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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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L-tryptophan + ATP
L-Trp-adenylate + diphosphate
the enzyme also catalyzes the exchange of diphosphate in the diphosphate-ATP exchange assay
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r
additional information
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
involvement of heme in regulation of TrpRS aminoacylation activity
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
bovine tRNATrp substrate, a two step reaction, the tryptophanyl-tRNA synthetase is a class I amino acid tRNA-synthetase, that catalyzes tryptophan activation in the absence of its cognate tRNA, cognate tRNA is not obligatory to catalyze amino acid activation, the integrated 3 end of the tRNA is necessary to activate the ATP-diphosphate exchange reaction, overview
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
tRNA substrate from Bos taurus, a two step reaction: the amino acid is first activated by ATP to form an aminoacyl-AMP, which is then transferred to the 3' end of the cognate tRNA to form an aminoacyl-tRNA, the discriminator base A73 of the tRNA is specifically recognized by an alpha-helix of the unique N-terminal domain and the anticodon loop by an alpha-helix insertion of the C-terminal domain, the N-terminal domain is involved in Trp activation, but is not essential for tRNA binding and acylation, tryptophan, anticodon, and acceptor arm recognition mechanisms, overview
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
tRNA substrate from Bos taurus, tryptophan binding pocket structure, overview, two distinct tRNA conformations: uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits, in this cross-dimer tRNA complex, the class I enzyme has a class II-like tRNA binding mode, the aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF-1a, suggesting that the product of aminoacylation can be directly handed off to EF-1alpha for the next step of protein synthesis, recognition mechanisms, overview
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
tRNA substrate from Saccharomyces cerevisiae
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
full-length and mini enzyme isoforms
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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enzyme contributes to biological processes involving cell signaling such as angiogenesis regulation
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
full-length and mini enzyme isoforms, enzyme expression is regulated by a dual system of interferon gamma and interferon regulatory factor 1 via 2 specific tandem promoters leading to alternative splicing
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
human mini, but not full-length, tryptophanyl-tRNA synthetase may play an important role in the intracellular regulation of protein synthesis under conditions of oxidative stress
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additional information
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the catalytic fragment exhibits potent angiostatic activity
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additional information
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the catalytic fragment exhibits potent angiostatic activity
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additional information
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the enzyme interacts directly with elongation factor 1alpha, which carries charged tRNA to the ribosome
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additional information
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the enzyme interacts directly with elongation factor 1alpha, which carries charged tRNA to the ribosome
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additional information
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vascular endothelial cadherins tryptophan side chains fit into the tryptophan-specific active site of the synthetase
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?
additional information
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vascular endothelial cadherins tryptophan side chains fit into the tryptophan-specific active site of the synthetase
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additional information
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binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
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additional information
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binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
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additional information
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potential complex formation between TLR4-MD2 and the WRS monomer, putative binding model of TLR4-MD2 with the enzyme WRS homodimer based on a protein-protein docking study, complex crystal structure analysis, overview
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additional information
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potential complex formation between TLR4-MD2 and the WRS monomer, putative binding model of TLR4-MD2 with the enzyme WRS homodimer based on a protein-protein docking study, complex crystal structure analysis, overview
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additional information
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mini isozyme specifically shows anti-proliferative and anti-angiogenic activity
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additional information
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the enzymes C-terminal domain, an EMAP II-like protein, inhibits angiogenesis signaling pathways and the development of blood vessels
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additional information
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interferon-gamma-inducible enzyme. Exposure to soluble cytotoxic T lymphocyte antigen-4 induces increased expression of tryptophanyl-tRNA synthetase in unseparated peripheral blood mononuclear cells, as well as in monocyte-derived mature dentritic cells. CD4+ cells and CD8+ cells isolated from peripheral blood mononuclear cells treated with soluble cytotoxic T lymphocyte antigen-4 show increased tryptophanyl-tRNA synthetase compared with untreated cells. Possibility that tryptophanyl-tRNA synthetase may be involved in an important mechanism regulating immune response
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additional information
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the vascular endothelial-cadherin-dependent pathway is proposed to link T2-TrpRS to inhibition of new blood vessel formation
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additional information
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tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
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?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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?
additional information
?
