A combined computational and functional approach identifies new residues involved in pH-dependent gating of ASIC1a.
about
Structure and activity of the acid-sensing ion channelsASIC and ENaC type sodium channels: conformational states and the structures of the ion selectivity filtersThe contact region between three domains of the extracellular loop of ASIC1a is critical for channel function.Binding site and inhibitory mechanism of the mambalgin-2 pain-relieving peptide on acid-sensing ion channel 1a.Na+ inhibits the epithelial Na+ channel by binding to a site in an extracellular acidic cleftInsights into the mechanism of pore opening of acid-sensing ion channel 1a.Second transmembrane domain modulates epithelial sodium channel gating in response to shear stressAtomic level characterization of the nonproton ligand-sensing domain of ASIC3 channels.Computational Tools for Interpreting Ion Channel pH-Dependence.Extracellular Subunit Interactions Control Transitions between Functional States of Acid-sensing Ion Channel 1a.Subtype-specific modulation of acid-sensing ion channel (ASIC) function by 2-guanidine-4-methylquinazoline.Proton and non-proton activation of ASIC channels.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.Independent contribution of extracellular proton binding sites to ASIC1a activation.Protonation controls ASIC1a activity via coordinated movements in multiple domains.Regulation of NhaA by protons.Structural domains underlying the activation of acid-sensing ion channel 2a.Random mutagenesis screening indicates the absence of a separate H(+)-sensor in the pH-sensitive Kir channels.Deactivation kinetics of acid-sensing ion channel 1a are strongly pH-sensitive.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.New insights into the signaling mechanism of the pH-responsive, membrane-integrated transcriptional activator CadC of Escherichia coliNaked mole-rat acid-sensing ion channel 3 forms nonfunctional homomers, but functional heteromers.
P2860
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P2860
A combined computational and functional approach identifies new residues involved in pH-dependent gating of ASIC1a.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
A combined computational and f ...... pH-dependent gating of ASIC1a.
@ast
A combined computational and f ...... pH-dependent gating of ASIC1a.
@en
type
label
A combined computational and f ...... pH-dependent gating of ASIC1a.
@ast
A combined computational and f ...... pH-dependent gating of ASIC1a.
@en
prefLabel
A combined computational and f ...... pH-dependent gating of ASIC1a.
@ast
A combined computational and f ...... pH-dependent gating of ASIC1a.
@en
P2093
P2860
P356
P1476
A combined computational and f ...... pH-dependent gating of ASIC1a
@en
P2093
Benoîte Bargeton
Justyna Iwaszkiewicz
Luz Angélica Liechti
Olivier Michielin
Sophie Roy
P2860
P304
16315-16329
P356
10.1074/JBC.M109.092015
P407
P577
2010-03-18T00:00:00Z