S
Stephen J. Tucker
Researcher at University of Oxford
Publications - 158
Citations - 9006
Stephen J. Tucker is an academic researcher from University of Oxford. The author has contributed to research in topics: Gating & Potassium channel. The author has an hindex of 47, co-authored 143 publications receiving 8165 citations. Previous affiliations of Stephen J. Tucker include Kyoto University & Pontifical Catholic University of Chile.
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Journal ArticleDOI
A divergent CFTR homologue: highly regulated salt transport in the euryhaline teleost F. heteroclitus
TL;DR: After abrupt exposure of FW-adapted killifish to SW, kfCFTR expression in the gill increased severalfold, suggesting a role for kf CFTR in salinity adaptation, and expression of kFCFTR in Xenopus oocytes generated adenosine 3',5'-cyclic monophosphate-activated, Cl--selective currents similar to those generated by hCFTR.
Journal ArticleDOI
The pore structure and gating mechanism of K2P channels: K2P channel gating
Paula L. Piechotta,Markus Rapedius,Phillip J. Stansfeld,Murali K. Bollepalli,Gunter Erhlich,Isabelle Andres-Enguix,Hariolf Fritzenschaft,Niels Decher,Mark S.P. Sansom,Stephen J. Tucker,Thomas Baukrowitz +10 more
TL;DR: In this paper, quaternary ammonium (QA) ions bind with high affinity deep within the pore of TREK-1 and have free access to their binding site before channel activation by intracellular pH or pressure.
Journal ArticleDOI
The pore structure and gating mechanism of K2P channels
Paula L. Piechotta,Markus Rapedius,Phillip J. Stansfeld,Murali K. Bollepalli,Gunter Ehrlich,Isabelle Andres-Enguix,Hariolf Fritzenschaft,Niels Decher,Mark S.P. Sansom,Stephen J. Tucker,Thomas Baukrowitz +10 more
TL;DR: It is reported that quaternary ammonium ions bind with high-affinity deep within the pore of TREK-1 and have free access to their binding site before channel activation by intracellular pH or pressure, demonstrating that, unlike most other K+ channels, the bundle-crossing gate in this K2P channel is constitutively open.
The Pore Structure and Gating Mechanism of K2P Channels
Paula L. Piechotta,Markus Rapedius,Phillip J. Stansfeld,Murali K. Bollepalli,Gunter Ehrlich,Isabelle Andres-Enguix,Hariolf Fritzenschaft,Niels Decher,Sansom,Stephen J. Tucker,Thomas Baukrowitz +10 more
TL;DR: It is reported that quaternary ammonium ions bind with high‐affinity deep within the pore of TREK‐1 and have free access to their binding site before channel activation by intracellular pH or pressure, demonstrating that, unlike most other K+ channels, the bundle‐crossing gate in this K2P channel is constitutively open.
Journal ArticleDOI
pH dependence of the inwardly rectifying potassium channel, Kir5.1, and localization in renal tubular epithelia.
TL;DR: Kir5.1/Kir4.1 heteromeric channel activity is extremely sensitive to inhibition by intracellular acidification and that this novel property is conferred predominantly by the Kir5.