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Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2016, Volume 113, Issue 8, pp. 2241 - 2246
The 2′,5′-oligoadenylate (2-5A) synthetase (OAS)–RNase L system is an IFN-induced antiviral pathway. RNase L activity depends on 2-5A, synthesized by OAS.... 
2-5A | Oligoadenylate synthetase 3 | Antiviral response | Type I interferon | Ribonuclease L | ENCEPHALOMYOCARDITIS VIRUS | L PATHWAY | HUMAN 2',5'-OLIGOADENYLATE SYNTHETASE | HUMAN-CELLS | MULTIDISCIPLINARY SCIENCES | HUMAN OLIGOADENYLATE SYNTHETASE | CRISPR-CAS9 SYSTEM | RIG-I | oligoadenylate synthetase 3 | VACCINIA VIRUS | antiviral response | type I interferon | MURINE CORONAVIRUS | ribonuclease L | ANTIVIRAL ACTIVITY | Endoribonucleases - genetics | Humans | 2',5'-Oligoadenylate Synthetase - antagonists & inhibitors | Endoribonucleases - antagonists & inhibitors | RNA, Ribosomal - genetics | Alphavirus Infections - genetics | Sindbis Virus | RNA, Viral - genetics | Alphavirus Infections - metabolism | RNA, Viral - metabolism | Virus Diseases - genetics | Vaccinia - metabolism | 2',5'-Oligoadenylate Synthetase - metabolism | Cell Line | Influenza, Human - metabolism | West Nile Fever - genetics | Endoribonucleases - metabolism | RNA, Ribosomal - metabolism | West Nile Fever - metabolism | Virus Diseases - metabolism | Gene Knockout Techniques | Vaccinia - genetics | 2',5'-Oligoadenylate Synthetase - genetics | Models, Biological | Influenza, Human - genetics | CRISPR-Cas Systems | Enzyme Activation | Genetic aspects | Interferon | Host-virus relationships | Gene expression | Observations | Health aspects | RNA polymerases | Biological Sciences
Journal Article
Cell Host & Microbe, ISSN 1931-3128, 02/2019, Volume 25, Issue 2, pp. 336 - 343.e4
Journal Article
Journal Article
EMBO molecular medicine, ISSN 1757-4684, 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
ChemBioChem, ISSN 1439-4227, 06/2017, Volume 18, Issue 12, pp. 1109 - 1116
Genetic code expansion through amber stop codon suppression provides a powerful tool for introducing non‐proteinogenic functionalities into proteins for a... 
aminoacyl–tRNA synthetases | crotonyl lysine | pyrrolysyl–tRNA synthetases | stop codon suppression | directed evolution | PYRROLYSINE ANALOGS | CHEMISTRY, MEDICINAL | aminoacyl-tRNA synthetases | CLICK CHEMISTRY | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | IN-VITRO | MACROCYCLIC PEPTIDES | pyrrolysyl-tRNA synthetases | COLI GENETIC-CODE | RECOMBINANT PROTEINS | RIBOSOMAL SYNTHESIS | ACID MUTAGENESIS | SITE-SPECIFIC INCORPORATION | Protein Biosynthesis | Genetic Code | Ribosomes - metabolism | Cloning, Molecular | Methanosarcina barkeri - genetics | Protein Engineering | Archaeal Proteins - genetics | Lysine - metabolism | Amino Acyl-tRNA Synthetases - metabolism | Amino Acyl-tRNA Synthetases - genetics | Archaeal Proteins - metabolism | Recombinant Proteins - metabolism | Lysine - analogs & derivatives | Methanosarcina barkeri - enzymology | Escherichia coli - enzymology | Bacterial Proteins - genetics | Ribosomes - chemistry | Directed Molecular Evolution | Recombinant Proteins - genetics | Lysine - genetics | High-Throughput Screening Assays | Escherichia coli - genetics | Bacterial Proteins - metabolism | Protein Processing, Post-Translational | Mutation | Codon, Terminator | Codon | Aminoacyl-tRNA synthetases | Lysine | Transfer RNA | Enzymes | Translation | Directed evolution | Amber | tRNA | Genes | Biological evolution | Tools | Amino acids | Stop codon | Colorimetry | Assaying | Proteins | Genetic code | Screening | Functional anatomy | Efficiency | Post-translation | Amber stop codon suppression | pyrrolysyl-tRNA synthetase | orthogonal aminoacyl-tRNA synthetases
Journal Article
Journal Article