Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. - Wikidata - awgldk - TriplyDB

Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin.

Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin.

http://www.wikidata.org/entity/Q36518008

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Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro Deamidation alters the structure and decreases the stability of human lens betaA3-crystallin The Human W42R D-Crystallin Mutant Structure Provides a Link between Congenital and Age-related Cataracts Modulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutations Conformational stability as a design target to control protein aggregation.Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin Biophysical chemistry of the ageing eye lens.A novel human CRYGD mutation in a juvenile autosomal dominant cataract The congenital cataract-linked G61C mutation destabilizes γD-crystallin and promotes non-native aggregation Therapeutic protein aggregation: mechanisms, design, and control.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.Role of anisotropic interactions for proteins and patchy nanoparticles.Comparative 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.Acetylation 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 βγ-crystallins: native state stability and pathways to aggregation.Rosin Surfactant QRMAE Can Be Utilized as an Amorphous Aggregate Inducer: A Case Study of Mammalian Serum Albumin Folding mechanism of the metastable serpin α1-antitrypsin.Structural and biochemical characterization of the childhood cataract-associated R76S mutant of human γD-crystallin.A novel mutation in CRYAA is associated with autosomal dominant suture cataracts in a Chinese family Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein UV-radiation induced disruption of dry-cavities in human γD-crystallin results in decreased stability and faster unfolding.Deamidation in human lens betaB2-crystallin destabilizes the dimer.Cooperativity, connectivity, and folding pathways of multidomain proteins Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain An alphaA-crystallin gene mutation, Arg12Cys, causing inherited cataract-microcornea exhibits an altered heat-shock response.A novel gammaD-crystallin mutation causes mild changes in protein properties but leads to congenital coralliform cataract 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.Dissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins.The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.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.

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P2860

Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin.

http://www.wikidata.org/entity/Q36518008

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Contributions of hydrophobic d ...... ty of human gammaD-crystallin.

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Contributions of hydrophobic d ...... ty of human gammaD-crystallin.

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Contributions of hydrophobic d ...... ty of human gammaD-crystallin.

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Contributions of hydrophobic d ...... ty of human gammaD-crystallin.

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Contributions of hydrophobic d ...... ty of human gammaD-crystallin.

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Jonathan King

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

Melissa S Kosinski-Collins

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Shannon L Flaugh

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P2860

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

Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens

Cloning, expression, and chaperone-like activity of human alphaA-crystallin

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

Fibril in senile systemic amyloidosis is derived from normal transthyretin

Crystal cataracts: human genetic cataract caused by protein crystallization

Molecular basis of a progressive juvenile-onset hereditary cataract

An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured

High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract

X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins

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