A pore-blocking hydrophobic motif at the cytoplasmic aperture of the closed-state Nav1.7 channel is disrupted by the erythromelalgia-associated F1449V mutation.
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Bisphenol A binds to the local anesthetic receptor site to block the human cardiac sodium channelStructure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closingChaperone-mediated native folding of a β-scorpion toxin in the periplasm of Escherichia coliNetwork topology of NaV1.7 mutations in sodium channel-related painful disorders.Single amino acid deletion in transmembrane segment D4S6 of sodium channel Scn8a (Nav1.6) in a mouse mutant with a chronic movement disorder.Evolutionarily conserved intracellular gate of voltage-dependent sodium channels.Translational pain research: Lessons from genetics and genomics.A novel mechanism for fine-tuning open-state stability in a voltage-gated potassium channel.Molecular architecture of a sodium channel S6 helix: radial tuning of the voltage-gated sodium channel 1.7 activation gateStructural modelling and mutant cycle analysis predict pharmacoresponsiveness of a Na(V)1.7 mutant channel.Erythromelalgia mutation Q875E Stabilizes the activated state of sodium channel Nav1.7.Can robots patch-clamp as well as humans? Characterization of a novel sodium channel mutation.Kinetic modeling of Nav1.7 provides insight into erythromelalgia-associated F1449V mutation.
P2860
Q27330612-F634E750-BB48-402E-8134-D5727914FA68Q27674040-A4A60B37-A9B3-44CA-8592-563D51142A0FQ27679850-F81F0607-7358-4D70-96FE-E6E4B61FAAA3Q36290427-39E2C4BB-17DD-4807-9981-1B8318E77682Q37191093-107BB8F8-9E1F-4D8B-9A8C-44A596B1ABE2Q37646643-6B2FE96D-C3DB-424C-B4A4-D42EEC0C97ACQ38239812-7A2EF158-B87B-4AE4-BFA3-FEC083E82299Q40383649-ED6BB8EF-050B-44C3-92CD-0B0A6FA2F795Q40601290-13E7E247-CB6B-4592-91D3-D0EE5C54510BQ42211742-F94D54DC-928D-43D8-B8C2-31A8A9F7D60FQ42249654-DD4E0AF5-B89F-4752-B014-BAFE3D606B34Q44180217-351B2317-F217-4163-BC97-35465E97A269Q51607050-594FE305-C3A4-40B6-AD90-917FE86C8960
P2860
A pore-blocking hydrophobic motif at the cytoplasmic aperture of the closed-state Nav1.7 channel is disrupted by the erythromelalgia-associated F1449V mutation.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
@zh-my
2008年学术文章
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2008年學術文章
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name
A pore-blocking hydrophobic mo ...... ia-associated F1449V mutation.
@en
A pore-blocking hydrophobic mo ...... ia-associated F1449V mutation.
@nl
type
label
A pore-blocking hydrophobic mo ...... ia-associated F1449V mutation.
@en
A pore-blocking hydrophobic mo ...... ia-associated F1449V mutation.
@nl
prefLabel
A pore-blocking hydrophobic mo ...... ia-associated F1449V mutation.
@en
A pore-blocking hydrophobic mo ...... ia-associated F1449V mutation.
@nl
P2093
P2860
P50
P356
P1476
A pore-blocking hydrophobic mo ...... gia-associated F1449V mutation
@en
P2093
Lynda Tyrrell
Stephen G Waxman
Sulayman D Dib-Hajj
P2860
P304
24118-24127
P356
10.1074/JBC.M802900200
P407
P577
2008-06-12T00:00:00Z