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Volumn 5, Issue 4, 2014, Pages 461-480

tRNA synthetase: TRNA aminoacylation and beyond

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; GLYCINE TRANSFER RNA LIGASE; TRANSFER RNA;

EID: 84902546406     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.1224     Document Type: Article
Times cited : (124)

References (248)
  • 1
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giegé R, Sissler M, Florentz C. Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res 1998, 26:5017-5035.
    • (1998) Nucleic Acids Res , vol.26 , pp. 5017-5035
    • Giegé, R.1    Sissler, M.2    Florentz, C.3
  • 2
    • 42349103482 scopus 로고    scopus 로고
    • Fidelity mechanisms of the aminoacyl-tRNA synthetases
    • In: RajBhandary UL, Köhrer C, eds. New York: Springer-Verlag
    • Mascarenhas AP, An S, Rosen AE, Martinis SA, Musier-Forsyth K. Fidelity mechanisms of the aminoacyl-tRNA synthetases. In: RajBhandary UL, Köhrer C, eds. Protein Engineering. New York: Springer-Verlag; 2008, 155-193.
    • (2008) Protein Engineering , pp. 155-193
    • Mascarenhas, A.P.1    An, S.2    Rosen, A.E.3    Martinis, S.A.4    Musier-Forsyth, K.5
  • 3
    • 71549128376 scopus 로고    scopus 로고
    • Functional expansion of human tRNA synthetases achieved by structural inventions
    • Guo M, Schimmel P, Yang XL. Functional expansion of human tRNA synthetases achieved by structural inventions. FEBS Lett 2010, 584:434-442.
    • (2010) FEBS Lett , vol.584 , pp. 434-442
    • Guo, M.1    Schimmel, P.2    Yang, X.L.3
  • 4
    • 79960522405 scopus 로고    scopus 로고
    • Chemistry of aminoacyl-tRNA synthetases
    • In: Begley TP, eds. New York: John Wiley & Sons;
    • Nawaz M, Martinis SA. Chemistry of aminoacyl-tRNA synthetases. In: Begley TP, eds. Encyclopedia of Chemical Biology. New York: John Wiley & Sons; 2009, 52-63.
    • (2009) Encyclopedia of Chemical Biology , pp. 52-63
    • Nawaz, M.1    Martinis, S.A.2
  • 5
    • 0343618479 scopus 로고    scopus 로고
    • Footprints of aminoacyl-tRNA synthetases are everywhere
    • Schimmel P, Ribas De Pouplana L. Footprints of aminoacyl-tRNA synthetases are everywhere. Trends Biochem Sci 2000, 25:207-209.
    • (2000) Trends Biochem Sci , vol.25 , pp. 207-209
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 6
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-tRNA synthetases beyond translation
    • Guo M, Yang XL, Schimmel P. New functions of aminoacyl-tRNA synthetases beyond translation. Nat Rev Mol Cell Biol 2010, 11:668-674.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 668-674
    • Guo, M.1    Yang, X.L.2    Schimmel, P.3
  • 7
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5Å
    • Cusack S, Berthet-Colominas C, Härtlein M, Nassar N, Leberman R. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5Å. Nature 1990, 347:249-255.
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Härtlein, M.3    Nassar, N.4    Leberman, R.5
  • 8
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 1990, 347:203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 9
    • 0035951403 scopus 로고    scopus 로고
    • Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem
    • Ribas de Pouplana L, Schimmel P. Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem. Cell 2001, 104:191-193.
    • (2001) Cell , vol.104 , pp. 191-193
    • Ribas de Pouplana, L.1    Schimmel, P.2
  • 10
    • 0026032475 scopus 로고
    • Assembly of a class I tRNA synthetase from products of an artificially split gene
    • Burbaum JJ, Schimmel P. Assembly of a class I tRNA synthetase from products of an artificially split gene. Biochemistry 1991, 30:319-324.
    • (1991) Biochemistry , vol.30 , pp. 319-324
    • Burbaum, J.J.1    Schimmel, P.2
  • 11
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack S. Eleven down and nine to go. Nat Struct Biol 1995, 2:824-831.
    • (1995) Nat Struct Biol , vol.2 , pp. 824-831
    • Cusack, S.1
  • 13
    • 0026591001 scopus 로고
    • Structural and functional relationships between aminoacyl-tRNA synthetases
    • Moras D. Structural and functional relationships between aminoacyl-tRNA synthetases. Trends Biochem Sci 1992, 17:159-164.
    • (1992) Trends Biochem Sci , vol.17 , pp. 159-164
    • Moras, D.1
  • 15
    • 0017121672 scopus 로고
    • The crystal structure of tyrosyl-transfer RNA synthetase at 2.7Å resolution
    • Irwin MJ, Nyborg J, Reid BR, Blow DM. The crystal structure of tyrosyl-transfer RNA synthetase at 2.7Å resolution. J Mol Biol 1976, 105:577-586.
    • (1976) J Mol Biol , vol.105 , pp. 577-586
    • Irwin, M.J.1    Nyborg, J.2    Reid, B.R.3    Blow, D.M.4
  • 16
    • 0024406896 scopus 로고
    • Structure of tyrosyl-tRNA synthetase refined at 2.3Å resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate
    • Brick P, Bhat TN, Blow DM. Structure of tyrosyl-tRNA synthetase refined at 2.3Å resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate. J Mol Biol 1989, 208:83-98.
    • (1989) J Mol Biol , vol.208 , pp. 83-98
    • Brick, P.1    Bhat, T.N.2    Blow, D.M.3
  • 17
    • 0024392753 scopus 로고
    • Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 Å resolution
    • Rould MA, Perona JJ, Soll D, Steitz TA. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 Å resolution. Science 1989, 246:1135-1142.
    • (1989) Science , vol.246 , pp. 1135-1142
    • Rould, M.A.1    Perona, J.J.2    Soll, D.3    Steitz, T.A.4
  • 18
    • 0028172539 scopus 로고
    • Methionyl-tRNA synthetase needs an intact and mobile 332KMSKS336 motif in catalysis of methionyl adenylate formation
    • Schmitt E, Meinnel T, Blanquet S, Mechulam Y. Methionyl-tRNA synthetase needs an intact and mobile 332KMSKS336 motif in catalysis of methionyl adenylate formation. J Mol Biol 1994, 242:566-576.
    • (1994) J Mol Biol , vol.242 , pp. 566-576
    • Schmitt, E.1    Meinnel, T.2    Blanquet, S.3    Mechulam, Y.4
  • 19
    • 0021746195 scopus 로고
    • Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase
    • Webster T, Tsai H, Kula M, Mackie GA, Schimmel P. Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase. Science 1984, 226:1315-1317.
    • (1984) Science , vol.226 , pp. 1315-1317
    • Webster, T.1    Tsai, H.2    Kula, M.3    Mackie, G.A.4    Schimmel, P.5
  • 21
    • 0033548581 scopus 로고    scopus 로고
    • Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine
    • Arnez JG, Dock-Bregeon AC, Moras D. Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine. J Mol Biol 1999, 286:1449-1459.
    • (1999) J Mol Biol , vol.286 , pp. 1449-1459
    • Arnez, J.G.1    Dock-Bregeon, A.C.2    Moras, D.3
  • 22
    • 0027165755 scopus 로고
    • Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase
    • Perona JJ, Rould MA, Steitz TA. Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Biochemistry 1993, 32:8758-8771.
    • (1993) Biochemistry , vol.32 , pp. 8758-8771
    • Perona, J.J.1    Rould, M.A.2    Steitz, T.A.3
  • 23
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • Arnez JG, Moras D. Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 1997, 22:211-216.
    • (1997) Trends Biochem Sci , vol.22 , pp. 211-216
    • Arnez, J.G.1    Moras, D.2
  • 24
    • 0023868490 scopus 로고
    • Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism
    • Fersht AR, Knill-Jones JW, Bedouelle H, Winter G. Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism. Biochemistry 1988, 27:1581-1587.
    • (1988) Biochemistry , vol.27 , pp. 1581-1587
    • Fersht, A.R.1    Knill-Jones, J.W.2    Bedouelle, H.3    Winter, G.4
  • 25
    • 0028902065 scopus 로고
    • Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles
    • First EA, Fersht AR. Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles. Biochemistry 1995, 34:5030-5043.
    • (1995) Biochemistry , vol.34 , pp. 5030-5043
    • First, E.A.1    Fersht, A.R.2
  • 26
    • 0033622155 scopus 로고    scopus 로고
    • 2.9Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site
    • Ilyin VA, Temple B, Hu M, Li G, Yin Y, Vachette P, Carter CW Jr. 2.9Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site. Protein Sci 2000, 9:218-231.
    • (2000) Protein Sci , vol.9 , pp. 218-231
    • Ilyin, V.A.1    Temple, B.2    Hu, M.3    Li, G.4    Yin, Y.5    Vachette, P.6    Carter Jr, C.W.7
  • 27
    • 0035861676 scopus 로고    scopus 로고
    • Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase
    • Nakama T, Nureki O, Yokoyama S. Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase. J Biol Chem 2001, 276:47387-47393.
    • (2001) J Biol Chem , vol.276 , pp. 47387-47393
    • Nakama, T.1    Nureki, O.2    Yokoyama, S.3
  • 28
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann MG, Moras D, Olsen KW. Chemical and biological evolution of nucleotide-binding protein. Nature 1974, 250:194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 29
    • 0029127816 scopus 로고
    • Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate
    • Arnez JG, Harris DC, Mitschler A, Rees B, Francklyn CS, Moras D. Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. EMBO J 1995, 14:4143-4155.
    • (1995) EMBO J , vol.14 , pp. 4143-4155
    • Arnez, J.G.1    Harris, D.C.2    Mitschler, A.3    Rees, B.4    Francklyn, C.S.5    Moras, D.6
  • 34
    • 0023110653 scopus 로고
    • Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine
    • Brick P, Blow DM. Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine. J Mol Biol 1987, 194:287-297.
