Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.
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Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallinsThe Human W42R D-Crystallin Mutant Structure Provides a Link between Congenital and Age-related CataractsThe congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of βB2-crystallinModulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutationsbeta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallinCoarse-grained model for colloidal protein interactions, B(22), and protein cluster formation.A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin.Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.αA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing αAG98R-crystallinComparative analysis of human γD-crystallin aggregation under physiological and low pH conditions.A novel CRYGD mutation (p.Trp43Arg) causing autosomal dominant congenital cataract in a Chinese family.Association properties and unfolding of a βγ-crystallin domain of a Vibrio-specific proteinAcetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands.The molecular refractive function of lens γ-Crystallins.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.Structural and biochemical characterization of the childhood cataract-associated R76S mutant of human γD-crystallin.Protein misfolding and aggregation in cataract disease and prospects for prevention.Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domainTryptophan cluster protects human γD-crystallin from ultraviolet radiation-induced photoaggregation in vitro.Tyrosine/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.Patterns of gene expression in microarrays and expressed sequence tags from normal and cataractous lensesGroup II archaeal chaperonin recognition of partially folded human γD-crystallin mutantsAggregation 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.Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin.Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation
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P2860
Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 16 September 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Hydrophobic core mutations ass ...... ilize human gammaD-crystallin.
@en
Hydrophobic core mutations ass ...... ilize human gammaD-crystallin.
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type
label
Hydrophobic core mutations ass ...... ilize human gammaD-crystallin.
@en
Hydrophobic core mutations ass ...... ilize human gammaD-crystallin.
@nl
prefLabel
Hydrophobic core mutations ass ...... ilize human gammaD-crystallin.
@en
Hydrophobic core mutations ass ...... ilize human gammaD-crystallin.
@nl
P2860
P356
P1476
Hydrophobic core mutations ass ...... ilize human gammaD-crystallin.
@en
P2093
Jonathan King
Kate L Moreau
P2860
P304
33285-33295
P356
10.1074/JBC.M109.031344
P407
P577
2009-09-16T00:00:00Z