Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.
about
Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitroPreferential and Specific Binding of Human αB-Crystallin to a Cataract-Related Variant of γS-CrystallinModulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutationsLens β-crystallins: the role of deamidation and related modifications in aging and cataract.Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.The βγ-crystallins: native state stability and pathways to aggregation.Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.Electrostatic origin of in vitro aggregation of human γ-crystallin.Tryptophan cluster protects human γD-crystallin from ultraviolet radiation-induced photoaggregation in vitro.An increase in phosphorylation and truncation of crystallin with the progression of cataracts.RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain.A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.BetaB2-crystallin mutations associated with cataract and glaucoma leads to mitochondrial alterations in lens epithelial cells and retinal neurons.Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutantsAn alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin.Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.Expression of Cataract-linked γ-Crystallin Variants in Zebrafish Reveals a Proteostasis Network That Senses Protein Stability.Proteomics analysis and proteogenomic characterization of different physiopathological human lenses.Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation
P2860
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P2860
Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@ast
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@en
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@nl
type
label
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@ast
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@en
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@nl
prefLabel
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@ast
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@en
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@nl
P2860
P1433
P1476
Cataract-causing defect of a m ...... by the α-crystallin chaperone.
@en
P2093
Jonathan A King
Kate L Moreau
P2860
P304
P356
10.1371/JOURNAL.PONE.0037256
P407
P577
2012-05-24T00:00:00Z