Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Kenton Jon, Swartz"'
Autor:
Mufeng Li, Yao Wang, Rahul Banerjee, Fabrizio Marinelli, Shai Silberberg, José D Faraldo-Gómez, Motoyuki Hattori, Kenton Jon Swartz
Publikováno v:
eLife, Vol 8 (2019)
P2X3 receptor channels expressed in sensory neurons are activated by extracellular ATP and serve important roles in nociception and sensory hypersensitization, making them attractive therapeutic targets. Although several P2X3 structures are known, it
Externí odkaz:
https://doaj.org/article/8c9f3248dbf547e6b13d0827376b0951
Autor:
Ferenc Papp, Suvendu Lomash, Orsolya Szilagyi, Erika Babikow, Jaime Smith, Tsg-Hui Chang, Maria Isabel Bahamonde, Gilman Ewan Stephen Toombes, Kenton Jon Swartz
Publikováno v:
eLife, Vol 8 (2019)
Voltage-activated ion channels contain S1-S4 domains that sense membrane voltage and control opening of ion-selective pores, a mechanism that is crucial for electrical signaling. Related S1-S4 domains have been identified in voltage-sensitive phospha
Externí odkaz:
https://doaj.org/article/719e833809284aff8bc7609104fd67f5
Publikováno v:
eLife, Vol 8 (2019)
The Transient Receptor Potential Vanilloid 1 (TRPV) channel is activated by an array of stimuli, including heat and vanilloid compounds. The TRPV1 homologues TRPV2 and TRPV3 are also activated by heat, but sensitivity to vanilloids and many other ago
Externí odkaz:
https://doaj.org/article/1c680bc014b84408a8491716d852fe9a
Autor:
Doreen Matthies, Chanhyung Bae, Gilman ES Toombes, Tara Fox, Alberto Bartesaghi, Sriram Subramaniam, Kenton Jon Swartz
Publikováno v:
eLife, Vol 7 (2018)
Voltage-activated potassium (Kv) channels open to conduct K+ ions in response to membrane depolarization, and subsequently enter non-conducting states through distinct mechanisms of inactivation. X-ray structures of detergent-solubilized Kv channels
Externí odkaz:
https://doaj.org/article/66eee0a717f34da399393babbf76f5ff
Publikováno v:
eLife, Vol 7 (2018)
The hair cell mechanotransduction (MET) channel complex is essential for hearing, yet it’s molecular identity and structure remain elusive. The transmembrane channel–like 1 (TMC1) protein localizes to the site of the MET channel, interacts with t
Externí odkaz:
https://doaj.org/article/11ac926701564aee8284ed73eb1ab5e5
Autor:
Ferenc, Papp, Suvendu, Lomash, Orsolya, Szilagyi, Erika, Babikow, Jaime, Smith, Tsg-Hui, Chang, Maria Isabel, Bahamonde, Gilman Ewan Stephen, Toombes, Kenton Jon, Swartz
Publikováno v:
eLife
Voltage-activated ion channels contain S1-S4 domains that sense membrane voltage and control opening of ion-selective pores, a mechanism that is crucial for electrical signaling. Related S1-S4 domains have been identified in voltage-sensitive phospha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5fb0fade84f9c518289ccb1b517157ed
https://pubmed.ncbi.nlm.nih.gov/30810529
https://pubmed.ncbi.nlm.nih.gov/30810529