메뉴 건너뛰기




Volumn 43, Issue 12, 2013, Pages 1172-1180

Amino acid discrimination by the nuclear encoded mitochondrial arginyl-tRNA synthetase of the larva of a bruchid beetle (Caryedes brasiliensis) from northwestern Costa Rica

Author keywords

Amino acid discrimination; Caryedes brasiliensis; L canavanine; Mitochondrial arginyl tRNA synthetase

Indexed keywords

AMINO ACID; ARGININE TRANSFER RNA LIGASE; CANAVANINE;

EID: 84887131589     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2013.10.004     Document Type: Article
Times cited : (11)

References (57)
  • 1
    • 84868256656 scopus 로고    scopus 로고
    • The absence of A-to-I editing in the anticodon of plant cytoplasmic tRNAArgACG demands a relaxation of the wobble decoding rules
    • Aldinger C.A., Leisinger A.-K., Gaston K.W., Limbach P.A., Igloi G.L. The absence of A-to-I editing in the anticodon of plant cytoplasmic tRNAArgACG demands a relaxation of the wobble decoding rules. RNA Biol. 2012, 9:1239-1246.
    • (2012) RNA Biol. , vol.9 , pp. 1239-1246
    • Aldinger, C.A.1    Leisinger, A.-K.2    Gaston, K.W.3    Limbach, P.A.4    Igloi, G.L.5
  • 2
    • 84866381226 scopus 로고    scopus 로고
    • The influence of identity elements on the aminoacylation of tRNA(Arg) by plant and E.coli arginyl-tRNA synthetases
    • Aldinger C.A., Leisinger A.-K., Igloi G.L. The influence of identity elements on the aminoacylation of tRNA(Arg) by plant and E.coli arginyl-tRNA synthetases. FEBS J. 2012, 279:3622-3638.
    • (2012) FEBS J. , vol.279 , pp. 3622-3638
    • Aldinger, C.A.1    Leisinger, A.-K.2    Igloi, G.L.3
  • 3
    • 0001483397 scopus 로고
    • Purification and substrate specificity of arginyl-ribonucleic acid synthetase from rat liver
    • Allende C.C., Allende J.E. Purification and substrate specificity of arginyl-ribonucleic acid synthetase from rat liver. J.Biol. Chem. 1964, 239:1102-1106.
    • (1964) J.Biol. Chem. , vol.239 , pp. 1102-1106
    • Allende, C.C.1    Allende, J.E.2
  • 4
    • 84871821553 scopus 로고    scopus 로고
    • Proteolytic control of mitochondrial function and morphogenesis
    • Anand R., Langer T., Baker M.J. Proteolytic control of mitochondrial function and morphogenesis. Biochim. Biophys. Acta 2013, 1833:195-204.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 195-204
    • Anand, R.1    Langer, T.2    Baker, M.J.3
  • 5
    • 34848848260 scopus 로고    scopus 로고
    • Small molecules: big players in the evolution of protein synthesis
    • Ataide S.F., Ibba M. Small molecules: big players in the evolution of protein synthesis. ACS Chem. Biol. 2006, 1:285-297.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 285-297
    • Ataide, S.F.1    Ibba, M.2
  • 6
    • 0024190509 scopus 로고
    • Biochemical ecology of canavanine-eating seed predators
    • Bleiler J.A., Rosenthal G.A., Janzen D.H. Biochemical ecology of canavanine-eating seed predators. Ecology 1988, 69:427-433.
    • (1988) Ecology , vol.69 , pp. 427-433
    • Bleiler, J.A.1    Rosenthal, G.A.2    Janzen, D.H.3
  • 10
    • 0034332436 scopus 로고    scopus 로고
    • TRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding
    • Delagoutte B., Moras D., Cavarelli J. tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding. EMBO J. 2000, 19:5599-5610.
    • (2000) EMBO J. , vol.19 , pp. 5599-5610
    • Delagoutte, B.1    Moras, D.2    Cavarelli, J.3
  • 11
    • 84859433793 scopus 로고    scopus 로고
    • Adaptation of aminoacylation identity rules to mammalian mitochondria
    • Fender A., Gaudry A., Jühling F., Sissler M., Florentz C. Adaptation of aminoacylation identity rules to mammalian mitochondria. Biochimie 2012, 94:1090-1097.
