Free radicals generated during the glycation reaction of amino acids by methylglyoxal. A model study of protein-cross-linked free radicals.
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TLDR
Results indicate that dicarbonyl compounds cross-link free amino groups of protein by forming Schiff bases, which donate electrons directly to dicarbon compounds to form the cross-linked radical cations and the methylglyoxal radical anions.About:
This article is published in Journal of Biological Chemistry.The article was published on 1995-11-24 and is currently open access. It has received 269 citations till now. The article focuses on the topics: Radical & Radical ion.read more
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Biochemistry and pathology of radical-mediated protein oxidation
TL;DR: Proteins are also key targets in defensive cytolysis and in inflammatory self-damage, and the possibility of selective protection against protein oxidation (antioxidation) is raised.
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Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease
TL;DR: There is strong evidence that peroxynitrite is involved in oxidative damage of Alzheimer’s disease, and the widespread occurrence of nitrotyrosine in neurons suggests that oxidative damage is not restricted to long-lived polymers such as NFTs, but instead reflects a generalized oxidative stress that is important in disease pathogenesis.
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Singlet oxygen-mediated damage to proteins and its consequences
TL;DR: This paper reviews the data available on singlet oxygen-mediated protein oxidation and concentrates primarily on the mechanisms by which this excited state species brings about changes to both the side-chains and backbone of amino acids, peptides, and proteins.
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Advanced glycation endproducts in food and their effects on health.
Malene W. Poulsen,Rikke Susanne Vingborg Hedegaard,Jeanette M. Andersen,Barbora de Courten,Barbora de Courten,Susanne Bügel,John Nielsen,Leif H. Skibsted,Lars O. Dragsted +8 more
TL;DR: The current review points out several research needs in order to address important questions on AGEs in foods and health.
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Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications.
TL;DR: A comprehensive overview of methylglyoxal research, extending discussion from chemistry to biological implications by reviewing some important characteristics of methyl glyoxal metabolism and toxicity in a wide variety of species, and emphasizing the action of methyl-oxoaldehyde production in the environment as a potential risk factor and to the possible role of this a-dicarbonyl in diseases as discussed by the authors.
References
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Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels☆
TL;DR: The staining procedure for localizing superoxide dismutase on polyacrylamide electrophoretograms has been applied to extracts obtained from a variety of sources and could thus be assayed either in crude extracts or in purified protein fractions.
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Role of Oxidative Stress in Development of Complications in Diabetes
TL;DR: Structural characterization of the cross-links and other products accumulating in collagen in diabetes is needed to gain a better understanding of the relationship between oxidative stress and the development of complications in diabetes.
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Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications.
TL;DR: This seminar reviews recent studies suggesting that the central pathologic features of diabetic complications are caused by the hyperglycemia-accelerated formation of nonenzymatic advanced gly...
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Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes.
Simon P. Wolff,Roger T. Dean +1 more
TL;DR: It is suggested that a component of protein glycosylation is dependent upon glucose autoxidation and subsequent covalent attachment of ketoaldehydes, and the chemical evidence for the currently accepted 'Amadori' product is consistent with the structure expected for the attachment of a glucose-derived ketoaldehyde to protein.
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Advanced glycosylation products quench nitric oxide and mediate defective endothelium-dependent vasodilatation in experimental diabetes.
TL;DR: It is demonstrated that advanced glycosylation products quench nitric oxide activity in vitro and in vivo and that inhibition of advanced glyCosylation with aminoguanidine preventsNitric oxide quenching, and ameliorates the vasodilatory impairment.