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Methods, ISSN 1046-2023, 01/2017, Volume 113, pp. 64 - 71
Differential scanning fluorimetry (DSF) is a fluorescence-based assay to evaluate protein stability by determining protein melting temperatures. Here, we... 
Amino acid | tRNA | Differential scanning fluorimetry | Aminoacyl-tRNA synthetase | Histidyl-tRNA synthetase | SYPRO Orange | CRYSTALLIZATION | CARBONIC-ANHYDRASE | PROTEIN | SPECIFICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | THERMAL SHIFT ASSAYS | BOMBYX-MORI | INHIBITION | STRUCTURAL BASIS | PURIFICATION | BINDING | Histidine-tRNA Ligase - antagonists & inhibitors | Protein Unfolding | Amino Acids - chemistry | RNA, Transfer, Amino Acid-Specific - metabolism | Substrate Specificity | Fluorometry - methods | Threonine-tRNA Ligase - genetics | Phase Transition | Histidine-tRNA Ligase - genetics | Threonine-tRNA Ligase - antagonists & inhibitors | Benzopyrans - chemistry | Amino Acids - metabolism | Threonine-tRNA Ligase - chemistry | Alanine-tRNA Ligase - genetics | Enzyme Inhibitors - chemistry | Escherichia coli Proteins - antagonists & inhibitors | Alanine-tRNA Ligase - metabolism | Fluorescent Dyes - chemistry | Transfer RNA Aminoacylation | Histidine-tRNA Ligase - metabolism | Escherichia coli - enzymology | Alanine-tRNA Ligase - antagonists & inhibitors | Muramidase - chemistry | Enzyme Stability | RNA, Transfer, Amino Acid-Specific - genetics | Escherichia coli Proteins - metabolism | Muramidase - metabolism | Histidine-tRNA Ligase - chemistry | Alanine-tRNA Ligase - chemistry | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Escherichia coli Proteins - chemistry | Threonine-tRNA Ligase - metabolism | Ligases | Transfer RNA | Amino acids | Usage | Analysis
Journal Article
Respirology, ISSN 1323-7799, 11/2018, Volume 23, Issue S2, pp. 158 - 158
Journal Article
Respirology, ISSN 1323-7799, 11/2018, Volume 23, Issue S2, pp. 23 - 23
Journal Article
Human Mutation, ISSN 1059-7794, 03/2018, Volume 39, Issue 3, pp. 415 - 432
Journal Article
Proteins: Structure, Function, and Bioinformatics, ISSN 0887-3585, 12/2011, Volume 79, Issue 12, pp. 3448 - 3468
Computational Protein Design (CPD) is a promising method for high throughput protein and ligand mutagenesis. Recently, we developed a CPD method that used a... 
molecular dynamics simulations | Asparaginyl‐tRNA synthetase | computational protein design | implicit solvent models | Poisson Boltzmann calculations | protein‐ligand interactions | generalized Born model | aminoacyl‐tRNA synthetases | genetic code | Generalized Born model | Genetic code | Protein-ligand interactions | Computational protein design | Asparaginyl-tRNA synthetase | Molecular dynamics simulations | Aminoacyl-tRNA synthetases | Implicit solvent models | protein-ligand interactions | aminoacyl-tRNA synthetases | LIGAND-BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | FREE-ENERGY SIMULATIONS | IMPLICIT SOLVENT | AMINOACYLATION REACTION | BIOPHYSICS | FORCE-FIELD | COMPUTER-SIMULATIONS | MOLECULAR-DYNAMICS SIMULATIONS | RANGE ELECTROSTATIC INTERACTIONS | AMINO-ACID SPECIFICITY | CONTINUUM ELECTROSTATICS | Protein Structure, Tertiary | Amino Acid Sequence | Tyrosine-tRNA Ligase - chemistry | Computational Biology - methods | RNA, Transfer, Amino Acyl - chemistry | Amino Acids - chemistry | Models, Molecular | Substrate Specificity | Tyrosine-tRNA Ligase - genetics | Molecular Dynamics Simulation | Protein Folding | Aspartate-tRNA Ligase - genetics | Amino Acids - metabolism | Point Mutation | Aspartate-tRNA Ligase - metabolism | RNA, Transfer, Amino Acyl - metabolism | Protein Binding | Ligands | Protein Conformation | Aspartate-tRNA Ligase - chemistry | Binding Sites | Index Medicus | Tyrosine-tRNA Ligase | RNA, Transfer, Amino Acyl | Biochemistry, Molecular Biology | Computational Biology | Amino Acids | Life Sciences | Aspartate-tRNA Ligase
Journal Article
Human Mutation, ISSN 1059-7794, 08/2014, Volume 35, Issue 8, pp. 983 - 989
ABSTRACT By way of whole‐exome sequencing, we identified a homozygous missense mutation in VARS2 in one subject with microcephaly and epilepsy associated with... 
