about
Resin-acid derivatives as potent electrostatic openers of voltage-gated K channels and suppressors of neuronal excitabilityChemoselective tarantula toxins report voltage activation of wild-type ion channels in live cellsStructural interactions of a voltage sensor toxin with lipid membranes.Tarantula toxins use common surfaces for interacting with Kv and ASIC ion channels.Structural insights into the mechanism of activation of the TRPV1 channel by a membrane-bound tarantula toxinMechanisms of activation of voltage-gated potassium channels.Fatty acid analogue N-arachidonoyl taurine restores function of IKs channels with diverse long QT mutations.Molecular Interactions between Tarantula Toxins and Low-Voltage-Activated Calcium Channels.Structural basis for the inhibition of voltage-dependent K+ channel by gating modifier toxin.The envenomation of general physiology throughout the last century.Heat activation is intrinsic to the pore domain of TRPV1.
P2860
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P2860
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Opening the shaker K+ channel with hanatoxin.
@ast
Opening the shaker K+ channel with hanatoxin.
@en
type
label
Opening the shaker K+ channel with hanatoxin.
@ast
Opening the shaker K+ channel with hanatoxin.
@en
prefLabel
Opening the shaker K+ channel with hanatoxin.
@ast
Opening the shaker K+ channel with hanatoxin.
@en
P2093
P2860
P356
P1476
Opening the shaker K+ channel with hanatoxin.
@en
P2093
Chan Hyung Bae
Jae Il Kim
Kenton J Swartz
Mirela Milescu
P2860
P304
P356
10.1085/JGP.201210914
P577
2013-02-01T00:00:00Z