    • (1987) J Mol Biol , vol.194 , pp. 287-297
    • Brick, P.1    Blow, D.M.2
  • 36
    • 0016744245 scopus 로고
    • Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine
    • Sprinzl M, Cramer F. Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine. Proc Natl Acad Sci U S A 1975, 72:3049-3053.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 3049-3053
    • Sprinzl, M.1    Cramer, F.2
  • 37
    • 0023202876 scopus 로고
    • Evidence for dispensable sequences inserted into a nucleotide fold
    • Starzyk RM, Webster TA, Schimmel P. Evidence for dispensable sequences inserted into a nucleotide fold. Science 1987, 237:1614-1618.
    • (1987) Science , vol.237 , pp. 1614-1618
    • Starzyk, R.M.1    Webster, T.A.2    Schimmel, P.3
  • 38
    • 34249687080 scopus 로고    scopus 로고
    • Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity
    • Betha AK, Williams AM, Martinis SA. Isolated CP1 domain of Escherichia coli leucyl-tRNA synthetase is dependent on flanking hinge motifs for amino acid editing activity. Biochemistry 2007, 46:6258-6267.
    • (2007) Biochemistry , vol.46 , pp. 6258-6267
    • Betha, A.K.1    Williams, A.M.2    Martinis, S.A.3
  • 39
    • 0029854940 scopus 로고    scopus 로고
    • Aminoacylation error correction
    • Lin L, Hale SP, Schimmel P. Aminoacylation error correction. Nature 1996, 384:33-34.
    • (1996) Nature , vol.384 , pp. 33-34
    • Lin, L.1    Hale, S.P.2    Schimmel, P.3
  • 40
    • 0034254919 scopus 로고    scopus 로고
    • Hydrolytic editing by a class II aminoacyl-tRNA synthetase
    • Beuning PJ, Musier-Forsyth K. Hydrolytic editing by a class II aminoacyl-tRNA synthetase. Proc Natl Acad Sci U S A 2000, 97:8916-8920.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8916-8920
    • Beuning, P.J.1    Musier-Forsyth, K.2
  • 41
    • 0037018949 scopus 로고    scopus 로고
    • Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing
    • Wong FC, Beuning PJ, Nagan M, Shiba K, Musier-Forsyth K. Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing. Biochemistry 2002, 41:7108-7115.
    • (2002) Biochemistry , vol.41 , pp. 7108-7115
    • Wong, F.C.1    Beuning, P.J.2    Nagan, M.3    Shiba, K.4    Musier-Forsyth, K.5
  • 42
    • 0347993060 scopus 로고    scopus 로고
    • An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing
    • Wong FC, Beuning PJ, Silvers C, Musier-Forsyth K. An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing. J Biol Chem 2003, 278:52857-52864.
    • (2003) J Biol Chem , vol.278 , pp. 52857-52864
    • Wong, F.C.1    Beuning, P.J.2    Silvers, C.3    Musier-Forsyth, K.4
  • 48
    • 0023700973 scopus 로고
    • Evidence for interaction of an aminoacyl transfer RNA synthetase with a region important for the identity of its cognate transfer RNA
    • Park SJ, Schimmel P. Evidence for interaction of an aminoacyl transfer RNA synthetase with a region important for the identity of its cognate transfer RNA. J Biol Chem 1988, 263:16527-16530.
    • (1988) J Biol Chem , vol.263 , pp. 16527-16530
    • Park, S.J.1    Schimmel, P.2
  • 49
    • 38349090724 scopus 로고    scopus 로고
    • A flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases
    • Hsu JL, Martinis SA. A flexible peptide tether controls accessibility of a unique C-terminal RNA-binding domain in leucyl-tRNA synthetases. J Mol Biol 2008, 376:482-491.
    • (2008) J Mol Biol , vol.376 , pp. 482-491
    • Hsu, J.L.1    Martinis, S.A.2
  • 52
    • 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 U S A 1994, 91:7435-7439.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7435-7439
    • Shiba, K.1    Suzuki, N.2    Shigesada, K.3    Namba, Y.4    Schimmel, P.5    Noda, T.6
  • 53
    • 0023669147 scopus 로고
    • A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof
    • Akins RA, Lambowitz AM. A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof. Cell 1987, 50:331-345.
    • (1987) Cell , vol.50 , pp. 331-345
    • Akins, R.A.1    Lambowitz, A.M.2
  • 54
    • 0024989581 scopus 로고
    • Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases
    • Cherniack AD, Garriga G, Kittle JD Jr, Akins RA, Lambowitz AM. Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases. Cell 1990, 62:745-755.
    • (1990) Cell , vol.62 , pp. 745-755
    • Cherniack, A.D.1    Garriga, G.2    Kittle Jr, J.D.3    Akins, R.A.4    Lambowitz, A.M.5
  • 55
    • 0035896040 scopus 로고    scopus 로고
    • Function of the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase in RNA splicing. Role of the idiosyncratic N-terminal extension and different modes of interaction with different group I introns
    • Mohr G, Rennard R, Cherniack AD, Stryker J, Lambowitz AM. Function of the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase in RNA splicing. Role of the idiosyncratic N-terminal extension and different modes of interaction with different group I introns. J Mol Biol 2001, 307:75-92.
    • (2001) J Mol Biol , vol.307 , pp. 75-92
    • Mohr, G.1    Rennard, R.2    Cherniack, A.D.3    Stryker, J.4    Lambowitz, A.M.5
  • 56
    • 13244292332 scopus 로고    scopus 로고
    • A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface
    • Paukstelis PJ, Coon R, Madabusi L, Nowakowski J, Monzingo A, Robertus J, Lambowitz AM. A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface. Mol Cell 2005, 17:417-428.
    • (2005) Mol Cell , vol.17 , pp. 417-428
    • Paukstelis, P.J.1    Coon, R.2    Madabusi, L.3    Nowakowski, J.4    Monzingo, A.5    Robertus, J.6    Lambowitz, A.M.7
  • 57
    • 38049086319 scopus 로고    scopus 로고
    • Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA
    • Paukstelis PJ, Chen JH, Chase E, Lambowitz AM, Golden BL. Structure of a tyrosyl-tRNA synthetase splicing factor bound to a group I intron RNA. Nature 2008, 451:94-97.
    • (2008) Nature , vol.451 , pp. 94-97
    • Paukstelis, P.J.1    Chen, J.H.2    Chase, E.3    Lambowitz, A.M.4    Golden, B.L.5
  • 58
    • 0033551781 scopus 로고    scopus 로고
    • Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase
    • Wakasugi K, Schimmel P. Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. J Biol Chem 1999, 274:23155-23159.
    • (1999) J Biol Chem , vol.274 , pp. 23155-23159
    • Wakasugi, K.1    Schimmel, P.2
  • 59
    • 0033515887 scopus 로고    scopus 로고
    • Two distinct cytokines released from a human aminoacyl-tRNA synthetase
    • Wakasugi K, Schimmel P. Two distinct cytokines released from a human aminoacyl-tRNA synthetase. Science 1999, 284:147-151.
    • (1999) Science , vol.284 , pp. 147-151
    • Wakasugi, K.1    Schimmel, P.2
  • 60
    • 0030945598 scopus 로고    scopus 로고
    • Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine
    • Kleeman TA, Wei D, Simpson KL, First EA. Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. J Biol Chem 1997, 272:14420-14425.
    • (1997) J Biol Chem , vol.272 , pp. 14420-14425
    • Kleeman, T.A.1    Wei, D.2    Simpson, K.L.3    First, E.A.4
  • 62
    • 0026781869 scopus 로고
    • Endothelial monocyte-activating polypeptide II. A novel tumor-derived polypeptide that activates host-response mechanisms
    • Kao J, Ryan J, Brett G, Chen J, Shen H, Fan YG, Godman G, Familletti PC, Wang F, Pan Y-C, et al. Endothelial monocyte-activating polypeptide II. A novel tumor-derived polypeptide that activates host-response mechanisms. J Biol Chem 1992, 267:20239-20247.
    • (1992) J Biol Chem , vol.267 , pp. 20239-20247
    • Kao, J.1    Ryan, J.2    Brett, G.3    Chen, J.4    Shen, H.5    Fan, Y.G.6    Godman, G.7    Familletti, P.C.8    Wang, F.9    Pan, Y.-C.10
  • 63
    • 0028006545 scopus 로고
    • Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor (EF) 1 β γ δ complex. Essential roles of the NH2-terminal extension of valyl-tRNA synthetase and of the EF-1 δ subunit in complex formation
    • Bec G, Kerjan P, Waller JP. Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor (EF) 1 β γ δ complex. Essential roles of the NH2-terminal extension of valyl-tRNA synthetase and of the EF-1 δ subunit in complex formation. J Biol Chem 1994, 269:2086-2092.
    • (1994) J Biol Chem , vol.269 , pp. 2086-2092
    • Bec, G.1    Kerjan, P.2    Waller, J.P.3
  • 64
    • 27544439561 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the δ subunit
    • Jiang S, Wolfe CL, Warrington JA, Norcum MT. Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the δ subunit. FEBS Lett 2005, 579:6049-6054.
    • (2005) FEBS Lett , vol.579 , pp. 6049-6054
    • Jiang, S.1    Wolfe, C.L.2    Warrington, J.A.3    Norcum, M.T.4
  • 65
    • 0034255114 scopus 로고    scopus 로고
    • An elongation factor-associating domain is inserted into human cysteinyl-tRNA synthetase by alternative splicing
    • Kim JE, Kim KH, Lee SW, Seol W, Shiba K, Kim S. An elongation factor-associating domain is inserted into human cysteinyl-tRNA synthetase by alternative splicing. Nucleic Acids Res 2000, 28:2866-2872.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2866-2872
    • Kim, J.E.1    Kim, K.H.2    Lee, S.W.3    Seol, W.4    Shiba, K.5    Kim, S.6
  • 66
    • 46649105125 scopus 로고    scopus 로고
    • Determination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM
    • Kim KJ, Park MC, Choi SJ, Oh YS, Choi EC, Cho HJ, Kim MH, Kim SH, Kim DW, Kim S, et al. Determination of three-dimensional structure and residues of the novel tumor suppressor AIMP3/p18 required for the interaction with ATM. J Biol Chem 2008, 283:14032-14040.
