PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
10780454-4	1999	The results suggest that aminoacylation of proto-tRNA might have started through the direct hydrophobic (or stacking) interaction between the large, hydrophobic amino acid residue (now utilizing a class I aaRS) of aminoacyl-AMP and the 3"-terminal adenine.	aminoacyl-amp	214-227	alanyl-tRNA synthetase 1	Homo sapiens	205-209
10780454-4	1999	The results suggest that aminoacylation of proto-tRNA might have started through the direct hydrophobic (or stacking) interaction between the large, hydrophobic amino acid residue (now utilizing a class I aaRS) of aminoacyl-AMP and the 3"-terminal adenine.	Adenine	248-255	alanyl-tRNA synthetase 1	Homo sapiens	205-209
9122826-1	1996	We present two cases of interstitial pneumonia (IP) whose sera contain autoantibodies to PL-12 (alanyl tRNA synthetase).	pl-12	89-94	alanyl-tRNA synthetase 1	Homo sapiens	96-118
9607303-1	1998	The diadenosine oligophosphates (Ap(n)A) were discovered in the mid-sixties in the course of studies on aminoacyl-tRNA synthetases (aaRS).	diadenosine oligophosphates	4-31	alanyl-tRNA synthetase 1	Homo sapiens	104-130
9607303-1	1998	The diadenosine oligophosphates (Ap(n)A) were discovered in the mid-sixties in the course of studies on aminoacyl-tRNA synthetases (aaRS).	diadenosine oligophosphates	4-31	alanyl-tRNA synthetase 1	Homo sapiens	132-136
9204708-1	1997	Aminoacyl-tRNA synthetases (aaRS) bind their substrates-ATP, amino acids and tRNA- and stabilize putative transition states in the aminoacylation reaction.	Adenosine Triphosphate	56-59	alanyl-tRNA synthetase 1	Homo sapiens	0-26
9204708-1	1997	Aminoacyl-tRNA synthetases (aaRS) bind their substrates-ATP, amino acids and tRNA- and stabilize putative transition states in the aminoacylation reaction.	Adenosine Triphosphate	56-59	alanyl-tRNA synthetase 1	Homo sapiens	28-32
8422978-1	1993	Our present understanding of the molecular mechanisms responsible for the recognition of tRNAs by their cognate aminoacyl-tRNA synthetases (aaRS) is essentially based on three sources of information: 1) the characterization of tRNA identity determinants using in vivo and in vitro approaches, 2) the classification of synthetases from primary sequence analysis: aaRS can be partitioned into two classes according to the spatial structure of their ATP binding domain, and 3) the structural results of crystallographic investigations and solution studies.	Adenosine Triphosphate	447-450	alanyl-tRNA synthetase 1	Homo sapiens	112-138
7647112-1	1995	The superimposable dinucleotide fold domains of MetRS, GlnRS and TyrRS define structurally equivalent amino acids which have been used to constrain the sequence alignments of the 10 class I aminoacyl-tRNA synthetases (aaRS).	Dinucleoside Phosphates	19-31	alanyl-tRNA synthetase 1	Homo sapiens	190-216
7647112-1	1995	The superimposable dinucleotide fold domains of MetRS, GlnRS and TyrRS define structurally equivalent amino acids which have been used to constrain the sequence alignments of the 10 class I aminoacyl-tRNA synthetases (aaRS).	Dinucleoside Phosphates	19-31	alanyl-tRNA synthetase 1	Homo sapiens	218-222
7647112-2	1995	The conservation of those residues which have been shown to be critical in some aaRS enables to predict their location and function in the other synthetases, particularly: i) a conserved negatively-charged residue which binds the alpha-amino group of the amino acid substrate; ii) conserved residues within the inserted domain bridging the two halves of the dinucleotide-binding fold; and iii) conserved residues in the second half of the fold which bind the amino acid and ATP substrate.	Dinucleoside Phosphates	358-370	alanyl-tRNA synthetase 1	Homo sapiens	80-84
7647112-2	1995	The conservation of those residues which have been shown to be critical in some aaRS enables to predict their location and function in the other synthetases, particularly: i) a conserved negatively-charged residue which binds the alpha-amino group of the amino acid substrate; ii) conserved residues within the inserted domain bridging the two halves of the dinucleotide-binding fold; and iii) conserved residues in the second half of the fold which bind the amino acid and ATP substrate.	Adenosine Triphosphate	474-477	alanyl-tRNA synthetase 1	Homo sapiens	80-84
7742303-4	1995	Using microhelix substrates containing only the first four base pairs of the alanine tRNA acceptor helix, we demonstrated that the catalytic center of AlaRS with the three class-defining sequence motifs contains determinants for recognition of A73 and G2.C71.	Alanine	77-84	alanyl-tRNA synthetase 1	Homo sapiens	151-156
8422978-1	1993	Our present understanding of the molecular mechanisms responsible for the recognition of tRNAs by their cognate aminoacyl-tRNA synthetases (aaRS) is essentially based on three sources of information: 1) the characterization of tRNA identity determinants using in vivo and in vitro approaches, 2) the classification of synthetases from primary sequence analysis: aaRS can be partitioned into two classes according to the spatial structure of their ATP binding domain, and 3) the structural results of crystallographic investigations and solution studies.	Adenosine Triphosphate	447-450	alanyl-tRNA synthetase 1	Homo sapiens	140-144
2178410-5	1990	PATIENTS AND METHODS: Sera from patients with polymyositis and sera found to contain anticytoplasmic antibodies were screened for antibody to PL-12 by testing for inhibition of ARS enzymatic activity by serum, and by immunoprecipitation.	pl-12	142-147	alanyl-tRNA synthetase 1	Homo sapiens	177-180
1932086-0	1991	X-ray crystallographic conformational study of 5"-O-[N-(L-alanyl)-sulfamoyl]adenosine, a substrate analogue for alanyl-tRNA synthetase.	5'-O-(N-(alanyl)sulfamoyl)adenosine	47-85	alanyl-tRNA synthetase 1	Homo sapiens	112-134
1932086-1	1991	In order to elucidate the substrate specificity of alanyl-tRNA synthetase, 5"-O-[N-(L-alanyl)sulfamoyl]adenosine (Ala-SA), an analogue of alanyl-AMP, was chemically synthesized.	5'-O-(N-(alanyl)sulfamoyl)adenosine	75-112	alanyl-tRNA synthetase 1	Homo sapiens	51-73
1932086-1	1991	In order to elucidate the substrate specificity of alanyl-tRNA synthetase, 5"-O-[N-(L-alanyl)sulfamoyl]adenosine (Ala-SA), an analogue of alanyl-AMP, was chemically synthesized.	5'-O-(N-(alanyl)sulfamoyl)adenosine	114-120	alanyl-tRNA synthetase 1	Homo sapiens	51-73
1932086-1	1991	In order to elucidate the substrate specificity of alanyl-tRNA synthetase, 5"-O-[N-(L-alanyl)sulfamoyl]adenosine (Ala-SA), an analogue of alanyl-AMP, was chemically synthesized.	alanyl-amp	138-148	alanyl-tRNA synthetase 1	Homo sapiens	51-73
