Formation of amyloid fibrils in vitro by human gammaD-crystallin and its isolated domains.
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Modulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutationsMultiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.The congenital cataract-linked G61C mutation destabilizes γD-crystallin and promotes non-native aggregationA single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin.Therapeutic protein aggregation: mechanisms, design, and control.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.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.Characterization of a transient unfolding intermediate in a core mutant of γS-crystallin.Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutant.The βγ-crystallins: native state stability and pathways to aggregation.Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils.Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin ProteinProtein misfolding and aggregation in cataract disease and prospects for prevention.Electrostatic origin of in vitro aggregation of human γ-crystallin.Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamageStudy of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.Tyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.Dissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins.A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.Patterns of gene expression in microarrays and expressed sequence tags from normal and cataractous lensesAn 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.How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy.Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.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 by human gammaD-crystallin and its isolated domains.
description
2008 nî lūn-bûn
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2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Formation of amyloid fibrils i ...... llin and its isolated domains.
@ast
Formation of amyloid fibrils i ...... llin and its isolated domains.
@en
type
label
Formation of amyloid fibrils i ...... llin and its isolated domains.
@ast
Formation of amyloid fibrils i ...... llin and its isolated domains.
@en
prefLabel
Formation of amyloid fibrils i ...... llin and its isolated domains.
@ast
Formation of amyloid fibrils i ...... llin and its isolated domains.
@en
P2093
P2860
P1433
P1476
Formation of amyloid fibrils in vitro by human gammaD-crystallin and its isolated domains
@en
P2093
Abby A R Gross
Ishara Mills-Henry
Jonathan King
Katerina Papanikolopoulou
Sean M Decatur
Shannon L Thol
Yongting Wang
P2860
P577
2008-01-16T00:00:00Z