    • (2008) J Biol Chem , vol.283 , pp. 14032-14040
    • Kim, K.J.1    Park, M.C.2    Choi, S.J.3    Oh, Y.S.4    Choi, E.C.5    Cho, H.J.6    Kim, M.H.7    Kim, S.H.8    Kim, D.W.9    Kim, S.10
  • 67
    • 0033582434 scopus 로고    scopus 로고
    • Functional interaction of mammalian valyl-tRNA synthetase with elongation factor EF-1α in the complex with EF-1H
    • Negrutskii BS, Shalak VF, Kerjan P, El'skaya AV, Mirande M. Functional interaction of mammalian valyl-tRNA synthetase with elongation factor EF-1α in the complex with EF-1H. J Biol Chem 1999, 274:4545-4550.
    • (1999) J Biol Chem , vol.274 , pp. 4545-4550
    • Negrutskii, B.S.1    Shalak, V.F.2    Kerjan, P.3    El'skaya, A.V.4    Mirande, M.5
  • 68
    • 0033534561 scopus 로고    scopus 로고
    • Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein
    • Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M. Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. J Mol Biol 1999, 285:183-195.
    • (1999) J Mol Biol , vol.285 , pp. 183-195
    • Quevillon, S.1    Robinson, J.C.2    Berthonneau, E.3    Siatecka, M.4    Mirande, M.5
  • 69
    • 33748568146 scopus 로고    scopus 로고
    • Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes
    • Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D. Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes. Nucleic Acids Res 2006, 34:3968-3979.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3968-3979
    • Simader, H.1    Hothorn, M.2    Kohler, C.3    Basquin, J.4    Simos, G.5    Suck, D.6
  • 70
    • 0034141480 scopus 로고    scopus 로고
    • A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases
    • Cahuzac B, Berthonneau E, Birlirakis N, Guittet E, Mirande M. A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases. EMBO J 2000, 19:445-452.
    • (2000) EMBO J , vol.19 , pp. 445-452
    • Cahuzac, B.1    Berthonneau, E.2    Birlirakis, N.3    Guittet, E.4    Mirande, M.5
  • 71
    • 0031049460 scopus 로고    scopus 로고
    • Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex
    • Cerini C, Semeriva M, Gratecos D. Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex. Eur J Biochem 1997, 244:176-185.
    • (1997) Eur J Biochem , vol.244 , pp. 176-185
    • Cerini, C.1    Semeriva, M.2    Gratecos, D.3
  • 73
    • 40849118528 scopus 로고    scopus 로고
    • WHEP domains direct noncanonical function of glutamyl-prolyl tRNA synthetase in translational control of gene expression
    • Jia J, Arif A, Ray PS, Fox PL. WHEP domains direct noncanonical function of glutamyl-prolyl tRNA synthetase in translational control of gene expression. Mol Cell 2008, 29:679-690.
    • (2008) Mol Cell , vol.29 , pp. 679-690
    • Jia, J.1    Arif, A.2    Ray, P.S.3    Fox, P.L.4
  • 74
    • 0026504411 scopus 로고
    • Mammalian prolyl-tRNA synthetase corresponds to the approximately 150kDa subunit of the high-M(r) aminoacyl-tRNA synthetase complex
    • Kerjan P, Triconnet M, Waller JP. Mammalian prolyl-tRNA synthetase corresponds to the approximately 150kDa subunit of the high-M(r) aminoacyl-tRNA synthetase complex. Biochimie 1992, 74:195-205.
    • (1992) Biochimie , vol.74 , pp. 195-205
    • Kerjan, P.1    Triconnet, M.2    Waller, J.P.3
  • 76
    • 0000781162 scopus 로고    scopus 로고
    • A multifunctional repeated motif is present in human bifunctional tRNA synthetase
    • Rho SB, Lee JS, Jeong EJ, Kim KS, Kim YG, Kim S. A multifunctional repeated motif is present in human bifunctional tRNA synthetase. J Biol Chem 1998, 273:11267-11273.
    • (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
  • 77
    • 0346103681 scopus 로고    scopus 로고
    • Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains
    • Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L. Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. Proc Natl Acad Sci U S A 2003, 100:15376-15380.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 15376-15380
    • Yang, X.L.1    Otero, F.J.2    Skene, R.J.3    McRee, D.E.4    Schimmel, P.5    Ribas de Pouplana, L.6
  • 78
    • 0034671820 scopus 로고    scopus 로고
    • A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation
    • Kaminska M, Deniziak M, Kerjan P, Barciszewski J, Mirande M. A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation. EMBO J 2000, 19:6908-6917.
    • (2000) EMBO J , vol.19 , pp. 6908-6917
    • Kaminska, M.1    Deniziak, M.2    Kerjan, P.3    Barciszewski, J.4    Mirande, M.5
  • 79
    • 0034282428 scopus 로고    scopus 로고
    • A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases
    • Kim Y, Shin J, Li R, Cheong C, Kim K, Kim S. A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases. J Biol Chem 2000, 275:27062-27068.
    • (2000) J Biol Chem , vol.275 , pp. 27062-27068
    • Kim, Y.1    Shin, J.2    Li, R.3    Cheong, C.4    Kim, K.5    Kim, S.6
  • 80
    • 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 JC, 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 1997, 272:32573-32579.
    • (1997) J Biol Chem , vol.272 , pp. 32573-32579
    • Quevillon, S.1    Agou, F.2    Robinson, J.C.3    Mirande, M.4
  • 82
    • 0034671360 scopus 로고    scopus 로고
    • Macromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly
    • Robinson JC, Kerjan P, Mirande M. Macromolecular assemblage of aminoacyl-tRNA synthetases: quantitative analysis of protein-protein interactions and mechanism of complex assembly. J Mol Biol 2000, 304:983-994.
    • (2000) J Mol Biol , vol.304 , pp. 983-994
    • Robinson, J.C.1    Kerjan, P.2    Mirande, M.3
  • 83
    • 29244468267 scopus 로고    scopus 로고
    • Coiled-coil protein composition of 22 proteomes-differences and common themes in subcellular infrastructure and traffic control
    • Rose A, Schraegle SJ, Stahlberg EA, Meier I. Coiled-coil protein composition of 22 proteomes-differences and common themes in subcellular infrastructure and traffic control. BMC Evol Biol 2005, 5:66.
    • (2005) BMC Evol Biol , vol.5 , pp. 66
    • Rose, A.1    Schraegle, S.J.2    Stahlberg, E.A.3    Meier, I.4
  • 84
    • 0021858690 scopus 로고
    • Comparison of the complexed and free forms of rat liver arginyl-tRNA synthetase and origin of the free form
    • Vellekamp G, Sihag RK, Deutscher MP. Comparison of the complexed and free forms of rat liver arginyl-tRNA synthetase and origin of the free form. J Biol Chem 1985, 260:9843-9847.
    • (1985) J Biol Chem , vol.260 , pp. 9843-9847
    • Vellekamp, G.1    Sihag, R.K.2    Deutscher, M.P.3
  • 85
    • 31544478796 scopus 로고    scopus 로고
    • Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two translation initiations by a single mRNA
    • Zheng YG, Wei H, Ling C, Xu MG, Wang ED. Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two translation initiations by a single mRNA. Biochemistry 2006, 45:1338-1344.
    • (2006) Biochemistry , vol.45 , pp. 1338-1344
    • Zheng, Y.G.1    Wei, H.2    Ling, C.3    Xu, M.G.4    Wang, E.D.5
  • 86
    • 0013824051 scopus 로고
    • On the evolution of the genetic code
    • Woese CR. On the evolution of the genetic code. Proc Natl Acad Sci U S A 1965, 54:1546-1552.
    • (1965) Proc Natl Acad Sci U S A , vol.54 , pp. 1546-1552
    • Woese, C.R.1
  • 87
    • 0037173066 scopus 로고    scopus 로고
    • On the evolution of cells
    • Woese CR. On the evolution of cells. Proc Natl Acad Sci U S A 2002, 99:8742-8747.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 8742-8747
    • Woese, C.R.1
  • 88
    • 33845944361 scopus 로고    scopus 로고
    • A viable amino acid editing activity in the leucyl-tRNA synthetase CP1-splicing domain is not required in the yeast mitochondria
    • Karkhanis VA, Boniecki MT, Poruri K, Martinis SA. A viable 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
  • 89
    • 36749054592 scopus 로고    scopus 로고
    • Amino acid toxicities of Escherichia coli that are prevented by leucyl-tRNA synthetase amino acid editing
    • Karkhanis VA, Mascarenhas AP, Martinis SA. Amino acid toxicities of Escherichia coli that are prevented by leucyl-tRNA synthetase amino acid editing. J Bacteriol 2007, 189:8765-8768.
    • (2007) J Bacteriol , vol.189 , pp. 8765-8768
    • Karkhanis, V.A.1    Mascarenhas, A.P.2    Martinis, S.A.3
  • 91
    • 33749669848 scopus 로고    scopus 로고
    • Global effects of mistranslation from an editing defect in mammalian cells
    • Nangle LA, Motta CM, Schimmel P. Global effects of mistranslation from an editing defect in mammalian cells. Chem Biol 2006, 13:1091-1100.
    • (2006) Chem Biol , vol.13 , pp. 1091-1100
    • Nangle, L.A.1    Motta, C.M.2    Schimmel, P.3
  • 92
    • 7444241391 scopus 로고    scopus 로고
    • Regulation of RNA function by aminoacylation and editing?
    • Geslain R, Ribas de Pouplana L. Regulation of RNA function by aminoacylation and editing? Trends Genet 2004, 20:604-610.
    • (2004) Trends Genet , vol.20 , pp. 604-610
    • Geslain, R.1    Ribas de Pouplana, L.2
  • 93
    • 2342431929 scopus 로고    scopus 로고
    • Transfer RNA-dependent amino acid discrimination by aminoacyl-tRNA synthetases
    • In: Lapointe J, Brakier-Gingras L, eds. Georgetown, TX: Landes Bioscience;
    • Hendrickson TL, Schimmel P. Transfer RNA-dependent amino acid discrimination by aminoacyl-tRNA synthetases. In: Lapointe J, Brakier-Gingras L, eds. Translation Mechanisms. Georgetown, TX: Landes Bioscience; 2002, 34-64.