33799176-3	2021	Three aaRS inhibitors are already in clinical practice; antibacterial mupirocin inhibits the synthetic site of isoleucyl-tRNA synthetase, antifungal tavaborole inhibits the editing site of leucyl-tRNA synthetase, and antiprotozoal halofuginone inhibits proline-tRNA synthetase.	Mupirocin	70-79	alanyl-tRNA synthetase 1	Homo sapiens	6-10
33799176-3	2021	Three aaRS inhibitors are already in clinical practice; antibacterial mupirocin inhibits the synthetic site of isoleucyl-tRNA synthetase, antifungal tavaborole inhibits the editing site of leucyl-tRNA synthetase, and antiprotozoal halofuginone inhibits proline-tRNA synthetase.	tavaborole	149-159	alanyl-tRNA synthetase 1	Homo sapiens	6-10
34425806-5	2021	The activity of beta-ARs was modulated by an agonist, norepinephrine (NE), and antagonists, including propranolol, atenolol, nebivolol, and nadolol.	Norepinephrine	54-68	alanyl-tRNA synthetase 1	Homo sapiens	16-24
33799176-3	2021	Three aaRS inhibitors are already in clinical practice; antibacterial mupirocin inhibits the synthetic site of isoleucyl-tRNA synthetase, antifungal tavaborole inhibits the editing site of leucyl-tRNA synthetase, and antiprotozoal halofuginone inhibits proline-tRNA synthetase.	halofuginone	231-243	alanyl-tRNA synthetase 1	Homo sapiens	6-10
33799176-3	2021	Three aaRS inhibitors are already in clinical practice; antibacterial mupirocin inhibits the synthetic site of isoleucyl-tRNA synthetase, antifungal tavaborole inhibits the editing site of leucyl-tRNA synthetase, and antiprotozoal halofuginone inhibits proline-tRNA synthetase.	Proline	253-260	alanyl-tRNA synthetase 1	Homo sapiens	6-10
33799176-10	2021	The most promising aaRS inhibitor as an antimycobacterial compound is GSK656 (compound 8), the only aaRS inhibitor in clinical trials (Phase IIa) for systemic use against tuberculosis.	GSK656	70-76	alanyl-tRNA synthetase 1	Homo sapiens	19-23
33799176-10	2021	The most promising aaRS inhibitor as an antimycobacterial compound is GSK656 (compound 8), the only aaRS inhibitor in clinical trials (Phase IIa) for systemic use against tuberculosis.	GSK656	70-76	alanyl-tRNA synthetase 1	Homo sapiens	100-104
34425806-5	2021	The activity of beta-ARs was modulated by an agonist, norepinephrine (NE), and antagonists, including propranolol, atenolol, nebivolol, and nadolol.	Propranolol	102-113	alanyl-tRNA synthetase 1	Homo sapiens	16-24
34425806-5	2021	The activity of beta-ARs was modulated by an agonist, norepinephrine (NE), and antagonists, including propranolol, atenolol, nebivolol, and nadolol.	Atenolol	115-123	alanyl-tRNA synthetase 1	Homo sapiens	16-24
34425806-5	2021	The activity of beta-ARs was modulated by an agonist, norepinephrine (NE), and antagonists, including propranolol, atenolol, nebivolol, and nadolol.	Nebivolol	125-134	alanyl-tRNA synthetase 1	Homo sapiens	16-24
34425806-5	2021	The activity of beta-ARs was modulated by an agonist, norepinephrine (NE), and antagonists, including propranolol, atenolol, nebivolol, and nadolol.	Nadolol	140-147	alanyl-tRNA synthetase 1	Homo sapiens	16-24
35143333-1	2022	The role of beta-adrenergic receptors (betaARs) in adipose tissue to promote lipolysis and the release of fatty acids and nonshivering thermogenesis in brown fat has been studied for so many decades that one would think there is nothing left to discover.	Fatty Acids	106-117	alanyl-tRNA synthetase 1	Homo sapiens	39-46
34401545-7	2021	In addition, the screening results of four UNAAs, p-propargyloxy-l-phenylalanine (pPaF), p-azyl-phenylalanine (pAzF), p-acetyl-l-phenylalanine (pAcF), and p-benzoyl-l-phenylalanine (pBpF), showed that o-aaRS and o-tRNA of pPaF had good orthogonality.	ppaf	82-86	alanyl-tRNA synthetase 1	Homo sapiens	203-207
34401545-7	2021	In addition, the screening results of four UNAAs, p-propargyloxy-l-phenylalanine (pPaF), p-azyl-phenylalanine (pAzF), p-acetyl-l-phenylalanine (pAcF), and p-benzoyl-l-phenylalanine (pBpF), showed that o-aaRS and o-tRNA of pPaF had good orthogonality.	pazf	111-115	alanyl-tRNA synthetase 1	Homo sapiens	203-207
34401545-7	2021	In addition, the screening results of four UNAAs, p-propargyloxy-l-phenylalanine (pPaF), p-azyl-phenylalanine (pAzF), p-acetyl-l-phenylalanine (pAcF), and p-benzoyl-l-phenylalanine (pBpF), showed that o-aaRS and o-tRNA of pPaF had good orthogonality.	pacf	144-148	alanyl-tRNA synthetase 1	Homo sapiens	203-207
34401545-7	2021	In addition, the screening results of four UNAAs, p-propargyloxy-l-phenylalanine (pPaF), p-azyl-phenylalanine (pAzF), p-acetyl-l-phenylalanine (pAcF), and p-benzoyl-l-phenylalanine (pBpF), showed that o-aaRS and o-tRNA of pPaF had good orthogonality.	pbpf	182-186	alanyl-tRNA synthetase 1	Homo sapiens	203-207
33158106-3	2020	The exposure of the cardiovascular system to the increased locally released and circulating levels of catecholamines leads to a well-described downregulation and desensitization of beta-ARs.	Catecholamines	102-116	alanyl-tRNA synthetase 1	Homo sapiens	181-189
33260297-1	2020	The KARS gene encodes the aminoacyl-tRNA synthetase (aaRS), which activates and joins the lysin with its corresponding transfer RNA (tRNA) through the ATP-dependent aminoacylation of the amino acid.	Adenosine Triphosphate	151-154	alanyl-tRNA synthetase 1	Homo sapiens	26-51
33260297-1	2020	The KARS gene encodes the aminoacyl-tRNA synthetase (aaRS), which activates and joins the lysin with its corresponding transfer RNA (tRNA) through the ATP-dependent aminoacylation of the amino acid.	Adenosine Triphosphate	151-154	alanyl-tRNA synthetase 1	Homo sapiens	53-57
32484512-3	2020	However, no specific mechanism within an aaRS is known to handle the scenario where a cognate amino acid is mischarged onto a wrong tRNA, as exemplified by AlaRS mischarging alanine to G4:U69-containing tRNAThr.	Alanine	174-181	alanyl-tRNA synthetase 1	Homo sapiens	41-45
33081246-3	2020	These compounds were designed as aaRS inhibitors and can be considered as 1,3-dideazaadenine analogues carrying a 2-hydroxymethyl substituent.	1,3-dideazaadenine	74-92	alanyl-tRNA synthetase 1	Homo sapiens	33-37
33081246-7	2020	Upon the evaluation of the inhibitory potency of the newly obtained analogues, nanomolar inhibitory activities were noted for the leucine and isoleucine analogues targeting class I aaRS enzymes, while rather weak inhibitory activity against the corresponding class II aaRSs was observed.	Leucine	130-137	alanyl-tRNA synthetase 1	Homo sapiens	181-185
33081246-7	2020	Upon the evaluation of the inhibitory potency of the newly obtained analogues, nanomolar inhibitory activities were noted for the leucine and isoleucine analogues targeting class I aaRS enzymes, while rather weak inhibitory activity against the corresponding class II aaRSs was observed.	Isoleucine	142-152	alanyl-tRNA synthetase 1	Homo sapiens	181-185
32484512-3	2020	However, no specific mechanism within an aaRS is known to handle the scenario where a cognate amino acid is mischarged onto a wrong tRNA, as exemplified by AlaRS mischarging alanine to G4:U69-containing tRNAThr.	Alanine	174-181	alanyl-tRNA synthetase 1	Homo sapiens	156-161
