Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.
about
N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperoneStructure and Dynamics of the Fish Eye Lens Protein, γM7-CrystallinPreferential and Specific Binding of Human αB-Crystallin to a Cataract-Related Variant of γS-CrystallinThe mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataractStructural study of the G57W mutant of human gamma-S-crystallin, associated with congenital cataractModulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutationsCa2+-binding motif of βγ-crystallins.Conformational stability as a design target to control protein aggregation.beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallinAggregation of deamidated human betaB2-crystallin and incomplete rescue by alpha-crystallin chaperone.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.γS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.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 molecular refractive function of lens γ-Crystallins.The role of macromolecular crowding in the evolution of lens crystallins with high molecular refractive index.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.Cooperativity, connectivity, and folding pathways of multidomain proteinsElectrostatic origin of in vitro aggregation of human γ-crystallin.The G18V CRYGS mutation associated with human cataracts increases gammaS-crystallin sensitivity to thermal and chemical stressAmyloid 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.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 cataractIncreased hydrophobic surface exposure in the cataract-related G18V variant of human γS-crystallin.Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forces.Exploring the sequence-structure-function relationship for the intrinsically disordered βγ-crystallin Hahellin.The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutantsAn alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin.Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone.Inhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate.Mechanism of the very efficient quenching of tryptophan fluorescence in human gamma D- and gamma S-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage.Structural analysis of the mutant protein D26G of human γS-crystallin, associated with Coppock cataract.Increase in surface hydrophobicity of the cataract-associated P23T mutant of human gammaD-crystallin is responsible for its dramatically lower, retrograde solubility.
P2860
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P2860
Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Folding and stability of the i ...... stallin and gammaS-crystallin.
@en
Folding and stability of the i ...... stallin and gammaS-crystallin.
@nl
type
label
Folding and stability of the i ...... stallin and gammaS-crystallin.
@en
Folding and stability of the i ...... stallin and gammaS-crystallin.
@nl
prefLabel
Folding and stability of the i ...... stallin and gammaS-crystallin.
@en
Folding and stability of the i ...... stallin and gammaS-crystallin.
@nl
P2093
P2860
P356
P1433
P1476
Folding and stability of the i ...... stallin and gammaS-crystallin.
@en
P2093
Ishara A Mills
Jonathan A King
Melissa S Kosinski-Collins
Shannon L Flaugh
P2860
P304
P356
10.1110/PS.072970207
P577
2007-09-28T00:00:00Z