High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract
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Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallinsBiophysical Properties of γC-Crystallin in Human and Mouse Eye Lens: The Role of Molecular DipolesThe Structure of the Cataract-Causing P23T Mutant of Human γD-Crystallin Exhibits Distinctive Local Conformational and Dynamic Changes † , ‡The Human W42R D-Crystallin Mutant Structure Provides a Link between Congenital and Age-related CataractsCrystal structure of the cataract-causing P23T γD-crystallin mutantA novel interdomain interface in crystallins: structural characterization of the βγ-crystallin from Geodia cydonium at 0.99 Å resolutionNuclear Magnetic Resonance Structure of a Major Lens Protein, Human γC-Crystallin: Role of the Dipole Moment in Protein SolubilityFunctions of crystallins in and out of lens: roles in elongated and post-mitotic cellsModulating non-native aggregation and electrostatic protein-protein interactions with computationally designed single-point mutationsLens β-crystallins: the role of deamidation and related modifications in aging and cataract.Predicting protein backbone chemical shifts from Cα coordinates: extracting high resolution experimental observables from low resolution models.Examining the influence of ultraviolet C irradiation on recombinant human γD-crystallin.Age-dependent deamidation of lifelong proteins in the human lens.Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.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 aggregationA single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin.Phase behavior of mixtures of human lens proteins Gamma D and Beta B1.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.A serine-type protease activity of human lens βA3-crystallin is responsible for its autodegradation.Cataract-associated mutant E107A of human gammaD-crystallin shows increased attraction to alpha-crystallin and enhanced light scattering.Separating instability from aggregation propensity in γS-crystallin variants.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 transparencyMolecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin.Combinational analysis of linkage and exome sequencing identifies the causative mutation in a Chinese family with congenital cataract.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.Characterization of a transient unfolding intermediate in a core mutant of γS-crystallin.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.Molecular Mechanism for the Thermo-Sensitive Phenotype of CHO-MT58 Cell Line Harbouring a Mutant CTP:Phosphocholine CytidylyltransferaseA Novel Insertion Variant of CRYGD Is Associated with Congenital Nuclear Cataract in a Chinese Family.Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils.Conversion and compensatory evolution of the gamma-crystallin genes and identification of a cataractogenic mutation that reverses the sequence of the human CRYGD gene to an ancestral stateAltered phase diagram due to a single point mutation in human gammaD-crystallin.Femtosecond fluorescence spectra of tryptophan in human gamma-crystallin mutants: site-dependent ultrafast quenching.Protein anisotropy turns solubility on its head.Enhancement of ubiquitin conjugation activity reduces intracellular aggregation of V76D mutant γD-crystallin.
P2860
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P2860
High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract
description
2003 nî lūn-bûn
@nan
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
High-resolution X-ray crystal ...... iated with aculeiform cataract
@ast
High-resolution X-ray crystal ...... iated with aculeiform cataract
@en
High-resolution X-ray crystal ...... iated with aculeiform cataract
@nl
type
label
High-resolution X-ray crystal ...... iated with aculeiform cataract
@ast
High-resolution X-ray crystal ...... iated with aculeiform cataract
@en
High-resolution X-ray crystal ...... iated with aculeiform cataract
@nl
prefLabel
High-resolution X-ray crystal ...... iated with aculeiform cataract
@ast
High-resolution X-ray crystal ...... iated with aculeiform cataract
@en
High-resolution X-ray crystal ...... iated with aculeiform cataract
@nl
P2093
P1476
High-resolution X-ray crystal ...... iated with aculeiform cataract
@en
P2093
Ajay Pande
Ajit Basak
Christine Slingsby
George B Benedek
Jayanti Pande
Neer Asherie
Olutayo Ogun
Orval Bateman
P304
P356
10.1016/S0022-2836(03)00375-9
P407
P577
2003-05-16T00:00:00Z