31862734-4	2020	Here, using LC-MS-purified BMAA and several biochemical assays, we sought to determine whether any aminoacyl-tRNA synthetase (aaRS) utilizes BMAA as a substrate for aminoacylation.	methylaminoalanine-copper(II)	141-145	alanyl-tRNA synthetase 1	Homo sapiens	126-130
32253314-5	2020	Like HF, the threonyl-tRNA synthetase inhibitor borrelidin suppresses the induction of tissue remodeling and inflammatory mediators in cytokine-stimulated fibroblast-like synoviocytes without GCN2, but both aminoacyl-tRNA synthetase (aaRS) inhibitors are sensitive to the removal of GCN1.	borrelidin	48-58	alanyl-tRNA synthetase 1	Homo sapiens	207-232
32253314-5	2020	Like HF, the threonyl-tRNA synthetase inhibitor borrelidin suppresses the induction of tissue remodeling and inflammatory mediators in cytokine-stimulated fibroblast-like synoviocytes without GCN2, but both aminoacyl-tRNA synthetase (aaRS) inhibitors are sensitive to the removal of GCN1.	borrelidin	48-58	alanyl-tRNA synthetase 1	Homo sapiens	234-238
32016368-3	2020	To understand system responses to aaRS depletion, the yeast glutamine aaRS gene (GLN4) was transcriptionally regulated using doxycycline by tet-off control.	arginyl-glutamine	60-69	alanyl-tRNA synthetase 1	Homo sapiens	34-38
32016368-3	2020	To understand system responses to aaRS depletion, the yeast glutamine aaRS gene (GLN4) was transcriptionally regulated using doxycycline by tet-off control.	arginyl-glutamine	60-69	alanyl-tRNA synthetase 1	Homo sapiens	70-74
32016368-3	2020	To understand system responses to aaRS depletion, the yeast glutamine aaRS gene (GLN4) was transcriptionally regulated using doxycycline by tet-off control.	Doxycycline	125-136	alanyl-tRNA synthetase 1	Homo sapiens	70-74
32251275-6	2020	Here, we report a ligand-free AAR structure, and three AAR-ADO complex structures in which AARs bind various ligands.	aar	55-58	alanyl-tRNA synthetase 1	Homo sapiens	91-95
32251275-6	2020	Here, we report a ligand-free AAR structure, and three AAR-ADO complex structures in which AARs bind various ligands.	ado	59-62	alanyl-tRNA synthetase 1	Homo sapiens	91-95
31862734-6	2020	Instead, we observed that BMAA is a substrate for human alanyl-tRNA synthetase (AlaRS) and can form BMAA-tRNAAla by escaping from the intrinsic AlaRS proofreading activity.	methylaminoalanine-copper(II)	26-30	alanyl-tRNA synthetase 1	Homo sapiens	56-78
31862734-6	2020	Instead, we observed that BMAA is a substrate for human alanyl-tRNA synthetase (AlaRS) and can form BMAA-tRNAAla by escaping from the intrinsic AlaRS proofreading activity.	methylaminoalanine-copper(II)	26-30	alanyl-tRNA synthetase 1	Homo sapiens	80-85
31912229-1	2020	PURPOSE: Members of the aaRS (aminoacyl-tRNA synthetase) family are proteins controlling the aminoacylation process, in which YARS (tyrosyl-tRNA synthetase) catalyzes the binding of tyrosine to its cognate tRNA and plays an important role in basic biosynthesis.	Tyrosine	182-190	alanyl-tRNA synthetase 1	Homo sapiens	24-28
31912229-1	2020	PURPOSE: Members of the aaRS (aminoacyl-tRNA synthetase) family are proteins controlling the aminoacylation process, in which YARS (tyrosyl-tRNA synthetase) catalyzes the binding of tyrosine to its cognate tRNA and plays an important role in basic biosynthesis.	Tyrosine	182-190	alanyl-tRNA synthetase 1	Homo sapiens	30-55
31862734-6	2020	Instead, we observed that BMAA is a substrate for human alanyl-tRNA synthetase (AlaRS) and can form BMAA-tRNAAla by escaping from the intrinsic AlaRS proofreading activity.	methylaminoalanine-copper(II)	26-30	alanyl-tRNA synthetase 1	Homo sapiens	144-149
31862734-7	2020	Furthermore, we found that BMAA inhibits both the cognate amino acid activation and the editing functions of AlaRS.	methylaminoalanine-copper(II)	27-31	alanyl-tRNA synthetase 1	Homo sapiens	109-114
31572855-1	2019	Throughout evolution, the presence of a single G3 U70 mismatch in the acceptor stem of tRNAAla is the major determinant for aminoacylation with alanine by alanyl-tRNA synthetase (AlaRS).	Alanine	144-151	alanyl-tRNA synthetase 1	Homo sapiens	155-177
31839000-3	2019	Diseases related to mt-aaRS mutations are associated with specific syndromes that affect the central nervous system and produce highly characteristic MRI patterns, prototypically the DARS2, EARS, and AARS2 leukodystrophies, which are caused by mutations in mitochondrial aspartyl-tRNA synthetase, mitochondria glutamate tRNA synthetase, and mitochondrial alanyl-tRNA synthetase, respectively.	Glutamic Acid	310-319	alanyl-tRNA synthetase 1	Homo sapiens	23-27
31839000-3	2019	Diseases related to mt-aaRS mutations are associated with specific syndromes that affect the central nervous system and produce highly characteristic MRI patterns, prototypically the DARS2, EARS, and AARS2 leukodystrophies, which are caused by mutations in mitochondrial aspartyl-tRNA synthetase, mitochondria glutamate tRNA synthetase, and mitochondrial alanyl-tRNA synthetase, respectively.	acetyl-alanyl-alanyl-alanyl-alanyl-alanyl-alanyl-lysine	355-361	alanyl-tRNA synthetase 1	Homo sapiens	23-27
31591268-8	2019	aaRS, EF-Tu, and the ribosome act as "chiral checkpoints" by preferentially binding to l-amino acids or l-aminoacyl-tRNAs, thereby excluding d-amino acids.	Amino Acids	87-100	alanyl-tRNA synthetase 1	Homo sapiens	0-4
31591268-8	2019	aaRS, EF-Tu, and the ribosome act as "chiral checkpoints" by preferentially binding to l-amino acids or l-aminoacyl-tRNAs, thereby excluding d-amino acids.	l-aminoacyl	104-115	alanyl-tRNA synthetase 1	Homo sapiens	0-4
31591268-8	2019	aaRS, EF-Tu, and the ribosome act as "chiral checkpoints" by preferentially binding to l-amino acids or l-aminoacyl-tRNAs, thereby excluding d-amino acids.	d-amino acids	141-154	alanyl-tRNA synthetase 1	Homo sapiens	0-4
31572855-1	2019	Throughout evolution, the presence of a single G3 U70 mismatch in the acceptor stem of tRNAAla is the major determinant for aminoacylation with alanine by alanyl-tRNA synthetase (AlaRS).	Alanine	144-151	alanyl-tRNA synthetase 1	Homo sapiens	179-184
31280959-13	2019	AARS2 encodes mitochondrial alanyl-tRNA synthetase, which attaches alanine onto tRNA-ala. AARS2 mutations were previously reported in female leukodystrophy patients with POI.	Alanine	67-74	alanyl-tRNA synthetase 1	Homo sapiens	28-50
31083552-5	2019	For aaRS enzyme redesign, photocaged ortho-nitrobenzyl tyrosine (ONBY) was chosen as substrate due to commercial availability and its diverse applications.	ortho-nitrobenzyl tyrosine	37-63	alanyl-tRNA synthetase 1	Homo sapiens	4-8
31190358-4	2019	The thermodynamic differences appear to be exploited by secondary structural differences between models for the ancestral aaRS called synthetase Urzymes and reinforced by packing of aromatic amino acid side chains against the nonpolar face of the ribose of A76 if and only if the tRNA CCA sequence forms a hairpin.	Amino Acids, Aromatic	182-201	alanyl-tRNA synthetase 1	Homo sapiens	122-126
