Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.
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Biophysical studies of protein solubility and amorphous aggregation by systematic mutational analysis and a helical polymerization model.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Methionine oxidized apolipoprotein A-I at the crossroads of HDL biogenesis and amyloid formation.Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.New applications of solid-state NMR in structural biology
P2860
Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.
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
Cataract-associated P23T γD-cr ...... es formed at physiological pH.
@ast
Cataract-associated P23T γD-cr ...... es formed at physiological pH.
@en
type
label
Cataract-associated P23T γD-cr ...... es formed at physiological pH.
@ast
Cataract-associated P23T γD-cr ...... es formed at physiological pH.
@en
prefLabel
Cataract-associated P23T γD-cr ...... es formed at physiological pH.
@ast
Cataract-associated P23T γD-cr ...... es formed at physiological pH.
@en
P2860
P50
P356
P1476
Cataract-associated P23T γD-cr ...... es formed at physiological pH.
@en
P2093
Angela M Gronenborn
Mingyue Li
P2860
P2888
P356
10.1038/NCOMMS15137
P407
P577
2017-05-05T00:00:00Z
P6179
1085174497