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Trans-editing of mischarged tRNAs
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
14663147
retrieved
1 December 2016
title
Trans-editing of mischarged tRNAs
(English)
1 reference
stated in
PubMed
PubMed ID
14663147
retrieved
1 December 2016
main subject
Ser(Gly)-tRNA(Ala) hydrolase activity
1 reference
stated in
Gene Ontology release 2020-05-02
Gene Ontology ID
GO:0043908
aminoacyl-tRNA editing activity
1 reference
stated in
Gene Ontology release 2020-05-02
Gene Ontology ID
GO:0002161
Ala-tRNA(Pro) hydrolase activity
1 reference
stated in
Gene Ontology release 2020-05-02
Gene Ontology ID
GO:0043906
Putative alanine--tRNA ligase YNL040W
1 reference
stated in
GOA release 2020-03-11
author
Dieter Söll
series ordinal
4
0 references
author name string
Ivan Ahel
series ordinal
1
0 references
Dragana Korencic
series ordinal
2
0 references
Michael Ibba
series ordinal
3
0 references
language of work or name
English
0 references
publication date
23 December 2003
0 references
published in
Proceedings of the National Academy of Sciences of the United States of America
1 reference
stated in
PubMed
PubMed ID
14663147
retrieved
1 December 2016
volume
100
0 references
page(s)
15422-7
0 references
issue
26
0 references
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Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases
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Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem
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A view into the origin of life: aminoacyl-tRNA synthetases
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The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site
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Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability
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Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase
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Footprints of aminoacyl-tRNA synthetases are everywhere
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Universal rules and idiosyncratic features in tRNA identity
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Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases
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Enzymic editing mechanisms and the genetic code
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Editing of errors in selection of amino acids for protein synthesis
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Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing
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Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases
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Dwarf mice and the ageing process.
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Aminoacylation error correction
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/14663147
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1073/PNAS.2136934100
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1850947
ADS bibcode
2003PNAS..10015422A
0 references
OpenCitations bibliographic resource ID
1850947
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1850947
PMCID
307583
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1850947
PubMed ID
14663147
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1850947
ResearchGate publication ID
8970222
0 references
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