31190358-4	2019	The thermodynamic differences appear to be exploited by secondary structural differences between models for the ancestral aaRS called synthetase Urzymes and reinforced by packing of aromatic amino acid side chains against the nonpolar face of the ribose of A76 if and only if the tRNA CCA sequence forms a hairpin.	Ribose	247-253	alanyl-tRNA synthetase 1	Homo sapiens	122-126
31443422-7	2019	The code evolved from a proto-tRNA a tetramer XCCA interacting with a proto-aminoacyl-tRNA synthetase (aaRS) activating Glycine and Proline, the initial expanded code is found in the acceptor arm of the tRNA, the operational code.	Glycine	120-127	alanyl-tRNA synthetase 1	Homo sapiens	70-101
31443422-7	2019	The code evolved from a proto-tRNA a tetramer XCCA interacting with a proto-aminoacyl-tRNA synthetase (aaRS) activating Glycine and Proline, the initial expanded code is found in the acceptor arm of the tRNA, the operational code.	Glycine	120-127	alanyl-tRNA synthetase 1	Homo sapiens	103-107
31443422-7	2019	The code evolved from a proto-tRNA a tetramer XCCA interacting with a proto-aminoacyl-tRNA synthetase (aaRS) activating Glycine and Proline, the initial expanded code is found in the acceptor arm of the tRNA, the operational code.	Proline	132-139	alanyl-tRNA synthetase 1	Homo sapiens	70-101
31443422-7	2019	The code evolved from a proto-tRNA a tetramer XCCA interacting with a proto-aminoacyl-tRNA synthetase (aaRS) activating Glycine and Proline, the initial expanded code is found in the acceptor arm of the tRNA, the operational code.	Proline	132-139	alanyl-tRNA synthetase 1	Homo sapiens	103-107
31083552-5	2019	For aaRS enzyme redesign, photocaged ortho-nitrobenzyl tyrosine (ONBY) was chosen as substrate due to commercial availability and its diverse applications.	O-(2-NITROBENZYL)-L-TYROSINE HYDROCHLORIDE	65-69	alanyl-tRNA synthetase 1	Homo sapiens	4-8
30345400-2	2018	Genetic code expansion technique reassigns codons and incorporates noncanonical amino acids (ncAAs) through orthogonal aminoacyl-tRNA synthetase (aaRS)/tRNA pairs.	ncaas	93-98	alanyl-tRNA synthetase 1	Homo sapiens	119-144
31046663-12	2019	Sequence alignments of helminth-encoded lysyl, prolyl, leucyl and threonyl tRNA synthetases suggest that various known aaRS inhibitors like Cladosporin, Halofuginone, Benzoborale and Borrelidin may be of utility against helminths.	cladosporin	140-151	alanyl-tRNA synthetase 1	Homo sapiens	119-123
31046663-12	2019	Sequence alignments of helminth-encoded lysyl, prolyl, leucyl and threonyl tRNA synthetases suggest that various known aaRS inhibitors like Cladosporin, Halofuginone, Benzoborale and Borrelidin may be of utility against helminths.	halofuginone	153-165	alanyl-tRNA synthetase 1	Homo sapiens	119-123
31046663-12	2019	Sequence alignments of helminth-encoded lysyl, prolyl, leucyl and threonyl tRNA synthetases suggest that various known aaRS inhibitors like Cladosporin, Halofuginone, Benzoborale and Borrelidin may be of utility against helminths.	benzoborale	167-178	alanyl-tRNA synthetase 1	Homo sapiens	119-123
31046663-12	2019	Sequence alignments of helminth-encoded lysyl, prolyl, leucyl and threonyl tRNA synthetases suggest that various known aaRS inhibitors like Cladosporin, Halofuginone, Benzoborale and Borrelidin may be of utility against helminths.	borrelidin	183-193	alanyl-tRNA synthetase 1	Homo sapiens	119-123
30776522-11	2019	AARs were more frequent in children with higher specific IgE (sIgE) for alpha-lactalbumine and casein at baseline (1.11 [95% confidence interval (CI): 1.01, 1.22] and 1.01 [1.0, 1.03], respectively).	alpha-lactalbumine	72-90	alanyl-tRNA synthetase 1	Homo sapiens	0-4
29395657-5	2019	The codon CGC encoding arginine amino acid and the codon TTA encoding leucine were uniformly distributed in BRCA1 and AARS genes, respectively in mammals including human.	arginine amino acid	23-42	alanyl-tRNA synthetase 1	Homo sapiens	118-122
29395657-5	2019	The codon CGC encoding arginine amino acid and the codon TTA encoding leucine were uniformly distributed in BRCA1 and AARS genes, respectively in mammals including human.	Leucine	70-77	alanyl-tRNA synthetase 1	Homo sapiens	118-122
31937997-3	2018	PheRS was selected as it is structurally unique enzyme among the aminoacyl-tRNA synthetases (aaRS), it is considerably different from human cytosolic and human mitochondrial aaRS and it is essential and conserved across bacterial species.	(ethylenediamine)-3-aminoacyl-2,4,6-triiodobenzoyl amide	65-74	alanyl-tRNA synthetase 1	Homo sapiens	93-97
30345400-2	2018	Genetic code expansion technique reassigns codons and incorporates noncanonical amino acids (ncAAs) through orthogonal aminoacyl-tRNA synthetase (aaRS)/tRNA pairs.	ncaas	93-98	alanyl-tRNA synthetase 1	Homo sapiens	146-150
27622773-3	2016	Here we found human and not E. coli AlaRS has an intrinsic capacity for mispairing alanine onto nonalanyl-tRNAs including tRNACys.	Alanine	83-90	alanyl-tRNA synthetase 1	Homo sapiens	36-41
29967150-7	2018	Alternatively, Homo sapiens AlaRS selects G:U without positive recognition and uses Asp instead to repel a competitor.	Aspartic Acid	84-87	alanyl-tRNA synthetase 1	Homo sapiens	28-33
29659563-2	2018	One key component of this machinery are aminoacyl tRNA synthetases (aaRS), which ligate tRNAs to amino acids while consuming ATP.	Adenosine Triphosphate	125-128	alanyl-tRNA synthetase 1	Homo sapiens	40-66
29659563-2	2018	One key component of this machinery are aminoacyl tRNA synthetases (aaRS), which ligate tRNAs to amino acids while consuming ATP.	Adenosine Triphosphate	125-128	alanyl-tRNA synthetase 1	Homo sapiens	68-72
29360343-2	2018	Specifically, we genetically encoded a thioester-activated aspartic acid (ThioD) in bacteria in good yield and with high fidelity using an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.	Aspartic Acid	59-72	alanyl-tRNA synthetase 1	Homo sapiens	170-200
29360343-2	2018	Specifically, we genetically encoded a thioester-activated aspartic acid (ThioD) in bacteria in good yield and with high fidelity using an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.	Aspartic Acid	59-72	alanyl-tRNA synthetase 1	Homo sapiens	202-206
29360343-2	2018	Specifically, we genetically encoded a thioester-activated aspartic acid (ThioD) in bacteria in good yield and with high fidelity using an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.	(2S)-2-amino-4-[2-(cyclopentyloxycarbonylamino)ethylsulfanyl]-4-oxobutanoic acid	74-79	alanyl-tRNA synthetase 1	Homo sapiens	170-200