    • (2002) Translation Mechanisms , pp. 34-64
    • Hendrickson, T.L.1    Schimmel, P.2
  • 94
    • 0002085978 scopus 로고
    • The probability of errors in the process of synthesis of protein molecules
    • In: Birkhauser A, eds. Basel: Birkhauser Verlag
    • Pauling L. The probability of errors in the process of synthesis of protein molecules. In: Birkhauser A, eds. Festschrift Authur Stöll Siebzigsten Geburtstag. Basel: Birkhauser Verlag; 1958, 597-602.
    • (1958) Festschrift Authur Stöll Siebzigsten Geburtstag , pp. 597-602
    • Pauling, L.1
  • 95
    • 0002435406 scopus 로고
    • The frequency of errors in protein biosynthesis
    • Loftfield RB. The frequency of errors in protein biosynthesis. Biochem J 1963, 89:82-92.
    • (1963) Biochem J , vol.89 , pp. 82-92
    • Loftfield, R.B.1
  • 96
    • 0014027087 scopus 로고
    • Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase
    • Baldwin AN, Berg P. Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase. J Biol Chem 1966, 241:839-845.
    • (1966) J Biol Chem , vol.241 , pp. 839-845
    • Baldwin, A.N.1    Berg, P.2
  • 97
    • 0017326738 scopus 로고
    • Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase
    • Fersht AR. Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase. Biochemistry 1977, 16:1025-1030.
    • (1977) Biochemistry , vol.16 , pp. 1025-1030
    • Fersht, A.R.1
  • 98
    • 0037178055 scopus 로고    scopus 로고
    • Rational design to block amino acid editing of a tRNA synthetase
    • Mursinna RS, Martinis SA. Rational design to block amino acid editing of a tRNA synthetase. J Am Chem Soc 2002, 124:7286-7287.
    • (2002) J Am Chem Soc , vol.124 , pp. 7286-7287
    • Mursinna, R.S.1    Martinis, S.A.2
  • 99
    • 0029867730 scopus 로고    scopus 로고
    • Mutational analysis suggests the same design for editing activities of two tRNA synthetases
    • Lin L, Schimmel P. Mutational analysis suggests the same design for editing activities of two tRNA synthetases. Biochemistry 1996, 35:5596-5601.
    • (1996) Biochemistry , vol.35 , pp. 5596-5601
    • Lin, L.1    Schimmel, P.2
  • 100
    • 0028305036 scopus 로고
    • Mutational isolation of a sieve for editing in a transfer RNA synthetase
    • Schmidt E, Schimmel P. Mutational isolation of a sieve for editing in a transfer RNA synthetase. Science 1994, 264:265-267.
    • (1994) Science , vol.264 , pp. 265-267
    • Schmidt, E.1    Schimmel, P.2
  • 101
    • 0029130510 scopus 로고
    • Residues in a class I tRNA synthetase which determine selectivity of amino acid recognition in the context of tRNA
    • Schmidt E, Schimmel P. Residues in a class I tRNA synthetase which determine selectivity of amino acid recognition in the context of tRNA. Biochemistry 1995, 34:11204-11210.
    • (1995) Biochemistry , vol.34 , pp. 11204-11210
    • Schmidt, E.1    Schimmel, P.2
  • 105
    • 5644229591 scopus 로고    scopus 로고
    • Pro by Haemophilus influenzae YbaK protein
    • Pro by Haemophilus influenzae YbaK protein. J Biol Chem 2004, 279:42359-42362.
    • (2004) J Biol Chem , vol.279 , pp. 42359-42362
    • An, S.1    Musier-Forsyth, K.2
  • 106
    • 57649155164 scopus 로고    scopus 로고
    • Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation
    • Chong YE, Yang XL, Schimmel P. Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation. J Biol Chem 2008, 283:30073-30078.
    • (2008) J Biol Chem , vol.283 , pp. 30073-30078
    • Chong, Y.E.1    Yang, X.L.2    Schimmel, P.3
  • 107
    • 66449135374 scopus 로고    scopus 로고
    • Defects in transient tRNA translocation bypass tRNA synthetase quality control mechanisms
    • Hellmann RA, Martinis SA. Defects in transient tRNA translocation bypass tRNA synthetase quality control mechanisms. J Biol Chem 2009, 284:11478-11484.
    • (2009) J Biol Chem , vol.284 , pp. 11478-11484
    • Hellmann, R.A.1    Martinis, S.A.2
  • 108
    • 84863723708 scopus 로고    scopus 로고
    • Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase
    • Palencia A, Crepin T, Vu MT, Lincecum TL Jr, Martinis SA, Cusack S. Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase. Nat Struct Mol Biol 2012, 19:677-684.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 677-684
    • Palencia, A.1    Crepin, T.2    Vu, M.T.3    Lincecum Jr, T.L.4    Martinis, S.A.5    Cusack, S.6
  • 109
    • 42349092094 scopus 로고    scopus 로고
    • Functional segregation of a predicted "hinge" site within the β-strand linkers of Escherichia coli leucyl-tRNA synthetase
    • Mascarenhas AP, Martinis SA. Functional segregation of a predicted "hinge" site within the β-strand linkers of Escherichia coli leucyl-tRNA synthetase. Biochemistry 2008, 47:4808-4816.
    • (2008) Biochemistry , vol.47 , pp. 4808-4816
    • Mascarenhas, A.P.1    Martinis, S.A.2
  • 110
    • 70350292212 scopus 로고    scopus 로고
    • A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase
    • Mascarenhas AP, Martinis SA. A glycine hinge for tRNA-dependent translocation of editing substrates to prevent errors by leucyl-tRNA synthetase. FEBS Lett 2009, 583:3443-3447.
    • (2009) FEBS Lett , vol.583 , pp. 3443-3447
    • Mascarenhas, A.P.1    Martinis, S.A.2
  • 111
    • 0037154266 scopus 로고    scopus 로고
    • Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase
    • Bishop AC, Nomanbhoy TK, Schimmel P. Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase. Proc Natl Acad Sci U S A 2002, 99:585-590.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 585-590
    • Bishop, A.C.1    Nomanbhoy, T.K.2    Schimmel, P.3
  • 112
    • 0015500925 scopus 로고
    • Rapid deacylation by isoleucyl transfer ribonucleic acid synthetase of isoleucine-specific transfer ribonucleic acid aminoacylated with valine
    • Eldred EW, Schimmel PR. Rapid deacylation by isoleucyl transfer ribonucleic acid synthetase of isoleucine-specific transfer ribonucleic acid aminoacylated with valine. J Biol Chem 1972, 247:2961-2964.
    • (1972) J Biol Chem , vol.247 , pp. 2961-2964
    • Eldred, E.W.1    Schimmel, P.R.2
  • 113
    • 0030885191 scopus 로고    scopus 로고
    • Aminoacyl thioester chemistry of class II aminoacyl-tRNA synthetases
    • Jakubowski H. Aminoacyl thioester chemistry of class II aminoacyl-tRNA synthetases. Biochemistry 1997, 36:11077-11085.
    • (1997) Biochemistry , vol.36 , pp. 11077-11085
    • Jakubowski, H.1
  • 114
    • 58049211881 scopus 로고    scopus 로고
    • CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase
    • Boniecki MT, Vu MT, Betha AK, Martinis SA. CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase. Proc Natl Acad Sci U S A 2008, 105:19223-19228.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19223-19228
    • Boniecki, M.T.1    Vu, M.T.2    Betha, A.K.3    Martinis, S.A.4
  • 115
    • 77954908008 scopus 로고    scopus 로고
    • Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases
    • Dulic M, Cvetesic N, Perona JJ, Gruic-Sovulj I. Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases. J Biol Chem 2010, 285:23799-23809.
    • (2010) J Biol Chem , vol.285 , pp. 23799-23809
    • Dulic, M.1    Cvetesic, N.2    Perona, J.J.3    Gruic-Sovulj, I.4
  • 116
    • 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 JJ. 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
  • 117
    • 77954943220 scopus 로고    scopus 로고
    • Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase
    • Minajigi A, Francklyn CS. Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase. J Biol Chem 2010, 285:23810-23817.
    • (2010) J Biol Chem , vol.285 , pp. 23810-23817
    • Minajigi, A.1    Francklyn, C.S.2
  • 121
    • 0023046295 scopus 로고
    • The proofreading of hydroxy analogues of leucine and isoleucine by leucyl-tRNA synthetases from E. coli and yeast
    • Englisch S, Englisch U, von der Haar F, Cramer F. The proofreading of hydroxy analogues of leucine and isoleucine by leucyl-tRNA synthetases from E. coli and yeast. Nucleic Acids Res 1986, 14:7529-7539.
    • (1986) Nucleic Acids Res , vol.14 , pp. 7529-7539
    • Englisch, S.1    Englisch, U.2    von der Haar, F.3    Cramer, F.4
  • 122
    • 0018788756 scopus 로고
    • Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases
    • Fersht AR, Dingwall C. Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases. Biochemistry 1979, 18:2627-2631.
    • (1979) Biochemistry , vol.18 , pp. 2627-2631
    • Fersht, A.R.1    Dingwall, C.2
  • 123
    • 71549121009 scopus 로고    scopus 로고
    • The balance between pre- and post-transfer editing in tRNA synthetases
    • Martinis SA, Boniecki MT. The balance between pre- and post-transfer editing in tRNA synthetases. FEBS Lett 2010, 584:455-459.
    • (2010) FEBS Lett , vol.584 , pp. 455-459
    • Martinis, S.A.1    Boniecki, M.T.2
  • 124
    • 33644858728 scopus 로고    scopus 로고
    • Mutational unmasking of a tRNA-dependent pathway for preventing genetic code ambiguity
    • Williams AM, Martinis SA. Mutational unmasking of a tRNA-dependent pathway for preventing genetic code ambiguity. Proc Natl Acad Sci U S A 2006, 103:3586-3591.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3586-3591
    • Williams, A.M.1    Martinis, S.A.2
  • 125
    • 38649129772 scopus 로고    scopus 로고
    • In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity
    • Splan KE, Musier-Forsyth K, Boniecki MT, Martinis SA. In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity. Methods 2008, 44:119-128.
