Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Rémy Sounier"'
Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
Autor:
Ieva Vasiliauskaité-Brooks, Robert D. Healey, Pascal Rochaix, Julie Saint-Paul, Rémy Sounier, Claire Grison, Thierry Waltrich-Augusto, Mathieu Fortier, François Hoh, Essa M. Saied, Christoph Arenz, Shibom Basu, Cédric Leyrat, Sébastien Granier
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. Here authors solve the Xray structure of human ACER3 and uncover a Ca2+ binding site providing an explanation for the known
Externí odkaz:
https://doaj.org/article/9944c8e0584f421dad2c7d0bf7a0b051
Autor:
Julien Bous, Aurélien Fouillen, Hélène Orcel, Stefano Trapani, Xiaojing Cong, Simon Fontanel, Julie Saint-Paul, Joséphine Lai-Kee-Him, Serge Urbach, Nathalie Sibille, Rémy Sounier, Sébastien Granier, Bernard Mouillac, Patrick Bron
Publikováno v:
Science Advances
Science Advances, 2022, 8 (35), pp.eabo7761. ⟨10.1126/sciadv.abo7761⟩
Science Advances, 2022, 8 (35), pp.eabo7761. ⟨10.1126/sciadv.abo7761⟩
Arrestins interact with G protein-coupled receptors (GPCRs) to stop G protein activation and to initiate key signaling pathways. Recent structural studies shed light on the molecular mechanisms involved in GPCR-arrestin coupling, but whether this pro
Publikováno v:
Membranes, Vol 13, Iss 6, p 606 (2023)
G-protein coupled receptors (GPCRs) are versatile signaling proteins that regulate key physiological processes in response to a wide variety of extracellular stimuli. The last decade has seen a revolution in the structural biology of clinically impor
Externí odkaz:
https://doaj.org/article/60257346674b40799933fc4f4e29f2f0
Autor:
Diego F. Gauto, Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin, Pavel Macek, Remy Sounier, Astrid C. Sivertsen, Elena Schmidt, Rime Kerfah, Guillaume Mas, Jacques-Philippe Colletier, Peter Güntert, Adrien Favier, Guy Schoehn, Paul Schanda, Jerome Boisbouvier
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
NMR structure determination is challenging for proteins with a molecular weight above 30 kDa and atomic-resolution structure determination from cryo-EM data is currently not the rule. Here the authors describe an integrated structure determination ap
Externí odkaz:
https://doaj.org/article/b46e113a51c845d98317d17073be2ebe