29360343-2	2018	Specifically, we genetically encoded a thioester-activated aspartic acid (ThioD) in bacteria in good yield and with high fidelity using an orthogonal nonsense suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.	(2S)-2-amino-4-[2-(cyclopentyloxycarbonylamino)ethylsulfanyl]-4-oxobutanoic acid	74-79	alanyl-tRNA synthetase 1	Homo sapiens	202-206
29727262-3	2018	From sequence alignments, a structurally conserved Zn-binding domain common to class I and class II aaRS was identified.	Zinc	51-53	alanyl-tRNA synthetase 1	Homo sapiens	100-104
29727262-5	2018	Five mechanisms toward code closure are highlighted: 1) aaRS proofreading to remove mischarged amino acids from tRNA; 2) accurate aaRS active site specification of amino acid substrates; 3) aaRS-tRNA anticodon recognition; 4) conformational coupling proofreading of the anticodon-codon interaction; and 5) deamination of tRNA wobble adenine to inosine.	Adenine	333-340	alanyl-tRNA synthetase 1	Homo sapiens	56-60
29727262-5	2018	Five mechanisms toward code closure are highlighted: 1) aaRS proofreading to remove mischarged amino acids from tRNA; 2) accurate aaRS active site specification of amino acid substrates; 3) aaRS-tRNA anticodon recognition; 4) conformational coupling proofreading of the anticodon-codon interaction; and 5) deamination of tRNA wobble adenine to inosine.	Adenine	333-340	alanyl-tRNA synthetase 1	Homo sapiens	130-134
29727262-5	2018	Five mechanisms toward code closure are highlighted: 1) aaRS proofreading to remove mischarged amino acids from tRNA; 2) accurate aaRS active site specification of amino acid substrates; 3) aaRS-tRNA anticodon recognition; 4) conformational coupling proofreading of the anticodon-codon interaction; and 5) deamination of tRNA wobble adenine to inosine.	Adenine	333-340	alanyl-tRNA synthetase 1	Homo sapiens	130-134
29727262-5	2018	Five mechanisms toward code closure are highlighted: 1) aaRS proofreading to remove mischarged amino acids from tRNA; 2) accurate aaRS active site specification of amino acid substrates; 3) aaRS-tRNA anticodon recognition; 4) conformational coupling proofreading of the anticodon-codon interaction; and 5) deamination of tRNA wobble adenine to inosine.	Inosine	344-351	alanyl-tRNA synthetase 1	Homo sapiens	56-60
29727262-5	2018	Five mechanisms toward code closure are highlighted: 1) aaRS proofreading to remove mischarged amino acids from tRNA; 2) accurate aaRS active site specification of amino acid substrates; 3) aaRS-tRNA anticodon recognition; 4) conformational coupling proofreading of the anticodon-codon interaction; and 5) deamination of tRNA wobble adenine to inosine.	Inosine	344-351	alanyl-tRNA synthetase 1	Homo sapiens	130-134
29727262-5	2018	Five mechanisms toward code closure are highlighted: 1) aaRS proofreading to remove mischarged amino acids from tRNA; 2) accurate aaRS active site specification of amino acid substrates; 3) aaRS-tRNA anticodon recognition; 4) conformational coupling proofreading of the anticodon-codon interaction; and 5) deamination of tRNA wobble adenine to inosine.	Inosine	344-351	alanyl-tRNA synthetase 1	Homo sapiens	130-134
29477072-3	2018	Aminoacyl-sulfamoyl adenosines (aaSAs) are potent orthologue specific aaRS inhibitors that demonstrate nanomolar affinities in vitro but have limited uptake.	aminoacyl-sulfamoyl adenosines	0-30	alanyl-tRNA synthetase 1	Homo sapiens	70-74
29477072-3	2018	Aminoacyl-sulfamoyl adenosines (aaSAs) are potent orthologue specific aaRS inhibitors that demonstrate nanomolar affinities in vitro but have limited uptake.	aasas	32-37	alanyl-tRNA synthetase 1	Homo sapiens	70-74
28493438-4	2017	Whole-exome sequencing identified that the affected individuals were compound heterozygous for mutations in AARS gene, c.2067dupC (p.Tyr690Leufs*3) and c.2738G>A (p.Gly913Asp).	tyr690leufs	133-144	alanyl-tRNA synthetase 1	Homo sapiens	108-112
28230768-7	2017	However, our protein structure prediction identified a putative HIGH-motif and KMSKS-motif as well as many alpha-helices that are characteristic of class I aminoacyl-tRNA synthetase (aaRS) homologs.	kmsks	79-84	alanyl-tRNA synthetase 1	Homo sapiens	183-187
27911835-0	2016	Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS.	Alanine	59-62	alanyl-tRNA synthetase 1	Homo sapiens	79-84
27911835-4	2016	In human cells, C-Ala is also a splice variant of AlaRS.	c-ala	16-21	alanyl-tRNA synthetase 1	Homo sapiens	50-55
27622773-8	2016	Thus, the expanded tRNA specificity of AlaRS appears to be an evolutionary gain-of-function to provide posttranscriptional alanine substitutions in eukaryotic proteins for potential regulations.	Alanine	123-130	alanyl-tRNA synthetase 1	Homo sapiens	39-44
27200345-3	2016	However, due to presence of D-amino acids in the cell, sometimes aaRS charges tRNA with D-amino acids resulting in the hampering of protein translational process, which is lethal to the cell.	d-amino acids	28-41	alanyl-tRNA synthetase 1	Homo sapiens	65-69
27200345-3	2016	However, due to presence of D-amino acids in the cell, sometimes aaRS charges tRNA with D-amino acids resulting in the hampering of protein translational process, which is lethal to the cell.	d-amino acids	88-101	alanyl-tRNA synthetase 1	Homo sapiens	65-69
26337976-11	2015	CONCLUSION: AARS, AURKA, AURKB, CENPA, CCNB1, CCNE2, and CDK may contribute to MTX resistance via aminoacyl-tRNA biosynthesis pathway, cell cycle pathway, or p53 signaling pathway.	Methotrexate	79-82	alanyl-tRNA synthetase 1	Homo sapiens	12-16
23536246-1	2014	In this chapter we describe aminoacyl-tRNA synthetase (aaRS) production of dinucleotide polyphosphate in response to stimuli, their interaction with various signaling pathways, and the role of diadenosine tetraphosphate and diadenosine triphosphate as second messengers.	dinucleotide polyphosphate	75-101	alanyl-tRNA synthetase 1	Homo sapiens	28-53
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Serine	46-52	alanyl-tRNA synthetase 1	Homo sapiens	154-158
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Proline	54-61	alanyl-tRNA synthetase 1	Homo sapiens	154-158
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Glycine	63-70	alanyl-tRNA synthetase 1	Homo sapiens	154-158
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Asparagine	72-82	alanyl-tRNA synthetase 1	Homo sapiens	154-158
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Leucine	84-91	alanyl-tRNA synthetase 1	Homo sapiens	127-152
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Leucine	84-91	alanyl-tRNA synthetase 1	Homo sapiens	154-158
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Histidine	97-106	alanyl-tRNA synthetase 1	Homo sapiens	127-152
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Histidine	97-106	alanyl-tRNA synthetase 1	Homo sapiens	154-158
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Luminol	228-235	alanyl-tRNA synthetase 1	Homo sapiens	127-152
