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- W2305000973 endingPage "BCI.S36141" @default.
- W2305000973 startingPage "BCI.S36141" @default.
- W2305000973 abstract "Diabetes and its complications are hyperglycemic toxicity diseases. Many metabolic pathways in this array of diseases become aberrant, which is accompanied with a variety of posttranslational protein modifications that in turn reflect diabetic glucotoxicity. In this review, we summarize some of the most widely studied protein modifications in diabetes and its complications. These modifications include glycation, carbonylation, nitration, cysteine S-nitrosylation, acetylation, sumoylation, ADP-ribosylation, O-GlcNAcylation, and succination. All these posttranslational modifications can be significantly attributed to oxidative stress and/or carbon stress induced by diabetic redox imbalance that is driven by activation of pathways, such as the polyol pathway and the ADP-ribosylation pathway. Exploring the nature of these modifications should facilitate our understanding of the pathological mechanisms of diabetes and its associated complications." @default.
- W2305000973 created "2016-06-24" @default.
- W2305000973 creator A5046378016 @default.
- W2305000973 creator A5064369996 @default.
- W2305000973 creator A5071374687 @default.
- W2305000973 creator A5083848125 @default.
- W2305000973 date "2016-01-01" @default.
- W2305000973 modified "2023-10-13" @default.
- W2305000973 title "Protein Modifications as Manifestations of Hyperglycemic Glucotoxicity in Diabetes and Its Complications" @default.
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