    • (2008) Methods , vol.44 , pp. 119-128
    • Splan, K.E.1    Musier-Forsyth, K.2    Boniecki, M.T.3    Martinis, S.A.4
  • 126
    • 78651286311 scopus 로고    scopus 로고
    • Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase
    • Chen X, Ma JJ, Tan M, Yao P, Hu QH, Eriani G, Wang ED. Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase. Nucleic Acids Res 2011, 39:235-247.
    • (2011) Nucleic Acids Res , vol.39 , pp. 235-247
    • Chen, X.1    Ma, J.J.2    Tan, M.3    Yao, P.4    Hu, Q.H.5    Eriani, G.6    Wang, E.D.7
  • 127
    • 83055179308 scopus 로고    scopus 로고
    • Amino-acid-dependent shift in tRNA synthetase editing mechanisms
    • Sarkar J, Martinis SA. Amino-acid-dependent shift in tRNA synthetase editing mechanisms. J Am Chem Soc 2011, 133:18510-18513.
    • (2011) J Am Chem Soc , vol.133 , pp. 18510-18513
    • Sarkar, J.1    Martinis, S.A.2
  • 128
    • 70349772016 scopus 로고    scopus 로고
    • A paradigm shift for the amino acid editing mechanism of human cytoplasmic leucyl-tRNA synthetase
    • Pang YL, Martinis SA. A paradigm shift for the amino acid editing mechanism of human cytoplasmic leucyl-tRNA synthetase. Biochemistry 2009, 48:8958-8964.
    • (2009) Biochemistry , vol.48 , pp. 8958-8964
    • Pang, Y.L.1    Martinis, S.A.2
  • 129
    • 0029045375 scopus 로고
    • The CUG codon is decoded in vivo as serine and not leucine in Candida albicans
    • Santos MAS, Tuite MF. The CUG codon is decoded in vivo as serine and not leucine in Candida albicans. Nucleic Acids Res 1995, 23:1481-1486.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1481-1486
    • Santos, M.A.S.1    Tuite, M.F.2
  • 131
    • 0003126296 scopus 로고
    • Phe and general structural features of other tRNAs
    • In: Schimmel P, Söll D, Abelson JM, eds.Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    • Phe and general structural features of other tRNAs. In: Schimmel P, Söll D, Abelson JM, eds. Transfer RNA: Structure, Properties, and Recognition. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory; 1979, 83-100.
    • (1979) Transfer RNA: Structure, Properties, and Recognition , pp. 83-100
    • Kim, S.-H.1
  • 132
    • 0024284965 scopus 로고
    • A simple structural feature is a major determinant of the identity of a transfer RNA
    • Hou YM, Schimmel P. A simple structural feature is a major determinant of the identity of a transfer RNA. Nature 1988, 333:140-145.
    • (1988) Nature , vol.333 , pp. 140-145
    • Hou, Y.M.1    Schimmel, P.2
  • 133
    • 0024279871 scopus 로고
    • Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end
    • McClain WH, Foss K. Changing the identity of a tRNA by introducing a G-U wobble pair near the 3' acceptor end. Science 1988, 240:793-796.
    • (1988) Science , vol.240 , pp. 793-796
    • McClain, W.H.1    Foss, K.2
  • 134
    • 0026625691 scopus 로고
    • Eight base changes are sufficient to convert a leucine-inserting tRNA into a serine-inserting tRNA
    • Normanly J, Ollick T, Abelson J. Eight base changes are sufficient to convert a leucine-inserting tRNA into a serine-inserting tRNA. Proc Natl Acad Sci U S A 1992, 89:5680-5684.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 5680-5684
    • Normanly, J.1    Ollick, T.2    Abelson, J.3
  • 137
    • 0024295537 scopus 로고
    • Association of transfer RNA acceptor identity with a helical irregularity
    • McClain WH, Chen YM, Foss K, Schneider J. Association of transfer RNA acceptor identity with a helical irregularity. Science 1988, 242:1681-1684.
    • (1988) Science , vol.242 , pp. 1681-1684
    • McClain, W.H.1    Chen, Y.M.2    Foss, K.3    Schneider, J.4
  • 138
    • 0027208742 scopus 로고
    • Ser: sequence elements necessary for serylation and maturation of a tRNA with a long extra arm
    • Ser: sequence elements necessary for serylation and maturation of a tRNA with a long extra arm. EMBO J 1993, 12:3333-3338.
    • (1993) EMBO J , vol.12 , pp. 3333-3338
    • Achsel, T.1    Gross, H.J.2
  • 139
    • 0023734317 scopus 로고
    • Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification
    • Muramatsu T, Nishikawa K, Nemoto F, Kuchino Y, Nishimura S, Miyazawa T, Yokoyama S. Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification. Nature 1988, 336:179-181.
    • (1988) Nature , vol.336 , pp. 179-181
    • Muramatsu, T.1    Nishikawa, K.2    Nemoto, F.3    Kuchino, Y.4    Nishimura, S.5    Miyazawa, T.6    Yokoyama, S.7
  • 140
    • 0025267036 scopus 로고
    • Relaxation of a transfer RNA specificity by removal of modified nucleotides
    • Perret V, Garcia A, Grosjean H, Ebel JP, Florentz C, Giegé R. Relaxation of a transfer RNA specificity by removal of modified nucleotides. Nature 1990, 344:787-789.
    • (1990) Nature , vol.344 , pp. 787-789
    • Perret, V.1    Garcia, A.2    Grosjean, H.3    Ebel, J.P.4    Florentz, C.5    Giegé, R.6
  • 141
    • 0028508568 scopus 로고
    • A single methyl group prevents the mischarging of a tRNA
    • Putz J, Florentz C, Benseler F, Giegé R. A single methyl group prevents the mischarging of a tRNA. Nat Struct Biol 1994, 1:580-582.
    • (1994) Nat Struct Biol , vol.1 , pp. 580-582
    • Putz, J.1    Florentz, C.2    Benseler, F.3    Giegé, R.4
  • 145
    • 4444369924 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase complexes: beyond translation
    • Lee SW, Cho BH, Park SG, Kim S. Aminoacyl-tRNA synthetase complexes: beyond translation. J Cell Sci 2004, 117(Pt 17):3725-3734.
    • (2004) J Cell Sci , vol.117 , Issue.PT 17 , pp. 3725-3734
    • Lee, S.W.1    Cho, B.H.2    Park, S.G.3    Kim, S.4
  • 146
    • 0021243715 scopus 로고
    • The eucaryotic aminoacyl-tRNA synthetase complex: suggestions for its structure and function
    • Deutscher MP. The eucaryotic aminoacyl-tRNA synthetase complex: suggestions for its structure and function. J Cell Biol 1984, 99:373-377.
    • (1984) J Cell Biol , vol.99 , pp. 373-377
    • Deutscher, M.P.1
  • 147
    • 34247131410 scopus 로고    scopus 로고
    • Macromolecular complexes as depots for releasable regulatory proteins
    • Ray PS, Arif A, Fox PL. Macromolecular complexes as depots for releasable regulatory proteins. Trends Biochem Sci 2007, 32:158-164.
    • (2007) Trends Biochem Sci , vol.32 , pp. 158-164
    • Ray, P.S.1    Arif, A.2    Fox, P.L.3
  • 148
    • 0034737704 scopus 로고    scopus 로고
    • A gene fusion event in the evolution of aminoacyl-tRNA synthetases
    • Berthonneau E, Mirande M. A gene fusion event in the evolution of aminoacyl-tRNA synthetases. FEBS Lett 2000, 470:300-304.
    • (2000) FEBS Lett , vol.470 , pp. 300-304
    • Berthonneau, E.1    Mirande, M.2
  • 149
    • 0034719153 scopus 로고    scopus 로고
    • Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats
    • Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS. Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry 2000, 39:15775-15782.
    • (2000) Biochemistry , vol.39 , pp. 15775-15782
    • Jeong, E.J.1    Hwang, G.S.2    Kim, K.H.3    Kim, M.J.4    Kim, S.5    Kim, K.S.6
  • 151
    • 25144489447 scopus 로고    scopus 로고
    • Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers
    • Park SG, Ewalt KL, Kim S. Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers. Trends Biochem Sci 2005, 30:569-574.
    • (2005) Trends Biochem Sci , vol.30 , pp. 569-574
    • Park, S.G.1    Ewalt, K.L.2    Kim, S.3
  • 152
    • 0037070188 scopus 로고    scopus 로고
    • Three-dimensional architecture of the eukaryotic multisynthetase complex determined from negatively stained and cryoelectron micrographs
    • Norcum MT, Boisset N. Three-dimensional architecture of the eukaryotic multisynthetase complex determined from negatively stained and cryoelectron micrographs. FEBS Lett 2002, 512(1-3):298-302.
    • (2002) FEBS Lett , vol.512 , Issue.1-3 , pp. 298-302
    • Norcum, M.T.1    Boisset, N.2
  • 153
    • 0031939704 scopus 로고    scopus 로고
    • Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: a three-domain model based on reversible chemical crosslinking
    • Norcum MT, Warrington JA. Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: a three-domain model based on reversible chemical crosslinking. Protein Sci 1998, 7:79-87.
    • (1998) Protein Sci , vol.7 , pp. 79-87
    • Norcum, M.T.1    Warrington, J.A.2
  • 154
    • 0038405007 scopus 로고    scopus 로고
    • Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43
    • Ahn HC, Kim S, Lee BJ. Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43. FEBS Lett 2003, 542(1-3):119-124.
    • (2003) FEBS Lett , vol.542 , Issue.1-3 , pp. 119-124
    • Ahn, H.C.1    Kim, S.2    Lee, B.J.3
  • 155
    • 0034674708 scopus 로고    scopus 로고
    • The cytokine portion of p43 occupies a central position within the eukaryotic multisynthetase complex
    • Norcum MT, Warrington JA. The cytokine portion of p43 occupies a central position within the eukaryotic multisynthetase complex. J Biol Chem 2000, 275:17921-17924.
    • (2000) J Biol Chem , vol.275 , pp. 17921-17924
    • Norcum, M.T.1    Warrington, J.A.2
  • 156
    • 0000666250 scopus 로고    scopus 로고
    • Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase
    • Park SG, Jung KH, Lee JS, Jo YJ, Motegi H, Kim S, Shiba K. Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase. J Biol Chem 1999, 274:16673-16676.
