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1
The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.
EMBO J. 2001 Sep 17;20(18):5290-301. doi: 10.1093/emboj/20.18.5290.
3
Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step.
EMBO J. 1999 Nov 15;18(22):6532-41. doi: 10.1093/emboj/18.22.6532.
5
Crystal structure of the N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori.
Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):62-69. doi: 10.1107/S2053230X16020586. Epub 2017 Jan 19.
7
An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase.
J Mol Biol. 2000 Jun 16;299(4):1051-60. doi: 10.1006/jmbi.2000.3819.
8
Yeast tRNA(Asp) recognition by its cognate class II aminoacyl-tRNA synthetase.
Nature. 1993 Mar 11;362(6416):181-4. doi: 10.1038/362181a0.
10
Construction of an Escherichia coli knockout strain for functional analysis of tRNA(Asp).
J Mol Biol. 2001 Jul 13;310(3):537-42. doi: 10.1006/jmbi.2001.4785.

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Mitochondrial RNA in Inflammation.
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Natural product-mediated reaction hijacking mechanism validates Plasmodium aspartyl-tRNA synthetase as an antimalarial drug target.
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3
Reaction hijacking inhibition of Plasmodium falciparum asparagine tRNA synthetase.
Nat Commun. 2024 Jan 31;15(1):937. doi: 10.1038/s41467-024-45224-z.
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The tRNA identity landscape for aminoacylation and beyond.
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Structure and Dynamics of the Human Multi-tRNA Synthetase Complex.
Subcell Biochem. 2022;99:199-233. doi: 10.1007/978-3-031-00793-4_6.
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Mycobacterium tuberculosis Phe-tRNA synthetase: structural insights into tRNA recognition and aminoacylation.
Nucleic Acids Res. 2021 May 21;49(9):5351-5368. doi: 10.1093/nar/gkab272.
7
Drugging tRNA aminoacylation.
RNA Biol. 2018;15(4-5):667-677. doi: 10.1080/15476286.2018.1429879. Epub 2018 Feb 2.
9
Aminoacyl-tRNA Synthetases in the Bacterial World.
EcoSal Plus. 2016 May;7(1). doi: 10.1128/ecosalplus.ESP-0002-2016.
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An atlas of RNA base pairs involving modified nucleobases with optimal geometries and accurate energies.
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本文引用的文献

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Crystallization of Escherichia coli aspartyl-tRNA synthetase in its free state and in a complex with yeast tRNA(Asp).
Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):211-4. doi: 10.1107/S090744499500727X.
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The CCP4 suite: programs for protein crystallography.
Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):760-3. doi: 10.1107/S0907444994003112.
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Plasmid systems to study RNA function in Escherichia coli.
J Mol Biol. 2001 Jul 13;310(3):543-8. doi: 10.1006/jmbi.2001.4786.
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Construction of an Escherichia coli knockout strain for functional analysis of tRNA(Asp).
J Mol Biol. 2001 Jul 13;310(3):537-42. doi: 10.1006/jmbi.2001.4785.
6
An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase.
J Mol Biol. 2000 Jun 16;299(4):1051-60. doi: 10.1006/jmbi.2000.3819.
7
Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step.
EMBO J. 1999 Nov 15;18(22):6532-41. doi: 10.1093/emboj/18.22.6532.
8
Correlation of deformability at a tRNA recognition site and aminoacylation specificity.
Proc Natl Acad Sci U S A. 1999 Oct 12;96(21):11764-9. doi: 10.1073/pnas.96.21.11764.
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Crystallography & NMR system: A new software suite for macromolecular structure determination.
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