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.
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The Human W42R D-Crystallin Mutant Structure Provides a Link between Congenital and Age-related CataractsStructure and Dynamics of the Fish Eye Lens Protein, γM7-CrystallinFunctions of crystallins in and out of lens: roles in elongated and post-mitotic cellsTwo-photon excited UV fluorescence for protein crystal detectionMultiple 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-crystallinBiophysical chemistry of the ageing eye lens.UV-B induced fibrillization of crystallin protein mixturesFormation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.Separating instability from aggregation propensity in γS-crystallin variants.A novel CRYGD mutation (p.Trp43Arg) causing autosomal dominant congenital cataract in a Chinese family.γS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.Integrated nonlinear optical imaging microscope for on-axis crystal detection and centering at a synchrotron beamline.The molecular refractive function of lens γ-Crystallins.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.γ-Crystallins of the chicken lens: remnants of an ancient vertebrate gene family in birds.Femtosecond fluorescence spectra of tryptophan in human gamma-crystallin mutants: site-dependent ultrafast quenching.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.Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domainTryptophan cluster protects human γD-crystallin from ultraviolet radiation-induced photoaggregation in vitro.Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamageSolution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.Tyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.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.Effects of green and red light in βL-crystallin and ovalbumin.Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin.A novel mutation impairing the tertiary structure and stability of γC-crystallin (CRYGC) leads to cataract formation in humans and zebrafish lens.Protection of human γB-crystallin from UV-induced damage by epigallocatechin gallate: spectroscopic and docking studies.The advantage of 7-diethylamino-3-(4-maleimidophenyl)-4-methylcoumarin fluorogenic tagging of sulfhydryl groups in oligopeptides for tandem mass spectrometry.Conformational rearrangements of the C1 ring in KaiC measure the timing of assembly with KaiB.Fundus autofluorescence beyond lipofuscin: lesson learned from ex vivo fluorescence lifetime imaging in porcine eyes.The Molecular Background of the Differential UV Absorbance of the Human Lens in the 240-400 nm Range
P2860
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P2860
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.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Mechanism of the very efficien ...... from ultraviolet photodamage.
@en
Mechanism of the very efficien ...... from ultraviolet photodamage.
@nl
type
label
Mechanism of the very efficien ...... from ultraviolet photodamage.
@en
Mechanism of the very efficien ...... from ultraviolet photodamage.
@nl
prefLabel
Mechanism of the very efficien ...... from ultraviolet photodamage.
@en
Mechanism of the very efficien ...... from ultraviolet photodamage.
@nl
P2093
P2860
P356
P1433
P1476
Mechanism of the very efficien ...... from ultraviolet photodamage.
@en
P2093
Jiejin Chen
Jonathan King
Patrik R Callis
P2860
P304
P356
10.1021/BI802177G
P407
P577
2009-05-01T00:00:00Z