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Interactions between lipids and voltage sensor paddles detected with tarantula toxins

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

http://www.wikidata.org/entity/Q24650954

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Solution structure of GxTX-1E, a high-affinity tarantula toxin interacting with voltage sensors in Kv2.1 potassium channels The hitchhiker's guide to the voltage-gated sodium channel galaxy Voltage gated ion channel function: gating, conduction, and the role of water and protons From foe to friend: using animal toxins to investigate ion channel function Mechanosensitive gating of Kv channels Exploring volatile general anesthetic binding to a closed membrane-bound bacterial voltage-gated sodium channel via computation A distinct sodium channel voltage-sensor locus determines insect selectivity of the spider toxin Dc1a Structural basis of Nav1.7 inhibition by an isoform-selective small-molecule antagonist Connection between oligomeric state and gating characteristics of mechanosensitive ion channels TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action Structure and hydration of membranes embedded with voltage-sensing domains.Electrostatic tuning of cellular excitability.Transient and big are key features of an invertebrate T-type channel (LCav3) from the central nervous system of Lymnaea stagnalis Targeting voltage sensors in sodium channels with spider toxins.Toxin diversity revealed by a transcriptomic study of Ornithoctonus huwena.Structure and orientation of a voltage-sensor toxin in lipid membranes.A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain Directional interactions and cooperativity between mechanosensitive membrane proteins.Structural interactions between lipids, water and S1-S4 voltage-sensing domains Position and motions of the S4 helix during opening of the Shaker potassium channel.Paxilline inhibits BK channels by an almost exclusively closed-channel block mechanism.A shaker K+ channel with a miniature engineered voltage sensor.Chemoselective tarantula toxins report voltage activation of wild-type ion channels in live cells Structural interactions of a voltage sensor toxin with lipid membranes.An efficient strategy for heterologous expression and purification of active peptide hainantoxin-IV.Functional properties and toxin pharmacology of a dorsal root ganglion sodium channel viewed through its voltage sensors Tarantula toxins use common surfaces for interacting with Kv and ASIC ion channels.Palmitoylation influences the function and pharmacology of sodium channels.Solution structure of kurtoxin: a gating modifier selective for Cav3 voltage-gated Ca(2+) channels The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel Sphingomyelinase D inhibits store-operated Ca2+ entry in T lymphocytes by suppressing ORAI current.Sphingomyelin, ORAI1 channels, and cellular Ca2+ signaling.Opposite Effects of the S4-S5 Linker and PIP(2) on Voltage-Gated Channel Function: KCNQ1/KCNE1 and Other Channels.Autonomous transmembrane segment S4 of the voltage sensor domain partitions into the lipid membrane A novel epileptic encephalopathy mutation in KCNB1 disrupts Kv2.1 ion selectivity, expression, and localization.PIP2 controls voltage-sensor movement and pore opening of Kv channels through the S4-S5 linker.Animal toxins can alter the function of Nav1.8 and Nav1.9.Binding of hanatoxin to the voltage sensor of Kv2.1.Opening the shaker K+ channel with hanatoxin.Structural insights into the mechanism of activation of the TRPV1 channel by a membrane-bound tarantula toxin

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P2860

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

http://www.wikidata.org/entity/Q24650954

description

2009 nî lūn-bûn

@nan

2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

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Interactions between lipids and voltage sensor paddles detected with tarantula toxins

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Interactions between lipids and voltage sensor paddles detected with tarantula toxins

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type

label

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

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Interactions between lipids and voltage sensor paddles detected with tarantula toxins

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Interactions between lipids and voltage sensor paddles detected with tarantula toxins

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prefLabel

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

@ast

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

@en

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

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Nature Structural & Molecular Biology

P1476

Interactions between lipids and voltage sensor paddles detected with tarantula toxins

@en

P2093

AbdulRasheed A Alabi

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

Jae Il Kim

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

Kenton J Swartz

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

Mirela Milescu

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

Seungkyu Lee

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

P2860

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

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

Portability of paddle motif function and pharmacology in voltage sensors

Tarantula toxins interact with voltage sensors within lipid membranes

Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment

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

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

Two tarantula peptides inhibit activation of multiple sodium channels.

Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel.

Removal of phospho-head groups of membrane lipids immobilizes voltage sensors of K+ channels.

P2888

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1080-1085

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scholarly article

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2487180

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10.1038/NSMB.1679

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10

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16

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2009-09-27T00:00:00Z

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26840801

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1007676902

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19783984

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structural biology

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2782670

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