Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins - Wikidata - wikimedia - TriplyDB

Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

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Advanced protein formulations Role of αA-crystallin-derived αA66-80 peptide in guinea pig lens crystallin aggregation and insolubilization.Age-related changes in the kinetics of human lenses: prevention of the cataract Protective effects of carnosine on dehydroascorbate-induced structural alteration and opacity of lens crystallins: important implications of carnosine pleiotropic functions to combat cataractogenesis.Large-scale binding of α-crystallin to cell membranes of aged normal human lenses: a phenomenon that can be induced by mild thermal stress UVA light-excited kynurenines oxidize ascorbate and modify lens proteins through the formation of advanced glycation end products: implications for human lens aging and cataract formation.Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidation Anaerobic vs aerobic pathways of carbonyl and oxidant stress in human lens and skin during aging and in diabetes: A comparative analysis Topical application of L-arginine blocks advanced glycation by ascorbic acid in the lens of hSVCT2 transgenic mice.Determination of dideoxyosone precursors of AGEs in human lens proteins.Inverse association of vitamin C with cataract in older people in India Antioxidant capacity of lenses with age-related cataract Glycation of bovine serum albumin by ascorbate in vitro: Possible contribution of the ascorbyl radical?Hydrodynamic size-based separation and characterization of protein aggregates from total cell lysates.Lens aging: effects of crystallins.The aging eye and the role of L-carnitine and its derivatives.Lens Endogenous Peptide αA66-80 Generates Hydrogen Peroxide and Induces Cell Apoptosis.The pathogenic role of Maillard reaction in the aging eye.Lens Biology and Biochemistry Small molecules, both dietary and endogenous, influence the onset of lens cataracts.Proteomic and redox-proteomic evaluation of homogentisic acid and ascorbic acid effects on human articular chondrocytes.Comparative study of plasma ascorbic acid levels in senile cataract patients and in normal individuals.Antioxidant delivery pathways in the anterior eye.The combined effect of acetylation and glycation on the chaperone and anti-apoptotic functions of human α-crystallin.Simultaneous chemical and photochemical protein crosslinking induced by irradiation of eye lens proteins in the presence of ascorbate: the photosensitizing role of an UVA-visible-absorbing decomposition product of vitamin C.High-dose supplements of vitamins C and E, low-dose multivitamins, and the risk of age-related cataract: a population-based prospective cohort study of men.The Major Chromophore Arising from Glucose Degradation and Oxidative Stress Occurrence during Lens Proteins Glycation Induced by Glucose.UVA Light-mediated Ascorbate Oxidation in Human Lenses.Rosmarinic Acid Restores Complete Transparency of Sonicated Human Cataract Ex Vivo and Delays Cataract Formation In Vivo.

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P2860

Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

http://www.wikidata.org/entity/Q42174300

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

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Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

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type

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Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

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Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

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Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

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Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

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J.BBADIS.2007.10.003

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Biochimica et Biophysica Acta

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Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins

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Beryl J Ortwerth

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Ekaterina Shipova

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Mikhail Linetsky

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Rongzhu Cheng

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P2860

Laser light-scattering evidence for an altered association of beta B1-crystallin deamidated in the connecting peptide

Molecular basis of a progressive juvenile-onset hereditary cataract

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Identification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound

Contribution of glycation to human lens coloration

N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins

Superoxide free radical generation by Amadori compounds: the role of acyclic forms and metal ions.

Protein crosslinking by the Maillard reaction: dicarbonyl-derived imidazolium crosslinks in aging and diabetes.

2-ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) is a newly identified advanced glycation end product in cataractous and aged human lenses.

K2P--a novel cross-link from human lens protein.

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10.1016/J.BBADIS.2007.10.003

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