    • (1999) J Biol Chem , vol.274 , pp. 16673-16676
    • Park, S.G.1    Jung, K.H.2    Lee, J.S.3    Jo, Y.J.4    Motegi, H.5    Kim, S.6    Shiba, K.7
  • 160
    • 77953611585 scopus 로고    scopus 로고
    • Toll-like receptor 4-mediated c-Jun N-terminal kinase activation induces gp96 cell surface expression via AIMP1 phosphorylation
    • Kim G, Han JM, Kim S. Toll-like receptor 4-mediated c-Jun N-terminal kinase activation induces gp96 cell surface expression via AIMP1 phosphorylation. Biochem Biophys Res Commun 2010, 397:100-105.
    • (2010) Biochem Biophys Res Commun , vol.397 , pp. 100-105
    • Kim, G.1    Han, J.M.2    Kim, S.3
  • 161
    • 1342287127 scopus 로고    scopus 로고
    • The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcεRI-activated mast cells
    • Lee YN, Nechushtan H, Figov N, Razin E. The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcεRI-activated mast cells. Immunity 2004, 20:145-151.
    • (2004) Immunity , vol.20 , pp. 145-151
    • Lee, Y.N.1    Nechushtan, H.2    Figov, N.3    Razin, E.4
  • 163
    • 69949183262 scopus 로고    scopus 로고
    • The physiological role of lysyl tRNA synthetase in the immune system
    • Nechushtan H, Kim S, Kay G, Razin E. The physiological role of lysyl tRNA synthetase in the immune system. Adv Immunol 2009, 103:1-27.
    • (2009) Adv Immunol , vol.103 , pp. 1-27
    • Nechushtan, H.1    Kim, S.2    Kay, G.3    Razin, E.4
  • 164
    • 0142227209 scopus 로고    scopus 로고
    • Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control
    • Mazumder B, Sampath P, Seshadri V, Maitra RK, DiCorleto PE, Fox PL. Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control. Cell 2003, 115:187-198.
    • (2003) Cell , vol.115 , pp. 187-198
    • Mazumder, B.1    Sampath, P.2    Seshadri, V.3    Maitra, R.K.4    DiCorleto, P.E.5    Fox, P.L.6
  • 166
    • 0029790980 scopus 로고    scopus 로고
    • The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases
    • Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, Hurt EC. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. EMBO J 1996, 15:5437-5448.
    • (1996) EMBO J , vol.15 , pp. 5437-5448
    • Simos, G.1    Segref, A.2    Fasiolo, F.3    Hellmuth, K.4    Shevchenko, A.5    Mann, M.6    Hurt, E.C.7
  • 167
    • 65449172879 scopus 로고    scopus 로고
    • Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS
    • Frechin M, Senger B, Brayé M, Kern D, Martin RP, Becker HD. Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS. Genes Dev 2009, 23:1119-1130.
    • (2009) Genes Dev , vol.23 , pp. 1119-1130
    • Frechin, M.1    Senger, B.2    Brayé, M.3    Kern, D.4    Martin, R.P.5    Becker, H.D.6
  • 168
  • 170
    • 35548983465 scopus 로고    scopus 로고
    • An aminoacyl-tRNA synthetase:elongation factor complex for substrate channeling in archaeal translation
    • Hausmann CD, Praetorius-Ibba M, Ibba M. An aminoacyl-tRNA synthetase:elongation factor complex for substrate channeling in archaeal translation. Nucleic Acids Res 2007, 35:6094-6102.
    • (2007) Nucleic Acids Res , vol.35 , pp. 6094-6102
    • Hausmann, C.D.1    Praetorius-Ibba, M.2    Ibba, M.3
  • 171
    • 13244272361 scopus 로고    scopus 로고
    • The novel cytokine p43 stimulates dermal fibroblast proliferation and wound repair
    • Park SG, Shin H, Shin YK, Lee Y, Choi EC, Park BJ, Kim S. The novel cytokine p43 stimulates dermal fibroblast proliferation and wound repair. Am J Pathol 2005, 166:387-398.
    • (2005) Am J Pathol , vol.166 , pp. 387-398
    • Park, S.G.1    Shin, H.2    Shin, Y.K.3    Lee, Y.4    Choi, E.C.5    Park, B.J.6    Kim, S.7
  • 172
    • 32644460680 scopus 로고    scopus 로고
    • Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1
    • Han JM, Park SG, Lee Y, Kim S. Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1. Biochem Biophys Res Commun 2006, 342:113-118.
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 113-118
    • Han, J.M.1    Park, S.G.2    Lee, Y.3    Kim, S.4
  • 174
    • 34447295947 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase-interacting multifunctional protein 1/p43 controls endoplasmic reticulum retention of heat shock protein gp96: its pathological implications in lupus-like autoimmune diseases
    • Han JM, Park SG, Liu B, Park BJ, Kim JY, Jin CH, Song YW, Li Z, Kim S. Aminoacyl-tRNA synthetase-interacting multifunctional protein 1/p43 controls endoplasmic reticulum retention of heat shock protein gp96: its pathological implications in lupus-like autoimmune diseases. Am J Pathol 2007, 170:2042-2054.
    • (2007) Am J Pathol , vol.170 , pp. 2042-2054
    • Han, J.M.1    Park, S.G.2    Liu, B.3    Park, B.J.4    Kim, J.Y.5    Jin, C.H.6    Song, Y.W.7    Li, Z.8    Kim, S.9
  • 177
    • 0033198765 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases: a family of expanding functions
    • Martinis SA, Plateau P, Cavarelli J, Florentz C. Aminoacyl-tRNA synthetases: a family of expanding functions. EMBO J 1999, 18:4591-4596.
    • (1999) EMBO J , vol.18 , pp. 4591-4596
    • Martinis, S.A.1    Plateau, P.2    Cavarelli, J.3    Florentz, C.4
  • 178
    • 37149020819 scopus 로고    scopus 로고
    • Jekyll & Hyde: evolution of a superfamily
    • Martinis SA, Joy Pang YL. Jekyll & Hyde: evolution of a superfamily. Chem Biol 2007, 14:1307-1308.
    • (2007) Chem Biol , vol.14 , pp. 1307-1308
    • Martinis, S.A.1    Joy Pang, Y.L.2
  • 179
    • 49649110170 scopus 로고    scopus 로고
    • Aminoacyl tRNA synthetases and their connections to disease
    • Park SG, Schimmel P, Kim S. Aminoacyl tRNA synthetases and their connections to disease. Proc Natl Acad Sci U S A 2008, 105:11043-11049.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11043-11049
    • Park, S.G.1    Schimmel, P.2    Kim, S.3
  • 180
    • 0023958916 scopus 로고
    • The NAM2 proteins from S. cerevisiae and S. douglasii are mitochondrial leucyl-tRNA synthetases, and are involved in mRNA splicing
    • Herbert CJ, Labouesse M, Dujardin G, Slonimski PP. The NAM2 proteins from S. cerevisiae and S. douglasii are mitochondrial leucyl-tRNA synthetases, and are involved in mRNA splicing. EMBO J 1988, 7:473-483.
    • (1988) EMBO J , vol.7 , pp. 473-483
    • Herbert, C.J.1    Labouesse, M.2    Dujardin, G.3    Slonimski, P.P.4
  • 181
    • 0026586258 scopus 로고
    • The mitochondrial tyrosyl-tRNA synthetase of Podospora anserina is a bifunctional enzyme active in protein synthesis and RNA splicing
    • Kämper U, Kuck U, Cherniack AD, Lambowitz AM. The mitochondrial tyrosyl-tRNA synthetase of Podospora anserina is a bifunctional enzyme active in protein synthesis and RNA splicing. Mol Cell Biol 1992, 12:499-511.
    • (1992) Mol Cell Biol , vol.12 , pp. 499-511
    • Kämper, U.1    Kuck, U.2    Cherniack, A.D.3    Lambowitz, A.M.4
  • 182
    • 0025604577 scopus 로고
    • The yeast mitochondrial leucyl-tRNA synthetase is a splicing factor for the excision of several group I introns
    • Labouesse M. The yeast mitochondrial leucyl-tRNA synthetase is a splicing factor for the excision of several group I introns. Mol Gen Genet 1990, 224:209-221.
    • (1990) Mol Gen Genet , vol.224 , pp. 209-221
    • Labouesse, M.1
  • 183
    • 0021887990 scopus 로고
    • The yeast nuclear gene NAM2 is essential for mitochondrial DNA integrity and can cure a mitochondrial RNA-maturase deficiency
    • Labouesse M, Dujardin G, Slonimski PP. The yeast nuclear gene NAM2 is essential for mitochondrial DNA integrity and can cure a mitochondrial RNA-maturase deficiency. Cell 1985, 41:133-143.
    • (1985) Cell , vol.41 , pp. 133-143
    • Labouesse, M.1    Dujardin, G.2    Slonimski, P.P.3
  • 184
    • 10344237522 scopus 로고    scopus 로고
    • The expression of E. coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions
    • Romby P, Caillet J, Ebel C, Sacerdot C, Graffe M, Eyermann F, Brunel C, Moine H, Ehresmann C, Ehresmann B, et al. The expression of E. coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions. EMBO J 1996, 15:5976-5987.
    • (1996) EMBO J , vol.15 , pp. 5976-5987
    • Romby, P.1    Caillet, J.2    Ebel, C.3    Sacerdot, C.4    Graffe, M.5    Eyermann, F.6    Brunel, C.7    Moine, H.8    Ehresmann, C.9    Ehresmann, B.10
  • 185
    • 0029804257 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetase gene regulation in Bacillus subtilis
    • Condon C, Grunberg-Manago M, Putzer H. Aminoacyl-tRNA synthetase gene regulation in Bacillus subtilis. Biochimie 1996, 78:381-389.
    • (1996) Biochimie , vol.78 , pp. 381-389
    • Condon, C.1    Grunberg-Manago, M.2    Putzer, H.3
  • 186
    • 0019828465 scopus 로고
    • An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription
    • Putney SD, Schimmel P. An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription. Nature 1981, 291:632-635.