    • (2012) Biochimie , vol.94 , pp. 1090-1097
    • Fender, A.1    Gaudry, A.2    Jühling, F.3    Sissler, M.4    Florentz, C.5
  • 12
    • 38649136232 scopus 로고    scopus 로고
    • Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases
    • Francklyn C.S., First E.A., Perona J.J., Hou Y.-M. Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases. Methods 2008, 44:100-118.
    • (2008) Methods , vol.44 , pp. 100-118
    • Francklyn, C.S.1    First, E.A.2    Perona, J.J.3    Hou, Y.-M.4
  • 14
    • 84865713635 scopus 로고    scopus 로고
    • Re-designed N-terminus enhances expression, solubility and crystallizability of mitochondrial protein
    • Gaudry A., Lorber B., Neuenfeldt A., Sauter C., Florentz C., Sissler M. Re-designed N-terminus enhances expression, solubility and crystallizability of mitochondrial protein. Protein Eng. Des. Sel. 2012, 25:473-481.
    • (2012) Protein Eng. Des. Sel. , vol.25 , pp. 473-481
    • Gaudry, A.1    Lorber, B.2    Neuenfeldt, A.3    Sauter, C.4    Florentz, C.5    Sissler, M.6
  • 15
    • 0348224052 scopus 로고    scopus 로고
    • Limited set of amino acid residues in a class Ia aminoacyl-tRNA synthetase is crucial for tRNA binding
    • Geslain R., Bey G., Cavarelli J., Eriani G. Limited set of amino acid residues in a class Ia aminoacyl-tRNA synthetase is crucial for tRNA binding. Biochemistry 2003, 42:15092-15101.
    • (2003) Biochemistry , vol.42 , pp. 15092-15101
    • Geslain, R.1    Bey, G.2    Cavarelli, J.3    Eriani, G.4
  • 16
    • 21244439199 scopus 로고    scopus 로고
    • TRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase
    • Gruic-Sovulj I., Uter N., Bullock T., Perona J.J. tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase. J.Biol. Chem. 2005, 280:23978-23986.
    • (2005) J.Biol. Chem. , vol.280 , pp. 23978-23986
    • Gruic-Sovulj, I.1    Uter, N.2    Bullock, T.3    Perona, J.J.4
  • 17
    • 29244449030 scopus 로고    scopus 로고
    • Determinants in tRNA for activation of arginyl-tRNA synthetase: evidence that tRNA flexibility is required for the induced-fit mechanism
    • Guigou L., Mirande M. Determinants in tRNA for activation of arginyl-tRNA synthetase: evidence that tRNA flexibility is required for the induced-fit mechanism. Biochemistry 2005, 44:16540-16548.
    • (2005) Biochemistry , vol.44 , pp. 16540-16548
    • Guigou, L.1    Mirande, M.2
  • 18
    • 50049131644 scopus 로고    scopus 로고
    • Expression and properties of arginyl-tRNA synthetase from jack bean (Canavalia ensiformis)
    • Hogg J., Schiefermayr E., Schiltz E., Igloi G.L. Expression and properties of arginyl-tRNA synthetase from jack bean (Canavalia ensiformis). Prot. Expr. Purif. 2008, 61:163-167.
    • (2008) Prot. Expr. Purif. , vol.61 , pp. 163-167
    • Hogg, J.1    Schiefermayr, E.2    Schiltz, E.3    Igloi, G.L.4
  • 19
    • 0020792066 scopus 로고
    • Sequences of three transfer RNAs from mosquito mitochondria
    • HsuChen C.C., Cleaves G.R., Dubin D.T. Sequences of three transfer RNAs from mosquito mitochondria. Plasmid 1983, 10:55-65.
    • (1983) Plasmid , vol.10 , pp. 55-65
    • HsuChen, C.C.1    Cleaves, G.R.2    Dubin, D.T.3
  • 20
    • 60349093669 scopus 로고    scopus 로고
    • Amino acid discrimination by arginyl-tRNA synthetases as revealed by an examination of natural specificity variants
    • Igloi G.L., Schiefermayr E. Amino acid discrimination by arginyl-tRNA synthetases as revealed by an examination of natural specificity variants. FEBS J. 2009, 276:1307-1318.
