Paper · 9287

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.

Riesner D and 4 others. Eur J Biochem, 1976. Cited by 79 papers, by iCite.

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ConductScience Library. 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. Papers, record 9287. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/9287

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Paper

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

Title: 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.; PubMed
Journal: Eur J Biochem; PubMed
Year: 1976; PubMed
Publication types: Journal Article; PubMed
PubMed: https://pubmed.ncbi.nlm.nih.gov/9287/; PubMed
DOI: https://doi.org/10.1111/j.1432-1033.1976.tb10765.x; PubMed
The journal: https://conductscience.org/library/journal-index/0107600; PubMed
Citations, by iCite: 79; iCite
Relative citation ratio, by iCite: 2; iCite
Revised in PubMed: 2019-06-20; PubMed

Authors5

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

Order	Author	Forename
1	Riesner D	D
2	Pingoud A	A
3	Boehme D	D
4	Peters F	F
5	Maass G	G

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
Saccharomyces cerevisiae	Major topic
Serine-tRNA Ligase	Major topic
Tyrosine-tRNA Ligase	Major topic
Binding Sites
Hydrogen-Ion Concentration
Kinetics
Mathematics
Protein Binding
Protein Conformation
RNA, Transfer
Serine
Temperature

Source PubMed

Grants0

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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.

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References0

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Cited by14

The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 79 citations.

PMID	Title	Journal	Year	In Papers	Source
27,402,839	High Affinity Binding of the Receptor-associated Protein D1D2 Domains with the Low Density Lipoprotein Receptor-related Protein (LRP1) Involves Bivalent Complex Formation: CRITICAL ROLES OF LYSINES 60 AND 191.	J Biol Chem	2016	https://conductscience.org/library/papers/27402839	PubMed
19,734,148	Identification of amino acids in the N-terminal domain of atypical methanogenic-type Seryl-tRNA synthetase critical for tRNA recognition.	J Biol Chem	2009	https://conductscience.org/library/papers/19734148	PubMed
17,206,068	The early history of tRNA recognition by aminoacyl-tRNA synthetases.	J Biosci	2006	https://conductscience.org/library/papers/17206068	PubMed
8,786,969	A novel oligodeoxynucleotide inhibitor of thrombin. I. In vitro metabolic stability in plasma and serum.	Pharm Res	1995	https://conductscience.org/library/papers/8786969	PubMed
6,932,025	Conformational changes during enzyme catalysis: role of water in the transition state.	Proc Natl Acad Sci U S A	1980	https://conductscience.org/library/papers/6932025	PubMed
6,777,760	Serine activation is the rate limiting step of tRNASer aminoacylation by yeast seryl tRNA synthetase.	Nucleic Acids Res	1980	https://conductscience.org/library/papers/6777760	PubMed
909,773	Mechanism of tRNA-synthetase recognition: role of terminal A.	Nucleic Acids Res	1977	https://conductscience.org/library/papers/909773	PubMed
866,174	Conformation of viroids.	Nucleic Acids Res	1977	https://conductscience.org/library/papers/866174	PubMed
732,818	Why should transfer RNAs be so elaborate?	Mol Cell Biochem	1978	https://conductscience.org/library/papers/732818	PubMed
643,623	Yeast seryl tRNA synthetase: two sets of substrate sites involved in aminoacylation.	Nucleic Acids Res	1978	https://conductscience.org/library/papers/643623	PubMed

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None in this release.

Drugs0

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None in this release.

Data0

The data bank entries PubMed's record names. Trial numbers are under Trials.

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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
HGNCCC0
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
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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