Protein crosslinking by the Maillard reaction: dicarbonyl-derived imidazolium crosslinks in aging and diabetes.
about
Age effect on myocellular remodeling: response to exercise and nutrition in humansIdentification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compoundAdvanced glycation: an important pathological event in diabetic and age related ocular diseaseHydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimicsDifferential effects of glycation on protein aggregation and amyloid formation.Kinetic characterization and comparison of various protein crosslinking reagents for matrix modification.Insulin glycation by methylglyoxal results in native-like aggregation and inhibition of fibril formationFavored and disfavored pathways of protein crosslinking by glucose: glucose lysine dimer (GLUCOLD) and crossline versus glucosepane.Life and death: metabolic rate, membrane composition, and life span of animals.Involvement of Maillard reactions in Alzheimer disease.Hohenheimer Consensus Talk. Oxidative and premature skin ageing.Dicarbonyl Induced Structural Perturbations Make Histone H1 Highly Immunogenic and Generate an Auto-Immune Response in CancerStructural changes in histone H2A by methylglyoxal generate highly immunogenic amorphous aggregates with implications in auto-immune response in cancer.Creating proteins with novel functionality via the Maillard reaction: a review.Glyoxalase I activity and immunoreactivity in the aging human lens.Aldehydes and disturbance of carbohydrate metabolism: some consequences and possible approaches to its normalization.A brief critical overview of the biological effects of methylglyoxal and further evaluation of a methylglyoxal-based anticancer formulation in treating cancer patients.Lens aging: effects of crystallins.The pathogenic role of Maillard reaction in the aging eye.Molecular strategies to prevent, inhibit, and degrade advanced glycoxidation and advanced lipoxidation end products.Pathways of the Maillard reaction under physiological conditions.Sciadopitysin alleviates methylglyoxal-mediated glycation in osteoblastic MC3T3-E1 cells by enhancing glyoxalase system and mitochondrial biogenesis.Effect of site-directed mutagenesis of methylglyoxal-modifiable arginine residues on the structure and chaperone function of human alphaA-crystallin.Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assaysHydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability.Effect of high sugar levels on miRNA expression. Studies with galactosemic mice lenses.Is There Inflammatory Synergy in Type II Diabetes Mellitus and Alzheimer's Disease?Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatization by 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and application to Nepsilon-carboxymethyl-lysine- and Nepsilon-(1-carboxyethyl)lysine-modiGlycation by ascorbic acid oxidation products leads to the aggregation of lens proteinsInhibition of methylglyoxal-mediated protein modification in glyoxalase I overexpressing mouse lenses.Glycation of Wild-Type Apomyoglobin Induces Formation of Highly Cytotoxic Oligomeric Species.Role of cysteine residues in the enhancement of chaperone function in methylglyoxal-modified human alpha A-crystallin.Effect of glycation on alpha-crystallin structure and chaperone-like function.Evidence for non-enzymatic glycosylation in Escherichia coli.Amides are novel protein modifications formed by physiological sugars.Oxidative deamination of lysine residue in plasma protein of diabetic rats. Novel mechanism via the Maillard reaction.High sugar-induced repression of antioxidant and anti-apoptotic genes in lens: reversal by pyruvate.Unexpected crosslinking and diglycation as advanced glycation end-products from glyoxal.Immunomodulation by Processed Animal Feed: The Role of Maillard Reaction Products and Advanced Glycation End-Products (AGEs)
P2860
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P2860
Protein crosslinking by the Maillard reaction: dicarbonyl-derived imidazolium crosslinks in aging and diabetes.
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Protein crosslinking by the Ma ...... sslinks in aging and diabetes.
@ast
Protein crosslinking by the Ma ...... sslinks in aging and diabetes.
@en
type
label
Protein crosslinking by the Ma ...... sslinks in aging and diabetes.
@ast
Protein crosslinking by the Ma ...... sslinks in aging and diabetes.
@en
prefLabel
Protein crosslinking by the Ma ...... sslinks in aging and diabetes.
@ast
Protein crosslinking by the Ma ...... sslinks in aging and diabetes.
@en
P356
P1476
Protein crosslinking by the Ma ...... sslinks in aging and diabetes.
@en
P2093
P304
P356
10.1006/ABBI.1999.1291
P407
P577
1999-08-01T00:00:00Z