    • (2009) FEBS J. , vol.276 , pp. 1307-1318
    • Igloi, G.L.1    Schiefermayr, E.2
  • 21
    • 0004891261 scopus 로고
    • Escape of juvenile Dioclea megacarpa (Leguminosae) vines from predators in a deciduous tropical forest
    • Janzen D.H. Escape of juvenile Dioclea megacarpa (Leguminosae) vines from predators in a deciduous tropical forest. Am. Nat. 1971, 105:97-112.
    • (1971) Am. Nat. , vol.105 , pp. 97-112
    • Janzen, D.H.1
  • 22
    • 0000371962 scopus 로고
    • When is it coevolution
    • Janzen D.H. When is it coevolution. Evolution (N. Y) 1980, 34:611-612.
    • (1980) Evolution (N. Y) , vol.34 , pp. 611-612
    • Janzen, D.H.1
  • 24
    • 33845944361 scopus 로고    scopus 로고
    • Aviable amino acid editing activity in the leucyl-tRNA synthetase CP1-splicing domain is not required in the yeast mitochondria
    • Karkhanis V.A., Boniecki M.T., Poruri K., Martinis S.A. Aviable amino acid editing activity in the leucyl-tRNA synthetase CP1-splicing domain is not required in the yeast mitochondria. J.Biol. Chem. 2006, 281:33217-33225.
    • (2006) J.Biol. Chem. , vol.281 , pp. 33217-33225
    • Karkhanis, V.A.1    Boniecki, M.T.2    Poruri, K.3    Martinis, S.A.4
  • 25
    • 0026021530 scopus 로고
    • Unilateral aminoacylation specificity between bovine mitochondria and eubacteria
    • Kumazawa Y., Himeno H., Miura K., Watanabe K. Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. J.Biochem. 1991, 109:421-427.
    • (1991) J.Biochem. , vol.109 , pp. 421-427
    • Kumazawa, Y.1    Himeno, H.2    Miura, K.3    Watanabe, K.4
  • 26
    • 6044249065 scopus 로고    scopus 로고
    • Mitochondrial tRNA 3' end metabolism and human disease
    • Levinger L., Mörl M., Florentz C. Mitochondrial tRNA 3' end metabolism and human disease. Nucl. Acids Res. 2004, 32:5430-5441.
    • (2004) Nucl. Acids Res. , vol.32 , pp. 5430-5441
    • Levinger, L.1    Mörl, M.2    Florentz, C.3
  • 27
    • 0032737525 scopus 로고    scopus 로고
    • Asingle base substitution in the variable pocket of yeast tRNA(Arg) eliminates species-specific aminoacylation
    • Liu W., Huang Y., Eriani G., Gangloff J., Wang E., Wang Y. Asingle base substitution in the variable pocket of yeast tRNA(Arg) eliminates species-specific aminoacylation. Biochim. Biophys. Acta 1999, 1473:356-362.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 356-362
    • Liu, W.1    Huang, Y.2    Eriani, G.3    Gangloff, J.4    Wang, E.5    Wang, Y.6
  • 28
    • 14344250347 scopus 로고    scopus 로고
    • An aminoacyl-tRNA synthetase with a defunct editing site
    • Lue S.W., Kelley S.O. An aminoacyl-tRNA synthetase with a defunct editing site. Biochemistry 2005, 44:3010-3016.
    • (2005) Biochemistry , vol.44 , pp. 3010-3016
    • Lue, S.W.1    Kelley, S.O.2
  • 29
    • 34247232561 scopus 로고    scopus 로고
    • Asingle residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation
    • Lue S.W., Kelley S.O. Asingle residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation. Biochemistry 2007, 46:4466-4472.
    • (2007) Biochemistry , vol.46 , pp. 4466-4472
    • Lue, S.W.1    Kelley, S.O.2
  • 30
    • 0014199531 scopus 로고
    • The arginyl transfer ribonucleic acid synthetase of E.coli
    • Mitra S.K., Mehler A.H. The arginyl transfer ribonucleic acid synthetase of E.coli. J.Biol. Chem. 1967, 242:5490-5494.