    • (1981) Nature , vol.291 , pp. 632-635
    • Putney, S.D.1    Schimmel, P.2
  • 190
    • 34547478151 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect
    • Nangle LA, Zhang W, Xie W, Yang XL, Schimmel P. Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect. Proc Natl Acad Sci U S A 2007, 104:11239-11244.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 11239-11244
    • Nangle, L.A.1    Zhang, W.2    Xie, W.3    Yang, X.L.4    Schimmel, P.5
  • 191
    • 0020560563 scopus 로고
    • Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity
    • Mathews MB, Bernstein RM. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity. Nature 1983, 304:177-179.
    • (1983) Nature , vol.304 , pp. 177-179
    • Mathews, M.B.1    Bernstein, R.M.2
  • 192
    • 0027983773 scopus 로고
    • A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope
    • Raben N, Nichols R, Dohlman J, McPhie P, Sridhar V, Hyde C, Leff R, Plotz P. A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope. J Biol Chem 1994, 269:24277-24283.
    • (1994) J Biol Chem , vol.269 , pp. 24277-24283
    • Raben, N.1    Nichols, R.2    Dohlman, J.3    McPhie, P.4    Sridhar, V.5    Hyde, C.6    Leff, R.7    Plotz, P.8
  • 193
    • 0032518176 scopus 로고    scopus 로고
    • Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen
    • Beaulande M, Tarbouriech N, Hartlein M. Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen. Nucleic Acids Res 1998, 26:521-524.
    • (1998) Nucleic Acids Res , vol.26 , pp. 521-524
    • Beaulande, M.1    Tarbouriech, N.2    Hartlein, M.3
  • 194
    • 0033558132 scopus 로고    scopus 로고
    • Anti-KS: identification of autoantibodies to asparaginyl-transfer RNA synthetase associated with interstitial lung disease
    • Hirakata M, Suwa A, Nagai S, Kron MA, Trieu EP, Mimori T, Akizuki M, Targoff IN. Anti-KS: identification of autoantibodies to asparaginyl-transfer RNA synthetase associated with interstitial lung disease. J Immunol 1999, 162:2315-2320.
    • (1999) J Immunol , vol.162 , pp. 2315-2320
    • Hirakata, M.1    Suwa, A.2    Nagai, S.3    Kron, M.A.4    Trieu, E.P.5    Mimori, T.6    Akizuki, M.7    Targoff, I.N.8
  • 195
    • 0030027480 scopus 로고    scopus 로고
    • Autoantibodies to glycyl-transfer RNA synthetase in myositis. Association with dermatomyositis and immunologic heterogeneity
    • Hirakata M, Suwa A, Takeda Y, Matsuoka Y, Irimajiri S, Targoff IN, Hardin JA, Craft J. Autoantibodies to glycyl-transfer RNA synthetase in myositis. Association with dermatomyositis and immunologic heterogeneity. Arthritis Rheum 1996, 39:146-151.
    • (1996) Arthritis Rheum , vol.39 , pp. 146-151
    • Hirakata, M.1    Suwa, A.2    Takeda, Y.3    Matsuoka, Y.4    Irimajiri, S.5    Targoff, I.N.6    Hardin, J.A.7    Craft, J.8
  • 196
    • 0025281492 scopus 로고
    • Autoantibodies to aminoacyl-transfer RNA synthetases for isoleucine and glycine. Two additional synthetases are antigenic in myositis
    • Targoff IN. Autoantibodies to aminoacyl-transfer RNA synthetases for isoleucine and glycine. Two additional synthetases are antigenic in myositis. J Immunol 1990, 144:1737-1743.
    • (1990) J Immunol , vol.144 , pp. 1737-1743
    • Targoff, I.N.1
  • 197
    • 0027311314 scopus 로고
    • Reaction of anti-OJ autoantibodies with components of the multi-enzyme complex of aminoacyl-tRNA synthetases in addition to isoleucyl-tRNA synthetase
    • Targoff IN, Trieu EP, Miller FW. Reaction of anti-OJ autoantibodies with components of the multi-enzyme complex of aminoacyl-tRNA synthetases in addition to isoleucyl-tRNA synthetase. J Clin Invest 1993, 91:2556-2564.
    • (1993) J Clin Invest , vol.91 , pp. 2556-2564
    • Targoff, I.N.1    Trieu, E.P.2    Miller, F.W.3
  • 198
    • 82555174606 scopus 로고    scopus 로고
    • Entamoeba lysyl-tRNA synthetase contains a cytokine-like domain with chemokine activity towards human endothelial cells
    • Castro de Moura M, Miro F, Han JM, Kim S, Celada A, Ribas de Pouplana L. Entamoeba lysyl-tRNA synthetase contains a cytokine-like domain with chemokine activity towards human endothelial cells. PLoS Negl Trop Dis 2011, 5:e1398.
    • (2011) PLoS Negl Trop Dis , vol.5
    • Castro de Moura, M.1    Miro, F.2    Han, J.M.3    Kim, S.4    Celada, A.5    Ribas de Pouplana, L.6
  • 201
    • 0037120002 scopus 로고    scopus 로고
    • Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells
    • Howard OM, Dong HF, Yang D, Raben N, Nagaraju K, Rosen A, Casciola-Rosen L, Hartlein M, Kron M, Yang D, et al. Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells. J Exp Med 2002, 196:781-791.
    • (2002) J Exp Med , vol.196 , pp. 781-791
    • Howard, O.M.1    Dong, H.F.2    Yang, D.3    Raben, N.4    Nagaraju, K.5    Rosen, A.6    Casciola-Rosen, L.7    Hartlein, M.8    Kron, M.9    Yang, D.10
  • 203
    • 79952129827 scopus 로고    scopus 로고
    • Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translational control
    • Arif A, Jia J, Moodt RA, DiCorleto PE, Fox PL. Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translational control. Proc Natl Acad Sci U S A 2011, 108:1415-1420.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 1415-1420
    • Arif, A.1    Jia, J.2    Moodt, R.A.3    DiCorleto, P.E.4    Fox, P.L.5
  • 205
    • 70349414307 scopus 로고    scopus 로고
    • Fibroblast growth factor 2-induced cytoplasmic asparaginyl-tRNA synthetase promotes survival of osteoblasts by regulating anti-apoptotic PI3K/Akt signaling
    • Park SJ, Kim SH, Choi HS, Rhee Y, Lim SK. Fibroblast growth factor 2-induced cytoplasmic asparaginyl-tRNA synthetase promotes survival of osteoblasts by regulating anti-apoptotic PI3K/Akt signaling. Bone 2009, 45:994-1003.
    • (2009) Bone , vol.45 , pp. 994-1003
    • Park, S.J.1    Kim, S.H.2    Choi, H.S.3    Rhee, Y.4    Lim, S.K.5
  • 206
    • 33645783942 scopus 로고    scopus 로고
    • Brugia malayi asparaginyl-transfer RNA synthetase induces chemotaxis of human leukocytes and activates G-protein-coupled receptors CXCR1 and CXCR2
    • Ramirez BL, Howard OM, Dong HF, Edamatsu T, Gao P, Härtlein M, Kron M. Brugia malayi asparaginyl-transfer RNA synthetase induces chemotaxis of human leukocytes and activates G-protein-coupled receptors CXCR1 and CXCR2. J Infect Dis 2006, 193:1164-1171.
    • (2006) J Infect Dis , vol.193 , pp. 1164-1171
    • Ramirez, B.L.1    Howard, O.M.2    Dong, H.F.3    Edamatsu, T.4    Gao, P.5    Härtlein, M.6    Kron, M.7
  • 208
    • 0037121930 scopus 로고    scopus 로고
    • An inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing
    • Rho SB, Lincecum TL Jr, Martinis SA. An inserted region of leucyl-tRNA synthetase plays a critical role in group I intron splicing. EMBO J 2002, 21:6874-6881.
    • (2002) EMBO J , vol.21 , pp. 6874-6881
    • Rho, S.B.1    Lincecum Jr, T.L.2    Martinis, S.A.3
  • 209
  • 210
    • 0029869019 scopus 로고    scopus 로고
    • A tyrosyl-tRNA synthetase protein induces tertiary folding of the group I intron catalytic core
    • Caprara MG, Mohr G, Lambowitz AM. A tyrosyl-tRNA synthetase protein induces tertiary folding of the group I intron catalytic core. J Mol Biol 1996, 257:512-531.
    • (1996) J Mol Biol , vol.257 , pp. 512-531
    • Caprara, M.G.1    Mohr, G.2    Lambowitz, A.M.3
  • 213
    • 3142720576 scopus 로고    scopus 로고
    • Cellular distribution of lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly
    • Halwani R, Cen S, Javanbakht H, Saadatmand J, Kim S, Shiba K, Kleiman L. Cellular distribution of lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly. J Virol 2004, 78:7553-7564.
    • (2004) J Virol , vol.78 , pp. 7553-7564
    • Halwani, R.1    Cen, S.2    Javanbakht, H.3    Saadatmand, J.4    Kim, S.5    Shiba, K.6    Kleiman, L.7
  • 215
    • 0346373687 scopus 로고    scopus 로고
    • Lys incorporation into human immunodeficiency virus type 1
    • Lys incorporation into human immunodeficiency virus type 1. J Virol 2004, 78:1595-1601.
    • (2004) J Virol , vol.78 , pp. 1595-1601
    • Cen, S.1    Javanbakht, H.2    Niu, M.3    Kleiman, L.4
  • 216
    • 0036721002 scopus 로고    scopus 로고
    • 3 concentration in human immunodeficiency virus type 1 upon its annealing to viral RNA, GagPol incorporation, and viral infectivity
    • 3 concentration in human immunodeficiency virus type 1 upon its annealing to viral RNA, GagPol incorporation, and viral infectivity. J Virol 2002, 76:9096-9102.
    • (2002) J Virol , vol.76 , pp. 9096-9102
    • Gabor, J.1    Cen, S.2    Javanbakht, H.3    Niu, M.4    Kleiman, L.5
  • 218
    • 79960369440 scopus 로고    scopus 로고
    • Association of mitochondrial lysyl-tRNA synthetase with HIV-1 GagPol involves catalytic domain of the synthetase and transframe and integrase domains of Pol
    • Kobbi L, Octobre G, Dias J, Comisso M, Mirande M. Association of mitochondrial lysyl-tRNA synthetase with HIV-1 GagPol involves catalytic domain of the synthetase and transframe and integrase domains of Pol. J Mol Biol 2011, 410:875-886.
