Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer - Wikidata - wikimedia - TriplyDB

Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer

Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer

http://www.wikidata.org/entity/Q35127506

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The activated state of a sodium channel voltage sensor in a membrane environment Multi-scale electrophysiology modeling: from atom to organ Change in permeant size selectivity by phosphorylation of connexin 43 gap-junctional hemichannels by PKC.Hinge-bending motions in the pore domain of a bacterial voltage-gated sodium channel In vivo measurement of intramolecular distances using genetically encoded reporters.Coupling between the voltage-sensing and pore domains in a voltage-gated potassium channel.Mechanistic Insights into the Modulation of Voltage-Gated Ion Channels by Inhalational Anesthetics A limited 4 Å radial displacement of the S4-S5 linker is sufficient for internal gate closing in Kv channels.Models of voltage-dependent conformational changes in NaChBac channels.Models of the structure and gating mechanisms of the pore domain of the NaChBac ion channel.The voltage-gated Na+ channel NaVBP co-localizes with methyl-accepting chemotaxis protein at cell poles of alkaliphilic Bacillus pseudofirmus OF4.Fluorescence detection of the movement of single KcsA subunits reveals cooperativity.β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel Structural dynamics of an isolated voltage-sensor domain in a lipid bilayer.NaChBac: the long lost sodium channel ancestor Application of fluorescence resonance energy transfer in protein studies Small molecule modulation of voltage gated sodium channels.Nano-positioning system for structural analysis of functional homomeric proteins in multiple conformations In vitro folding of KvAP, a voltage-gated K+ channel.Arrangement and mobility of the voltage sensor domain in prokaryotic voltage-gated sodium channels.Extent of voltage sensor movement during gating of shaker K+ channels.The structure of the lipid-embedded potassium channel voltage sensor determined by double-electron-electron resonance spectroscopy.The specificity of Av3 sea anemone toxin for arthropods is determined at linker DI/SS2-S6 in the pore module of target sodium channels.Design of a specific activator for skeletal muscle sodium channels uncovers channel architecture.

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P2860

Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer

http://www.wikidata.org/entity/Q35127506

description

2006 nî lūn-bûn

@nan

2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Distance measurements reveal a ...... channels in the lipid bilayer

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Distance measurements reveal a ...... channels in the lipid bilayer

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PNAS.0607532103

P1433

Proceedings of the National Academy of Sciences of the United States of America

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Distance measurements reveal a ...... channels in the lipid bilayer

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P2093

Ana M Correa

http://www.w3.org/2001/XMLSchema#string

Diane M Papazian

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Francisco Bezanilla

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Jessica Richardson

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Paul R Selvin

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Pinghua Ge

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P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

X-ray structure of a voltage-dependent K+ channel

Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy

Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane

A prokaryotic voltage-gated sodium channel

Crystal structure of a mammalian voltage-dependent Shaker family K+ channel

Molecular architecture of the KvAP voltage-dependent K+ channel in a lipid bilayer.

Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: the effect of nucleotides and actin.

Potassium channels: some assembly required.

Answers and questions from the KvAP structures.

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