    • (1967) J.Biol. Chem. , vol.242 , pp. 5490-5494
    • Mitra, S.K.1    Mehler, A.H.2
  • 31
    • 0016156049 scopus 로고
    • Physical and kinetic studies of arginyl transfer ribonucleic acid ligase of Neurospora. A sequential ordered mechanism
    • Nazario M., Evans J.A. Physical and kinetic studies of arginyl transfer ribonucleic acid ligase of Neurospora. A sequential ordered mechanism. J.Biol. Chem. 1974, 249:4934-4936.
    • (1974) J.Biol. Chem. , vol.249 , pp. 4934-4936
    • Nazario, M.1    Evans, J.A.2
  • 32
    • 84868529168 scopus 로고    scopus 로고
    • Structural diversity and protein engineering of the aminoacyl-tRNA synthetases
    • Perona J.J., Hadd A. Structural diversity and protein engineering of the aminoacyl-tRNA synthetases. Biochemistry 2012, 51:8705-8729.
    • (2012) Biochemistry , vol.51 , pp. 8705-8729
    • Perona, J.J.1    Hadd, A.2
  • 33
    • 0027157726 scopus 로고
    • Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase
    • Puglisi J.D., Pütz J., Florentz C., Giegé R. Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase. Nucl. Acids Res. 1993, 21:41-49.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 41-49
    • Puglisi, J.D.1    Pütz, J.2    Florentz, C.3    Giegé, R.4
  • 34
    • 0035859026 scopus 로고    scopus 로고
    • Co-evolution and plant resistance to natural enemies
    • Rausher M.D. Co-evolution and plant resistance to natural enemies. Nature 2001, 411:857-864.
    • (2001) Nature , vol.411 , pp. 857-864
    • Rausher, M.D.1
  • 36
    • 43049116810 scopus 로고    scopus 로고
    • Misincorporation of amino acid analogues into proteins by biosynthesis
    • Rodgers K.J., Shiozawa N. Misincorporation of amino acid analogues into proteins by biosynthesis. Int. J. Biochem. Cell Biol. 2008, 40:1452-1466.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1452-1466
    • Rodgers, K.J.1    Shiozawa, N.2
  • 37
    • 0017615108 scopus 로고
    • Preparation and colorimetric analysis of l-canavanine
    • Rosenthal G. preparation and colorimetric analysis of l-canavanine. Anal. Biochem. 1977, 77:147-151.
    • (1977) Anal. Biochem. , vol.77 , pp. 147-151
    • Rosenthal, G.1
  • 38
    • 0000801562 scopus 로고
    • The biochemical basis for the deleterious effects of L-canavanine
    • Rosenthal G.A. The biochemical basis for the deleterious effects of L-canavanine. Phytochemistry 1991, 30:1055-1058.
    • (1991) Phytochemistry , vol.30 , pp. 1055-1058
    • Rosenthal, G.A.1
  • 39
    • 0023198058 scopus 로고
    • Aberrant, canavanyl protein formation and the ability to tolerate or utilize L-canavanine
    • Rosenthal G.A., Berge M.A., Bleiler J.A., Rudd T.P. Aberrant, canavanyl protein formation and the ability to tolerate or utilize L-canavanine. Experientia 1987, 43:558-561.
    • (1987) Experientia , vol.43 , pp. 558-561
    • Rosenthal, G.A.1    Berge, M.A.2    Bleiler, J.A.3    Rudd, T.P.4
  • 40
    • 0017253755 scopus 로고
    • Anovel means for dealing with L-canavanine, a toxic metabolite
    • Rosenthal G.A., Dahlman D.L., Janzen D.H. Anovel means for dealing with L-canavanine, a toxic metabolite. Science 1976, 192:256-258.
    • (1976) Science , vol.192 , pp. 256-258
    • Rosenthal, G.A.1    Dahlman, D.L.2    Janzen, D.H.3
  • 41
    • 0017397650 scopus 로고
    • Degradation and detoxification of canavanine by a specialized seed predator
    • Rosenthal G.A., Janzen D.H., Dahlman D.L. Degradation and detoxification of canavanine by a specialized seed predator. Science 1977, 196:658-660.