-
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
-
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophanyl-tRNATrp
involvement of heme in regulation of TrpRS aminoacylation activity
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
-
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?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
-
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophyl-tRNATrp
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?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
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ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
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?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
-
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?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
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?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
enzyme contributes to biological processes involving cell signaling such as angiogenesis regulation
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?
ATP + L-tryptophan + tRNATrp
AMP + diphosphate + L-tryptophan-tRNATrp
-
full-length and mini enzyme isoforms, enzyme expression is regulated by a dual system of interferon gamma and interferon regulatory factor 1 via 2 specific tandem promoters leading to alternative splicing
-
?
additional information
?
-
the catalytic fragment exhibits potent angiostatic activity
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?
additional information
?
-
-
the catalytic fragment exhibits potent angiostatic activity
-
?
additional information
?
-
binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
-
-
?
additional information
?
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-
binding of vascular endothelial (VE)-cadherin, the NH2-terminal Trp2 and Trp4 residues of VE-cadherin are docked into the Trp- and adenosine-binding pockets of human TrpRS
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-
?
additional information
?
-
-
mini isozyme specifically shows anti-proliferative and anti-angiogenic activity
-
?
additional information
?
-
-
the enzymes C-terminal domain, an EMAP II-like protein, inhibits angiogenesis signaling pathways and the development of blood vessels
-
?
additional information
?
-
-
interferon-gamma-inducible enzyme. Exposure to soluble cytotoxic T lymphocyte antigen-4 induces increased expression of tryptophanyl-tRNA synthetase in unseparated peripheral blood mononuclear cells, as well as in monocyte-derived mature dentritic cells. CD4+ cells and CD8+ cells isolated from peripheral blood mononuclear cells treated with soluble cytotoxic T lymphocyte antigen-4 show increased tryptophanyl-tRNA synthetase compared with untreated cells. Possibility that tryptophanyl-tRNA synthetase may be involved in an important mechanism regulating immune response
-
-
?
additional information
?
-
-
the vascular endothelial-cadherin-dependent pathway is proposed to link T2-TrpRS to inhibition of new blood vessel formation
-
-
?
additional information
?
-
-
tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell models, the dietary supplementation with tryptophan as a tryptamine competitor may not counteract the deleterious influence of tryptamine, overview
-
-
?
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Acidosis, Lactic
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Acidosis, Lactic
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) Due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Alzheimer Disease
Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease.
Alzheimer Disease
Synthetic Peptide Corresponding to The Amino-Terminal Region of the Human Tryptophanyl-Trna Synthetase, a Component Of Alzheimer'S Disease Special Congophlic Plaques Aggregates In Vitro to Form Amyloid-Like Fibrils.
Ataxia
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Athetosis
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Brain Diseases
Biallelic variants in WARS2 encoding mitochondrial tryptophanyl-tRNA synthase in six individuals with mitochondrial encephalopathy.
Breast Neoplasms
Concurrent Gene Signatures for Han Chinese Breast Cancers.
Breast Neoplasms
Tryptophanyl-tRNA Synthetase Sensitizes Hormone Receptor-Positive Breast Cancer to Docetaxel-Based Chemotherapy.
Carcinogenesis
Tryptamine-mediated stabilization of tryptophanyl-tRNA synthetase in human cervical carcinoma cell line.
Carcinoma
Tryptamine-mediated stabilization of tryptophanyl-tRNA synthetase in human cervical carcinoma cell line.
Colonic Neoplasms
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Colorectal Neoplasms
Hypoxia signature of splice forms of tryptophanyl-tRNA synthetase marks pancreatic cancer cells with distinct metastatic abilities.
Colorectal Neoplasms
Identification of differential proteins in colorectal cancer cells treated with caffeic acid phenethyl ester.
