Paper4581817

The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH.

Blanquet S and 2 others. Eur J Biochem, 1973. Cited by 109 papers, by iCite.

11 sourcespapers-2026-11-12-0.1.0

Cite this record

ConductScience Library. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH. Papers, record 4581817. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/4581817

Paper

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

Title: The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH.; PubMed
Journal: Eur J Biochem; PubMed
Year: 1973; PubMed
Publication types: Journal Article; PubMed
PubMed: https://pubmed.ncbi.nlm.nih.gov/4581817/; PubMed
DOI: https://doi.org/10.1111/j.1432-1033.1973.tb02903.x; PubMed
The journal: https://conductscience.org/library/journal-index/0107600; PubMed
Citations, by iCite: 109; iCite
Relative citation ratio, by iCite: 2.57; iCite
Revised in PubMed: 2019-06-20; PubMed

Authors3

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

Order	Author	Forename
1	Blanquet S	S
2	Iwatsubo M	M
3	Waller JP	J P

Source PubMed

Topics15

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

MeSH term	Major
Amino Acyl-tRNA Synthetases	Major topic
Escherichia coli	Major topic
Protein Binding	Major topic
Binding Sites
Hydrogen-Ion Concentration
Kinetics
Magnesium
Methionine
Potassium Chloride
Protein Conformation
RNA, Transfer
Spectrometry, Fluorescence
Spermidine
Spermine
Trypsin

Source PubMed

Show 9 more topicsShow fewer topics

Cited by16

The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 109 citations.

PMID	Title	Journal	Year	In Papers	Source
25,191,528	The CCA-end of P-tRNA Contacts Both the Human RPL36AL and the A-site Bound Translation Termination Factor eRF1 at the Peptidyl Transferase Center of the Human 80S Ribosome.	Open Biochem J	2014	https://conductscience.org/library/papers/25191528	PubMed
19,015,366	Inhibition of methionyl-tRNA synthetase by REP8839 and effects of resistance mutations on enzyme activity.	Antimicrob Agents Chemother	2009	https://conductscience.org/library/papers/19015366	PubMed
11,118,226	A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation.	EMBO J	2000	https://conductscience.org/library/papers/11118226	PubMed
8,887,566	Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.	EMBO J	1996	https://conductscience.org/library/papers/8887566	PubMed
6,294,608	E. coli initiator tRNA analogs with different nucleotides in the discriminator base position.	Nucleic Acids Res	1982	https://conductscience.org/library/papers/6294608	PubMed
4,607,244	The role of the anticodon in the interaction between methionyl-tRNA synthetase and bacterial initiator tRNA.	Nucleic Acids Res	1974	https://conductscience.org/library/papers/4607244	PubMed
3,419,903	Fast purification of a functional elongator tRNAmet expressed from a synthetic gene in vivo.	Nucleic Acids Res	1988	https://conductscience.org/library/papers/3419903	PubMed
3,320,968	Peptides at the tRNA binding site of the crystallizable monomeric form of E. coli methionyl-tRNA synthetase.	Nucleic Acids Res	1987	https://conductscience.org/library/papers/3320968	PubMed
1,986,377	Selection of suppressor methionyl-tRNA synthetases: mapping the tRNA anticodon binding site.	Proc Natl Acad Sci U S A	1991	https://conductscience.org/library/papers/1986377	PubMed
1,408,786	Involvement of the size and sequence of the anticodon loop in tRNA recognition by mammalian and E. coli methionyl-tRNA synthetases.	Nucleic Acids Res	1992	https://conductscience.org/library/papers/1408786	PubMed
1,101,259	Proton nuclear magnetic resonance of spin-labeled Escherichia coli tRNAf1MET.	Proc Natl Acad Sci U S A	1975	https://conductscience.org/library/papers/1101259	PubMed
1,097,418	Enhanced level and metabolic regulation of methionyl-transfer ribonucleic acid synthetase in different strains of Escherichia coli K-12.	J Bacteriol	1975	https://conductscience.org/library/papers/1097418	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
353,807	Aminoacyl-tRNA synthetases: affinity labeling of the ATP binding site by 2', 3' -ribose oxidized ATP.	Proc Natl Acad Sci U S A	1978	https://conductscience.org/library/papers/353807	PubMed
325,520	On the binding of aminoalkyl adenylates to isoleucyl-tRNA synthetase from Escherichia coli MRE 600.	Nucleic Acids Res	1977	https://conductscience.org/library/papers/325520	PubMed
8,772	Affinity labelling of phenylalanyl-tRNA synthetase from E. coli MRE-600 by E. coli tRNAphe containing photoreactive group.	Nucleic Acids Res	1976	https://conductscience.org/library/papers/8772	PubMed

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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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ClinicalTrials.govNo license stated
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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
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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