Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Driss El Moustaine"'
Autor:
Pauline Scholler, Damien Nevoltris, Dimitri de Bundel, Simon Bossi, David Moreno-Delgado, Xavier Rovira, Thor C. Møller, Driss El Moustaine, Michaël Mathieu, Emilie Blanc, Heather McLean, Elodie Dupuis, Gérard Mathis, Eric Trinquet, Hervé Daniel, Emmanuel Valjent, Daniel Baty, Patrick Chames, Philippe Rondard, Jean-Philippe Pin
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
G protein-coupled receptors are considered promising therapeutic targets. Here, the authors have identified nanobodies, or single-domain llama antibodies, that specifically enhance agonist-induced activity of a type of G protein-coupled receptor, the
Externí odkaz:
https://doaj.org/article/816648732d614ed3bfb0746f18dd9438
Autor:
Patrick Bron, Jean-Philippe Pin, Pauline Scholler, Philippe Rondard, Driss El Moustaine, Jean-Louis Banères, Bernard Mouillac, Rita Rahmeh, Etienne Doumazane, Sébastien Granier
Publikováno v:
Proceedings of the National Academy of Sciences. 109:16342-16347
The eight metabotropic glutamate receptors (mGluRs) are key modulators of synaptic transmission and are considered promising targets for the treatment of various brain disorders. Whereas glutamate acts at a large extracellular domain, allosteric modu
Publikováno v:
Zeitschrift fur Naturforschung B
Zeitschrift fur Naturforschung B, Verlag der Zeitschrift Fuer Naturforschung, 2008, 63, pp.747-755. ⟨10.1515/znb-2008-0624⟩
Zeitschrift fur Naturforschung B, Verlag der Zeitschrift Fuer Naturforschung, 2008, 63, pp.747-755. ⟨10.1515/znb-2008-0624⟩
Copper ions (Cu2+) and heparan sulfate (HS) are suspected to act as regulatory agents in the conversion of cellular prion protein (PrPC) to its infectious isoform. However, the mechanism of this reaction is still largely unknown. Our previous report
Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways
Publikováno v:
FEBS Journal. 275:2021-2031
As limited structural information is available on prion protein (PrP) misfolding and aggregation, a causative link between the specific (supra)molecular structure of PrP and transmissible spongiform encephalopathies remains to be elucidated. In this