Colorectal Neoplasms
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Dyskinesias
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Dyskinesias
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) Due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Epilepsy
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Eye Diseases
A fragment of human TrpRS as a potent antagonist of ocular angiogenesis.
Gastrointestinal Stromal Tumors
Role of Immune Microenvironment in Gastrointestinal Stromal Tumors.
Hyperkinesis
Mutation of the WARS2 Gene as the Cause of a Severe Hyperkinetic Movement Disorder.
Infections
Corrigendum: Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection.
Infections
Secreted tryptophanyl-tRNA synthetase as a primary defence system against infection.
Intellectual Disability
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Intellectual Disability
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Intellectual Disability
Mutations of the aminoacyl-tRNA-synthetases SARS and WARS2 are implicated in the etiology of autosomal recessive intellectual disability.
Leukemia
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Leukemia, Myeloid
Interferons induce accumulation of diadenosine triphosphate (Ap3A) in human cultured cells.
Leukoencephalopathies
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Leukoencephalopathies
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Leukoencephalopathies
Mutations in the mitochondrial tryptophanyl-tRNA synthetase cause growth retardation and progressive leukoencephalopathy.
Lymphatic Metastasis
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Lymphoma
Design and synthesis of novel spirooxindole-indenoquinoxaline derivatives as novel tryptophanyl-tRNA synthetase inhibitors.
Lymphoma, B-Cell
Design and synthesis of novel spirooxindole-indenoquinoxaline derivatives as novel tryptophanyl-tRNA synthetase inhibitors.
Lymphoma, Large B-Cell, Diffuse
Design and synthesis of novel spirooxindole-indenoquinoxaline derivatives as novel tryptophanyl-tRNA synthetase inhibitors.
Malaria
An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase.
Melanoma
Tryptophanyl-tRNA synthetase (WARS) expression in uveal melanoma - possible contributor during uveal melanoma progression.
Microcephaly
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Mitochondrial Diseases
Biallelic variants in WARS2 encoding mitochondrial tryptophanyl-tRNA synthase in six individuals with mitochondrial encephalopathy.
Mitochondrial Diseases
Mutations in the mitochondrial tryptophanyl-tRNA synthetase cause growth retardation and progressive leukoencephalopathy.
Mouth Neoplasms
Overexpressed tryptophanyl-tRNA synthetase, an angiostatic protein, enhances oral cancer cell invasiveness.
Movement Disorders
Co-occurring WARS2 and CHRNA6 mutations in a child with a severe form of infantile parkinsonism.
Movement Disorders
Mutation of the WARS2 Gene as the Cause of a Severe Hyperkinetic Movement Disorder.
Myocardial Infarction
Different angiogenesis effect of mini-TyrRS/mini-TrpRS by systemic administration of modified siRNAs in rats with acute myocardial infarction.
Myocardial Infarction
Effect of mini-tyrosyl-tRNA synthetase/mini-tryptophanyl-tRNA synthetase on ischemic angiogenesis in rats: proliferation and migration of endothelial cells.
Myocardial Infarction
Tryptophanyl-tRNA synthetase gene polymorphisms and risk of incident myocardial infarction.
Neoplasm Metastasis
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Neoplasms
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Neoplasms
Differential protein synthesis and expression levels in normal and neoplastic human prostate cells and their regulation by type I and II interferons.
Neoplasms
Evidence for the involvement of SDF-1 and CXCR4 in the disruption of endothelial cell-branching morphogenesis and angiogenesis by TNF-alpha and IFN-gamma.
Neoplasms
Hypoxia signature of splice forms of tryptophanyl-tRNA synthetase marks pancreatic cancer cells with distinct metastatic abilities.
Neoplasms
Overexpressed tryptophanyl-tRNA synthetase, an angiostatic protein, enhances oral cancer cell invasiveness.
Neoplasms
Prediction of Recurrence and Survival for Triple-Negative Breast Cancer (TNBC) by a Protein Signature in Tissue Samples.
Neoplasms
Role of Immune Microenvironment in Gastrointestinal Stromal Tumors.
Neoplasms
The prognostic significance of tryptophanyl-tRNA synthetase in colorectal cancer.