25935222-5	2015	For the recognition of each amino acid (here, serine, proline, glycine, asparagine, leucine, and histidine), the corresponding aminoacyl-tRNA synthetase (aaRS) was employed, and multiple enzymatic reactions were combined with a luminol chemiluminescence reaction.	Luminol	228-235	alanyl-tRNA synthetase 1	Homo sapiens	154-158
25724653-3	2015	For example, the AlaX family of editing domains, including the editing domain of alanyl-tRNA synthetase and the related free-standing trans-editing AlaX enzymes, are thought to specifically act on tRNA(Ala), whereas the editing domains of threonyl-tRNA synthetases are specific for tRNA(Thr).	Alanine	17-20	alanyl-tRNA synthetase 1	Homo sapiens	81-103
25724653-3	2015	For example, the AlaX family of editing domains, including the editing domain of alanyl-tRNA synthetase and the related free-standing trans-editing AlaX enzymes, are thought to specifically act on tRNA(Ala), whereas the editing domains of threonyl-tRNA synthetases are specific for tRNA(Thr).	Threonine	287-290	alanyl-tRNA synthetase 1	Homo sapiens	81-103
25791872-0	2015	Ancestral Reconstruction of a Pre-LUCA Aminoacyl-tRNA Synthetase Ancestor Supports the Late Addition of Trp to the Genetic Code.	Tryptophan	104-107	alanyl-tRNA synthetase 1	Homo sapiens	39-64
25791872-7	2015	This is consistent with the paralog ancestor being specific for the utilization of Tyr, with Trp being a subsequent addition to the genetic code facilitated by a process of aaRS divergence and neofunctionalization.	Tryptophan	93-96	alanyl-tRNA synthetase 1	Homo sapiens	173-177
25686591-0	2015	5"-(N-aminoacyl)-sulfonamido-5"-deoxyadenosine: attempts for a stable alternative for aminoacyl-sulfamoyl adenosines as aaRS inhibitors.	5"-(n-aminoacyl)-sulfonamido-5"-deoxyadenosine	0-46	alanyl-tRNA synthetase 1	Homo sapiens	120-124
25686591-0	2015	5"-(N-aminoacyl)-sulfonamido-5"-deoxyadenosine: attempts for a stable alternative for aminoacyl-sulfamoyl adenosines as aaRS inhibitors.	aminoacyl-sulfamoyl adenosines	86-116	alanyl-tRNA synthetase 1	Homo sapiens	120-124
25686591-1	2015	Synthesis of aminoacyl-sulfamoyl adenosines (aaSAs) and their peptidyl conjugates as aminoacyl tRNA synthetase (aaRS) inhibitors remains problematic due to the low yield of the aminoacylation and the subsequent conjugation reaction causing concomitant formation of a cyclic adenosine derivative.	aminoacyl-sulfamoyl adenosines	13-43	alanyl-tRNA synthetase 1	Homo sapiens	85-110
25686591-1	2015	Synthesis of aminoacyl-sulfamoyl adenosines (aaSAs) and their peptidyl conjugates as aminoacyl tRNA synthetase (aaRS) inhibitors remains problematic due to the low yield of the aminoacylation and the subsequent conjugation reaction causing concomitant formation of a cyclic adenosine derivative.	aminoacyl-sulfamoyl adenosines	13-43	alanyl-tRNA synthetase 1	Homo sapiens	112-116
25686591-1	2015	Synthesis of aminoacyl-sulfamoyl adenosines (aaSAs) and their peptidyl conjugates as aminoacyl tRNA synthetase (aaRS) inhibitors remains problematic due to the low yield of the aminoacylation and the subsequent conjugation reaction causing concomitant formation of a cyclic adenosine derivative.	aasas	45-50	alanyl-tRNA synthetase 1	Homo sapiens	85-110
25686591-1	2015	Synthesis of aminoacyl-sulfamoyl adenosines (aaSAs) and their peptidyl conjugates as aminoacyl tRNA synthetase (aaRS) inhibitors remains problematic due to the low yield of the aminoacylation and the subsequent conjugation reaction causing concomitant formation of a cyclic adenosine derivative.	aasas	45-50	alanyl-tRNA synthetase 1	Homo sapiens	112-116
25686591-1	2015	Synthesis of aminoacyl-sulfamoyl adenosines (aaSAs) and their peptidyl conjugates as aminoacyl tRNA synthetase (aaRS) inhibitors remains problematic due to the low yield of the aminoacylation and the subsequent conjugation reaction causing concomitant formation of a cyclic adenosine derivative.	cyclic adenosine	267-283	alanyl-tRNA synthetase 1	Homo sapiens	112-116
28553457-2	2015	The programmed incorporation of UAAs into recombinant proteins relies on the reassignment or suppression of canonical codons with an amino-acyl tRNA synthetase/tRNA (aaRS/tRNA) pair, selective for the UAA of choice.	6-Carboxymethyluracil	32-35	alanyl-tRNA synthetase 1	Homo sapiens	166-170
23536246-1	2014	In this chapter we describe aminoacyl-tRNA synthetase (aaRS) production of dinucleotide polyphosphate in response to stimuli, their interaction with various signaling pathways, and the role of diadenosine tetraphosphate and diadenosine triphosphate as second messengers.	dinucleotide polyphosphate	75-101	alanyl-tRNA synthetase 1	Homo sapiens	55-59
23536246-1	2014	In this chapter we describe aminoacyl-tRNA synthetase (aaRS) production of dinucleotide polyphosphate in response to stimuli, their interaction with various signaling pathways, and the role of diadenosine tetraphosphate and diadenosine triphosphate as second messengers.	diadenosine tetraphosphate	193-219	alanyl-tRNA synthetase 1	Homo sapiens	55-59
23536246-1	2014	In this chapter we describe aminoacyl-tRNA synthetase (aaRS) production of dinucleotide polyphosphate in response to stimuli, their interaction with various signaling pathways, and the role of diadenosine tetraphosphate and diadenosine triphosphate as second messengers.	diadenosine triphosphate	224-248	alanyl-tRNA synthetase 1	Homo sapiens	55-59
23536246-5	2014	The dinucleotide polyphosphates produced by aaRS are biologically active both extra- and intra-cellularly, and seem to function as important signaling molecules.	dinucleotide polyphosphates	4-31	alanyl-tRNA synthetase 1	Homo sapiens	44-48
23852030-3	2014	In a common two-step reaction, each aaRS first uses the energy stored in ATP to synthesize an activated aminoacyl adenylate intermediate.	aminoacyl adenylate	104-123	alanyl-tRNA synthetase 1	Homo sapiens	36-40
23852030-3	2014	In a common two-step reaction, each aaRS first uses the energy stored in ATP to synthesize an activated aminoacyl adenylate intermediate.	Adenosine Triphosphate	73-76	alanyl-tRNA synthetase 1	Homo sapiens	36-40
23924161-2	2013	Here we report that the fluorescent amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), can be site-specifically incorporated into proteins in mammalian cells in response to the TAG codon with high efficiency using an orthogonal amber suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.	3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid	48-102	alanyl-tRNA synthetase 1	Homo sapiens	269-299
23973428-4	2013	Pyrophosphate released by the amino acid-aaRS binding reaction was detected by luminol chemiluminescence; the method provided selective quantitation of 1.0-30 muM histidine and 1.0-60 muM lysine.	diphosphoric acid	0-13	alanyl-tRNA synthetase 1	Homo sapiens	41-45
