The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
about
Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallinsShotgun identification of protein modifications from protein complexes and lens tissueModifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncationMethylation and carbamylation of human gamma-crystallinsLaser light-scattering evidence for an altered association of beta B1-crystallin deamidated in the connecting peptideCrystal structure of truncated human betaB1-crystallinDeamidation alters the structure and decreases the stability of human lens betaA3-crystallinThe X-ray crystal structure of human gamma S-crystallin C-terminal domainProtein homeostasis: live long, won't prosperThe LEGSKO mouse: a mouse model of age-related nuclear cataract based on genetic suppression of lens glutathione synthesisLens β-crystallins: the role of deamidation and related modifications in aging and cataract.Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins.Patterns of crystallin distribution in porcine eye lenses.Characterization of covalent multimers of crystallins in aging human lenses.Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.DNA damage-induced Bcl-xL deamidation is mediated by NHE-1 antiport regulated intracellular pH.Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formationAnti-chaperone betaA3/A1(102-117) peptide interacting sites in human alphaB-crystallinDeamidation alters interactions of beta-crystallins in hetero-oligomersAge-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry.Age-dependent deamidation of lifelong proteins in the human lens.Identification of crystallin modifications in the human lens cortex and nucleus using laser capture microdissection and CyDye labeling.Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.Light-induced phosphorylation of crystallins in the retinal pigment epithelium.Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.Glutamine deamidation: differentiation of glutamic acid and gamma-glutamic acid in peptides by electron capture dissociation.Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidationStructural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin.Heat-induced irreversible denaturation of the camelid single domain VHH antibody is governed by chemical modifications.Solvent accessibility of betaB2-crystallin and local structural changes due to deamidation at the dimer interface.Aggregation of lens crystallins in an in vivo hyperbaric oxygen guinea pig model of nuclear cataract: dynamic light-scattering and HPLC analysis.Comparative analysis of human γD-crystallin aggregation under physiological and low pH conditions.Phosphoproteomics characterization of novel phosphorylated sites of lens proteins from normal and cataractous human eye lensesAcetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.The ageing lens and cataract: a model of normal and pathological ageing.The common modification in alphaA-crystallin in the lens, N101D, is associated with increased opacity in a mouse model.Cataract-specific posttranslational modifications and changes in the composition of urea-soluble protein fraction from the rat lens.Preventing disulfide bond formation weakens non-covalent forces among lysozyme aggregatesReview of the impact of presbyopia on quality of life in the developing and developed world.Comparison of modification sites in glycated crystallin in vitro and in vivo.
P2860
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P2860
The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The major in vivo modification ...... xidation and backbone cleavage
@ast
The major in vivo modification ...... xidation and backbone cleavage
@en
The major in vivo modification ...... xidation and backbone cleavage
@nl
type
label
The major in vivo modification ...... xidation and backbone cleavage
@ast
The major in vivo modification ...... xidation and backbone cleavage
@en
The major in vivo modification ...... xidation and backbone cleavage
@nl
prefLabel
The major in vivo modification ...... xidation and backbone cleavage
@ast
The major in vivo modification ...... xidation and backbone cleavage
@en
The major in vivo modification ...... xidation and backbone cleavage
@nl
P2093
P3181
P356
P1476
The major in vivo modification ...... xidation and backbone cleavage
@en
P2093
P304
P3181
P356
10.1006/EXER.2000.0868
P407
P577
2000-08-01T00:00:00Z