Rhinovirus 2A proteinase mediated stimulation of rhinovirus RNA translation is additive to the stimulation effected by cellular RNA binding proteins (Q73044032)

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scientific article published on 01 August 1999

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English	Rhinovirus 2A proteinase mediated stimulation of rhinovirus RNA translation is additive to the stimulation effected by cellular RNA binding proteins	scientific article published on 01 August 1999

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10507322%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

Rhinovirus 2A proteinase mediated stimulation of rhinovirus RNA translation is additive to the stimulation effected by cellular RNA binding proteins (English)

1 reference

Europe PubMed Central

PubMed publication ID

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31 October 2019

2

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31 October 2019

author name string

S L Hunt

1

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31 October 2019

H D Liebig

3

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31 October 2019

E Kuechler

4

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31 October 2019

R J Jackson

5

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31 October 2019

publication date

1 August 1999

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31 October 2019

1 reference

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31 October 2019

62

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31 October 2019

2

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31 October 2019

119-128

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31 October 2019

Poly(rC) binding protein 2 binds to stem-loop IV of the poliovirus RNA 5' noncoding region: identification by automated liquid chromatography-tandem mass spectrometry

1 reference

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Requirement of poly(rC) binding protein 2 for translation of poliovirus RNA

1 reference

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Initiation of translation of human rhinovirus RNA: mapping the internal ribosome entry site

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The involvement of a spliceosome component in internal initiation of human rhinovirus RNA translation

1 reference

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Picornavirus internal ribosome entry segments: comparison of translation efficiency and the requirements for optimal internal initiation of translation in vitro

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Comparison of picornaviral IRES-driven internal initiation of translation in cultured cells of different origins.

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On the fidelity of mRNA translation in the nuclease-treated rabbit reticulocyte lysate system

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In vitro translation of poliovirus RNA: utilization of internal initiation sites in reticulocyte lysate

1 reference

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Polypyrimidine-tract binding protein (PTB) is necessary, but not sufficient, for efficient internal initiation of translation of human rhinovirus-2 RNA

1 reference

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7 January 2021

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unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA

1 reference

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7 January 2021

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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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Nucleic acid binding and intracellular localization of unr, a protein with five cold shock domains

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Translation eukaryotic initiation factor 4G recognizes a specific structural element within the internal ribosome entry site of encephalomyocarditis virus RNA.

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Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation

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Purification of two picornaviral 2A proteinases: interaction with eIF-4 gamma and influence on in vitro translation

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Proteolytic cleavage of initiation factor eIF-4 gamma in the reticulocyte lysate inhibits translation of capped mRNAs but enhances that of uncapped mRNAs.

1 reference

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7 January 2021

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The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E.

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Dissection of the mouse N-ras gene upstream regulatory sequences and identification of the promoter and a negative regulatory element

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Characterization and molecular cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing

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Multiple RRMs contribute to RNA binding specificity and affinity for polypyrimidine tract binding protein

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Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry

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Identifiers

10.1016/S0168-1702(99)00039-8

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10507322%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10507322%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

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