About us

Jean-Paul Renaud

President & CSO and acting CEO, cofounder.


Jean-Paul Renaud created the company in October 2015. He was previously CSO Science & Technology at NovAliX, an innovative drug discovery CRO (2010-2014) ; President & CEO-CSO of AliX (2002-2008), another spinoff company from IGBMC he created in 2002 (AliX’ merger with Novalyst Discovery gave birth to NovAliX in 2009) ; CNRS Research Director at IGBMC (2000-2002, 2008-2009 and 2014-2015) ; CNRS Research Associate at IGBMC (1993-2000) and previously at LCBPT (1988-1993). He was a post-doc at the MRC Laboratory of Molecular Biology in Cambridge, UK (1987-1988) under the mentoring of Kiyoshi Nagai. He obtained his PhD in Organic Chemistry from University Pierre & Marie Curie (Paris 6) in 1986 (Eugène Schueller Prize 1986) and an Engineering Diploma from the École Nationale Supérieure de Chimie de Paris (now Chimie ParisTech) in 1982. Jean-Paul Renaud was twice laureate of the french iLAB Contest (Concours national d’aide à la création d’entreprises de technologie innovantes) in the Creation – Development category : in 2002 for AliX and in 2017 for Urania Therapeutics, formerly called RiboStruct. He was also laureate of Réseau Entreprendre Alsace in 2006 for AliX.

News


2021/12/01

In collaboration with the Yusupov lab at IGBMC, Urania publishes today an article in Nature entitled "Accuracy mechanism of eukaryotic ribosome translocation" describing the 3.2-Å-resolution X-ray structure of the eukaryotic 80S ribosome in a translocation-intermediate state containing mRNA, the elongation factor eEF2 and tRNAs. The model demonstrates how the decoding centre releases a codon–anticodon duplex, allowing its movement on the ribosome. This experimental structure suggests how the 80S ribosome, eEF2 and tRNAs undergo large-scale molecular reorganizations to ensure maintenance of the mRNA reading frame during the complex process of translocation.

This article demonstrates Urania's scientists' capacity to solve high-resolution structures of eukaryotic ribosome complex, to understand at the molecular level the mechanism of the eukaryotic ribosome and to make use of this knowledge to design using a structure-based approach new drug candidates modulating the human ribosome.

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