    • (2011) J Mol Biol , vol.410 , pp. 875-886
    • Kobbi, L.1    Octobre, G.2    Dias, J.3    Comisso, M.4    Mirande, M.5
  • 219
    • 0027166763 scopus 로고
    • Identification of tRNAs incorporated into wild-type and mutant human immunodeficiency virus type 1
    • Jiang M, Mak J, Ladha A, Cohen E, Klein M, Rovinski B, Kleiman L. Identification of tRNAs incorporated into wild-type and mutant human immunodeficiency virus type 1. J Virol 1993, 67:3246-3253.
    • (1993) J Virol , vol.67 , pp. 3246-3253
    • Jiang, M.1    Mak, J.2    Ladha, A.3    Cohen, E.4    Klein, M.5    Rovinski, B.6    Kleiman, L.7
  • 220
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler KC, Waller PR, Sauer RT. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 1996, 271:990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 222
    • 42449118064 scopus 로고    scopus 로고
    • RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors
    • Roy H, Ibba M. RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors. Proc Natl Acad Sci U S A 2008, 105:4667-4672.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4667-4672
    • Roy, H.1    Ibba, M.2
  • 223
    • 84857694990 scopus 로고    scopus 로고
    • Viral tRNAs and tRNA-like structures
    • Dreher TW. Viral tRNAs and tRNA-like structures. Wiley Interdiscip Rev RNA 2010, 1:402-414.
    • (2010) Wiley Interdiscip Rev RNA , vol.1 , pp. 402-414
    • Dreher, T.W.1
  • 224
    • 0026787504 scopus 로고
    • Specific valylation of turnip yellow mosaic virus RNA by wheat germ valyl-tRNA synthetase determined by three anticodon loop nucleotides
    • Dreher TW, Tsai CH, Florentz C, Giegé R. Specific valylation of turnip yellow mosaic virus RNA by wheat germ valyl-tRNA synthetase determined by three anticodon loop nucleotides. Biochemistry 1992, 31:9183-9189.
    • (1992) Biochemistry , vol.31 , pp. 9183-9189
    • Dreher, T.W.1    Tsai, C.H.2    Florentz, C.3    Giegé, R.4
  • 225
    • 0026085291 scopus 로고
    • Specific valylation identity of turnip yellow mosaic virus RNA by yeast valyl-tRNA synthetase is directed by the anticodon in a kinetic rather than affinity-based discrimination
    • Florentz C, Dreher TW, Rudinger J, Giegé R. Specific valylation identity of turnip yellow mosaic virus RNA by yeast valyl-tRNA synthetase is directed by the anticodon in a kinetic rather than affinity-based discrimination. Eur J Biochem 1991, 195:229-234.
    • (1991) Eur J Biochem , vol.195 , pp. 229-234
    • Florentz, C.1    Dreher, T.W.2    Rudinger, J.3    Giegé, R.4
  • 226
    • 0027959313 scopus 로고
    • A histidine accepting tRNA-like fold at the 3'-end of satellite tobacco mosaic virus RNA
    • Felden B, Florentz C, McPherson A, Giegé R. A histidine accepting tRNA-like fold at the 3'-end of satellite tobacco mosaic virus RNA. Nucleic Acids Res 1994, 22:2882-2886.
    • (1994) Nucleic Acids Res , vol.22 , pp. 2882-2886
    • Felden, B.1    Florentz, C.2    McPherson, A.3    Giegé, R.4
  • 227
    • 0000847459 scopus 로고
    • The three-dimensional folding of the tRNA-like structure of tobacco mosaic virus RNA. A new building principle applied twice
    • Rietveld K, Linschooten K, Pleij CW, Bosch L. The three-dimensional folding of the tRNA-like structure of tobacco mosaic virus RNA. A new building principle applied twice. EMBO J 1984, 3:2613-2619.
    • (1984) EMBO J , vol.3 , pp. 2613-2619
    • Rietveld, K.1    Linschooten, K.2    Pleij, C.W.3    Bosch, L.4
  • 228
    • 0030948634 scopus 로고    scopus 로고
    • Strategy for RNA recognition by yeast histidyl-tRNA synthetase
    • Rudinger J, Felden B, Florentz C, Giegé R. Strategy for RNA recognition by yeast histidyl-tRNA synthetase. Bioorg Med Chem 1997, 5:1001-1009.
    • (1997) Bioorg Med Chem , vol.5 , pp. 1001-1009
    • Rudinger, J.1    Felden, B.2    Florentz, C.3    Giegé, R.4
  • 229
    • 0035366419 scopus 로고    scopus 로고
    • Specific tyrosylation of the bulky tRNA-like structure of brome mosaic virus RNA relies solely on identity nucleotides present in its amino acid-accepting domain
    • Fechter P, Giegé R, Rudinger-Thirion J. Specific tyrosylation of the bulky tRNA-like structure of brome mosaic virus RNA relies solely on identity nucleotides present in its amino acid-accepting domain. J Mol Biol 2001, 309:387-399.
    • (2001) J Mol Biol , vol.309 , pp. 387-399
    • Fechter, P.1    Giegé, R.2    Rudinger-Thirion, J.3
  • 230
  • 231
    • 0002296970 scopus 로고
    • tRNA-like structures in plant viral RNAs
    • In: Söll D, RajBhandary U, eds. Washington, DC: ASM Press;
    • Florentz C, Giegé R. tRNA-like structures in plant viral RNAs. In: Söll D, RajBhandary U, eds. tRNA: Structure, Biosynthesis and Function. Washington, DC: ASM Press; 1995, 141-163.
    • (1995) tRNA: Structure, Biosynthesis and Function , pp. 141-163
    • Florentz, C.1    Giegé, R.2
  • 232
    • 0022423219 scopus 로고
    • A new principle of RNA folding based on pseudoknotting
    • Pleij CW, Rietveld K, Bosch L. A new principle of RNA folding based on pseudoknotting. Nucleic Acids Res 1985, 13:1717-1731.
    • (1985) Nucleic Acids Res , vol.13 , pp. 1717-1731
    • Pleij, C.W.1    Rietveld, K.2    Bosch, L.3
  • 233
    • 0020675179 scopus 로고
    • Three-dimensional models of the tRNA-like 3' termini of some plant viral RNAs
    • Rietveld K, Pleij CW, Bosch L. Three-dimensional models of the tRNA-like 3' termini of some plant viral RNAs. EMBO J 1983, 2:1079-1085.
    • (1983) EMBO J , vol.2 , pp. 1079-1085
    • Rietveld, K.1    Pleij, C.W.2    Bosch, L.3
  • 234
    • 0023042689 scopus 로고
    • Contact areas of the turnip yellow mosaic virus tRNA-like structure interacting with yeast valyl-tRNA synthetase
    • Florentz C, Giegé R. Contact areas of the turnip yellow mosaic virus tRNA-like structure interacting with yeast valyl-tRNA synthetase. J Mol Biol 1986, 191:117-130.
    • (1986) J Mol Biol , vol.191 , pp. 117-130
    • Florentz, C.1    Giegé, R.2
  • 239
    • 0018159737 scopus 로고
    • Inhibition of isoleucyl-transfer ribonucleic acid synthetase in Escherichia coli by pseudomonic acid
    • Hughes J, Mellows G. Inhibition of isoleucyl-transfer ribonucleic acid synthetase in Escherichia coli by pseudomonic acid. Biochem J 1978, 176:305-318.
    • (1978) Biochem J , vol.176 , pp. 305-318
    • Hughes, J.1    Mellows, G.2
  • 240
    • 0019164866 scopus 로고
    • Interaction of pseudomonic acid A with Escherichia coli B isoleucyl-tRNA synthetase
    • Hughes J, Mellows G. Interaction of pseudomonic acid A with Escherichia coli B isoleucyl-tRNA synthetase. Biochem J 1980, 191:209-219.
    • (1980) Biochem J , vol.191 , pp. 209-219
    • Hughes, J.1    Mellows, G.2
  • 242
    • 0028050510 scopus 로고
    • Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase
    • Yanagisawa T, Lee JT, Wu HC, Kawakami M. Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coli. A proposed mode of action of pseudomonic acid as an inhibitor of isoleucyl-tRNA synthetase. J Biol Chem 1994, 269:24304-24309.
    • (1994) J Biol Chem , vol.269 , pp. 24304-24309
    • Yanagisawa, T.1    Lee, J.T.2    Wu, H.C.3    Kawakami, M.4
  • 243
    • 33746701345 scopus 로고    scopus 로고
    • Discovery of a new boron-containing antifungal agent, 5-fluoro-1,3-dihydro-1-hydroxy-2,1- benzoxaborole (AN2690), for the potential treatment of onychomycosis
    • Baker SJ, Zhang YK, Akama T, Lau A, Zhou H, Hernandez V, Mao W, Alley MR, Sanders V, Plattner JJ. Discovery of a new boron-containing antifungal agent, 5-fluoro-1, 3-dihydro-1-hydroxy-2, 1- benzoxaborole (AN2690), for the potential treatment of onychomycosis. J Med Chem 2006, 49:4447-4450.
    • (2006) J Med Chem , vol.49 , pp. 4447-4450
    • Baker, S.J.1    Zhang, Y.K.2    Akama, T.3    Lau, A.4    Zhou, H.5    Hernandez, V.6    Mao, W.7    Alley, M.R.8    Sanders, V.9    Plattner, J.J.10
  • 244
    • 43249106267 scopus 로고    scopus 로고
    • The novel fragment of tyrosyl tRNA synthetase, mini-TyrRS, is secreted to induce an angiogenic response in endothelial cells
    • Greenberg Y, King M, Kiosses WB, Ewalt K, Yang X, Schimmel P, Reader JS, Tzima E. The novel fragment of tyrosyl tRNA synthetase, mini-TyrRS, is secreted to induce an angiogenic response in endothelial cells. FASEB J 2008, 22:1597-1605.
    • (2008) FASEB J , vol.22 , pp. 1597-1605
    • Greenberg, Y.1    King, M.2    Kiosses, W.B.3    Ewalt, K.4    Yang, X.5    Schimmel, P.6    Reader, J.S.7    Tzima, E.8


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