Zobrazeno 1 - 10
of 60
pro vyhledávání: '"ELIC"'
Publikováno v:
Canadian Journal of Urban Research, 2006 Jan 01. 15(2), 96-122.
Externí odkaz:
https://www.jstor.org/stable/26192516
Akademický článek
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Autor:
Marijke Brams, Diletta Pasini, Akshay Sridhar, Chris Ulens, Sarah C. R. Lummis, Kumiko Kambara, Rebecca J. Howard, Aujan Mehregan, Erik Lindahl, Daniel Bertrand
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry
Journal of Biological Chemistry
Pentameric ligand-gated ion channels (pLGICs) are crucial mediators of electrochemical signal transduction in various organisms from bacteria to humans. Lipids play an important role in regulating pLGIC function, yet the structural bases for specific
Autor:
Juan Francisco Viso, Fernando Zamarreño, Alejandro Giorgetti, María Julia Amundarain, Marcelo Daniel Costabel
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
γ-aminobutyric acid-type A (GABA A ) receptors mediate fast synaptic inhibition in the central nervous system of mammals. They are modulated via several sites by numerous compounds, which include GABA, benzodiazepines, ethanol, neurosteroids and ana
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::784f249e84350989d9c4f70674e73db4
http://hdl.handle.net/11562/992826
http://hdl.handle.net/11562/992826
Autor:
Gielen, Marc, Corringer, Pierre-Jean
Publikováno v:
The Journal of Physiology
The Journal of Physiology, Wiley, 2018, ⟨10.1113/JP275100⟩
The Journal of Physiology, 2018, ⟨10.1113/JP275100⟩
The Journal of Physiology, Wiley, 2018, ⟨10.1113/JP275100⟩
The Journal of Physiology, 2018, ⟨10.1113/JP275100⟩
International audience; Pentameric ligand-gated ion channels (pLGICs) mediate fast neurotransmission in the nervous system. Their dysfunction is associated with psychiatric, neurological and neurodegenerative disorders such as schizophrenia, epilepsy
Autor:
Price, Kerry L, Lummis, Sarah CR
Cys-loop receptors are major sites of action for many important therapeutically active compounds, but the sites of action of those that do not act at the orthosteric binding site or at the pore are mostly poorly understood. To help understand these,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a18b87d1682886793e64252867ac228
https://www.repository.cam.ac.uk/handle/1810/278983
https://www.repository.cam.ac.uk/handle/1810/278983
Publikováno v:
Neuropharmacology
Neuropharmacology; Vol 63
Neuropharmacology; Vol 63
The Erwinia ligand-gated ion channel (ELIC) is a bacterial homologue of vertebrate Cys-loop ligand-gated ion channels. It is activated by GABA, and this property, combined with its structural similarity to GABAA and other Cys-loop receptors, makes it
Autor:
Sun, Jiayin
In lipid membranes lacking activating lipids, the nicotinic acetylcholine receptor adopts an uncoupled conformation that binds ligand, but does not transition into an open conformation. Understanding the mechanisms of lipid-dependent uncoupling is es
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0df5ecd40b1558b82ae1af4500647756
The pentameric ligand gated ion channel super family plays a central role in fast synaptic communication between neurons and at the neuromuscular junction. Extensive studies on the prototypic pLGIC, the Torpedo nicotinic acetylcholine receptor (nAChR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b452d7bf17963c513ae96d9ed24c2821
Autor:
Rebecca J. Howard, Sonia Bertrand, Sergei V. Strelkov, Sarah Debaveye, David A. Weston, Sarah C. R. Lummis, Chris Ulens, Jan Tytgat, Marijke Brams, Daniel Bertrand, Bert Billen, Radovan Spurny, Kerry L. Price
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry; Vol 288
Journal of Biological Chemistry; Vol 288
Background: Pentameric ligand-gated ion channels are modulated by general anesthetics. Results: The crystal structure of ELIC in complex with bromoform reveals anesthetic binding in the channel pore and in novel sites in the transmembrane and extrace