ArticleThe EMBO journal2001
The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
38 citing papers in PubMed, 100 citations in OpenAlex.
- Molecular basis of tRNA substrate recognition and modification by the atypical SPOUT methyltransferase Trm10.Nucleic acids research · 2026Article
- Structure of ergosteryl-aspartate synthase reveals how an entrapped tRNA is used like a prosthetic swinging arm in the synthesis of aminoacylated sterols.Nature communications · 2026Article
- Natural product-mediated reaction hijacking mechanism validates Plasmodium aspartyl-tRNA synthetase as an antimalarial drug target.PLoS pathogens · 2025Article
- Mitochondrial RNA in Inflammation.International journal of biological sciences · 2025Review
- Reaction hijacking inhibition of Plasmodium falciparum asparagine tRNA synthetase.Nature communications · 2024Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Structure and Dynamics of the Human Multi-tRNA Synthetase Complex.Sub-cellular biochemistry · 2022Article
- Mycobacterium tuberculosis Phe-tRNA synthetase: structural insights into tRNA recognition and aminoacylation.Nucleic acids research · 2021Article
- Discovery and Characterization of Chemical Compounds That Inhibit the Function of Aspartyl-tRNA Synthetase from Pseudomonas aeruginosa.SLAS discovery : advancing life sciences R & D · 2018Article
- Drugging tRNA aminoacylation.RNA biology · 2018Review
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- An atlas of RNA base pairs involving modified nucleobases with optimal geometries and accurate energies.Nucleic acids research · 2015Article
- Structure based approach for understanding organism specific recognition of protein-RNA complexes.Biology direct · 2015Article
- Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS.The protein journal · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture.Nucleic acids research · 2013Article
- The asparagine-transamidosome from Helicobacter pylori: a dual-kinetic mode in non-discriminating aspartyl-tRNA synthetase safeguards the genetic code.Nucleic acids research · 2012Article
- Mapping hidden potential identity elements by computing the average discriminating power of individual tRNA positions.DNA research : an international journal for rapid publication of reports on genes and genomes · 2012Article
- PoxA, yjeK, and elongation factor P coordinately modulate virulence and drug resistance in Salmonella enterica.Molecular cell · 2010Article
- Crystal structure of the aspartyl-tRNA synthetase from Entamoeba histolytica.Molecular and biochemical parasitology · 2010Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
The 2.6 A resolution crystal structure of an inactive complex between yeast tRNA(Asp) and Escherichia coli aspartyl-tRNA synthetase reveals the molecular details of a tRNA-induced mechanism that controls the specificity of the reaction. The dimer is asymmetric, with only one of the two bound tRNAs entering the active site cleft of its subunit. However, the flipping loop, which controls the proper positioning of the amino acid substrate, acts as a lid and prevents the correct positioning of the terminal adenosine. The structure suggests that the acceptor stem regulates the loop movement through sugar phosphate backbone- protein interactions. Solution and cellular studies on mutant tRNAs confirm the crucial role of the tRNA three-dimensional structure versus a specific recognition of bases in the control mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.