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threonine-trna ligase - metabolism (96) 96
threonine-trna ligase - genetics (61) 61
molecular sequence data (42) 42
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threonine-trna ligase - chemistry (32) 32
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threonine-trna ligase - antagonists & inhibitors (16) 16
amino acids (15) 15
aminoacylation (15) 15
escherichia coli - metabolism (15) 15
multidisciplinary sciences (15) 15
protein structure, tertiary (15) 15
proteins (15) 15
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trna (15) 15
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saccharomyces cerevisiae - enzymology (14) 14
threonyl-trna synthetase (14) 14
ligases (13) 13
protein-synthesis (13) 13
rna, messenger - genetics (13) 13
rna, transfer - metabolism (13) 13
threonine-trna ligase - isolation & purification (13) 13
translation (13) 13
aminoacyl-trna synthetase (12) 12
crystallography, x-ray (12) 12
saccharomyces cerevisiae - genetics (12) 12
threonine-trna ligase (12) 12
active-site (11) 11
aminoacyl-trna synthetases (11) 11
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genes, bacterial (11) 11
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rna editing (11) 11
rna, transfer, amino acyl - metabolism (11) 11
zinc ion (11) 11
catalytic domain (10) 10
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expression (10) 10
messenger-rna (10) 10
rna, transfer, thr - genetics (10) 10
threonine (10) 10
transfer rna aminoacylation (10) 10
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Human Mutation, ISSN 1059-7794, 08/2014, Volume 35, Issue 8, pp. 983 - 989
By way of whole‐exome sequencing, we identified a homozygous missense mutation in VARS2 in one subject with microcephaly and epilepsy associated with isolated... 
aminoacyl tRNA syntethases | TARS2 | encephalomyopathy | VARS2 | OXPHOS defect | mitochondrial disease | Encephalomyopathy | Aminoacyl tRNA syntethases | Mitochondrial disease | CELLS | CARDIOMYOPATHY | INVOLVEMENT | BRAIN-STEM | TRANSFER-RNA SYNTHETASES | LEUKOENCEPHALOPATHY | GENE | DISEASE | GENETICS & HEREDITY | LACTIC-ACIDOSIS | COMPLEX-I DEFICIENCY | Mitochondria - enzymology | Saccharomyces cerevisiae - genetics | Humans | Mitochondrial Encephalomyopathies - enzymology | Infant | Male | Threonine-tRNA Ligase - genetics | HLA Antigens - genetics | RNA, Messenger - metabolism | Electron Transport Complex I - metabolism | Saccharomyces cerevisiae - metabolism | RNA, Transfer, Val - genetics | DNA, Mitochondrial - genetics | Mitochondria - genetics | Electron Transport Complex I - genetics | Isoenzymes - metabolism | Valine-tRNA Ligase - metabolism | Valine-tRNA Ligase - genetics | Child | RNA, Transfer, Thr - genetics | Fibroblasts - metabolism | Cell Line | DNA, Mitochondrial - metabolism | RNA, Transfer, Thr - metabolism | Isoenzymes - genetics | Mitochondrial Encephalomyopathies - genetics | RNA, Messenger - genetics | Mitochondria - pathology | HLA Antigens - metabolism | Polymorphism, Genetic | Mitochondrial Encephalomyopathies - pathology | RNA, Transfer, Val - metabolism | Homozygote | Heterozygote | Fibroblasts - cytology | Mutation | Threonine-tRNA Ligase - metabolism | Proteins | Care and treatment | Analysis | Epilepsy | Genetic aspects | Single nucleotide polymorphisms | Aminoacyl-tRNA synthetases | Transfer RNA | Index Medicus
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2013, Volume 8, Issue 12, pp. e81734 - e81734
Twenty different aminoacyl-tRNA synthetases (ARSs) link each amino acid to their cognate tRNAs. Individual ARSs are also associated with various non-canonical... 
BREAST-CANCER | TARGET | SIGNAL | AIMP2 | PROTEIN INTERACTIONS | FANCD2 | INTERACTS | MULTIDISCIPLINARY SCIENCES | C-MYC | ASSIGNMENT | TRANSLATION | Humans | Molecular Sequence Data | Neoplasm Proteins - metabolism | Cytokines - chemistry | Mass Spectrometry | HEK293 Cells | Carrier Proteins - chemistry | Amino Acyl-tRNA Synthetases - chemistry | Amino Acyl-tRNA Synthetases - metabolism | Amino Acid Sequence | Computational Biology - methods | Threonine-tRNA Ligase - analysis | Cytokines - metabolism | RNA-Binding Proteins - chemistry | Neoplasm Proteins - chemistry | Nuclear Proteins | Protein Interaction Mapping - methods | Algorithms | Carrier Proteins - metabolism | Chromatography, Affinity | Threonine-tRNA Ligase - isolation & purification | Lysine-tRNA Ligase - metabolism | Protein Processing, Post-Translational | RNA-Binding Proteins - metabolism | Threonine-tRNA Ligase - metabolism | Physiological aspects | Usage | Research | Aminoacyl-tRNA synthetases | Mass spectrometry | Multiple sclerosis | Biomedical research | Peptides | Amino acids | Kinases | Proteins | Signal transduction | Cell growth | Tumor necrosis factor-TNF | Life sciences | Spectroscopy | Purification | tRNA | Threonine-tRNA ligase | Cloning | Mass spectroscopy | Topology | Precipitates | Computer science | Contaminants | Affinity | Scientific imaging | Autoimmune diseases | Aminoacyl-tRNA ligase | Cancer | Apoptosis | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2010, Volume 107, Issue 51, pp. 22117 - 22121
Editing/proofreading by aminoacyl-tRNA synthetases is an important quality control step in the accurate translation of the genetic code that removes noncognate... 
