Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin. - Wikidata - awgldk - TriplyDB

Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.

Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.

http://www.wikidata.org/entity/Q42971021

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N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone Structure and Dynamics of the Fish Eye Lens Protein, γM7-Crystallin Preferential and Specific Binding of Human αB-Crystallin to a Cataract-Related Variant of γS-Crystallin The mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataract Structural study of the G57W mutant of human gamma-S-crystallin, associated with congenital cataract Modulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutations Ca2+-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-crystallin Aggregation 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 transparency 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.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 proteins Electrostatic 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 stress Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage Study 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 cataract Increased 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 mutants An 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.

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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.

http://www.wikidata.org/entity/Q42971021

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Folding and stability of the i ...... stallin and gammaS-crystallin.

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Folding and stability of the i ...... stallin and gammaS-crystallin.

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type

label

Folding and stability of the i ...... stallin and gammaS-crystallin.

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Folding and stability of the i ...... stallin and gammaS-crystallin.

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prefLabel

Folding and stability of the i ...... stallin and gammaS-crystallin.

@en

Folding and stability of the i ...... stallin and gammaS-crystallin.

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Protein Science

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Folding and stability of the i ...... stallin and gammaS-crystallin.

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Ishara A Mills

http://www.w3.org/2001/XMLSchema#string

Jonathan A King

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Melissa S Kosinski-Collins

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Shannon L Flaugh

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P2860

Progressive juvenile-onset punctate cataracts caused by mutation of the gammaD-crystallin gene

Novel mutations in the gamma-crystallin genes cause autosomal dominant congenital cataracts

Domain interaction sites of human lens betaB2-crystallin

Homology models of human gamma-crystallins: structural study of the extensive charge network in gamma-crystallins

The gamma-crystallins and human cataracts: a puzzle made clearer

Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation

Unfolding crystallins: the destabilizing role of a beta-hairpin cysteine in betaB2-crystallin by simulation and experiment

Crystal structure of truncated human betaB1-crystallin

Deamidation alters the structure and decreases the stability of human lens betaA3-crystallin

Mutation of interfaces in domain-swapped human betaB2-crystallin

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2427-2444

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scholarly article

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10.1110/PS.072970207

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11

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16

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2007-09-28T00:00:00Z

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5938754

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17905830

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protein folding

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2211709

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