Neoplasms
The role of indoleamine 2,3-dioxygenase in the anti-tumour activity of human interferon-gamma in vivo.
Neuroblastoma
Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease.
Neurodegenerative Diseases
Tryptamine Induces Tryptophanyl-tRNA Synthetase-Mediated Neurodegeneration With Neurofibrillary Tangles in Human Cell and Mouse Models.
Obesity, Abdominal
Mutant Wars2 gene in spontaneously hypertensive rats impairs brown adipose tissue function and predisposes to visceral obesity.
Ovarian Neoplasms
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Pancreatic Neoplasms
Hypoxia signature of splice forms of tryptophanyl-tRNA synthetase marks pancreatic cancer cells with distinct metastatic abilities.
Pancreatic Neoplasms
Mapping and molecular characterization of novel monoclonal antibodies to conformational epitopes on NH2 and COOH termini of mammalian tryptophanyl-tRNA synthetase reveal link of the epitopes to aggregation and Alzheimer's disease.
Parkinsonian Disorders
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
Parkinsonian Disorders
Co-occurring WARS2 and CHRNA6 mutations in a child with a severe form of infantile parkinsonism.
Protein Deficiency
Diet-Related Metabolic Perturbations of Gut Microbial Shikimate Pathway-Tryptamine-tRNA Aminoacylation-Protein Synthesis in Human Health and Disease.
Quadriplegia
Deficiency of WARS2, encoding mitochondrial tryptophanyl tRNA synthetase, causes severe infantile onset leukoencephalopathy.
Renal Insufficiency, Chronic
Serum levels and activity of indoleamine2,3-dioxygenase and tryptophanyl-tRNA synthetase and their association with disease severity in patients with chronic kidney disease.
Sarcoma, Avian
Chaperon-like Activation of Serum-Inducible Tryptophanyl-tRNA Synthetase Phosphorylation through Refolding as a Tool for Analysis of Clinical Samples.
Seizures
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Seizures
Expanding the Phenotype: Neurodevelopmental Disorder, Mitochondrial, With Abnormal Movements and Lactic Acidosis, With or Without Seizures (NEMMLAS) Due to WARS2 Biallelic Variants, Encoding Mitochondrial Tryptophanyl-tRNA Synthase.
Sepsis
Clinical value of full-length tryptophanyl-tRNA synthetase for sepsis detection in critically ill patients - A retrospective clinical assessment.
Stomach Neoplasms
Expression of Indoleamine 2, 3-dioxygenase 1 (IDO1) and Tryptophanyl-tRNA Synthetase (WARS) in Gastric Cancer Molecular Subtypes.
tryptophan-trna ligase deficiency
Biallelic mutations in mitochondrial tryptophanyl-tRNA synthetase cause Levodopa-responsive infantile-onset Parkinsonism.
tryptophan-trna ligase deficiency
Severe hepatopathy and neurological deterioration after start of valproate treatment in a 6-year-old child with mitochondrial tryptophanyl-tRNA synthetase deficiency.
Virus Diseases
Released Tryptophanyl-tRNA Synthetase Stimulates Innate Immune Responses against Viral Infection.
