In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation. - Wikidata - awgldk - TriplyDB

In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation.

In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation.

http://www.wikidata.org/entity/Q43137351

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Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone Unfolding crystallins: the destabilizing role of a beta-hairpin cysteine in betaB2-crystallin by simulation and experiment Biophysical Properties of γC-Crystallin in Human and Mouse Eye Lens: The Role of Molecular Dipoles The Human W42R D-Crystallin Mutant Structure Provides a Link between Congenital and Age-related Cataracts Structure and Dynamics of the Fish Eye Lens Protein, γM7-Crystallin Functional characterization of a human aquaporin 0 mutation that leads to a congenital dominant lens cataract.Modulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutations Implementation of a project-based molecular biology laboratory emphasizing protein structure-function relationships in a large introductory biology laboratory course.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 Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.UV-B induced fibrillization of crystallin protein mixtures 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 aggregation A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin.Functional rescue of Kallmann syndrome-associated prokineticin receptor 2 (PKR2) mutants deficient in trafficking 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.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.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.Characterization of a transient unfolding intermediate in a core mutant of γS-crystallin.Macromolecular crowding induces holo α-lactalbumin aggregation by converting to its apo form 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.Kinetic refolding barrier of guanidinium chloride denatured goose delta-crystallin leads to regular aggregate formation.Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease.Identifying protein aggregation mechanisms and quantifying aggregation rates from combined monomer depletion and continuous scattering A γA-Crystallin Mouse Mutant Secc with Small Eye, Cataract and Closed Eyelid.A novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract.Degradation of C-terminal truncated alpha A-crystallins by the ubiquitin-proteasome pathway.Femtosecond fluorescence spectra of tryptophan in human gamma-crystallin mutants: site-dependent ultrafast quenching.Formation of amyloid fibrils in vitro by human gammaD-crystallin and its isolated domains.Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin.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.

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In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation.

http://www.wikidata.org/entity/Q43137351

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2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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In vitro unfolding, refolding, ...... nvolved in cataract formation.

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In vitro unfolding, refolding, ...... nvolved in cataract formation.

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In vitro unfolding, refolding, ...... nvolved in cataract formation.

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Protein Science

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In vitro unfolding, refolding, ...... nvolved in cataract formation.

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Jonathan King

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Melissa S Kosinski-Collins

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P2860

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

Crystal cataracts: human genetic cataract caused by protein crystallization

Molecular basis of a progressive juvenile-onset hereditary cataract

Link between a novel human gammaD-crystallin allele and a unique cataract phenotype explained by protein crystallography

Towards a molecular understanding of phase separation in the lens: a comparison of the X-ray structures of two high Tc gamma-crystallins, gammaE and gammaF, with two low Tc gamma-crystallins, gammaB and gammaD

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

Spectral and metal-binding properties of three single-point tryptophan mutants of the human transferrin N-lobe

A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding

ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling

Inclusion body formation by interleukin-1 beta depends on the thermal sensitivity of a folding intermediate.

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