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
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2010, Volume 107, Issue 33, pp. 14585 - 14590
Aminoacyl-tRNA synthetases (aaRSs) are ancient and evolutionary conserved enzymes catalyzing the formation of aminoacyl-tRNAs, that are used as substrates for... 
Proteins | Enzymes | Active sites | Carrier proteins | Protein synthesis | Amino acids | Biosynthesis | Kinetics | Transfer RNA | Prosthetics | Amino acid:[carrier protein] ligase | Seryl-tRNA synthetase | Noncanonical functions of aaRs | AaRS homologs | amino acid:[carrier protein] ligase | ANTIBIOTICS | aaRS homologs | MULTIDISCIPLINARY SCIENCES | COENZYME-A | SUBSTRATE RECOGNITION | seryl-tRNA synthetase | GENETIC-CODE | SERYL-TRANSFER-RNA | INHIBITION | BIOSYNTHESIS | noncanonical functions of aaRS | PARALOG | REVEALS | LIGASE | Bacterial Proteins - chemistry | Peptide Biosynthesis, Nucleic Acid-Independent | Agrobacterium tumefaciens - genetics | Molecular Sequence Data | Ribosomes - metabolism | Crystallography, X-Ray | Serine-tRNA Ligase - chemistry | Serine-tRNA Ligase - metabolism | Serine-tRNA Ligase - genetics | Bradyrhizobium - metabolism | Amino Acyl-tRNA Synthetases - chemistry | Amino Acyl-tRNA Synthetases - metabolism | Acylation | Amino Acyl-tRNA Synthetases - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Transfer RNA Aminoacylation | Catalytic Domain | Biocatalysis | Bacterial Proteins - genetics | Models, Molecular | Alanine - metabolism | Sequence Homology, Amino Acid | Bradyrhizobium - genetics | Carrier Proteins - genetics | Carrier Proteins - metabolism | Agrobacterium tumefaciens - metabolism | Models, Biological | Bacterial Proteins - metabolism | Protein biosynthesis | Biochemical genetics | Chemical properties | Research | Observations | Properties | Aminoacyl-tRNA synthetases | Translation | AMP | tRNA | Genomes | Methanogenic archaea | Genetic code | Enzymatic activity | Prosthetic groups | Ribosomal proteins | Evolutionary conservation | genomics | Peptide synthesis | Adenylation | Aminoacyl-tRNA ligase | Serine-tRNA ligase | Biological Sciences
Journal Article
Journal Article
EMBO Molecular Medicine, ISSN 1757-4676, 03/2013, Volume 5, Issue 3, pp. 332 - 343
Aminoacyl‐tRNA synthetases (ARSs) are essential and ubiquitous ‘house‐keeping’ enzymes responsible for charging amino acids to their cognate tRNAs and... 
therapeutics | tRNA | human disease | aminoacyl‐tRNA synthetases (ARSs) | Aminoacyl-tRNA synthetases (ARSs) | Human disease | TRNA | Therapeutics | ANTIFUNGAL AGENT | MEDICINE, RESEARCH & EXPERIMENTAL | aminoacyl-tRNA synthetases (ARSs) | BRAIN-STEM | NONCANONICAL FUNCTION | PROTEIN-SYNTHESIS | LEUKOENCEPHALOPATHY | GENE | CAUSES MYOPATHY | LACTIC-ACIDOSIS | MUTATIONS | SPINAL-CORD INVOLVEMENT | Aminoacylation | Charcot-Marie-Tooth Disease - enzymology | Humans | Fungal Proteins - antagonists & inhibitors | Antifungal Agents - therapeutic use | Charcot-Marie-Tooth Disease - genetics | Anti-Bacterial Agents - therapeutic use | Amino Acyl-tRNA Synthetases - metabolism | Amino Acyl-tRNA Synthetases - genetics | Mitochondrial Diseases - genetics | Bacterial Proteins - antagonists & inhibitors | Enzyme Replacement Therapy | Mitochondrial Diseases - drug therapy | Genetic Predisposition to Disease | Gene Expression Regulation | Charcot-Marie-Tooth Disease - drug therapy | Mitochondrial Diseases - enzymology | Amino Acyl-tRNA Synthetases - therapeutic use | Phenotype | Animals | Bacterial Proteins - metabolism | Protein Biosynthesis - drug effects | Mutation | Amino Acyl-tRNA Synthetases - antagonists & inhibitors | Fungal Proteins - metabolism | Aminoacyl-tRNA synthetases | Protein biosynthesis | Transfer RNA | Heart | Enzymes | Editing | Exploration | Cardiovascular disease | Amino acids | Mammals | Hearing impairment | Peripheral neuropathy | Cell adhesion & migration | Proteins | Signal transduction | Angiogenesis | Genotype & phenotype | Antibiotics | Protein synthesis | Etiology | Ataxia | Autoimmune diseases | Reviews
Journal Article