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Patrice Vende
Researcher at Institut national de la recherche agronomique
Publications - 21
Citations - 1206
Patrice Vende is an academic researcher from Institut national de la recherche agronomique. The author has contributed to research in topics: Gene & EIF4G. The author has an hindex of 14, co-authored 21 publications receiving 1133 citations. Previous affiliations of Patrice Vende include Centre national de la recherche scientifique & National Institutes of Health.
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Journal ArticleDOI
Rotavirus RNA‐binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F
TL;DR: It is shown that a physical link between the 5′ and the 3′ ends of mRNA is necessary for the efficient translation of viral mRNAs and strongly support the closed loop model for the initiation of translation.
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Efficient Translation of Rotavirus mRNA Requires Simultaneous Interaction of NSP3 with the Eukaryotic Translation Initiation Factor eIF4G and the mRNA 3′ End
TL;DR: The results reported here show that NSP3 forms a link between viral mRNA and the cellular translation machinery and hence is a functional analogue of cellular poly(A)-binding protein.
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Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus.
Jean-François Eléouët,Denis Rasschaert,Patrick Lambert,Laurent Levy,Patrice Vende,Hubert Laude +5 more
TL;DR: Analysis of the predicted ORF1a and OrF1b translation products revealed that the putative functional domains identified in infectious bronchitis virus (IBV), mouse hepatitis virus (MHV) and human coronavirus 229E (HCV 229E) are all present in TGEV.
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Nuclear Localization of Cytoplasmic Poly(A)-Binding Protein upon Rotavirus Infection Involves the Interaction of NSP3 with eIF4G and RoXaN
Maya Harb,Michelle M. Becker,Michelle M. Becker,Damien Vitour,Damien Vitour,Carolina Hilma Baron,Patrice Vende,Spencer Brown,Susanne Bolte,Stefan T. Arold,Didier Poncet +10 more
TL;DR: It is shown here that PABP-C1 evicted from eIF4G by NSP3 accumulates in the nucleus of rotavirus-infected cells and requires the interaction of N SP3 with a specific region in RoXaN, the leucine- and aspartic acid-rich (LD) domain.
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RNA-Binding Activity of the Rotavirus Phosphoprotein NSP5 Includes Affinity for Double-Stranded RNA
TL;DR: RNA-binding assays demonstrated that NSP5 has unique nonspecific RNA-binding activity, recognizing single-stranded RNA and dsRNA with similar affinities and possible functions are to cooperate with NSP2 in the destabilization of RNA secondary structures and in the packaging of RNA.