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PUBMED FOR HANDHELDS

Journal Abstract Search


209 related items for PubMed ID: 31486189

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  • 4. Improvement of substrate recognition in branched-chain aminoacyl-tRNA synthetases from Escherichia coli under conditions of pyrophosphate amplification.
    Nakatsuka-Mori T, Sato D, Aoki H.
    J Biosci Bioeng; 2022 May; 133(5):436-443. PubMed ID: 35216933
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  • 5. Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine.
    Fukunaga R, Fukai S, Ishitani R, Nureki O, Yokoyama S.
    J Biol Chem; 2004 Feb 27; 279(9):8396-402. PubMed ID: 14672940
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  • 6. The tRNA A76 Hydroxyl Groups Control Partitioning of the tRNA-dependent Pre- and Post-transfer Editing Pathways in Class I tRNA Synthetase.
    Cvetesic N, Bilus M, Gruic-Sovulj I.
    J Biol Chem; 2015 May 29; 290(22):13981-91. PubMed ID: 25873392
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  • 8. Gly56 in the synthetic site of isoleucyl-tRNA synthetase confers specificity and maintains communication with the editing site.
    Dulic M, Krpan N, Gruic-Sovulj I.
    FEBS Lett; 2023 Dec 29; 597(24):3114-3124. PubMed ID: 38015921
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  • 12. 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.
    J Biol Chem; 2010 Jul 30; 285(31):23799-809. PubMed ID: 20498377
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  • 16. Functional segregation of a predicted "hinge" site within the beta-strand linkers of Escherichia coli leucyl-tRNA synthetase.
    Mascarenhas AP, Martinis SA.
    Biochemistry; 2008 Apr 22; 47(16):4808-16. PubMed ID: 18363380
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  • 19. Residues in a class I tRNA synthetase which determine selectivity of amino acid recognition in the context of tRNA.
    Schmidt E, Schimmel P.
    Biochemistry; 1995 Sep 05; 34(35):11204-10. PubMed ID: 7669778
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  • 20. 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.
    Biochemistry; 2007 May 29; 46(21):6258-67. PubMed ID: 17474713
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