Results 31 to 40 of about 1,383,477 (261)

Activation gating in HCN2 channels. [PDF]

open access: yesPLoS Computational Biology, 2018
Hyperpolarization-activated cyclic nucleotide-modulated (HCN) channels control electrical rhythmicity in specialized brain and heart cells. We quantitatively analysed voltage-dependent activation of homotetrameric HCN2 channels and its modulation by the ...
Sabine Hummert   +5 more
doaj   +1 more source

Structural and Functional Characterization of a Novel Scorpion Toxin that Inhibits NaV1.8 via Interactions With the DI Voltage Sensor and DII Pore Module

open access: yesFrontiers in Pharmacology, 2022
Voltage-gated sodium channel NaV1.8 regulates transmission of pain signals to the brain. While NaV1.8 has the potential to serve as a drug target, the molecular mechanisms that shape NaV1.8 gating are not completely understood, particularly mechanisms ...
Kiran George   +18 more
doaj   +1 more source

Inter-subunit interactions across the upper voltage sensing-pore domain interface contribute to the concerted pore opening transition of Kv channels. [PDF]

open access: yesPLoS ONE, 2013
The tight electro-mechanical coupling between the voltage-sensing and pore domains of Kv channels lies at the heart of their fundamental roles in electrical signaling.
Tzilhav Shem-Ad, Orr Irit, Ofer Yifrach
doaj   +1 more source

Polyunsaturated fatty acids modify the gating of Kv channels

open access: yesFrontiers in Pharmacology, 2012
Polyunsaturated fatty acids (PUFAs) have been reported to exhibit antiarrhythmic properties, which are attributed to their capability to modulate ion channels.
Cristina eMoreno   +4 more
doaj   +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

Distinct gating mechanisms revealed by the structures of a multi-ligand gated K+ channel

open access: yeseLife, 2012
The gating ring-forming RCK domain regulates channel gating in response to various cellular chemical stimuli in eukaryotic Slo channel families and the majority of ligand-gated prokaryotic K+ channels and transporters.
Chunguang Kong   +7 more
doaj   +1 more source

Structure, dynamics and implied gating mechanism of a human cyclic nucleotide-gated channel.

open access: yesPLoS Computational Biology, 2014
Cyclic nucleotide-gated (CNG) ion channels are nonselective cation channels, essential for visual and olfactory sensory transduction. Although the channels include voltage-sensor domains (VSDs), their conductance is thought to be independent of the ...
Yana Gofman   +4 more
doaj   +1 more source

Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits [PDF]

open access: yes, 2003
The subunits that compose eukaryotic glutamate ion channel receptors have three transmembrane domains (TMs) and terminate with intracellular tails that are important for controlling channel expression and localization.
Schorge, S.   +3 more
core   +1 more source

Effects of ionic strength on gating and permeation of TREK-2 K2P channels.

open access: yesPLoS ONE, 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.
Linus J Conrad   +2 more
doaj   +1 more source

Cytoplasmic domains and voltage-dependent potassium channel gating

open access: yesFrontiers in Pharmacology, 2012
The basic architecture of the voltage-dependent K+ channels (Kv channels) corresponds to a transmembrane protein core in which the permeation pore, the voltage sensing components and the gating machinery (cytoplasmic facing gate and sensor-gate coupler ...
Francisco eBarros   +2 more
doaj   +1 more source

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