Paper8772

Affinity labelling of phenylalanyl-tRNA synthetase from E. coli MRE-600 by E. coli tRNAphe containing photoreactive group.

Gorshkova II and 3 others. Nucleic Acids Res, 1976. Cited by 12 papers, by iCite.

11 sourcespapers-2026-11-12-0.1.0

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ConductScience Library. Affinity labelling of phenylalanyl-tRNA synthetase from E. coli MRE-600 by E. coli tRNAphe containing photoreactive group. Papers, record 8772. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/8772

Paper

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

Title: Affinity labelling of phenylalanyl-tRNA synthetase from E. coli MRE-600 by E. coli tRNAphe containing photoreactive group.; PubMed
Journal: Nucleic Acids Res; PubMed
Year: 1976; PubMed
Publication types: Journal Article; PubMed
PubMed: https://pubmed.ncbi.nlm.nih.gov/8772/; PubMed
DOI: https://doi.org/10.1093/nar/3.6.1577; PubMed
PMC: https://pmc.ncbi.nlm.nih.gov/articles/PMC343015/; PubMed
The journal: https://conductscience.org/library/journal-index/0411011; PubMed
Citations, by iCite: 12; iCite
Relative citation ratio, by iCite: 0.4; iCite
Revised in PubMed: 2019-05-01; PubMed

Authors4

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

Order	Author	Forename
1	Gorshkova II	I I
2	Knorre DG	D G
3	Lavrik OI	O I
4	Nevinsky GA	G A

Source PubMed

Topics14

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

MeSH term	Major
Amino Acyl-tRNA Synthetases	Major topic
Escherichia coli	Major topic
Phenylalanine-tRNA Ligase	Major topic
Thiouridine	Major topic
Adenine Nucleotides
Affinity Labels
Azides
Binding Sites
Diphosphates
Hydrogen-Ion Concentration
Kinetics
Light
Phenylalanine
Protein Binding

Source PubMed

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References13

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

Order	PMID	Title	Journal	Year	In Papers	Source
1	235,467	The influence of the ATP, amino acids and their analogs on the kinetics of the affinity labelling of the phenylalanyl-tRNA synthetase.	FEBS Lett	1975	https://conductscience.org/library/papers/235467	PubMed
2	4,290,596	Selective inhibition of aminoacyl ribonucleic acid synthetases by aminoalkyl adenylates.	Biochemistry	1967	https://conductscience.org/library/papers/4290596	PubMed
3	4,305,463	Mechanism of action of amino acid transfer ribonucleic acid ligases.	J Biol Chem	1969	https://conductscience.org/library/papers/4305463	PubMed
4	4,359,386	Phenylalanyl-tRNA synthetase from Escherichia coli K10. Synergistic coupling between the sites for binding of L-phenylalanine and ATP.	Eur J Biochem	1973	https://conductscience.org/library/papers/4359386	PubMed
5	4,371,652	Kinetics of pyrophosphate-ATP exchange catalysed by L-tryptophan: tRNA ligase from Escherichia coli.	Eur J Biochem	1974	https://conductscience.org/library/papers/4371652	PubMed
6	4,581,817	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.	Eur J Biochem	1973	https://conductscience.org/library/papers/4581817	PubMed
7	4,612,535	The general structure of transfer RNA molecules.	Proc Natl Acad Sci U S A	1974	https://conductscience.org/library/papers/4612535	PubMed
8	4,613,574	Photoaffinity reagents for modification of aminoacyl-tRNA synthetases.	FEBS Lett	1974	https://conductscience.org/library/papers/4613574	PubMed
9	4,875,424	Fractionation of Escherichia coli transfer RNA on benzoylated DEAE-cellulose.	Biochim Biophys Acta	1968	https://conductscience.org/library/papers/4875424	PubMed
10	5,271,039	On the properties and utility of a membrane filter assay in the study of isoleucyl-tRNA synthetase.	Anal Biochem	1970	https://conductscience.org/library/papers/5271039	PubMed
11	5,335,910	The isolation and properties of phenylalanyl ribonucleic acid synthetase from Escherichia coli B.	J Biol Chem	1967	https://conductscience.org/library/papers/5335910	PubMed
12	5,782,965	Studies on nucleosides and nucleotides. 38. Synthesis of 8-bromoadenosine nucleotides.	Chem Pharm Bull (Tokyo)	1969	https://conductscience.org/library/papers/5782965	PubMed
13	778,590	[Affinity modification of phenylalanyl-tRNA-synthetase in the presence of ligands].	Mol Biol (Mosk)	1975	https://conductscience.org/library/papers/778590	PubMed

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Cited by1

The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 12 citations.

PMID	Title	Journal	Year	In Papers
331,263	Analogs of methionyl-tRNA synthetase substrates containing photolabile groups.	Nucleic Acids Res	1977	https://conductscience.org/library/papers/331263

Source PubMed

Data dates

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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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PMC's ID filePublic domain (US government)
PubMedNLM's terms
PubTator 3Public domain
UniProtCC BY 4.0

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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

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