The βγ-crystallins: native state stability and pathways to aggregation.
about
Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutant.Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin ProteinCataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domainModeling phase transitions in mixtures of β-γ lens crystallins.An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin.Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.Effects of green and red light in βL-crystallin and ovalbumin.Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregationγ-Crystallin redox-detox in the lens
P2860
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P2860
The βγ-crystallins: native state stability and pathways to aggregation.
description
2014 nî lūn-bûn
@nan
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
2014年论文
@zh
2014年论文
@zh-cn
name
The βγ-crystallins: native state stability and pathways to aggregation.
@ast
The βγ-crystallins: native state stability and pathways to aggregation.
@en
type
label
The βγ-crystallins: native state stability and pathways to aggregation.
@ast
The βγ-crystallins: native state stability and pathways to aggregation.
@en
prefLabel
The βγ-crystallins: native state stability and pathways to aggregation.
@ast
The βγ-crystallins: native state stability and pathways to aggregation.
@en
P2860
P1476
The βγ-crystallins: native state stability and pathways to aggregation.
@en
P2093
Eugene Serebryany
Jonathan A King
P2860
P356
10.1016/J.PBIOMOLBIO.2014.05.002
P577
2014-05-14T00:00:00Z