23973428-4	2013	Pyrophosphate released by the amino acid-aaRS binding reaction was detected by luminol chemiluminescence; the method provided selective quantitation of 1.0-30 muM histidine and 1.0-60 muM lysine.	Luminol	79-86	alanyl-tRNA synthetase 1	Homo sapiens	41-45
23973428-4	2013	Pyrophosphate released by the amino acid-aaRS binding reaction was detected by luminol chemiluminescence; the method provided selective quantitation of 1.0-30 muM histidine and 1.0-60 muM lysine.	Histidine	163-172	alanyl-tRNA synthetase 1	Homo sapiens	41-45
23973428-4	2013	Pyrophosphate released by the amino acid-aaRS binding reaction was detected by luminol chemiluminescence; the method provided selective quantitation of 1.0-30 muM histidine and 1.0-60 muM lysine.	Lysine	188-194	alanyl-tRNA synthetase 1	Homo sapiens	41-45
23924161-2	2013	Here we report that the fluorescent amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), can be site-specifically incorporated into proteins in mammalian cells in response to the TAG codon with high efficiency using an orthogonal amber suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.	3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid	48-102	alanyl-tRNA synthetase 1	Homo sapiens	301-305
23924161-2	2013	Here we report that the fluorescent amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), can be site-specifically incorporated into proteins in mammalian cells in response to the TAG codon with high efficiency using an orthogonal amber suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.	3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid	104-108	alanyl-tRNA synthetase 1	Homo sapiens	269-299
23924161-2	2013	Here we report that the fluorescent amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), can be site-specifically incorporated into proteins in mammalian cells in response to the TAG codon with high efficiency using an orthogonal amber suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair.	3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid	104-108	alanyl-tRNA synthetase 1	Homo sapiens	301-305
22009580-8	2012	Genotyping analysis indicated that this mutation arose on three distinct haplotypes, and the results of bisulfite sequencing suggested that methylation-mediated deamination of a CpG dinucleotide gives rise to the recurrent p.Arg329His AARS mutation.	hydrogen sulfite	104-113	alanyl-tRNA synthetase 1	Homo sapiens	235-239
23867455-9	2013	By tracing aaRS catalytic activities back to simpler ancestral peptides, we demonstrate key steps for a simpler and hence more probable peptide RNA development of rapid coding systems matching amino acids with anticodon trinucleotides.	trinucleotides	220-234	alanyl-tRNA synthetase 1	Homo sapiens	11-15
22009580-8	2012	Genotyping analysis indicated that this mutation arose on three distinct haplotypes, and the results of bisulfite sequencing suggested that methylation-mediated deamination of a CpG dinucleotide gives rise to the recurrent p.Arg329His AARS mutation.	cytidylyl-3'-5'-guanosine	178-194	alanyl-tRNA synthetase 1	Homo sapiens	235-239
21647378-6	2011	We exploited the space spanned by the CPs in order to identify similarities between aaRS families that are not observed using sequence alignment methods, identifying different inter-aaRS associations across different kingdom of life.	cps	38-41	alanyl-tRNA synthetase 1	Homo sapiens	84-88
21930589-8	2011	However, serine-for-alanine mistranslation is so challenging that a separate, genome-encoded fragment of the editing domain of AlaRS is distributed throughout the Tree of Life to redundantly prevent serine-to-alanine mistranslation.	Serine	9-15	alanyl-tRNA synthetase 1	Homo sapiens	127-132
21930589-8	2011	However, serine-for-alanine mistranslation is so challenging that a separate, genome-encoded fragment of the editing domain of AlaRS is distributed throughout the Tree of Life to redundantly prevent serine-to-alanine mistranslation.	Alanine	20-27	alanyl-tRNA synthetase 1	Homo sapiens	127-132
21930589-8	2011	However, serine-for-alanine mistranslation is so challenging that a separate, genome-encoded fragment of the editing domain of AlaRS is distributed throughout the Tree of Life to redundantly prevent serine-to-alanine mistranslation.	Serine	199-205	alanyl-tRNA synthetase 1	Homo sapiens	127-132
21930589-8	2011	However, serine-for-alanine mistranslation is so challenging that a separate, genome-encoded fragment of the editing domain of AlaRS is distributed throughout the Tree of Life to redundantly prevent serine-to-alanine mistranslation.	Alanine	209-216	alanyl-tRNA synthetase 1	Homo sapiens	127-132
21224416-4	2011	The highest fidelity NAA systems derived from the Methanocaldococcus jannaschii tyrosyl AARS feature specific mutations to two residues reported to interact with the hydroxyl group of the substrate tyrosine.	1-naphthaleneacetic acid	21-24	alanyl-tRNA synthetase 1	Homo sapiens	88-92
21224416-4	2011	The highest fidelity NAA systems derived from the Methanocaldococcus jannaschii tyrosyl AARS feature specific mutations to two residues reported to interact with the hydroxyl group of the substrate tyrosine.	Tyrosine	198-206	alanyl-tRNA synthetase 1	Homo sapiens	88-92
21224416-7	2011	Similarly, we reinvestigated a tryptophanyl AARS reported to allow the site-selective incorporation of 5-hydroxy tryptophan within mammalian cells.	tryptophanyl	31-43	alanyl-tRNA synthetase 1	Homo sapiens	44-48
21224416-7	2011	Similarly, we reinvestigated a tryptophanyl AARS reported to allow the site-selective incorporation of 5-hydroxy tryptophan within mammalian cells.	5-Hydroxytryptophan	103-123	alanyl-tRNA synthetase 1	Homo sapiens	44-48
21285181-0	2011	Autoantibody to PL-12 (Anti-Alanyl-tRNA synthetase) in an African American girl with juvenile dermatomyositis and resolution of interstitial lung disease.	pl-12	16-21	alanyl-tRNA synthetase 1	Homo sapiens	28-50
21647378-6	2011	We exploited the space spanned by the CPs in order to identify similarities between aaRS families that are not observed using sequence alignment methods, identifying different inter-aaRS associations across different kingdom of life.	cps	38-41	alanyl-tRNA synthetase 1	Homo sapiens	182-186
19549823-1	2009	Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA(Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA(Ala) at 2 different catalytic sites.	ala-trna	54-62	alanyl-tRNA synthetase 1	Homo sapiens	0-22
19549823-1	2009	Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA(Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA(Ala) at 2 different catalytic sites.	ala-trna	54-62	alanyl-tRNA synthetase 1	Homo sapiens	24-29
19549823-1	2009	Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA(Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA(Ala) at 2 different catalytic sites.	Alanine	0-3	alanyl-tRNA synthetase 1	Homo sapiens	24-29
