X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (2101) 2101
Newsletter (466) 466
Publication (372) 372
Book Chapter (51) 51
Dissertation (35) 35
Book Review (13) 13
Newspaper Article (9) 9
Book / eBook (8) 8
Conference Proceeding (5) 5
Paper (4) 4
Data Set (2) 2
Magazine Article (1) 1
Web Resource (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
aminoacyl-trna synthetases (1363) 1363
transfer rna (1155) 1155
aminoacyl-trna synthetase (781) 781
index medicus (778) 778
biochemistry & molecular biology (743) 743
research (580) 580
trna (476) 476
amino acids (423) 423
humans (421) 421
protein biosynthesis (407) 407
amino acyl-trna synthetases - metabolism (400) 400
molecular sequence data (396) 396
escherichia-coli (380) 380
proteins (340) 340
amino acid sequence (311) 311
animals (305) 305
analysis (301) 301
amino acyl-trna synthetases - genetics (260) 260
aminoacylation (257) 257
enzymes (253) 253
models, molecular (252) 252
base sequence (228) 228
amino acyl-trna synthetases - chemistry (219) 219
transfer-rna-synthetase (219) 219
crystal-structure (217) 217
evolution (216) 216
recognition (211) 211
translation (210) 210
biochemistry (208) 208
genetic code (207) 207
reports (204) 204
mutation (200) 200
ligases (190) 190
escherichia coli - enzymology (188) 188
kinetics (187) 187
cell biology (186) 186
biophysics (182) 182
escherichia coli - genetics (178) 178
binding sites (175) 175
rna, transfer - metabolism (174) 174
multidisciplinary sciences (173) 173
aminoacyl-trna ligase (172) 172
substrate specificity (170) 170
physiological aspects (169) 169
nucleic acid conformation (165) 165
escherichia coli (161) 161
genetic aspects (153) 153
protein synthesis (145) 145
protein conformation (144) 144
article (143) 143
protein binding (139) 139
genetic-code (133) 133
rna (133) 133
protein structure, tertiary (131) 131
universities and colleges (131) 131
aminoacyl-trna (130) 130
evolution, molecular (130) 130
aminoacyl trna synthetase (129) 129
protein (126) 126
crystallography, x-ray (122) 122
life sciences (120) 120
sequence homology, amino acid (114) 114
rna, transfer - genetics (112) 112
binding (111) 111
mitochondria (111) 111
anticodon (107) 107
biological sciences (107) 107
biology (106) 106
catalysis (104) 104
genetics & heredity (104) 104
female (102) 102
rna, transfer - chemistry (102) 102
structure (102) 102
structure-activity relationship (100) 100
bacteria (99) 99
genes (99) 99
synthetase (98) 98
complex (96) 96
genetic research (96) 96
sequence (96) 96
transfer-rna synthetase (95) 95
male (94) 94
sequence alignment (94) 94
genetic translation (93) 93
protein-synthesis (93) 93
molecular biology (88) 88
nucleotides (86) 86
catalytic domain (85) 85
phylogeny (85) 85
yeast (85) 85
codon (83) 83
crystals (83) 83
acylation (82) 82
biochemical research methods (81) 81
expression (80) 80
mechanism (75) 75
escherichia coli - metabolism (74) 74
microbiology (74) 74
structural basis (74) 74
thermus-thermophilus (73) 73
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (2618) 2618
Japanese (17) 17
Chinese (11) 11
Russian (9) 9
Croatian (4) 4
Korean (4) 4
Portuguese (3) 3
German (2) 2
Spanish (2) 2
French (1) 1
Lithuanian (1) 1
Polish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


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
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 | 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
Journal Article
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 09/2010, Volume 11, Issue 9, pp. 668 - 674
Journal Article
Human Mutation, ISSN 1059-7794, 06/2017, Volume 38, Issue 6, pp. 621 - 636
Journal Article