Kinetically driven refolding of the hyperstable EBNA1 origin DNA-binding dimeric beta-barrel domain into amyloid-like spherical oligomers.
about
The non-structural NS1 protein unique to respiratory syncytial virus: a two-state folding monomer in quasi-equilibrium with a stable spherical oligomerOrdered self-assembly mechanism of a spherical oncoprotein oligomer triggered by zinc removal and stabilized by an intrinsically disordered domainPB1-F2 influenza A virus protein adopts a beta-sheet conformation and forms amyloid fibers in membrane environments.Phosphorylation sites of Epstein-Barr virus EBNA1 regulate its functionMicrobial manipulation of the amyloid fold.Herpes simplex virus-1 disarms the unfolded protein response in the early stages of infection.
P2860
Kinetically driven refolding of the hyperstable EBNA1 origin DNA-binding dimeric beta-barrel domain into amyloid-like spherical oligomers.
description
2008 nî lūn-bûn
@nan
2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Kinetically driven refolding o ...... loid-like spherical oligomers.
@ast
Kinetically driven refolding o ...... loid-like spherical oligomers.
@en
type
label
Kinetically driven refolding o ...... loid-like spherical oligomers.
@ast
Kinetically driven refolding o ...... loid-like spherical oligomers.
@en
prefLabel
Kinetically driven refolding o ...... loid-like spherical oligomers.
@ast
Kinetically driven refolding o ...... loid-like spherical oligomers.
@en
P356
P1433
P1476
Kinetically driven refolding o ...... loid-like spherical oligomers.
@en
P2093
Cristian Oddo
Lori Frappier
P304
P356
10.1002/PROT.21580
P407
P577
2008-02-01T00:00:00Z