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catalytic fragment, hanging drop method, 0.002 ml protein solution: 8 mg/ml protein, 20 mM Tris-potassium phosphate, pH 6.8, 10 mM MgCl2, 5 mM 2-mercaptoethanol, plus equal volume of reservoir solution: 16% w/v polyethylene glycol 1500, 4% polyehylene glycol 3350, 0.2 M trisodium citrate dihydrate, pH 8.2, plus 0.0005 ml 30% 2-methyl-2,4-pentanediol, 7-10 days, 4°C, proteolytic cleavage of the enzyme into 2 fragments occurs during the crystallization process, X-ray diffraction structure determination at 2.5 A resolution using the MAD method, and analysis
crystal structure determination at 2.1 A resolution of the enzyme with a tryptophanyladenylate bound at the active site, cocrystal structure determination at 1.6 A resolution of an active fragment of the enzyme with its cognate amino acid analogue
crystal structure of hTrpRS in complexes with Trp, tryptophanamide and ATP and tryptophanyl-AMP, respectively, are all determined at 2.4 A resolution
crystals of native mini TrpRS are obtained by hanging-drop vapor diffusion at 4°C, crystal structure of human mini TrpRS is determined at a resolution of 2.3 A
purified protein in complex with uncharged tRNA and aminoacylated tRNA in a 1:1 mixture, sitting drop vapour diffusion method, 0.002 ml of protein in 10 mM HEPES, pH 7.5, 20 mM KCl, 0.02% NaN3, and 2 mM 2-mercaptoethanol, addition of 230 mM of TrpRS, 250 mM of tRNATrp, 5 mM tryptophan and 10 mM AMP-PNP, mixed with 0.002 ml reservoir solution containing 2 M ammonium sulfate and 0.1 M HEPES pH 6.9, 4°C, X-ray diffraction structure determination and analysis at 2.9 A resolution, SAD method using a selenium-labeled crystal
purified recombinant enzyme in complex with bovine tRNATrp, hanging drop vapor diffusion method, 4°C, 0.002 ml of protein solution containing 8 mg/ml of TrpRS with an equal amount of tRNA, 10 mM ATP, 1 mM Trp, 20 mM K2HPO4, pH 6.8, 10 mM MgCl2, 5 mM 2-mercaptoethanol and 0.5 mM PMSF, mixed with 0.002 ml reservoir solution containing 2 M (NH4)2SO4 and 50 mM HEPES, pH 7.0, 1-2 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, modeling
structure of full length TrpRS is solved at 2.1 A, structure of mini-TRpRS is solved at 2.0 A
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A310W
T2-TrpRS mutant, AMP pocket is blocked, angiostatic activity involves the tryptophan and adenosine pockets
A7D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
D382-TIEEHR-Q389
deletion of the tRNA anticodon-binding domain insertion, consisting of eight residues in the human TrpRS, abolishes the apoptotic activity of the enzyme for endothelial cells, whereas its translational catalysis and cell-binding activities remain unchanged
D99A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
D99E
site-directed mutagenesis, the mutant shows slightly reduced activity and kcat compared to the wild-type enzyme
D99K
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
D99V
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
E11L
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
E35G
site-directed mutagenesis, the mutant shows similar induction of TNF-alpha and MIP-1alpha production compared to wild-type
E451Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
G161W
T2-TrpRS mutant, tryptophan pocket is blocked by the bulky indole side chain of the tryptophan introduced at position 161, angiostatic activity involves the tryptophan and adenosine pockets
G172M
T2-TrpRS mutant, AMP pocket is blocked, angiostatic activity involves the tryptophan and adenosine pockets
H129A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H140A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H170A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H173A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H257A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H336A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H375A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H387A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H445A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
H73A
site-directed mutagenesis, hemin binding capacity of the mutant enzymes compared to the wild-type enzyme, overview
I311E
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
I311V
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
K102A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K102R
site-directed mutagenesis, the mutant shows slightly reduced activity and reduced kcat compared to the wild-type enzyme
K114Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
K153Q
site-directed mutagenesis, the human mini K153Q TrpRS mutant cannot inhibit VEGF-stimulated HUVEC migration and cannot bind to the extracellular domain of VE-cadherin
K418Q
site-directed mutagenesis, binds to VE-cadherin like the wild-type, full-length enzyme
K431A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
K431R
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
L10D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
L22G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
L9D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
M42D
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
N152G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
N30G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
Q145G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
Q194A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
Q194L
site-directed mutagenesis, the mutant is inactive
R106A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106D