Enzymes | Molecules | Quality assurance | Active sites | Proofreading | Amino acids | Titration | Electron density | Functional groups | Transfer RNA | X-ray crystallography | Editing | Enzyme mechanism | Aminoacyl-tRNA synthetases | Double-sieve model | DOMAIN | aminoacyl-tRNA synthetases | EDITING MECHANISM | RECOGNITION | MULTIDISCIPLINARY SCIENCES | QUALITY-CONTROL | PROTEIN-SYNTHESIS | editing | DEACYLASE | ARCHAEA | TRANSFER-RNA SYNTHETASE | double-sieve model | enzyme mechanism | SELECTION | Archaeal Proteins - metabolism | Protein Structure, Tertiary | Catalytic Domain | RNA, Transfer - metabolism | Humans | RNA, Archaeal - chemistry | Archaeal Proteins - chemistry | Protein Biosynthesis - physiology | Substrate Specificity | Crystallography, X-Ray | Threonine-tRNA Ligase - genetics | Threonine-tRNA Ligase - chemistry | RNA, Archaeal - metabolism | Nuclear Magnetic Resonance, Biomolecular | RNA, Transfer - genetics | Archaeal Proteins - genetics | Catalysis | RNA, Archaeal - genetics | RNA, Transfer - chemistry | Pyrococcus abyssi - enzymology | Threonine-tRNA Ligase - metabolism | Substrates (Biochemistry) | Physiological aspects | Genetic aspects | Research | Properties | Genetic translation | Genetics | Molecular structure | Binding sites | Index Medicus | Translation | RNA | Threonine-tRNA ligase | tRNA | Crystals | Hydrolysis | Genetic code | Neurodegeneration | Quality control | Calorimetry | Aminoacyl-tRNA ligase | Biological Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2012, Volume 109, Issue 9, pp. 3281 - 3286
Aminoacyl-tRNA synthetases (aaRSs) ensure faithful translation of mRNA into protein by coupling an amino acid to a set of tRNAs with conserved anticodon... 
Yeasts | Enzymes | Active sites | Crystals | Amino acids | Biochemistry | Codons | Anticodon | Transfer RNA | Crystal structure | Protein synthesis | Anticodon recognition | DOMAIN | PROTEIN | ZINC ION | MULTIDISCIPLINARY SCIENCES | protein synthesis | DUAL-MODE RECOGNITION | QUALITY-CONTROL | IDENTITY | IN-VITRO | MISTRANSLATION | DISCRIMINATION | anticodon recognition | ANTICODON LOOP | Mitochondria - enzymology | Staphylococcus aureus - enzymology | Species Specificity | RNA Editing | Saccharomyces cerevisiae - genetics | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Threonine-tRNA Ligase - genetics | Leucine | Threonine-tRNA Ligase - chemistry | RNA, Transfer, Amino Acyl - metabolism | Codon - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Catalytic Domain | Escherichia coli - enzymology | Threonine | Anticodon - genetics | Models, Molecular | RNA, Transfer, Amino Acyl - genetics | Saccharomyces cerevisiae Proteins - genetics | Sequence Alignment | Saccharomyces cerevisiae Proteins - metabolism | Aeropyrum - enzymology | Saccharomyces cerevisiae - enzymology | Protein Conformation | Threonine-tRNA Ligase - metabolism | Evolution, Molecular | Saccharomyces cerevisiae Proteins - chemistry | Mitochondria | Yeast fungi | RNA | Physiological aspects | Protein biosynthesis | Genetic aspects | Research | Molecular structure | Binding sites | Anticodons | Aminoacylation | Isoacceptors | Translation | Threonine-tRNA ligase | tRNA | Data processing | Genetic code | Aminoacyl-tRNA ligase | Index Medicus | ESCHERICHIA COLI | TRIPLETS | BASIC BIOLOGICAL SCIENCES | MITOCHONDRIA | SACCHAROMYCES CEREVISIAE | CRYSTAL STRUCTURE | SIMULATION | 60 APPLIED LIFE SCIENCES | CODONS | GENETICS | AMINO ACIDS | ENZYMES | YEASTS | LIGASES | SYNTHESIS | LEUCINE | PROTEINS | THREONINE | Biological Sciences
Journal Article
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 2016, Volume 44, Issue 3, pp. 1428 - 1439
Journal Article
Plant Cell Reports, ISSN 0721-7714, 07/2017, Volume 36, Issue 7, pp. 1053 - 1064
Key message An albinic rice is caused by mutation of threonyl-tRNA synthetase, which is essential for plant development by stabilizing of NEP and PEP gene... 
