J
Jean-Paul Renaud
Researcher at Centre national de la recherche scientifique
Publications - 31
Citations - 2071
Jean-Paul Renaud is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Ligand (biochemistry) & Orphan receptor. The author has an hindex of 20, co-authored 31 publications receiving 2019 citations. Previous affiliations of Jean-Paul Renaud include Laboratory of Molecular Biology.
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Journal ArticleDOI
Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3.
Holger Greschik,Jean-Marie Wurtz,Sarah Sanglier,William Bourguet,Alain Van Dorsselaer,Dino Moras,Jean-Paul Renaud +6 more
TL;DR: The crystal structure of the ligand binding domain (LBD) of the estrogen-related receptor 3 (ERR3) complexed with a steroid receptor coactivator-1 (SRC-1) peptide reveals a transcriptionally active conformation in absence of any ligand.
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Binding of Ligands and Activation of Transcription by Nuclear Receptors
TL;DR: The ensemble of NR structures, including those of DNA-binding domains, provides one of the foundations for the understanding of interactions with transcription intermediary factors up to the characterization of the link between NR complexes and the basal transcriptional machinery at the structural level.
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All-trans retinoic acid is a ligand for the orphan nuclear receptor ROR beta.
Catherine Stehlin-Gaon,Dominica Willmann,Denis Zeyer,Sarah Sanglier,Alain Van Dorsselaer,Jean-Paul Renaud,Dino Moras,Roland Schüle +7 more
TL;DR: This work finds that all-trans retinoic acid (ATRA) and several retinoids bind to the RORβ ligand-binding domain (LBD), providing a novel pathway for retinoid action.
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Cisplatin- and UV-damaged DNA lure the basal transcription factor TFIID/TBP.
Paul Vichi,Frédéric Coin,Jean-Paul Renaud,Wim Vermeulen,J.H.J. Hoeijmakers,Dino Moras,Jean-Marc Egly +6 more
TL;DR: It is found that microinjection of additional TBP in living human fibroblasts alleviates the reduction in RNA synthesis after UV irradiation and future anticancer drugs could be designed with the consideration of lesion recognition by TBP and their ability to reduce transcription.
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Structural Basis for the Deactivation of the Estrogen-related Receptor {gamma} by Diethylstilbestrol or 4-Hydroxytamoxifen and Determinants of Selectivity.
TL;DR: Crystal structures of the ERRγ ligand binding domain (LBD) complexed with diethylstilbestrol or 4-hydroxytamoxifen and structural differences with ERs are revealed that explain why ERR γ does not bind estradiol or raloxifene and will help to design new selective antagonists.