Amides are novel protein modifications formed by physiological sugars. - Wikidata - awgldk - TriplyDB

Amides are novel protein modifications formed by physiological sugars.

Amides are novel protein modifications formed by physiological sugars.

http://www.wikidata.org/entity/Q43700248

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Therapeutic modalities in diabetic nephropathy: standard and emerging approaches.Identification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound Cross-linking of the extracellular matrix by the maillard reaction in aging and diabetes: an update on "a puzzle nearing resolution"Pimagedine: a novel therapy for diabetic nephropathy.Comprehensive analysis of maillard protein modifications in human lenses: effect of age and cataract Extending the spectrum of α-dicarbonyl compounds in vivo.Maillard degradation pathways of vitamin C.Differential response to α-oxoaldehydes in tamoxifen resistant MCF-7 breast cancer cells.Favored 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.Chemical modification of proteins by lipids in diabetes.Molecular basis of maillard amide-advanced glycation end product (AGE) formation in vivo Diabetes-related adduct formation and retinopathy.Non-enzymatic glycation and glycoxidation protein products in foods and diseases: an interconnected, complex scenario fully open to innovative proteomic studies.Baking, ageing, diabetes: a short history of the Maillard reaction.Anti-melanogenic effects of resveratryl triglycolate, a novel hybrid compound derived by esterification of resveratrol with glycolic acid.Mass spectrometric determination of early and advanced glycation in biology.Pathways of the Maillard reaction under physiological conditions.Cell culture condition-dependent impact of AGE-rich food extracts on kinase activation and cell survival on human fibroblasts.Plasma Proteins Modified by Advanced Glycation End Products (AGEs) Reveal Site-specific Susceptibilities to Glycemic Control in Patients with Type 2 Diabetes.Characterization of the deoxyguanosine-lysine cross-link of methylglyoxal.Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins Glycation by ascorbic acid causes loss of activity of ribulose-1,5-bisphosphate carboxylase/oxygenase and its increased susceptibility to proteases.Unexpected crosslinking and diglycation as advanced glycation end-products from glyoxal.Maillard Proteomics: Opening New Pages.Probing Protein Glycation by Chromatography and Mass Spectrometry: Analysis of Glycation Adducts.Efficient and Mild Ullmann-Type N-Arylation of Amides, Carbamates, and Azoles in Water.

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P2860

Amides are novel protein modifications formed by physiological sugars.

http://www.wikidata.org/entity/Q43700248

description

2001 nî lūn-bûn

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2001年の論文

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

@zh-my

2001年学术文章

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2001年學術文章

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2001年學術文章

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name

Amides are novel protein modifications formed by physiological sugars.

@en

Amides are novel protein modifications formed by physiological sugars.

@nl

type

label

Amides are novel protein modifications formed by physiological sugars.

@en

Amides are novel protein modifications formed by physiological sugars.

@nl

prefLabel

Amides are novel protein modifications formed by physiological sugars.

@en

Amides are novel protein modifications formed by physiological sugars.

@nl

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P1476

Amides are novel protein modifications formed by physiological sugars.

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P2860

Pentosidine formation in skin correlates with severity of complications in individuals with long-standing IDDM

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

Amadorins: novel post-Amadori inhibitors of advanced glycation reactions.

Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose.

Protein glycation and oxidative stress in diabetes mellitus and ageing.

Structure of advanced Maillard reaction products and their pathological role.

Role of oxygen in cross-linking and chemical modification of collagen by glucose.

Evaluation of the extent of the early Maillard-reaction in milk products by direct measurement of the Amadori-product lactuloselysine.

Imidazolium crosslinks derived from reaction of lysine with glyoxal and methylglyoxal are increased in serum proteins of uremic patients: evidence for increased oxidative stress in uremia.

Synthesis of L-thiocitrulline, L-homothiocitrulline, and S-methyl-L-thiocitrulline: a new class of potent nitric oxide synthase inhibitors.

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41638-41647

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10.1074/JBC.M103557200

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45

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276

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