus 로고    scopus 로고
    • A multifunctional repeated motif is present in human bifunctional tRNA synthetase
    • Rho S. B., Lee J. S., Jeong E. J., Kim K. S., Kim Y. G., Kim S. A multifunctional repeated motif is present in human bifunctional tRNA synthetase. J. Biol. Chem. 273:1998;11267-11273.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11267-11273
    • Rho, S.B.1    Lee, J.S.2    Jeong, E.J.3    Kim, K.S.4    Kim, Y.G.5    Kim, S.6
  • 44
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70 % accuracy
    • Rost B., Sander C. Prediction of protein secondary structure at better than 70 % accuracy. J. Mol. Biol. 232:1993;584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 47
    • 0026475439 scopus 로고
    • Elongation factor-1 mRNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation
    • Sanders J., Maassen J. A., Möller W. Elongation factor-1 mRNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation. Nucl. Acids Res. 20:1992;5907-5910.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 5907-5910
    • Sanders, J.1    Maassen, J.A.2    Möller, W.3
  • 49
    • 0018369994 scopus 로고
    • Aminoacyl-tRNA synthetases: General features and recognition of transfer RNAs
    • Schimmel P., Söll D. Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Annu. Rev. Biochem. 48:1979;601-648.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 601-648
    • Schimmel, P.1    Söll, D.2
  • 50
    • 0028108750 scopus 로고
    • Human cytoplasmic isoleucyl-tRNA synthetase: Selective divergence of the anticodon-binding domain and acquisition of a new structural unit
    • Shiba K., Suzuki N., Shigesada K., Namba Y., Schimmel P., Noda T. Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit. Proc. Natl Acad. Sci. USA. 91:1994;7435-7439.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7435-7439
    • Shiba, K.1    Suzuki, N.2    Shigesada, K.3    Namba, Y.4    Schimmel, P.5    Noda, T.6
  • 51
    • 0021100143 scopus 로고
    • Perturbation of the aminoacyl-tRNA synthetase complex by salts and detergents: Importance of hydrophobic interactions and possible involvement of lipids
    • Sihag R. K., Deutscher M. P. Perturbation of the aminoacyl-tRNA synthetase complex by salts and detergents: importance of hydrophobic interactions and possible involvement of lipids. J. Biol. Chem. 258:1983;11846-11850.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11846-11850
    • Sihag, R.K.1    Deutscher, M.P.2
  • 52
    • 0031610693 scopus 로고    scopus 로고
    • A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases
    • Simos G., Sauer A., Fasiolo F., Hurt E. C. A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Mol. Cell. 1:1998;235-242.
    • (1998) Mol. Cell , vol.1 , pp. 235-242
    • Simos, G.1    Sauer, A.2    Fasiolo, F.3    Hurt, E.C.4
  • 53
    • 0025805898 scopus 로고
    • Mapping the functional domains of the eukaryotic elongation factor 1βγ
    • van Damme H., Amons R., Janssen G., Möller W. Mapping the functional domains of the eukaryotic elongation factor 1βγ Eur. J. Biochem. 197:1991;505-511.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 505-511
    • Van Damme, H.1    Amons, R.2    Janssen, G.3    Möller, W.4
  • 54
    • 0029687712 scopus 로고    scopus 로고
    • Mammalian aminoacyl-tRNA synthetases
    • Yang D. C. H. Mammalian aminoacyl-tRNA synthetases. Curr. Topics Cell. Reg. 34:1996;101-136.
    • (1996) Curr. Topics Cell. Reg. , vol.34 , pp. 101-136
    • Yang, D.C.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.