Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.
about
Single Pair Förster Resonance Energy Transfer: A Versatile Tool To Investigate Protein Conformational Dynamics.Porcine Mx1 protein inhibits classical swine fever virus replication by targeting nonstructural protein NS5B.Effects of allelic variations in the human Myxovirus resistance protein A on its antiviral activity.Tuning of resonance energy transfer from 4',6-diamidino-2-phenylindole to an ultrasmall silver nanocluster across the lipid bilayer.Structural basis for membrane tethering by a bacterial dynamin-like pair
P2860
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.
description
2017 nî lūn-bûn
@nan
2017 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2017 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2017年の論文
@ja
2017年論文
@yue
2017年論文
@zh-hant
2017年論文
@zh-hk
2017年論文
@zh-mo
2017年論文
@zh-tw
2017年论文
@wuu
name
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.
@ast
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.
@en
type
label
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.
@ast
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.
@en
prefLabel
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.
@ast
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.
@en
P2093
P2860
P50
P356
P1476
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET
@en
P2093
P2860
P2888
P356
10.1038/NCOMMS15744
P407
P577
2017-05-26T00:00:00Z
P6179
1085596679