Structure and mechanism of formation of human lens fluorophore LM-1. Relationship to vesperlysine A and the advanced Maillard reaction in aging, diabetes, and cataractogenesis.
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Glycation-altered proteolysis as a pathobiologic mechanism that links dietary glycemic index, aging, and age-related disease (in nondiabetics)Formation pathways for lysine-arginine cross-links derived from hexoses and pentoses by Maillard processes: unraveling the structure of a pentosidine precursorIdentification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compoundVitamin C-mediated Maillard reaction in the lens probed in a transgenic-mouse model.Protective effects of carnosine on dehydroascorbate-induced structural alteration and opacity of lens crystallins: important implications of carnosine pleiotropic functions to combat cataractogenesis.2-ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) is a newly identified advanced glycation end product in cataractous and aged human lenses.Structure elucidation of a novel yellow chromophore from human lens protein.K2P--a novel cross-link from human lens protein.Early glycation products produce pentosidine cross-links on native proteins. novel mechanism of pentosidine formation and propagation of glycation.Spectroscopic and biochemical correlations during the course of human lens aging.Partial characterization of the molecular nature of collagen-linked fluorescence: role of diabetes and end-stage renal disease.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.GWAS identifies an NAT2 acetylator status tag single nucleotide polymorphism to be a major locus for skin fluorescenceDietary carbohydrate in relation to cortical and nuclear lens opacities in the melbourne visual impairment project.Anaerobic vs aerobic pathways of carbonyl and oxidant stress in human lens and skin during aging and in diabetes: A comparative analysisFavored and disfavored pathways of protein crosslinking by glucose: glucose lysine dimer (GLUCOLD) and crossline versus glucosepane.Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): an overview of their mechanisms of formation.Vitamin C mediates chemical aging of lens crystallins by the Maillard reaction in a humanized mouse model.Involvement of Maillard reactions in Alzheimer disease.Vitamin C degradation products and pathways in the human lensEffects of non-enzymatic glycation on cancellous bone fragility.Effects of photobleaching on selected advanced glycation end products in the human lens.Multispecificity of immunoglobulin M antibodies raised against advanced glycation end products: involvement of electronegative potential of antigensDifferential role of arginine mutations on the structure and functions of α-crystallin.Changes in non-enzymatic glycation and its association with altered mechanical properties following 1-year treatment with risedronate or alendronate.Lens aging: effects of crystallins.Dietary hyperglycemia, glycemic index and metabolic retinal diseases.The pathogenic role of Maillard reaction in the aging eye.Common cell biologic and biochemical changes in aging and age-related diseases of the eye: toward new therapeutic approaches to age-related ocular diseasesPhotosensitizing Activity of Endogenous Eye Lens Chromophores: An Attempt to Unravel Their Contributions to Photo-Aging and Cataract Disease.Pathways of the Maillard reaction under physiological conditions.Modulation of advanced glycation endproduct synthesis by kynurenines in human lens proteins.Effect of cinnamoyl and flavonol glucosides derived from cherry blossom flowers on the production of advanced glycation end products (AGEs) and AGE-induced fibroblast apoptosis.Quantitative assessment of organ distribution of dietary protein-bound (13) C-labeled N(ɛ) -carboxymethyllysine after a chronic oral exposure in mice.Chemical and functional aspects of posttranslational modification of proteinsGlycation by ascorbic acid oxidation products leads to the aggregation of lens proteinsInhibition of methylglyoxal-mediated protein modification in glyoxalase I overexpressing mouse lenses.Triosidines: novel Maillard reaction products and cross-links from the reaction of triose sugars with lysine and arginine residues.Amides are novel protein modifications formed by physiological sugars.Novel protein modification by kynurenine in human lenses.
P2860
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P2860
Structure and mechanism of formation of human lens fluorophore LM-1. Relationship to vesperlysine A and the advanced Maillard reaction in aging, diabetes, and cataractogenesis.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Structure and mechanism of for ...... iabetes, and cataractogenesis.
@en
Structure and mechanism of for ...... iabetes, and cataractogenesis.
@nl
type
label
Structure and mechanism of for ...... iabetes, and cataractogenesis.
@en
Structure and mechanism of for ...... iabetes, and cataractogenesis.
@nl
prefLabel
Structure and mechanism of for ...... iabetes, and cataractogenesis.
@en
Structure and mechanism of for ...... iabetes, and cataractogenesis.
@nl
P2860
P356
P1476
Structure and mechanism of for ...... diabetes, and cataractogenesis
@en
P2093
M Obrenovich
V M Monnier
P2860
P304
20796-20804
P356
10.1074/JBC.274.30.20796
P407
P577
1999-07-01T00:00:00Z