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106I
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
R106K
site-directed mutagenesis, the mutant shows slightly reduced activity and reduced kcat compared to the wild-type enzyme
T18G
site-directed mutagenesis, the mutant shows reduced induction of TNF-alpha and MIP-1alpha production compared to wild-type
V85A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction
V85A/V90A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
V85E
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step
V85K
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the V85K mutant has barely detectable aminoacylation activity
V85L
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the V85L mutant is able to acylate bovine tRNATrp with very high effciency
V85S
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows no activity in the ATP-diphosphate exchange reaction, but retains aminoacylation activity
V90A
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction, the V90 mutation enhances the hydrophobic interaction between V85 and I311
V90S
mutation located at the appended beta1-beta2 hairpin and the AIDQ sequence of TrpRS that switch this enzyme to a tRNA-dependent mode in the tryptophan activation step, the mutant shows decreased, but visible tryptophan activation activity in the ATP-diphosphate exchange reaction, the V90 mutation enhances the hydrophobic interaction between V85 and I311
Y159A
site-directed mutagenesis, the mutant shows reduced kcat and activity compared to the wild-type enzyme
Y159A/Q194A
T2-TrpRS mutant, enzyme specific recognition of the indole nitrogen of tryptophan is disrupted, angiostatic activity involves the tryptophan and adenosine pockets
Y159F
site-directed mutagenesis, the mutant shows slightly reduced activity and reduce kcat compared to the wild-type enzyme
H130R
site-directed mutagenesis, the Zn2+-unbound mutant cannot bind heme in contrast to the Zn2+-free wild-type enzyme
H130R
full-length H130R TrpRS is constitutively active, the mini H130R TrpRS mutant forms disulfide bonds and there are additional functional differences between the full-length and mini forms
H130R
mutant, constitutively active
additional information
construction of truncated enzyme variants, hemin binding capacities, overview
additional information
-
construction of truncated enzyme variants, hemin binding capacities, overview
additional information
preparation of alpha17 deletion mini-TrpRS, DELTAD382Q389, by site-directed mutagensis, overview
additional information
-
preparation of alpha17 deletion mini-TrpRS, DELTAD382Q389, by site-directed mutagensis, overview
additional information
generation of N-terminal 51 amino acid-deleted enzyme WRS mutant (mDELTAN51-WRS). The full-length wild-type enzyme, but not mini-WRS, activates macrophages to prime innate immune responses. The N-terminal 47 aa that are lacking in mini-WRS may be necessary for the correct orientation of the TLR4-MD2 dimers that is required for the activation of downstream signal pathways. Reduced levels of TNF-alpha and MIP-1alpha in culture supernatants of bone marrow derived macrophages treated with WRS enzyme mutants, except for mutant E35G causing slightly increased levels
additional information
-
generation of N-terminal 51 amino acid-deleted enzyme WRS mutant (mDELTAN51-WRS). The full-length wild-type enzyme, but not mini-WRS, activates macrophages to prime innate immune responses. The N-terminal 47 aa that are lacking in mini-WRS may be necessary for the correct orientation of the TLR4-MD2 dimers that is required for the activation of downstream signal pathways. Reduced levels of TNF-alpha and MIP-1alpha in culture supernatants of bone marrow derived macrophages treated with WRS enzyme mutants, except for mutant E35G causing slightly increased levels
additional information
human mini TrpRS lacks the first 47 amino acids
additional information
-
human mini TrpRS lacks the first 47 amino acids
additional information
-
generation of TrpRS-knockdown OEC-M1 cells by siRNA expression
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Homo sapiens
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A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase
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Relationship of two human tRNA synthetases used in cell signaling
Trends Biochem. Sci.
29
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2004
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Human tryptophanyl-tRNA synthetase binds with heme to enhance its aminoacylation activity
Biochemistry
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2007
Homo sapiens (P23381), Homo sapiens
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Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis
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2006
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Tryptamine induces tryptophanyl-tRNA synthetase-mediated neurodegeneration with neurofibrillary tangles in human cell and mouse models
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2007
Homo sapiens, Mus musculus, Mus musculus BALB/c
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Structure of human tryptophanyl-tRNA synthetase in complex with tRNATrp reveals the molecular basis of tRNA recognition and specificity
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Human tryptophanyl-tRNA synthetase is switched to a tRNA-dependent mode for tryptophan activation by mutations at V85 and I311
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