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Théophile Ohlmann

Researcher at École normale supérieure de Lyon

Publications -  79
Citations -  4216

Théophile Ohlmann is an academic researcher from École normale supérieure de Lyon. The author has contributed to research in topics: Internal ribosome entry site & Translation (biology). The author has an hindex of 30, co-authored 73 publications receiving 3509 citations. Previous affiliations of Théophile Ohlmann include University of Lyon & University of Cambridge.

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Characterization of a novel RNA-binding region of eIF4GI critical for ribosomal scanning.

TL;DR: It is proposed that this 40 aa motif of eIF4GI is critical for ribosome scanning as demonstrated by studying poliovirus and foot‐and‐mouth disease virus translation.
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In Vitro Cleavage of eIF4GI but not eIF4GII by HIV-1 Protease and its Effects on Translation in the Rabbit Reticulocyte Lysate System

TL;DR: Investigation of the action of the HIV-1 protease on initiation factors eif4GI and eIF4GII using cell extracts and the rabbit reticulocyte lysate system shows that eIF 4GI, but not eIF2GII, is substrate for HIV- 1 protease and this effect can be prevented by a HIV-2 protease inhibitor, palinavir.
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Back to basics: the untreated rabbit reticulocyte lysate as a competitive system to recapitulate cap/poly(A) synergy and the selective advantage of IRES-driven translation

TL;DR: It is described that the non-nuclease-treated RRL (untreated RRL) is able to recapitulate the effects of poly(A) tail on translation in vitro, recapitulating the competitive advantage that the proteolytic processing of eIF4G confers to IRES-driven RNAs.
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miRNA repression of translation in vitro takes place during 43S ribosomal scanning

TL;DR: This work shows that miRNAs target exclusively the early steps of translation with no effect on 60S ribosomal subunit joining, elongation or termination, and finds that translational inhibition takes place during 43S Ribosomal scanning and requires both the poly(A) binding protein and eIF4G independently from their physical interaction.
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A new type of IRES within gag coding region recruits three initiation complexes on HIV-2 genomic RNA

TL;DR: The conservation of the IRES among fast evolving lentiviruses suggests an important physiological role and the structural and functional properties of gag coding sequence define a new type of IRES.