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Development of a tRNA-dependent in vitro translation system
scientific article
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instance of
scholarly article
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title
Development of a tRNA-dependent in vitro translation system
(English)
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author name string
R J Jackson
series ordinal
1
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S Napthine
series ordinal
2
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I Brierley
series ordinal
3
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language of work or name
English
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publication date
May 2001
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published in
RNA
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volume
7
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issue
5
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page(s)
765-73
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cites work
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The use of affinity chromatography on 2'5' ADP-sepharose reveals a requirement for NADPH, thioredoxin and thioredoxin reductase for the maintenance of high protein synthesis activity in rabbit reticulocyte lysates
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An efficient ribosomal frame-shifting signal in the polymerase-encoding region of the coronavirus IBV.
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29 September 2017
Messenger RNA translation in the presence of homologous and heterologous tRNA
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The influence of viral coding sequences on the efficiency of internal initiation of translation of cardiovirus RNAs
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2 June 2018
Characterization of an efficient coronavirus ribosomal frameshifting signal: requirement for an RNA pseudoknot
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2 June 2018
Mutational analysis of the "slippery-sequence" component of a coronavirus ribosomal frameshifting signal
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2 June 2018
Direct analysis of aminoacylation levels of tRNAs in vivo. Application to studying recognition of Escherichia coli initiator tRNA mutants by glutaminyl-tRNA synthetase
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The Q-base of asparaginyl-tRNA is dispensable for efficient -1 ribosomal frameshifting in eukaryotes.
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Nucleotide sequence of the brome mosaic virus genome and its implications for viral replication
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The Preparation and Properties of Gel-Filtered Rabbit-Reticulocyte Lysate Protein-Synthesis Systems
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The Roles of Sugar Phosphates and Thiol-Reducing Systems in the Control of Reticulocyte Protein Synthesis
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[4] Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA
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retrieved
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Identifiers
DOI
10.1017/S1355838201002539
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1340942
OpenCitations bibliographic resource ID
1340942
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1340942
PMCID
1370128
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1340942
PubMed ID
11350040
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1340942
ResearchGate publication ID
11987666
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