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The FEBS Journal, ISSN 1742-464X, 02/2019, Volume 286, Issue 3, pp. 536 - 554
The rules of the genetic code are established by aminoacyl‐tRNA synthetases (aaRSs) enzymes, which covalently link tRNA with the cognate amino acid. Many aaRSs... 
protein–protein interaction | BEN1 | disulfide bond | aminoacyl‐tRNA synthetase | brassinosteroid | aminoacyl-tRNA synthetase | TRNA(SER) | BRASSINOSTEROIDS | DOMAIN | SPECIFICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | FLEXIBILITY | MECHANISMS | SUBSTRATE RECOGNITION | TERNARY COMPLEX | GENE | protein-protein interaction | REVEALS | Arabidopsis - enzymology | Saccharomyces cerevisiae - genetics | Substrate Specificity | Crystallography, X-Ray | Serine-tRNA Ligase - chemistry | Serine-tRNA Ligase - metabolism | Alcohol Oxidoreductases - genetics | Arabidopsis Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Serine-tRNA Ligase - genetics | Cloning, Molecular | Brassinosteroids - biosynthesis | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Arabidopsis Proteins - genetics | Gene Expression | Arabidopsis - chemistry | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Alcohol Oxidoreductases - metabolism | Recombinant Proteins - genetics | Arabidopsis - genetics | Sequence Homology, Amino Acid | Two-Hybrid System Techniques | Sequence Alignment | Arabidopsis Proteins - chemistry | Protein Conformation, beta-Strand | Alcohol Oxidoreductases - chemistry | Protein Binding | Kinetics | Arabidopsis thaliana | Crystals | Physiological aspects | Aminoacyl-tRNA synthetases | Structure | Protein-protein interactions | Transfer RNA | Protein binding | Translation | Disulfide bonds | Aminoacylation | Yeast | tRNA | Amino acids | Hormones | Metabolism | Crystallography | Protein turnover | Proteins | Genetic code | Metabolic pathways | Catalysis | Protein structure | Crystal structure
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1992, In focus., ISBN 9780199630400, xv, 112
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Journal of molecular biology, ISSN 0022-2836, 08/2019, Volume 431, Issue 22, pp. 4475 - 4496
Aminoacyl-tRNA synthetases (AARSs) ligate amino acids to their cognate tRNAs during protein synthesis. In humans, eight AARSs and three non-enzymatic... 
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Nature Chemistry, ISSN 1755-4330, 08/2018, Volume 10, Issue 8, pp. 831 - 837
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Human Mutation, ISSN 1059-7794, 01/2013, Volume 34, Issue 1, pp. 191 - 199
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