M
Marc Ruff
Researcher at University of Strasbourg
Publications - 75
Citations - 5825
Marc Ruff is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Integrase & DNA. The author has an hindex of 24, co-authored 68 publications receiving 5460 citations. Previous affiliations of Marc Ruff include Centre national de la recherche scientifique & French Institute of Health and Medical Research.
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Journal ArticleDOI
Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha.
TL;DR: The crystal structure of the human retinoid-X receptor RXR-α ligand-binding domain reveals a previously undiscovered fold of an antiparallel α-helical sandwich, packed as dimeric units.
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Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid.
Jean-Paul Renaud,Natacha Rochel,Marc Ruff,Valéria Vivat,Pierre Chambon,Hinrich Gronemeyer,Dino Moras +6 more
TL;DR: In this paper, a mouse trap mechanism was proposed to reposition the amphi-pathic α-helix of the AF-2 activating domain and form a transcriptionally active receptor.
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Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp)
Marc Ruff,Sankaran Krishnaswamy,M. Boeglin,Arnaud Poterszman,Andre Mitschler,Alberto Podjarny,Bernard Rees,Jean-Claude Thierry,Dino Moras +8 more
TL;DR: The crystal structure of the binary complex tRNA(Asp)-aspartyl tRNA synthetase from yeast was solved with the use of multiple isomorphous replacement to 3 angstrom resolution.
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Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand: 9-cis retinoic acid
TL;DR: Comparison with the unliganded RXRα LBD structure reveals the molecular mechanisms of ligand‐induced conformational changes and allows us to describe at the atomic level how these changes generate the proper protein interface involved in nuclear receptor–coactivator interaction.
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HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.
TL;DR: This review focused on HSC70 structure-function considerations and put a particular emphasis on H SC70 targeting by small molecules and peptides in order to develop intervention strategies that deviate some of HSC60 properties for therapeutic purposes.