Interaction of the aromatics Tyr-72/Trp-288 in the interface of the extracellular and transmembrane domains is essential for proton gating of acid-sensing ion channels
about
ENaC regulation by proteases and shear stressStructure and activity of the acid-sensing ion channelsInherent dynamics of the acid-sensing ion channel 1 correlates with the gating mechanismASIC and ENaC type sodium channels: conformational states and the structures of the ion selectivity filtersA combined computational and functional approach identifies new residues involved in pH-dependent gating of ASIC1a.The contact region between three domains of the extracellular loop of ASIC1a is critical for channel function.The N-terminal domain allosterically regulates cleavage and activation of the epithelial sodium channel.The interaction between the first transmembrane domain and the thumb of ASIC1a is critical for its N-glycosylation and trafficking.Identification of a calcium permeable human acid-sensing ion channel 1 transcript variant.Base of the thumb domain modulates epithelial sodium channel gating.Insights into the mechanism of pore opening of acid-sensing ion channel 1a.ENaC structure and function in the wake of a resolved structure of a family member.Computational Tools for Interpreting Ion Channel pH-Dependence.Extracellular Subunit Interactions Control Transitions between Functional States of Acid-sensing Ion Channel 1a.Role of the wrist domain in the response of the epithelial sodium channel to external stimuli.Gain-of-Function Mutation W493R in the Epithelial Sodium Channel Allosterically Reconfigures Intersubunit Coupling.Gating transitions in the palm domain of ASIC1a.Exploration of the Peptide Recognition of an Amiloride-sensitive FMRFamide Peptide-gated Sodium Channel.Structural mechanisms underlying the function of epithelial sodium channel/acid-sensing ion channel.The Thumb Domain Mediates Acid-sensing Ion Channel Desensitization.Neurotoxic unc-8 mutants encode constitutively active DEG/ENaC channels that are blocked by divalent cations.Two residues in the extracellular domain convert a nonfunctional ASIC1 into a proton-activated channelIndependent contribution of extracellular proton binding sites to ASIC1a activation.Proton-mediated conformational changes in an acid-sensing ion channel.Insights into the molecular determinants of proton inhibition in an acid-inactivated degenerins and mammalian epithelial Na(+) channel.Protonation controls ASIC1a activity via coordinated movements in multiple domains.Conformational changes associated with proton-dependent gating of ASIC1a.Structure, function, and pharmacology of acid-sensing ion channels (ASICs): focus on ASIC1a.Insight into DEG/ENaC channel gating from genetics and structure.Structural domains underlying the activation of acid-sensing ion channel 2a.ASICs and neuropeptides.Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein.Deactivation kinetics of acid-sensing ion channel 1a are strongly pH-sensitive.Membrane anchoring and interaction between transmembrane domains are crucial for K+ channel function.Conformational dynamics and role of the acidic pocket in ASIC pH-dependent gating.Computational elucidation, Mutational and Hot spot-based designing of potential inhibitors against human acid-sensing ion channels (hASIC-1a) to treatment of various physiological conditions.Coupling of proton binding in extracellular domain to channel gating in acid-sensing ion channel.Structural elements for the generation of sustained currents by the acid pain sensor ASIC3.An acid-sensing ion channel from shark (Squalus acanthias) mediates transient and sustained responses to protons.Functional and structural identification of amino acid residues of the P2X2 receptor channel critical for the voltage- and [ATP]-dependent gating.
P2860
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P2860
Interaction of the aromatics Tyr-72/Trp-288 in the interface of the extracellular and transmembrane domains is essential for proton gating of acid-sensing ion channels
description
2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2009
@ast
im Februar 2009 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2009/02/13)
@sk
vědecký článek publikovaný v roce 2009
@cs
wetenschappelijk artikel (gepubliceerd op 2009/02/13)
@nl
наукова стаття, опублікована в лютому 2009
@uk
name
Interaction of the aromatics T ...... g of acid-sensing ion channels
@ast
Interaction of the aromatics T ...... g of acid-sensing ion channels
@en
Interaction of the aromatics T ...... g of acid-sensing ion channels
@nl
type
label
Interaction of the aromatics T ...... g of acid-sensing ion channels
@ast
Interaction of the aromatics T ...... g of acid-sensing ion channels
@en
Interaction of the aromatics T ...... g of acid-sensing ion channels
@nl
prefLabel
Interaction of the aromatics T ...... g of acid-sensing ion channels
@ast
Interaction of the aromatics T ...... g of acid-sensing ion channels
@en
Interaction of the aromatics T ...... g of acid-sensing ion channels
@nl
P2093
P2860
P356
P1476
Interaction of the aromatics T ...... g of acid-sensing ion channels
@en
P2093
Cecilia M. Canessa
Youshan Yang
P2860
P304
P356
10.1074/JBC.M805302200
P407
P577
2009-02-13T00:00:00Z