Binding modes of two scorpion toxins to the voltage-gated potassium channel kv1.3 revealed from molecular dynamics.
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Computational Studies of Venom Peptides Targeting Potassium ChannelsMargatoxin-bound quantum dots as a novel inhibitor of the voltage-gated ion channel Kv1.3.Modeling of the Binding of Peptide Blockers to Voltage-Gated Potassium Channels: Approaches and Evidence.Molecular Simulations of Disulfide-Rich Venom Peptides with Ion Channels and Membranes.In silico analysis of potential inhibitors of Ca(2+) activated K(+) channel blocker, Charybdotoxin-C from Leiurus quinquestriatus hebraeus through molecular docking and dynamics studies.Side chain flexibility and the pore dimensions in the GABAA receptor.
P2860
Binding modes of two scorpion toxins to the voltage-gated potassium channel kv1.3 revealed from molecular dynamics.
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2014 nî lūn-bûn
@nan
2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հուլիսին 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
Binding modes of two scorpion ...... ealed from molecular dynamics.
@ast
Binding modes of two scorpion ...... ealed from molecular dynamics.
@en
type
label
Binding modes of two scorpion ...... ealed from molecular dynamics.
@ast
Binding modes of two scorpion ...... ealed from molecular dynamics.
@en
prefLabel
Binding modes of two scorpion ...... ealed from molecular dynamics.
@ast
Binding modes of two scorpion ...... ealed from molecular dynamics.
@en
P2860
P356
P1433
P1476
Binding modes of two scorpion ...... ealed from molecular dynamics.
@en
P2093
Shin-Ho Chung
P2860
P304
P356
10.3390/TOXINS6072149
P577
2014-07-22T00:00:00Z