    • (1977) Science , vol.196 , pp. 658-660
    • Rosenthal, G.A.1    Janzen, D.H.2    Dahlman, D.L.3
  • 42
    • 33644677385 scopus 로고    scopus 로고
    • Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase
    • Roy H., Ling J., Alfonzo J.D., Ibba M. Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase. J. Biol. Chem. 2005, 280:38186-38192.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38186-38192
    • Roy, H.1    Ling, J.2    Alfonzo, J.D.3    Ibba, M.4
  • 43
    • 0024477337 scopus 로고
    • Nucleotides in yeast tRNAPhe required for the specific recognition by its cognate synthetase
    • Sampson J.R., DiRenzo A.B., Behlen L.S., Uhlenbeck O.C. Nucleotides in yeast tRNAPhe required for the specific recognition by its cognate synthetase. Science 1989, 243:1363-1366.
    • (1989) Science , vol.243 , pp. 1363-1366
    • Sampson, J.R.1    DiRenzo, A.B.2    Behlen, L.S.3    Uhlenbeck, O.C.4
  • 44
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed invitro
    • Sampson J.R., Uhlenbeck O.C. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed invitro. Proc. Natl. Acad. Sci. USA 1988, 85:1033-1037.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 45
    • 23144460836 scopus 로고    scopus 로고
    • The tRNAscan-SE, snoscan and snoGPS web servers for the detection of tRNAs and snoRNAs
    • Schattner P., Brooks A.N., Lowe T.M. The tRNAscan-SE, snoscan and snoGPS web servers for the detection of tRNAs and snoRNAs. Nucl. Acids Res. 2005, 33:W686-W689.
    • (2005) Nucl. Acids Res. , vol.33
    • Schattner, P.1    Brooks, A.N.2    Lowe, T.M.3
  • 46
    • 0015895306 scopus 로고
    • Amino acid dependent ATP-32PPi exchange measurement. A filter paper disk method
    • Simlot M.M., Pfaender P. Amino acid dependent ATP-32PPi exchange measurement. A filter paper disk method. FEBS Lett. 1973, 35:201-203.
    • (1973) FEBS Lett. , vol.35 , pp. 201-203
    • Simlot, M.M.1    Pfaender, P.2
  • 47
    • 1942469358 scopus 로고    scopus 로고
    • Aminoacylation properties of pathology-related human mitochondrial tRNA(Lys) variants
    • Sissler M., Helm M., Frugier M., Giege R., Florentz C. Aminoacylation properties of pathology-related human mitochondrial tRNA(Lys) variants. RNA 2004, 10:841-853.
    • (2004) RNA , vol.10 , pp. 841-853
    • Sissler, M.1    Helm, M.2    Frugier, M.3    Giege, R.4    Florentz, C.5
  • 48
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: a tool for rapidly screening proteomes for N-terminal targeting sequences
    • Small I., Peeters N., Legeai F., Lurin C. Predotar: a tool for rapidly screening proteomes for N-terminal targeting sequences. Proteomics 2004, 4:1581-1590.
    • (2004) Proteomics , vol.4 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 49
    • 0029941007 scopus 로고    scopus 로고
    • Sequence tags of provirus integration sites in DNAs of tumors induced by the murine retrovirus SL3-3
    • Sørensen A.B., Duch M., Amtoft H.W., Jørgensen P., Pedersen F.S. Sequence tags of provirus integration sites in DNAs of tumors induced by the murine retrovirus SL3-3. J.Virol. 1996, 70:4063-4070.
    • (1996) J.Virol. , vol.70 , pp. 4063-4070
    • Sørensen, A.B.1    Duch, M.2    Amtoft, H.W.3    Jørgensen, P.4    Pedersen, F.S.5
  • 50
    • 84858079447 scopus 로고    scopus 로고
    • Phylogenetically informative rearrangements in mitochondrial genomes of Coleoptera, and monophyly of aquatic elateriform beetles (Dryopoidea)
    • Timmermans M.J.T.N., Vogler A.P. Phylogenetically informative rearrangements in mitochondrial genomes of Coleoptera, and monophyly of aquatic elateriform beetles (Dryopoidea). Mol. Phylogen. Evol. 2012, 63:299-304.
