Paper · 199234
Ligand binding stoichiometries, subunit structure, and slow transitions in aminoacyl-tRNA synthetases.
Mulvey RS and 1 other. Biochemistry, 1977. Cited by 51 papers, by iCite.
11 sourcespapers-2026-11-12-0.1.0
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ConductScience Library. Ligand binding stoichiometries, subunit structure, and slow transitions in aminoacyl-tRNA synthetases. Papers, record 199234. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/199234
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Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
- Ligand binding stoichiometries, subunit structure, and slow transitions in aminoacyl-tRNA synthetases.
- PubMed
Topics16
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| Amino Acyl-tRNA Synthetases | Major topic |
| Adenine Nucleotides | |
| Adenosine Triphosphate | |
| Amino Acids | |
| Binding Sites | |
| Chromatography, Gel | |
| Dialysis | |
| Diphosphates | |
| Escherichia coli | |
| Geobacillus stearothermophilus | |
| Kinetics | |
| Ligands | |
| Molecular Weight | |
| Protein Conformation | |
| Structure-Activity Relationship | |
| Valine-tRNA Ligase |
Source PubMed
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References0
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Cited by8
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 51 citations.
| PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|
| 40,613,378 | Mechanisms and kinetic assays of aminoacyl-tRNA synthetases. | FEBS Lett | 2025 | https://conductscience.org/library/papers/40613378 | PubMed |
| 18,559,342 | The homotetrameric phosphoseryl-tRNA synthetase from Methanosarcina mazei exhibits half-of-the-sites activity. | J Biol Chem | 2008 | https://conductscience.org/library/papers/18559342 | PubMed |
| 12,110,594 | Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. | EMBO J | 2002 | https://conductscience.org/library/papers/12110594 | PubMed |
| 10,477,284 | Editing of non-cognate aminoacyl adenylates by peptide synthetases. | Biochem J | 1999 | https://conductscience.org/library/papers/10477284 | PubMed |
| 7,024,910 | Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases. | Nucleic Acids Res | 1981 | https://conductscience.org/library/papers/7024910 | PubMed |
| 6,991,306 | Molar absorptivity and A1%1 cm values for proteins at selected wavelengths of the ultraviolet and visible regions--XVIII. | Int J Biochem | 1980 | https://conductscience.org/library/papers/6991306 | PubMed |
| 743,207 | Phosphonate analogues of aminoacyl adenylates. | Biochem J | 1978 | https://conductscience.org/library/papers/743207 | PubMed |
| 377,229 | The binding of tyrosinyl-5'-AMP to tyrosyl-tRNA synthetase (E.coli). | Nucleic Acids Res | 1979 | https://conductscience.org/library/papers/377229 | PubMed |
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- Trials
- 2026-11-12
- Gene search
- 2026-11-11
- Pipelines
- 2026-09-18
Sources 11
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- 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
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- 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
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- 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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