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Paper7783225

The class II aminoacyl-tRNA synthetases and their active site: evolutionary conservation of an ATP binding site.

Eriani G and 7 others. J Mol Evol, 1995. Cited by 41 papers, by iCite.

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ConductScience Library. The class II aminoacyl-tRNA synthetases and their active site: evolutionary conservation of an ATP binding site. Papers, record 7783225. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/7783225

Paper

PubMed's record of the paper, with iCite's citation figures. No abstract is shown.

Title
The class II aminoacyl-tRNA synthetases and their active site: evolutionary conservation of an ATP binding site.
PubMed
Journal
J Mol Evol
PubMed
Year
1995
PubMed
Publication types
Comparative Study, Journal Article
PubMed
Citations, by iCite
41
iCite
Relative citation ratio, by iCite
0.91
iCite
Revised in PubMed
2026-10-10
PubMed

Authors8

The authors in the order PubMed's record lists them, with the ORCID iDs it states.

OrderAuthorForenameKindORCID iD
1Eriani GG
2Cavarelli JJ
3Martin FF
4Ador LL
5Rees BB
6Thierry JCJ C
7Gangloff JJ
8Moras DD

Source PubMed

Topics21

NLM's MeSH indexing of the paper, its major topics first.

MeSH termMajor
Adenosine TriphosphateMajor topic
Amino Acyl-tRNA SynthetasesMajor topic
Biological EvolutionMajor topic
Allosteric Site
Amino Acid Sequence
Aspartate-tRNA Ligase
Bacterial Proteins
Binding Sites
Consensus Sequence
Fungal Proteins
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
RNA, Transfer
RNA, Transfer, Asp
Saccharomyces cerevisiae
Sequence Alignment
Sequence Homology, Amino Acid
Species Specificity
Structure-Activity Relationship

Source PubMed

References38

The papers the reference list in PubMed's record names, those in our copy of PubMed, in the list's order.

OrderPMIDTitleJournalYearIn PapersSource
13,056,726Tyrosyl-tRNA synthetase from baker's yeast. Order of substrate addition, discrimination of 20 amino acids in aminoacylation of tRNATyr-C-C-A and tRNATyr-C-C-A(3'NH2).Eur J Biochem1988https://conductscience.org/library/papers/3056726PubMed
27,019,723Methionyl-tRNA synthetase shows the nucleotide binding fold observed in dehydrogenases.Nature1981https://conductscience.org/library/papers/7019723PubMed
38,360,919Origin of glutaminyl-tRNA synthetase: an example of palimpsest?J Mol Evol1993https://conductscience.org/library/papers/8360919PubMed
44,368,490Chemical and biological evolution of nucleotide-binding protein.Nature1974https://conductscience.org/library/papers/4368490PubMed
53,607,872A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof.Cell1987https://conductscience.org/library/papers/3607872PubMed
68,313,877The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction.EMBO J1994https://conductscience.org/library/papers/8313877PubMed
7356,880Aminoacyl-tRNA synthetases from yeast: generality of chemical proofreading in the prevention of misaminoacylation of tRNA.Biochemistry1978https://conductscience.org/library/papers/356880PubMed
83,315,663Isoleucyl-tRNA synthetase from baker's yeast and from Escherichia coli MRE 600. Discrimination of 20 amino acids in aminoacylation of tRNA(Ile)-C-C-A(3'NH2).Eur J Biochem1987https://conductscience.org/library/papers/3315663PubMed
92,693,216Asparaginyl-tRNA synthetase from Escherichia coli has significant sequence homologies with yeast aspartyl-tRNA synthetase.Gene1989https://conductscience.org/library/papers/2693216PubMed
101,103,136Amino acids are not all initially attached to the same position on transfer RNA molecules.Proc Natl Acad Sci U S A1975https://conductscience.org/library/papers/1103136PubMed
117,265,210Amino acid activation in crystalline tyrosyl-tRNA synthetase from Bacillus stearothermophilus.J Mol Biol1981https://conductscience.org/library/papers/7265210PubMed
128,248,175Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline.Proc Natl Acad Sci U S A1993https://conductscience.org/library/papers/8248175PubMed
132,183,178Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species.Nucleic Acids Res1990https://conductscience.org/library/papers/2183178PubMed
143,096,385Sequence similarities among the family of aminoacyl-tRNA synthetases.Biochimie1986https://conductscience.org/library/papers/3096385PubMed
158,199,244Phenylalanyl-tRNA synthetase from Thermus thermophilus has four antiparallel folds of which only two are catalytically functional.Biochimie1993https://conductscience.org/library/papers/8199244PubMed
162,691,248Arginyl-tRNA synthetase from yeast. Discrimination between 20 amino acids in aminoacylation of tRNA(Arg)-C-C-A and tRNA(Arg)-C-C-A(3'NH2).Eur J Biochem1989https://conductscience.org/library/papers/2691248PubMed
178,163,518The invariant arginine in motif 2 of Escherichia coli alanyl-tRNA synthetase is important for catalysis but not for substrate binding.J Biol Chem1994https://conductscience.org/library/papers/8163518PubMed
188,128,220The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser).Science1994https://conductscience.org/library/papers/8128220PubMed
19382,994Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs.Annu Rev Biochem1979https://conductscience.org/library/papers/382994PubMed
202,047,877Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp).Science1991https://conductscience.org/library/papers/2047877PubMed

See all 38 references

Cited by13

The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 41 citations.

