Cataract as a protein condensation disease: the Proctor Lecture.
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Progressive juvenile-onset punctate cataracts caused by mutation of the gammaD-crystallin geneCataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallinsObservation of liquid-liquid phase separation for eye lens gammaS-crystallinAging and age-related diseases of the ocular lens and vitreous bodyLauriston S. Taylor Lecture on radiation protection and measurements: what makes particle radiation so effective?Implementation of a project-based molecular biology laboratory emphasizing protein structure-function relationships in a large introductory biology laboratory course.Saturation with cholesterol increases vertical order and smoothes the surface of the phosphatidylcholine bilayer: a molecular simulation study.Electron tomography of fiber cell cytoplasm and dense cores of multilamellar bodies from human age-related nuclear cataracts.Mie light scattering calculations for an Indian age-related nuclear cataract with a high density of multilamellar bodies.The inverse and direct Hofmeister series for lysozymebeta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallinCataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Multilamellar spherical particles as potential sources of excessive light scattering in human age-related nuclear cataracts.Phase behavior of mixtures of human lens proteins Gamma D and Beta B1.Effect of polyethylene glycol on the liquid-liquid phase transition in aqueous protein solutions.Altered chaperone-like activity of alpha-crystallins promotes cataractogenesis.Cataract-associated mutant E107A of human gammaD-crystallin shows increased attraction to alpha-crystallin and enhanced light scattering.Guanidine-HCl dependent structural unfolding of M-crystallin: fluctuating native state like topologies and intermolecular association.Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparencyAltered ubiquitin causes perturbed calcium homeostasis, hyperactivation of calpain, dysregulated differentiation, and cataract.Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands.The role of macromolecular crowding in the evolution of lens crystallins with high molecular refractive index.FE65 and FE65L1 amyloid precursor protein-binding protein compound null mice display adult-onset cataract and muscle weaknessStructural and biochemical characterization of the childhood cataract-associated R76S mutant of human γD-crystallin.The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association.Altered phase diagram due to a single point mutation in human gammaD-crystallin.A conserved role of αA-crystallin in the development of the zebrafish embryonic lens.Analysis of nuclear fiber cell cytoplasmic texture in advanced cataractous lenses from Indian subjects using Debye-Bueche theory.UV-radiation induced disruption of dry-cavities in human γD-crystallin results in decreased stability and faster unfolding.Evolution of crystallins for a role in the vertebrate eye lens.Protein misfolding and aggregation in cataract disease and prospects for prevention.Clinical detection of precataractous lens protein changes using dynamic light scattering.Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domainElectrostatic origin of in vitro aggregation of human γ-crystallin.Effect of Mild Heating on Human Lens Epithelial Cells: A Possible Model of Lens Aging.Lens aging: effects of crystallins.Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated ChaperonesDissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins.Modeling phase transitions in mixtures of β-γ lens crystallins.Self-assembly of protein aggregates in ageing disorders: the lens and cataract model.
P2860
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P2860
Cataract as a protein condensation disease: the Proctor Lecture.
description
1997 nî lūn-bûn
@nan
1997 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
Cataract as a protein condensation disease: the Proctor Lecture.
@ast
Cataract as a protein condensation disease: the Proctor Lecture.
@en
Cataract as a protein condensation disease: the Proctor Lecture.
@nl
type
label
Cataract as a protein condensation disease: the Proctor Lecture.
@ast
Cataract as a protein condensation disease: the Proctor Lecture.
@en
Cataract as a protein condensation disease: the Proctor Lecture.
@nl
prefLabel
Cataract as a protein condensation disease: the Proctor Lecture.
@ast
Cataract as a protein condensation disease: the Proctor Lecture.
@en
Cataract as a protein condensation disease: the Proctor Lecture.
@nl
P1476
Cataract as a protein condensation disease: the Proctor Lecture
@en
P2093
Benedek GB
P304
P407
P577
1997-09-01T00:00:00Z