    • (2012) Mol. Phylogen. Evol. , vol.63 , pp. 299-304
    • Timmermans, M.J.T.N.1    Vogler, A.P.2
  • 51
    • 0033230183 scopus 로고    scopus 로고
    • Codon reading patterns in Drosophila melanogaster mitochondria based on their tRNA sequences: a unique wobble rule in animal mitochondria
    • Tomita K., Ueda T., Ishiwa S., Crain P.F., McCloskey J.A., Watanabe K. Codon reading patterns in Drosophila melanogaster mitochondria based on their tRNA sequences: a unique wobble rule in animal mitochondria. Nucl. Acids Res. 1999, 27:4291-4297.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 4291-4297
    • Tomita, K.1    Ueda, T.2    Ishiwa, S.3    Crain, P.F.4    McCloskey, J.A.5    Watanabe, K.6
  • 52
    • 21244444325 scopus 로고    scopus 로고
    • Amino acid-dependent transfer RNA affinity in a class I aminoacyl-tRNA synthetase
    • Uter N.T., Gruic-Sovulj I., Perona J.J. Amino acid-dependent transfer RNA affinity in a class I aminoacyl-tRNA synthetase. J.Biol. Chem. 2005, 280:23966-23977.
    • (2005) J.Biol. Chem. , vol.280 , pp. 23966-23977
    • Uter, N.T.1    Gruic-Sovulj, I.2    Perona, J.J.3
  • 53
    • 79955014697 scopus 로고    scopus 로고
    • Non-protein amino acids: plant, soil and ecosystem interactions
    • Vranova V., Rejsek K., Skene K.R., Formanek P. Non-protein amino acids: plant, soil and ecosystem interactions. Plant Soil 2010, 342:31-48.
    • (2010) Plant Soil , vol.342 , pp. 31-48
    • Vranova, V.1    Rejsek, K.2    Skene, K.R.3    Formanek, P.4
  • 54
    • 77952560288 scopus 로고    scopus 로고
    • Unique features of animal mitochondrial translation systems. The non-universal genetic code, unusual features of the translational apparatus and their relevance to human mitochondrial diseases
    • Watanabe K. Unique features of animal mitochondrial translation systems. The non-universal genetic code, unusual features of the translational apparatus and their relevance to human mitochondrial diseases. Proc. Jap. Acad. B 2010, 86:11-39.
    • (2010) Proc. Jap. Acad. B , vol.86 , pp. 11-39
    • Watanabe, K.1
  • 55
    • 0015039849 scopus 로고
    • Protein and glycoprotein synthesis in rat liver mitochondria and rat intraneural mitochondria and protein synthesis in rat liver microsomes in the presence of L-canavanine
    • Winston R.A., Bosmann H.B. Protein and glycoprotein synthesis in rat liver mitochondria and rat intraneural mitochondria and protein synthesis in rat liver microsomes in the presence of L-canavanine. Chem. Biol. Interact. 1971, 3:131-139.
    • (1971) Chem. Biol. Interact. , vol.3 , pp. 131-139
    • Winston, R.A.1    Bosmann, H.B.2
  • 56
    • 0037197259 scopus 로고    scopus 로고
    • Modulation of tRNAAla identity by inorganic pyrophosphatase
    • Wolfson A.D., Uhlenbeck O.C. Modulation of tRNAAla identity by inorganic pyrophosphatase. Proc. Natl. Acad. Sci. U S A 2002, 99:5965-5970.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 5965-5970
    • Wolfson, A.D.1    Uhlenbeck, O.C.2
  • 57
    • 84855892823 scopus 로고    scopus 로고
    • Quality control in aminoacyl-tRNA synthesis Its role in translational fidelity
    • Yadavalli S.S., Ibba M. Quality control in aminoacyl-tRNA synthesis Its role in translational fidelity. Adv. Prot. Chem. 2012, 86C:1-43.
    • (2012) Adv. Prot. Chem. , vol.86 C , pp. 1-43
    • Yadavalli, S.S.1    Ibba, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.