Zobrazeno 1 - 10
of 208
pro vyhledávání: '"Stephen J, Tucker"'
Autor:
Karin E. J. Rödström, Alexander Cloake, Janina Sörmann, Agnese Baronina, Kathryn H. M. Smith, Ashley C. W. Pike, Jackie Ang, Peter Proks, Marcus Schewe, Ingelise Holland-Kaye, Simon R. Bushell, Jenna Elliott, Els Pardon, Thomas Baukrowitz, Raymond J. Owens, Simon Newstead, Jan Steyaert, Elisabeth P. Carpenter, Stephen J. Tucker
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Potassium channels of the Two-Pore Domain (K2P) subfamily, KCNK1-KCNK18, play crucial roles in controlling the electrical activity of many different cell types and represent attractive therapeutic targets. However, the identification of high
Externí odkaz:
https://doaj.org/article/9ac3923cca8e4d1e92ffe481cfd471bf
Publikováno v:
Royal Society Open Science, Vol 10, Iss 8 (2023)
The Markov state model (MSM) is a popular theoretical tool for describing the hierarchy of time scales involved in the function of many proteins especially ion channel gating. An MSM is a particular case of the general non-Markovian model, where the
Externí odkaz:
https://doaj.org/article/16a19a3f7a2e4fbfa34ebe29fc413af4
Autor:
Mark Löbel, Sacha P. Salphati, Kamel El Omari, Armin Wagner, Stephen J. Tucker, Joanne L. Parker, Simon Newstead
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Mutations in CTNS, the lysosomal cystine-proton symporter, cause cystinosis. Here authors report crystal structures of CTNS from Arabidopsis thaliana in complex with cystine, and establish the mode of ligand recognition and mechanism for proton-coupl
Externí odkaz:
https://doaj.org/article/ee022449e04744b496cd09f7f59e0ee5
Autor:
Linda X. Phan, Victor Cruces Chamorro, Hector Martinez-Seara, Jason Crain, Mark S.P. Sansom, Stephen J. Tucker
Publikováno v:
Biophysical Journal. 122:1548-1556
The functional properties of some biological ion channels and membrane transport proteins are proposed to exploit anion-hydrophobic interactions. Here, we investigate a chloride-pumping rhodopsin (ClR) as an example of a membrane protein known to con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::111bfd909cc0ab4f687c36f9dc03bb86
https://doi.org/10.1016/j.bpj.2023.03.026
https://doi.org/10.1016/j.bpj.2023.03.026
Publikováno v:
PLoS ONE, Vol 16, Iss 10, p e0258275 (2021)
In addition to the classical voltage-dependent behavior mediated by the voltage-sensing-domains (VSD) of ion channels, a growing number of voltage-dependent gating behaviors are being described in channels that lack canonical VSDs. A common thread in
Externí odkaz:
https://doaj.org/article/e00ec64f68284455b9dbe1737546126d
Autor:
Janina Sörmann, Marcus Schewe, Peter Proks, Thibault Jouen-Tachoire, Shanlin Rao, Elena B. Riel, Katherine E. Agre, Amber Begtrup, John Dean, Maria Descartes, Jan Fischer, Alice Gardham, Carrie Lahner, Paul R. Mark, Srikanth Muppidi, Pavel N. Pichurin, Joseph Porrmann, Jens Schallner, Kirstin Smith, Volker Straub, Pradeep Vasudevan, Rebecca Willaert, Elisabeth P. Carpenter, Karin E. J. Rödström, Michael G. Hahn, Thomas Müller, Thomas Baukrowitz, Matthew E. Hurles, Caroline F. Wright, Stephen J. Tucker
Sleep apnea is a common disorder that represents a global public health burden. KCNK3 encodes TASK-1, a K+ channel implicated in the control of breathing, but its link with sleep apnea remains poorly understood. Here we describe a new developmental d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3de95186b04ef58aa01a12b0a5e88aa3
https://ora.ox.ac.uk/objects/uuid:9e4145cc-f7d2-4427-a681-824a5df36a17
https://ora.ox.ac.uk/objects/uuid:9e4145cc-f7d2-4427-a681-824a5df36a17
Transition between conformational states of the TREK-1 K2P channel promoted by interaction with PIP2
Members of the TREK family of two-pore domain potassium channels are highly sensitive to regulation by membrane lipids, including phosphatidylinositol-4,5-bisphosphate (PIP2). Previous studies have demonstrated that PIP2increases TREK-1 channel activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dda31b0bf854afb6514570b34929b9aa
https://ora.ox.ac.uk/objects/uuid:6cee08dd-6915-4427-b725-c969b9d52a03
https://ora.ox.ac.uk/objects/uuid:6cee08dd-6915-4427-b725-c969b9d52a03
Publikováno v:
Biophysical Journal. 122:112a-113a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ed521f67667daa8f46dce9564df8ace3
https://doi.org/10.1016/j.bpj.2022.11.788
https://doi.org/10.1016/j.bpj.2022.11.788
Autor:
Frances M. Ashcroft, Russell Joynson, Thomas Hill, Raul Terrón-Expósito, Peter Proks, Gregor Sachse, Elizabeth Haythorne, Liz Bentley, Roger D. Cox, Stephen J. Tucker
Publikováno v:
Diabetes. 70:1145-1156
The ATP-sensitive K+ (KATP) channel controls blood glucose levels by coupling glucose metabolism to insulin secretion in pancreatic β-cells. E23K, a common polymorphism in the pore-forming KATP channel subunit (KCNJ11) gene, has been linked to incre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc32a1fff09ce98744cb6b47e3f75177
https://doi.org/10.2337/db20-0691
https://doi.org/10.2337/db20-0691
Publikováno v:
The Journal of Physical Chemistry. B
Ion channels are proteins which form gated nanopores in biological membranes. Many channels exhibit hydrophobic gating, whereby functional closure of a pore occurs by local dewetting. The pentameric ligand gated ion channels (pLGICs) provide a biolog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f0106e65c0e3f9ce266eb4de0c9a239
https://doi.org/10.1021/acs.jpcb.0c09285
https://doi.org/10.1021/acs.jpcb.0c09285