PMIDTitleJournalYearIn PapersSource
40,627,786Natural product-mediated reaction hijacking mechanism validates Plasmodium aspartyl-tRNA synthetase as an antimalarial drug target.PLoS Pathog2025https://conductscience.org/library/papers/40627786PubMed
37,151,504Aminoacyl tRNA Synthetases: Implications of Structural Biology in Drug Development against Trypanosomatid Parasites.ACS Omega2023https://conductscience.org/library/papers/37151504PubMed
30,728,021Aminoacyl tRNA synthetases as malarial drug targets: a comparative bioinformatics study.Malar J2019https://conductscience.org/library/papers/30728021PubMed
30,140,040Identification and characterization of aspartyl-tRNA synthetase inhibitors against Mycobacterium tuberculosis by an integrated whole-cell target-based approach.Sci Rep2018https://conductscience.org/library/papers/30140040PubMed
25,476,837Evolutionary and structural annotation of disease-associated mutations in human aminoacyl-tRNA synthetases.BMC Genomics2014https://conductscience.org/library/papers/25476837PubMed
25,416,776Identification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.J Biol Chem2015https://conductscience.org/library/papers/25416776PubMed
24,493,149Guanidine hydrochloride mediated denaturation of E. coli Alanyl-tRNA synthetase: identification of an inactive dimeric intermediate.Protein J2014https://conductscience.org/library/papers/24493149PubMed
19,443,655Plasmodial aspartyl-tRNA synthetases and peculiarities in Plasmodium falciparum.J Biol Chem2009https://conductscience.org/library/papers/19443655PubMed
12,787,471Functional asymmetry in the lysyl-tRNA synthetase explored by molecular dynamics, free energy calculations and experiment.BMC Struct Biol2003https://conductscience.org/library/papers/12787471PubMed
9,409,149Archaea and the prokaryote-to-eukaryote transition.Microbiol Mol Biol Rev1997https://conductscience.org/library/papers/9409149PubMed
9,144,212Four primordial modes of tRNA-synthetase recognition, determined by the (G,C) operational code.Proc Natl Acad Sci U S A1997https://conductscience.org/library/papers/9144212PubMed
8,710,896Translocation events in the evolution of aminoacyl-tRNA synthetases.Proc Natl Acad Sci U S A1996https://conductscience.org/library/papers/8710896PubMed
8,643,439The presence of codon-anticodon pairs in the acceptor stem of tRNAs.Proc Natl Acad Sci U S A1996https://conductscience.org/library/papers/8643439PubMed

Data dates

The date of each source this release read.

PubMed
2026-11-06
PubMed
iCite
2026-11-05
iCite
PMC's ID file
2026-11-05
PMC's ID file
NIH RePORTER's grant and paper links
2026-11-01
NIH RePORTER's grant and paper links
Trials
2026-11-12
Gene search
2026-11-11
Pipelines
2026-09-18

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Sources 11

  • ChEMBL, through Open TargetsCC BY-SA 3.0
  • ClinicalTrials.govNo license stated
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  • iCiteCC BY 4.0
  • NCBI GenePublic domain (US government)
  • NIH RePORTER's grant and paper linksPublic domain
  • Open TargetsCC0 1.0
  • PMC's ID filePublic domain (US government)
  • PubMedNLM's terms
  • PubTator 3Public domain
  • UniProtCC BY 4.0
Each source's terms
  • ChEMBL, through Open TargetsCC BY-SA 3.0, for the parts from ChEMBL. Read on 8 Nov 2026 at https://platform-docs.opentargets.org/licence
  • ClinicalTrials.govnone stated
  • HGNCCC0: https://www.genenames.org/about/license/
  • iCiteCC BY 4.0
  • NCBI GeneNone named for the file. NCBI says information created by or for the US government on its site is in the public domain, and asks that NLM be acknowledged: https://www.ncbi.nlm.nih.gov/home/about/policies/
  • NIH RePORTER's grant and paper linksPublic domain (NIH RePORTER)
  • Open TargetsCC0 1.0. Open Targets asks that users cite its latest paper: Buniello et al. 2025, Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery, Nucleic Acids Research 53(D1):D1467, PMID 39657122. Read on 8 Nov 2026 at https://platform-docs.opentargets.org/licence
  • PMC's ID fileNone named for the file. NCBI says information created by or for the US government on its site is in the public domain, and asks that NLM be acknowledged: https://www.ncbi.nlm.nih.gov/home/about/policies/
  • PubMedNLM's terms
  • PubTator 3Public domain
  • UniProtCC BY 4.0. UniProt's licence file: "All databases and documents in the UniProt FTP directory may be copied and redistributed freely, without advance permission, provided that this copyright statement is reproduced with each copy." UniProt asks that users cite its latest paper: The UniProt Consortium, UniProt: the Universal Protein Knowledgebase in 2025, Nucleic Acids Research 53:D609-D617, https://doi.org/10.1093/nar/gkae1010. Read on 9 Nov 2026 at https://www.uniprot.org/help/license

ClinicalTrials.gov's data carry an international copyright outside the United States: https://clinicaltrials.gov/about-site/terms-conditions.

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