Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Delphine Bichet"'
Autor:
Franck C. Chatelain, Nicolas Gilbert, Delphine Bichet, Annaïse Jauch, Sylvain Feliciangeli, Florian Lesage, Olivier Bignucolo
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract Highly selective for K+ at neutral pH, the TWIK1 channel becomes permeable to Na+ upon acidification. Using molecular dynamics simulations, we identify a network of residues involved in this unique property. Between the open and closed state
Externí odkaz:
https://doaj.org/article/014500923e1e431389b15c7a56c2aa1e
Autor:
Frank S. Choveau, Ismail Ben Soussia, Delphine Bichet, Franck C. Chatelain, Sylvain Feliciangeli, Florian Lesage
Publikováno v:
Frontiers in Pharmacology, Vol 12 (2021)
Externí odkaz:
https://doaj.org/article/891b8670092a439983df64c08e0023d9
Autor:
Frank S Choveau, Ismail Ben Soussia, Delphine Bichet, Chatelain C. Franck, Sylvain Feliciangeli, Florian Lesage
Publikováno v:
Frontiers in Pharmacology, Vol 12 (2021)
Inhibitory potassium channels of the TREK1/TRAAK family are integrators of multiple stimuli, including temperature, membrane stretch, polyunsaturated fatty acids and pH. How these signals affect the gating of these channels is the subject of intense
Externí odkaz:
https://doaj.org/article/07d33a38848c4d0183ced9c73c1ad2aa
Autor:
Ismail Ben Soussia, Sonia El Mouridi, Dawon Kang, Alice Leclercq-Blondel, Lamyaa Khoubza, Philippe Tardy, Nora Zariohi, Marie Gendrel, Florian Lesage, Eun-Jin Kim, Delphine Bichet, Olga Andrini, Thomas Boulin
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Mutations that modulate the activity of ion channels are essential tools to understand the biophysical determinants that control their gating. Here authors reveal the role played by a single residue in the second transmembrane domain of vertebrate an
Externí odkaz:
https://doaj.org/article/89358a70ca0b4f15867e6e9b7f65b48a
Autor:
Ismail Ben Soussia, Frank S. Choveau, Sandy Blin, Eun-Jin Kim, Sylvain Feliciangeli, Franck C. Chatelain, Dawon Kang, Delphine Bichet, Florian Lesage
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 11 (2018)
TREK/TRAAK channels are polymodal K+ channels that convert very diverse stimuli, including bioactive lipids, mechanical stretch and temperature, into electrical signals. The nature of the structural changes that regulate their activity remains an ope
Externí odkaz:
https://doaj.org/article/67683d0d8ef84390be2c9f1f6e496be8
Autor:
Dawon Kang, Florian Lesage, Lamyaa Khoubza, Sylvain Feliciangeli, Eun-Jin Kim, Delphine Bichet, Franck C. Chatelain
Two-pore domain (K2P) potassium channels are active as dimers. They produce inhibitory currents regulated by a variety of stimuli. Among them, TALK1, TALK2 and TASK2 form a subfamily of structurally related K2P channels stimulated by extracellular al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f90e3516615c85a5be2bfe0737e7749d
https://doi.org/10.1101/2021.11.08.467666
https://doi.org/10.1101/2021.11.08.467666
Autor:
Sylvain Feliciangeli, Frank S. Choveau, Florian Lesage, Delphine Bichet, Ismail Ben Soussia, Franck C. Chatelain
Publikováno v:
Frontiers in Pharmacology, Vol 12 (2021)
Autor:
Ismail Ben Soussia, Chatelain C Franck, Florian Lesage, Frank S. Choveau, Sylvain Feliciangeli, Delphine Bichet
Publikováno v:
Frontiers in Pharmacology
Frontiers in Pharmacology, Frontiers, 2021, 12, ⟨10.3389/fphar.2021.755826⟩
Frontiers in Pharmacology, Frontiers, 2021, 12, pp.755826. ⟨10.3389/fphar.2021.755826⟩
Frontiers in Pharmacology, Vol 12 (2021)
Frontiers in Pharmacology, Frontiers, 2021, 12, ⟨10.3389/fphar.2021.755826⟩
Frontiers in Pharmacology, Frontiers, 2021, 12, pp.755826. ⟨10.3389/fphar.2021.755826⟩
Frontiers in Pharmacology, Vol 12 (2021)
International audience; Inhibitory potassium channels of the TREK1/TRAAK family are integrators of multiple stimuli, including temperature, membrane stretch, polyunsaturated fatty acids and pH. How these signals affect the gating of these channels is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91c09d12df5f13270474b1eac153037f
https://hal.archives-ouvertes.fr/hal-03440192
https://hal.archives-ouvertes.fr/hal-03440192
Autor:
Lamyaa Khoubza, Nicolas Gilbert, Eun-Jin Kim, Franck C. Chatelain, Sylvain Feliciangeli, Sophie Abelanet, Dawon Kang, Florian Lesage, Delphine Bichet
Publikováno v:
Journal of Biological Chemistry. 298:102447
Two-pore domain K
Publikováno v:
The Journal of Physiology
The Journal of Physiology, Wiley, 2021, 599 (4), pp.1041-1055. ⟨10.1113/JP279870⟩
The Journal of Physiology, Wiley, In press, ⟨10.1113/JP279870⟩
The Journal of Physiology, Wiley, 2021, 599 (4), pp.1041-1055. ⟨10.1113/JP279870⟩
The Journal of Physiology, Wiley, In press, ⟨10.1113/JP279870⟩
International audience; Potassium channels form the largest family of ion channels with more than 80 members involved in cell excitability and signaling. Most of them exist as homomeric channels, whereas specific conditions are required to obtain het
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa174d4e0ba6bad3a5c501660f9506bf
https://hal.archives-ouvertes.fr/hal-03384258
https://hal.archives-ouvertes.fr/hal-03384258