Exploring IRES region accessibility by interference of foot-and-mouth disease virus infectivity. - Wikidata - wikimedia - TriplyDB

Exploring IRES region accessibility by interference of foot-and-mouth disease virus infectivity.

Exploring IRES region accessibility by interference of foot-and-mouth disease virus infectivity.

http://www.wikidata.org/entity/Q31075115

about

Biological function of Foot-and-mouth disease virus non-structural proteins and non-coding elements Disruption of Specific RNA-RNA Interactions in a Double-Stranded RNA Virus Inhibits Genome Packaging and Virus Infectivity RNA-binding proteins impacting on internal initiation of translation.Multiple microRNAs targeted to internal ribosome entry site against foot-and-mouth disease virus infection in vitro and in vivo.Magnesium-dependent folding of a picornavirus IRES element modulates RNA conformation and eIF4G interaction.Local RNA flexibility perturbation of the IRES element induced by a novel ligand inhibits viral RNA translation.Insights into Structural and Mechanistic Features of Viral IRES Elements.

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Exploring IRES region accessibility by interference of foot-and-mouth disease virus infectivity.

http://www.wikidata.org/entity/Q31075115

description

2012 nî lūn-bûn

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2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2012 թվականի հուլիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Exploring IRES region accessib ...... uth disease virus infectivity.

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JOURNAL.PONE.0041382

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Exploring IRES region accessib ...... uth disease virus infectivity.

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Maria Flora Rosas

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Teodoro Fajardo

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P2860

Inhibition of dengue virus serotypes 1 to 4 in vero cell cultures with morpholino oligomers

Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells

Structural organization of a viral IRES depends on the integrity of the GNRA motif.

Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro

Sequence-specific inhibition of small RNA function

Inhibition of flavivirus infections by antisense oligomers specifically suppressing viral translation and RNA replication.

Susceptibility to viral infection is enhanced by stable expression of 3A or 3AB proteins from foot-and-mouth disease virus.

Riboproteomic analysis of polypeptides interacting with the internal ribosome-entry site element of foot-and-mouth disease viral RNA.

Identification of cellular genes affecting the infectivity of foot-and-mouth disease virus.

Foot-and-mouth disease virus: a long known virus, but a current threat.

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e41382

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scholarly article

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10.1371/JOURNAL.PONE.0041382

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7

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Encarnación Martínez-Salas

Francisco Sobrino

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2012-07-18T00:00:00Z

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229427998

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