A novel protein-RNA binding assay: functional interactions of the foot-and-mouth disease virus internal ribosome entry site with cellular proteins.
about
Structural organization of a viral IRES depends on the integrity of the GNRA motif.Biological function of Foot-and-mouth disease virus non-structural proteins and non-coding elementsStructural insights into the transcriptional and translational roles of Ebp1Truncated initiation factor eIF4G lacking an eIF4E binding site can support capped mRNA translation.Toward a structural understanding of IRES RNA functionFunctional analysis of Kaposi's sarcoma-associated herpesvirus vFLIP expression reveals a new mode of IRES-mediated translation.The translation of capped mRNAs has an absolute requirement for the central domain of eIF4G but not for the cap-binding initiation factor eIF4E.Candidate RNA structures for domain 3 of the foot-and-mouth-disease virus internal ribosome entry site.Functional and structural similarities between the internal ribosome entry sites of hepatitis C virus and porcine teschovirus, a picornavirus.Multiple microRNAs targeted to internal ribosome entry site against foot-and-mouth disease virus infection in vitro and in vivo.Conserved nucleotides within the J domain of the encephalomyocarditis virus internal ribosome entry site are required for activity and for interaction with eIF4G.Magnesium-dependent folding of a picornavirus IRES element modulates RNA conformation and eIF4G interaction.In-cell SHAPE uncovers dynamic interactions between the untranslated regions of the foot-and-mouth disease virus RNA.Specific interference between two unrelated internal ribosome entry site elements impairs translation efficiency.Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translationEvolutionary conserved motifs constrain the RNA structure organization of picornavirus IRES.Foot-and-Mouth Disease Virus Counteracts on Internal Ribosome Entry Site Suppression by G3BP1 and Inhibits G3BP1-Mediated Stress Granule Assembly via Post-Translational Mechanisms.
P2860
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P2860
A novel protein-RNA binding assay: functional interactions of the foot-and-mouth disease virus internal ribosome entry site with cellular proteins.
description
2001 nî lūn-bûn
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2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
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2001年の論文
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2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
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2001年論文
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2001年论文
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name
A novel protein-RNA binding as ...... ry site with cellular proteins
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A novel protein-RNA binding as ...... y site with cellular proteins.
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A novel protein-RNA binding as ...... y site with cellular proteins.
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A novel protein-RNA binding as ...... ry site with cellular proteins
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A novel protein-RNA binding as ...... y site with cellular proteins.
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A novel protein-RNA binding as ...... y site with cellular proteins.
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A novel protein-RNA binding as ...... ry site with cellular proteins
@nl
A novel protein-RNA binding as ...... y site with cellular proteins.
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A novel protein-RNA binding as ...... y site with cellular proteins.
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P2860
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A novel protein-RNA binding as ...... ry site with cellular proteins
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P2093
I A Stassinopoulos
P2860
P304
P3181
P356
10.1017/S1355838201001170
P407
P577
2001-01-01T00:00:00Z