19549823-1	2009	Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA(Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA(Ala) at 2 different catalytic sites.	Serine	99-102	alanyl-tRNA synthetase 1	Homo sapiens	0-22
19549823-1	2009	Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA(Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA(Ala) at 2 different catalytic sites.	Serine	99-102	alanyl-tRNA synthetase 1	Homo sapiens	24-29
19549823-1	2009	Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA(Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA(Ala) at 2 different catalytic sites.	Glycine	108-111	alanyl-tRNA synthetase 1	Homo sapiens	0-22
19549823-1	2009	Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA(Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA(Ala) at 2 different catalytic sites.	Glycine	108-111	alanyl-tRNA synthetase 1	Homo sapiens	24-29
19549823-1	2009	Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA(Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA(Ala) at 2 different catalytic sites.	Alanine	24-27	alanyl-tRNA synthetase 1	Homo sapiens	0-22
19549823-2	2009	Here, we describe the monomer structures of C-terminal truncated archaeal AlaRS, with both activation and editing domains in the apo form, in complex with an Ala-AMP analog, and in a high-resolution lysine-methylated form.	ala-amp	158-165	alanyl-tRNA synthetase 1	Homo sapiens	74-79
19549823-2	2009	Here, we describe the monomer structures of C-terminal truncated archaeal AlaRS, with both activation and editing domains in the apo form, in complex with an Ala-AMP analog, and in a high-resolution lysine-methylated form.	Lysine	199-205	alanyl-tRNA synthetase 1	Homo sapiens	74-79
19549823-8	2009	As Asn-194 in eubacterial AlaRS important for Ser misactivation is replaced by Thr-213 in archaeal AlaRS, a different Ser accommodation mechanism is proposed.	Asparagine	3-6	alanyl-tRNA synthetase 1	Homo sapiens	26-31
19549823-8	2009	As Asn-194 in eubacterial AlaRS important for Ser misactivation is replaced by Thr-213 in archaeal AlaRS, a different Ser accommodation mechanism is proposed.	Asparagine	3-6	alanyl-tRNA synthetase 1	Homo sapiens	99-104
19549823-8	2009	As Asn-194 in eubacterial AlaRS important for Ser misactivation is replaced by Thr-213 in archaeal AlaRS, a different Ser accommodation mechanism is proposed.	Serine	46-49	alanyl-tRNA synthetase 1	Homo sapiens	26-31
19549823-8	2009	As Asn-194 in eubacterial AlaRS important for Ser misactivation is replaced by Thr-213 in archaeal AlaRS, a different Ser accommodation mechanism is proposed.	Threonine	79-82	alanyl-tRNA synthetase 1	Homo sapiens	99-104
19549823-8	2009	As Asn-194 in eubacterial AlaRS important for Ser misactivation is replaced by Thr-213 in archaeal AlaRS, a different Ser accommodation mechanism is proposed.	Serine	118-121	alanyl-tRNA synthetase 1	Homo sapiens	26-31
19549823-8	2009	As Asn-194 in eubacterial AlaRS important for Ser misactivation is replaced by Thr-213 in archaeal AlaRS, a different Ser accommodation mechanism is proposed.	Serine	118-121	alanyl-tRNA synthetase 1	Homo sapiens	99-104
18241792-2	2008	To date, analysis of aaRSs function, including identification of residues of aaRS participating in amino acid and tRNA discrimination, has largely relied on the steady state kinetic pyrophosphate exchange and aminoacylation assays.	diphosphoric acid	182-195	alanyl-tRNA synthetase 1	Homo sapiens	21-25
18723508-3	2008	Because genome-encoded fragments of editing domains of other synthetases are scarce, the AlaXp redundancy of the editing domain of alanyl-tRNA synthetase is thought to reflect an unusual sensitivity of cells to mistranslation at codons for Ala.	Alanine	89-92	alanyl-tRNA synthetase 1	Homo sapiens	131-153
18723508-7	2008	Serine toxicity, experienced by a strain harboring an editing-defective alanyl-tRNA synthetase, was rescued by an AlaXp-encoding transgene.	Serine	0-6	alanyl-tRNA synthetase 1	Homo sapiens	72-94
19293994-6	2009	The procedure has been used to characterize the presence of BFAHs in the N-terminal extensions of the eukaryotic aminoacyl-tRNA synthetases and to indicate the presence of a BFAH in the tRNA binding site of alanyl-tRNA synthetase.	bfahs	60-65	alanyl-tRNA synthetase 1	Homo sapiens	207-229
14639923-4	2003	In order to learn the programs of TCs, we attend the programs of Walden house and Asian and American Recovery Services (AARS), which San Francisco and rehabilitation programs in Japan and how to introduce the TC methods into Japan.	Technetium	34-37	alanyl-tRNA synthetase 1	Homo sapiens	120-124
18172502-6	2008	Here we show that the editing site of alanyl-tRNA synthetase, as an artificial recombinant fragment, targets mischarged tRNA(Ala) using a structural motif unrelated to that for aminoacylation so that, remarkably, two motifs (one for aminoacylation and one for editing) in the same enzyme independently can provide determinants for tRNA(Ala) recognition.	Alanine	125-128	alanyl-tRNA synthetase 1	Homo sapiens	38-60
16537388-7	2006	Remarkably, many beta-amino acids, N-methyl amino acids, and alpha,alpha-disubstituted amino acids are also AARS substrates.	beta-amino acids	17-33	alanyl-tRNA synthetase 1	Homo sapiens	108-112
16537388-7	2006	Remarkably, many beta-amino acids, N-methyl amino acids, and alpha,alpha-disubstituted amino acids are also AARS substrates.	n-methyl amino acids	35-55	alanyl-tRNA synthetase 1	Homo sapiens	108-112
16537388-7	2006	Remarkably, many beta-amino acids, N-methyl amino acids, and alpha,alpha-disubstituted amino acids are also AARS substrates.	alpha,alpha-disubstituted amino acids	61-98	alanyl-tRNA synthetase 1	Homo sapiens	108-112
17924654-6	2007	Here, using ThrRS as an example, rapid single-turnover kinetics, mutagenesis, and solvent isotope analysis show that a strictly conserved histidine (between ThrRS and AlaRS) extracts a proton in the chemical step of the editing reaction.	Histidine	138-147	alanyl-tRNA synthetase 1	Homo sapiens	167-172
17726052-3	2007	Tryptophanyl-tRNA synthetase is a class I aaRS that catalyzes tryptophan activation in the absence of its cognate tRNA.	Tryptophan	62-72	alanyl-tRNA synthetase 1	Homo sapiens	42-46
12903114-4	2002	In addition to tRNA(Gln), tRNA(Ala) and tRNA(Asn) showed weak but significant serylation activities, which raises the possibility that each mammalian mt aaRS can misacylate several non-cognate mt tRNAs in varying degrees, but translational fidelity might be maintained by kinetic discrimination of tRNAs in the network of aaRSs.	Glutamine	20-23	alanyl-tRNA synthetase 1	Homo sapiens	153-157
10964400-4	2000	The usefulness of this approach was demonstrated by measurement of steady-state kinetic constants and inhibitor binding constants for a range of aaRS enzymes in comparison with data from standard, trichloroacetic acid-precipitation-based assays.	Trichloroacetic Acid	197-217	alanyl-tRNA synthetase 1	Homo sapiens	145-149