T
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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Journal ArticleDOI
Selenium, Selenoproteins and Viral Infection
TL;DR: The formal identification of viral selenoproteins in the genome of molluscum contagiosum and fowlpox viruses demonstrated the importance of selenocsteine in viral cycle.
Journal ArticleDOI
Homozygous mutation of AURKC yields large-headed polyploid spermatozoa and causes male infertility.
Klaus Dieterich,Ricardo Soto Rifo,Ricardo Soto Rifo,Anne Karen Faure,Anne Karen Faure,Sylviane Hennebicq,Sylviane Hennebicq,Baha Ben Amar,Mohamed Zahi,Julia Perrin,Delphine Martinez,B. Sèle,B. Sèle,Pierre-Simon Jouk,Théophile Ohlmann,Théophile Ohlmann,Sophie Rousseaux,Sophie Rousseaux,Joël Lunardi,Pierre F. Ray +19 more
TL;DR: It is concluded that the absence of AURKC causes male infertility owing to the production of large-headed multiflagellar polyploid spermatozoa.
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DEAD‐box protein DDX3 associates with eIF4F to promote translation of selected mRNAs
Ricardo Soto-Rifo,Ricardo Soto-Rifo,Paulina S. Rubilar,Paulina S. Rubilar,Taran Limousin,Taran Limousin,Sylvain de Breyne,Sylvain de Breyne,Didier Decimo,Didier Decimo,Théophile Ohlmann,Théophile Ohlmann +11 more
TL;DR: It is demonstrated that the requirement for DDX3 is highly specific to some selected transcripts, cannot be replaced or substituted by eIF4A and is only needed in the very early steps of ribosome binding and prior to 43S ribosomal scanning, defining an unprecedented role for a DEAD‐box RNA helicase in translation initiation.
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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.
TL;DR: It is demonstrated that translation of uncapped mRNAs normally exhibits a strong requirement for EIF4F, but this dependence is abolished when eIF4G is cleaved, with the Ct domain capable of supporting translation in the absence of the Nt domain.
Journal ArticleDOI
Conducting the initiation of protein synthesis: the role of eIF4G
TL;DR: The role of eif4G and protein partners as well as the cellular and viral events that modulate eIF4G activity in the initiation of translation are reviewed.