Zobrazeno 1 - 10
of 76
pro vyhledávání: '"Thomas Grutter"'
Autor:
Damien Gilabert, Alexia Duveau, Sara Carracedo, Nathalie Linck, Adeline Langla, Rieko Muramatsu, Friedrich Koch-Nolte, François Rassendren, Thomas Grutter, Pascal Fossat, Eric Boué-Grabot, Lauriane Ulmann
Publikováno v:
iScience, Vol 26, Iss 11, Pp 108110- (2023)
Summary: In neuropathic pain, recent evidence has highlighted a sex-dependent role of the P2X4 receptor in spinal microglia in the development of tactile allodynia following nerve injury. Here, using internalization-defective P2X4mCherryIN knockin mi
Externí odkaz:
https://doaj.org/article/fa9120bd2cce452d9255ae5d3ab437c4
Autor:
Francisco Andrés Peralta, Mélaine Balcon, Adeline Martz, Deniza Biljali, Federico Cevoli, Benoit Arnould, Antoine Taly, Thierry Chataigneau, Thomas Grutter
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
PIEZO proteins are large, mechanically-activated trimeric ion channels. Here the authors report a light-gated mouse PIEZO1 channel, mOP1, whereby an azobenzene-based photoswitch covalently localised at the extracellular apex of a transmembrane helix,
Externí odkaz:
https://doaj.org/article/6e2b23ec63e6488caee682f240ae2c00
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 13, p 10896 (2023)
Macropore formation and current facilitation are intriguing phenomena associated with ATP-gated P2X7 receptors (P2X7). Macropores are large pores formed in the cell membrane that allow the passage of large molecules. The precise mechanisms underlying
Externí odkaz:
https://doaj.org/article/595d1290953c438d935e4a4116b16b75
Autor:
Kate Dunning, Adeline Martz, Francisco Andrés Peralta, Federico Cevoli, Eric Boué-Grabot, Vincent Compan, Fanny Gautherat, Patrick Wolf, Thierry Chataigneau, Thomas Grutter
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 12, p 6542 (2021)
P2X7 receptors (P2X7) are cationic channels involved in many diseases. Following their activation by extracellular ATP, distinct signaling pathways are triggered, which lead to various physiological responses such as the secretion of pro-inflammatory
Externí odkaz:
https://doaj.org/article/2e8a3d1c04d940949caf6a55bc5b72b0
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 11 (2018)
The permeability of large cations through the P2X pore has remained arguably the most controversial and complicated topic in P2X-related research, with the emergence of conflicting studies on the existence, mechanism and physiological relevance of a
Externí odkaz:
https://doaj.org/article/072fd915a6e84948b417526f567e6acd
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 10 (2017)
The P2X2 receptor is an ATP-gated ion channel, assembled by three subunits. Recently, it has been found that heterozygous mutations of P2X2 V60L and G353R can cause autosomal dominant nonsyndromic hearing loss. However, the underlying mechanism remai
Externí odkaz:
https://doaj.org/article/3e8a36d0f4344ee69a1b73885c593604
Autor:
Chloé Habermacher, Adeline Martz, Nicolas Calimet, Damien Lemoine, Laurie Peverini, Alexandre Specht, Marco Cecchini, Thomas Grutter
Publikováno v:
eLife, Vol 5 (2016)
P2X receptors function by opening a transmembrane pore in response to extracellular ATP. Recent crystal structures solved in apo and ATP-bound states revealed molecular motions of the extracellular domain following agonist binding. However, the mecha
Externí odkaz:
https://doaj.org/article/7aba456c03d5411892aaca6dec7080a0
Publikováno v:
Toxins, Vol 3, Iss 3, Pp 260-293 (2011)
Ligand-gated ion channels (LGIC) play a central role in inter-cellular communication. This key function has two consequences: (i) these receptor channels are major targets for drug discovery because of their potential involvement in numerous human br
Externí odkaz:
https://doaj.org/article/332b46cbf8764d4b8f93235ed1b3407f
Publikováno v:
Current Opinion in Pharmacology. 62:109-116
Ligand-gated ion channels (LGIC, also referred to as ionotropic receptors) are important transmembrane proteins that open to allow ions to flow across the membrane and locally modify the membrane potential in response to the binding of a ligand. For