Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.
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Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Separating instability from aggregation propensity in γS-crystallin variants.Comparative analysis of human γD-crystallin aggregation under physiological and low pH conditions.Characterization of a transient unfolding intermediate in a core mutant of γS-crystallin.Anti-UVC irradiation and metal chelation properties of 6-benzoyl-5,7-dihydroxy-4-phenyl-chromen-2-one: an implications for anti-cataract agentThe βγ-crystallins: native state stability and pathways to aggregation.Dissecting the kinetic process of amyloid fiber formation through asymptotic analysis.Protein misfolding and aggregation in cataract disease and prospects for prevention.Electrostatic origin of in vitro aggregation of human γ-crystallin.Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamageTyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.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.Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.Inhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate.Structural changes in amelogenin upon self-assembly and mineral interactions.Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions.Mechanisms and rates of nucleation of amyloid fibrils.Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.Hydrophobic tail length plays a pivotal role in amyloid beta (25-35) fibril-surfactant interactions.Rosmarinic Acid Restores Complete Transparency of Sonicated Human Cataract Ex Vivo and Delays Cataract Formation In Vivo.
P2860
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P2860
Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Formation of amyloid fibrils i ...... es of human gammaC-crystallin.
@ast
Formation of amyloid fibrils i ...... es of human gammaC-crystallin.
@en
type
label
Formation of amyloid fibrils i ...... es of human gammaC-crystallin.
@ast
Formation of amyloid fibrils i ...... es of human gammaC-crystallin.
@en
prefLabel
Formation of amyloid fibrils i ...... es of human gammaC-crystallin.
@ast
Formation of amyloid fibrils i ...... es of human gammaC-crystallin.
@en
P2093
P2860
P356
P1476
Formation of amyloid fibrils i ...... es of human gammaC-crystallin.
@en
P2093
Amy Trojanowski
Daniel Goulet
Ishita Mukerji
Jonathan King
Kelly Knee
Sarah Petty
Yongting Wang
P2860
P304
P356
10.1167/IOVS.09-3987
P407
P577
2009-08-13T00:00:00Z