Results 11 to 20 of about 193,403 (262)

Drunk potassium channels [PDF]

open access: yesEuropace, 2011
We report the case of a 42-year-old woman who was admitted due to alcohol induced dehydration leading to cardiac symptoms. On physical examination severe hypokalaemia and long QT syndrome were apparent. During potassium (K+) supplementation we simultaneously observed QT interval recovery.
Amir M, Nia   +3 more
openaire   +2 more sources

Potassium channels [PDF]

open access: yesFEBS Letters, 2003
The atomic structures of K+ channels have added a new dimension to our understanding of K+ channel function. I will briefly review how structures have influenced our views on ion conduction, gating of the pore, and voltage sensing.
openaire   +3 more sources

Potassium Channels in Epilepsy [PDF]

open access: yesCold Spring Harbor Perspectives in Medicine, 2016
This review attempts to give a concise and up-to-date overview on the role of potassium channels in epilepsies. Their role can be defined from a genetic perspective, focusing on variants and de novo mutations identified in genetic studies or animal models with targeted, specific mutations in genes coding for a member of the large potassium channel ...
Rüdiger, Köhling, Jakob, Wolfart
openaire   +2 more sources

When Is a Potassium Channel Not a Potassium Channel?

open access: yesFunction, 2022
Abstract Ever since they were first observed in Purkinje fibers of the heart, funny channels have had close connections to potassium channels. Indeed, funny channels were initially thought to produce a potassium current in the heart called IK2.
openaire   +2 more sources

Structure of potassium channels [PDF]

open access: yesCellular and Molecular Life Sciences, 2015
Potassium channels ubiquitously exist in nearly all kingdoms of life and perform diverse but important functions. Since the first atomic structure of a prokaryotic potassium channel (KcsA, a channel from Streptomyces lividans) was determined, tremendous progress has been made in understanding the mechanism of potassium channels and channels conducting ...
Qie Kuang, Pasi Purhonen, Hans Hebert
openaire   +2 more sources

Potassium channel regulation [PDF]

open access: yesEMBO reports, 2003
The sulphonylurea receptor (SUR) is a member of the ATP-binding cassette (ABC) family of membrane proteins. It functions as the regulatory subunit of the ATP-sensitive potassium (KATP) channel, which comprises SUR and Kir6.x proteins. Here, we review data demonstrating functional differences between the two nucleotide binding domains (NBDs) of SUR1. In
Campbell, J, Sansom, MS, Ashcroft, F
openaire   +2 more sources

KCNE1 and KCNE2 provide a checkpoint governing voltage-gated potassium channel α-subunit composition [PDF]

open access: yes, 2011
Voltage-gated potassium (Kv) currents generated by N-type α-subunit homotetramers inactivate rapidly because an N-terminal ball domain blocks the channel pore after activation.
Abbott, G.   +12 more
core   +1 more source

Identification of putative potassium channel homologues in pathogenic protozoa [PDF]

open access: yes, 2012
K(+) channels play a vital homeostatic role in cells and abnormal activity of these channels can dramatically alter cell function and survival, suggesting that they might be attractive drug targets in pathogenic organisms.
Prole, D L   +3 more
core   +1 more source

The selectivity, voltage-dependence and acid sensitivity of the tandem pore potassium channel TASK-1 : contributions of the pore domains [PDF]

open access: yes, 2007
We have investigated the contribution to ionic selectivity of residues in the selectivity filter and pore helices of the P1 and P2 domains in the acid sensitive potassium channel TASK-1.
Sutcliffe, M. J.   +14 more
core   +1 more source

Two-Pore Domain Potassium Channels as Drug Targets: Anesthesia and Beyond.

open access: yes, 2021
Two-pore domain potassium (K2P) channels stabilize the resting membrane potential of both excitable and nonexcitable cells and, as such, are important regulators of cell activity.
Veale, E.L.   +4 more
core   +1 more source

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