Paper · 377229

The binding of tyrosinyl-5'-AMP to tyrosyl-tRNA synthetase (E.coli).

Grosse F and 3 others. Nucleic Acids Res, 1979. Cited by 3 papers, by iCite.

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ConductScience Library. The binding of tyrosinyl-5'-AMP to tyrosyl-tRNA synthetase (E.coli). Papers, record 377229. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/377229

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Paper

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

Title: The binding of tyrosinyl-5'-AMP to tyrosyl-tRNA synthetase (E.coli).; PubMed
Journal: Nucleic Acids Res; PubMed
Year: 1979; PubMed
Publication types: Journal Article; PubMed
PubMed: https://pubmed.ncbi.nlm.nih.gov/377229/; PubMed
DOI: https://doi.org/10.1093/nar/6.4.1631; PubMed
PMC: https://pmc.ncbi.nlm.nih.gov/articles/PMC327796/; PubMed
The journal: https://conductscience.org/library/journal-index/0411011; PubMed
Citations, by iCite: 3; iCite
Relative citation ratio, by iCite: 0.08; iCite
Revised in PubMed: 2019-12-10; PubMed

Authors4

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

Order	Author	Forename
1	Grosse F	F
2	Krauss G	G
3	Kownatzki R	R
4	Maass G	G

Source PubMed

Topics8

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

MeSH term	Major
Amino Acyl-tRNA Synthetases	Major topic
Escherichia coli	Major topic
Tyrosine	Major topic
Tyrosine-tRNA Ligase	Major topic
Adenosine Monophosphate
Kinetics
Protein Binding
Transfer RNA Aminoacylation

Source PubMed

Grants0

Each grant PubMed's record writes, matched to the NIH project NIH's grant and paper links name for this paper, and each of those links the record does not write.

None in this release.

Trials0

The trials whose ClinicalTrials.gov record lists the paper, and the trial numbers the paper's PubMed record names.

None in this release.

Comments and corrections0

PubMed's comments and corrections, NLM's own indexing: retractions first, then expressions of concern, errata and updates, and comments last.

None in this release.

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	691,047	Binding of tyrosine, adenosine triphosphate and analogues to crystalline tyrosyl transfer RNA synthetase.	J Mol Biol	1978	https://conductscience.org/library/papers/691047	PubMed
2	909,773	Mechanism of tRNA-synthetase recognition: role of terminal A.	Nucleic Acids Res	1977	https://conductscience.org/library/papers/909773	PubMed
3	199,234	Ligand binding stoichiometries, subunit structure, and slow transitions in aminoacyl-tRNA synthetases.	Biochemistry	1977	https://conductscience.org/library/papers/199234	PubMed
4	9,287	Distinct steps in the specific binding of tRNA to aminoacyl-tRNA synthetase. Temperature-jump studies on the serine-specific system from yeast and the tyrosine-specific system from Escherichia coli.	Eur J Biochem	1976	https://conductscience.org/library/papers/9287	PubMed
5	4,621,706	The mechanism of reaction of methionyl-tRNA synthetase from Escherichia coli. Interaction of the enzyme with ligands of the amino-acid-activation reaction.	Eur J Biochem	1972	https://conductscience.org/library/papers/4621706	PubMed
6	4,342,025	Isoleucyl transfer ribonucleic acid synthetase of Escherichia coli B. A rapid kinetic investigation of the L-isoleucine-activating reaction.	Biochemistry	1972	https://conductscience.org/library/papers/4342025	PubMed
7	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
8	1,109,589	Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-sites reactivity in oligomeric enzymes.	Biochemistry	1975	https://conductscience.org/library/papers/1109589	PubMed
9	162,826	Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase.	Biochemistry	1975	https://conductscience.org/library/papers/162826	PubMed
10	1,109,585	Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases.	Biochemistry	1975	https://conductscience.org/library/papers/1109585	PubMed

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Cited by0

The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 3 citations.

None in this release.

Genes0

The genes the Gene search release ties to the paper: Swiss-Prot's references first, then PubTator's text mining.

None in this release.

Drugs0

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None in this release.

Data0

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None in this release.

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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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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