Identification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound
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Identification of glucose-derived cross-linking sites in ribonuclease ASite-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetesRole of methylglyoxal in Alzheimer's diseaseGlucosepane is a major protein cross-link of the senescent human extracellular matrix. Relationship with diabetesExtending the spectrum of α-dicarbonyl compounds in vivo.NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.Covalent inactivation of factor VIII antibodies from hemophilia A patients by an electrophilic FVIII Analog.Structure elucidation of a novel yellow chromophore from human lens protein.K2P--a novel cross-link from human lens protein.Paradoxical impact of antioxidants on post-Amadori glycoxidation: Counterintuitive increase in the yields of pentosidine and Nepsilon-carboxymethyllysine using a novel multifunctional pyridoxamine derivative.Combining nano-physical and computational investigations to understand the nature of "aging" in dermal collagenDiabetes-induced alterations in the extracellular matrix and their impact on myocardial function.In situ accumulation of advanced glycation endproducts (AGEs) in bone matrix and its correlation with osteoclastic bone resorption.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.In vitro nonenzymatic glycation enhances the role of myoglobin as a source of oxidative stress.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.Determination of dideoxyosone precursors of AGEs in human lens proteins.Advanced glycation end products and oxidative stress in type 2 diabetes mellitus.Advanced glycation end-products reduce collagen molecular sliding to affect collagen fibril damage mechanisms but not stiffnessChemical modification of proteins by lipids in diabetes.Preferential sites for intramolecular glucosepane cross-link formation in type I collagen: A thermodynamic study.Glyoxalase I activity and immunoreactivity in the aging human lens.Identification of Kynoxazine, a Novel Fluorescent Product of the Reaction between 3-Hydroxykynurenine and Erythrulose in the Human Lens, and Its Role in Protein ModificationInhibition of crystallin ascorbylation by nucleophilic compounds in the hSVCT2 mouse model of lenticular aging.A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic diseaseA brief critical overview of the biological effects of methylglyoxal and further evaluation of a methylglyoxal-based anticancer formulation in treating cancer patients.Lens fluorescence and accommodative amplitude in pre-presbyopic and presbyopic subjects.Lens aging: effects of crystallins.Intra-molecular lysine-arginine derived advanced glycation end-product cross-linking in Type I collagen: A molecular dynamics simulation study.The pathogenic role of Maillard reaction in the aging eye.Molecular strategies to prevent, inhibit, and degrade advanced glycoxidation and advanced lipoxidation end products.Non-enzymatic glycation and glycoxidation protein products in foods and diseases: an interconnected, complex scenario fully open to innovative proteomic studies.Dicarbonyl proteome and genome damage in metabolic and vascular disease.Collagen modifications in postmenopausal osteoporosis: advanced glycation endproducts may affect bone volume, structure and quality.Baking, ageing, diabetes: a short history of the Maillard reaction.A new glycation product 'norpronyl-lysine,' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.Oxidation as an important factor of protein damage: Implications for Maillard reaction.Maillard reaction in food allergy: Pros and cons.
P2860
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P2860
Identification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Identification and quantificat ...... epane as the dominant compound
@ast
Identification and quantificat ...... epane as the dominant compound
@en
Identification and quantificat ...... epane as the dominant compound
@nl
type
label
Identification and quantificat ...... epane as the dominant compound
@ast
Identification and quantificat ...... epane as the dominant compound
@en
Identification and quantificat ...... epane as the dominant compound
@nl
prefLabel
Identification and quantificat ...... epane as the dominant compound
@ast
Identification and quantificat ...... epane as the dominant compound
@en
Identification and quantificat ...... epane as the dominant compound
@nl
P2093
P2860
P3181
P356
P1476
Identification and quantificat ...... epane as the dominant compound
@en
P2093
D Alexander Friedl
Klaus M Biemel
Markus O Lederer
P2860
P304
P3181
P356
10.1074/JBC.M202681200
P407
P577
2002-07-12T00:00:00Z