beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin
about
A novel interdomain interface in crystallins: structural characterization of the βγ-crystallin from Geodia cydonium at 0.99 Å resolutionInfrared study of the folding mechanism of a helical hairpin: porcine PYY.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Comparative analysis of human γD-crystallin aggregation under physiological and low pH conditions.Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparencyAggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands.The βγ-crystallins: native state stability and pathways to aggregation.The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association.UV-radiation induced disruption of dry-cavities in human γD-crystallin results in decreased stability and faster unfolding.Study of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.Dissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins.Increased hydrophobicity and decreased backbone flexibility explain the lower solubility of a cataract-linked mutant of γD-crystallin.An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin.Structural and aggregation behavior of the human γD-crystallin mutant E107A, associated with congenital nuclear cataractEvolutionary remodeling of βγ-crystallins for domain stability at cost of Ca2+ binding.The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.An alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin.Inhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate.Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin.Investigation of the early stages of human γD-crystallin aggregation process.
P2860
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P2860
beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
beta-Strand interactions at th ...... f human lens gammaD-crystallin
@ast
beta-Strand interactions at th ...... f human lens gammaD-crystallin
@en
type
label
beta-Strand interactions at th ...... f human lens gammaD-crystallin
@ast
beta-Strand interactions at th ...... f human lens gammaD-crystallin
@en
prefLabel
beta-Strand interactions at th ...... f human lens gammaD-crystallin
@ast
beta-Strand interactions at th ...... f human lens gammaD-crystallin
@en
P2093
P2860
P356
P1433
P1476
beta-Strand interactions at th ...... f human lens gammaD-crystallin
@en
P2093
Jonathan A King
Ruhong Zhou
P2860
P304
P356
10.1002/PRO.497
P577
2010-01-01T00:00:00Z