Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4. - Wikidata - wikimedia - TriplyDB

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

http://www.wikidata.org/entity/Q34792648

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Mechanism of Ion Permeation in Mammalian Voltage-Gated Sodium Channels.Lysine and the Na+/K+ Selectivity in Mammalian Voltage-Gated Sodium Channels.The Role of Individual Disulfide Bonds of μ-Conotoxin GIIIA in the Inhibition of NaV1.4.

P2860

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P2860

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

http://www.wikidata.org/entity/Q34792648

description

2014 nî lūn-bûn

@nan

2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@ast

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@en

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@nl

type

label

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@ast

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@en

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@nl

prefLabel

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@ast

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@en

Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@nl

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Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.

@en

P2093

Serdar Kuyucak

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

Somayeh Mahdavi

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

P2860

CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields

Using the deadly mu-conotoxins as probes of voltage-gated sodium channels

Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels

Structure-activity relationships of mu-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations

Design of Bioactive Peptides from Naturally Occurring -Conotoxin Structures

The crystal structure of a voltage-gated sodium channel

Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing

Distinct Disulfide Isomers of μ-Conotoxins KIIIA and KIIIB Block Voltage-Gated Sodium Channels

Mammalian Neuronal Sodium Channel Blocker μ-Conotoxin BuIIIB Has a Structured N-Terminus That Influences Potency

Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel.

P304

3454-3470

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scholarly article

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10.3390/TOXINS6123454

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12

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6

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2014-12-18T00:00:00Z

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269934861

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25529306

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4280544

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