Oryza sativa | Chloroplast development | Plastid-encoded RNA polymerase | Chloroplast protein synthesis | ARABIDOPSIS-THALIANA | MITOCHONDRIA | POLYMERASE | EARLY LEAF DEVELOPMENT | PLANT SCIENCES | EMBRYO DEVELOPMENT | NUCLEUS | GENE-EXPRESSION | CHLOROPLAST RIBOSOME BIOGENESIS | TRANSCRIPTION MACHINERIES | MAIZE | Chloroplast Proteins - genetics | Plants, Genetically Modified - genetics | Oryza - metabolism | Gene Expression Regulation, Plant - genetics | Seedlings - genetics | Threonine-tRNA Ligase - genetics | Seedlings - enzymology | Oryza - enzymology | Chloroplasts - metabolism | Plant Proteins - genetics | Plastids - enzymology | Plants, Genetically Modified - metabolism | Oryza - genetics | Genes, Plant - genetics | Gene Expression Regulation, Plant - physiology | Plastids - genetics | Plastids - metabolism | Plant Proteins - metabolism | Mutation | Chloroplast Proteins - metabolism | Chloroplasts - genetics | Threonine-tRNA Ligase - metabolism | Seedlings - metabolism | Proteins | Chlorophyll | Yuan (China) | Analysis | Genes | Plant genetics | Genetically modified organisms | Protein biosynthesis | Genetic engineering | Aminoacyl-tRNA synthetases | Genetic translation | Transfer RNA | rRNA 16S | Fluorescence | Biosynthesis | Plants (organisms) | Accumulation | Leaves | Chloroplasts | Coding | Evolution | Physiology | Pep gene | Rice | Construction | tRNA | Splicing | Threonine-tRNA ligase | Cloning | rRNA 23S | Gene expression | Ribonucleic acids | Protein synthesis | Index Medicus
Journal Article
Journal Article
Molecular Biology and Evolution, ISSN 0737-4038, 11/2008, Volume 25, Issue 11, pp. 2369 - 2389
A comparative genomic analysis of 35 cyanobacterial strains has revealed that the gene complement of aminoacyl-tRNA synthetases (AARSs) and routes for... 
Gene duplication | Phylogeny | Aminoacyl-tRNA synthetase | Cyanobacteria | Domain shuffling | Horizontal gene transfer | ASPARAGINE SYNTHETASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COLI YADB GENE | domain shuffling | MITOCHONDRIAL-DNA | horizontal gene transfer | MULTIPLE SEQUENCE ALIGNMENT | EVOLUTIONARY BIOLOGY | COMPLETE GENOME STRUCTURE | MOLECULAR PHYLOGENETICS | aminoacyl-tRNA synthetase | gene duplication | GLUTAMINYL-TRANSFER-RNA | HISTIDYL-TRANSFER-RNA | cyanobacteria | GENETICS & HEREDITY | phylogeny | HORIZONTAL GENE-TRANSFER | NUCLEOTIDE-SEQUENCE | Cyanobacteria - genetics | Gene Duplication | Cyanobacteria - classification | Threonine-tRNA Ligase - genetics | RNA, Transfer, Gln - metabolism | RNA, Transfer, Asn - metabolism | Histidine-tRNA Ligase - genetics | Genetic Variation | Arginine-tRNA Ligase - genetics | Aspartate-tRNA Ligase - metabolism | RNA, Transfer, Amino Acyl - metabolism | Amino Acyl-tRNA Synthetases - metabolism | RNA, Bacterial - metabolism | Amino Acyl-tRNA Synthetases - genetics | Protein Structure, Tertiary | Genome, Bacterial | Histidine-tRNA Ligase - metabolism | Bacterial Proteins - genetics | Arginine-tRNA Ligase - metabolism | RNA, Transfer, Amino Acyl - genetics | Cyanobacteria - enzymology | Amino Acid Motifs | Aspartate-tRNA Ligase - genetics | Glutamate-tRNA Ligase - metabolism | Glutamate-tRNA Ligase - genetics | Threonine-tRNA Ligase - metabolism | Evolution, Molecular | Proteins | Bacteria | Evolutionary biology | Molecular biology | Genomics | Index Medicus
Journal Article