Results 21 to 30 of about 2,447,449 (300)

Voltage Gated Lipid Ion Channels [PDF]

open access: yesBiophysical Journal, 2013
10 pages, 7 figures - Strongly revised version compared to first version.
Blicher, Andreas   +1 more
openaire   +7 more sources

A new polymodal gating model of the proton-activated chloride channel.

open access: yesPLoS Biology, 2023
The proton-activated chloride (PAC) channel plays critical roles in ischemic neuron death, but its activation mechanisms remain elusive. Here, we investigated the gating of PAC channels using its novel bifunctional modulator C77304.
Piao Zhao   +13 more
doaj   +1 more source

Theoretical implication of liganding reactions in axonal sodium channel gating [PDF]

open access: yes, 1980
Dorogi PL, Neumann E. Theoretical implication of liganding reactions in axonal sodium channel gating. Neurochemistry International. 1980;2:45-51.Mathematical simulation models for measured permeability properties of axonal Na+ channels point to the ...
Dorogi, Peter L., Neumann, Eberhard
core   +1 more source

Bubbles, Gating, and Anesthetics in Ion Channels [PDF]

open access: yesBiophysical Journal, 2008
We suggest that bubbles are the bistable hydrophobic gates responsible for the on-off transitions of single channel currents. In this view, many types of channels gate by the same physical mechanism-dewetting by capillary evaporation-but different types of channels use different sensors to modulate hydrophobic properties of the channel wall and thereby
Roth, R.   +3 more
openaire   +3 more sources

Structural and molecular insight into the pH-induced low-permeability of the voltage-gated potassium channel Kv1.2 through dewetting of the water cavity.

open access: yesPLoS Computational Biology, 2020
Understanding the gating mechanism of ion channel proteins is key to understanding the regulation of cell signaling through these channels. Channel opening and closing are regulated by diverse environmental factors that include temperature, electrical ...
Juhwan Lee   +3 more
doaj   +1 more source

Molecular mechanisms of the coupling of gating to voltage sensing in transmembrane proteins [PDF]

open access: yes, 2014
Voltage gated potassium ion (Kv) channels regulate action potentials of the nervous system by responding to changes in transmembrane voltage, enabling K+ transport across the membrane to restore cells to their resting potential.
Starek, Greg
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

Flexibility of the N-Terminal mVDAC1 Segment Controls the Channel’s Gating Behavior [PDF]

open access: yes, 2012
Since the solution of the molecular structures of members of the voltage dependent anion channels (VDACs), the N-terminal α-helix has been the main focus of attention, since its strategic location, in combination with its putative conformational ...
Grosse, Wolfgang   +23 more
core   +2 more sources

Mechanistic Insight into Subunit Stoichiometry for KIR Channel Gating: Ligand Binding, Gating, Binding-Gating Coupling, Coordination, and Cooperativity [PDF]

open access: yes, 2005
Ligand-gated ion channels couple intra- and extracellular chemical signals to cellular excitability. In response to a specific ligand, these channels change their permeability to certain ions by opening or closing their ion conductive pathway, a ...
Wang, Runping
core   +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

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