The carboxyl-terminal region of cyclic nucleotide-modulated channels is a gating ring, not a permeation path.
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Ion access pathway to the transmembrane pore in P2X receptor channelsC-terminal Movement during Gating in Cyclic Nucleotide-modulated ChannelsA Mechanism for the Auto-inhibition of Hyperpolarization-activated Cyclic Nucleotide-gated (HCN) Channel Opening and Its Relief by cAMPStructural correlates of selectivity and inactivation in potassium channels.cAMP Modulation of the cytoplasmic domain in the HCN2 channel investigated by molecular simulations.Cytoplasmic cAMP-sensing domain of hyperpolarization-activated cation (HCN) channels uses two structurally distinct mechanisms to regulate voltage gating.Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors).cAMP control of HCN2 channel Mg2+ block reveals loose coupling between the cyclic nucleotide-gating ring and the pore.Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7).Cooperative gating between single HCN pacemaker channels.Molecular mechanisms for drug interactions with hERG that cause long QT syndrome.hERG gating microdomains defined by S6 mutagenesis and molecular modeling.Patch-clamp fluorometry-based channel counting to determine HCN channel conductance.Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening.The enigmatic cytoplasmic regions of KCNH channels.C-terminal dimerization activates the nociceptive transduction channel transient receptor potential vanilloid 1.Cysteine 723 in the C-linker segment confers oxidative inhibition of hERG1 potassium channels.Role of Dynamics in the Autoinhibition and Activation of the Hyperpolarization-activated Cyclic Nucleotide-modulated (HCN) Ion Channels.Ion binding in the open HCN pacemaker channel pore: fast mechanisms to shape "slow" channels.The HCN4 channel mutation D553N associated with bradycardia has a C-linker mediated gating defect.Regulation of HCN Ion Channels by Non-canonical Cyclic Nucleotides.
P2860
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P2860
The carboxyl-terminal region of cyclic nucleotide-modulated channels is a gating ring, not a permeation path.
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年學術文章
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name
The carboxyl-terminal region o ...... g ring, not a permeation path.
@ast
The carboxyl-terminal region o ...... g ring, not a permeation path.
@en
type
label
The carboxyl-terminal region o ...... g ring, not a permeation path.
@ast
The carboxyl-terminal region o ...... g ring, not a permeation path.
@en
prefLabel
The carboxyl-terminal region o ...... g ring, not a permeation path.
@ast
The carboxyl-terminal region o ...... g ring, not a permeation path.
@en
P2860
P356
P1476
The carboxyl-terminal region o ...... g ring, not a permeation path.
@en
P2093
J P Johnson
William N Zagotta
P2860
P304
P356
10.1073/PNAS.0408323102
P407
P577
2005-02-14T00:00:00Z