{"title":"Post-Translational Modifications of Proteins Exacerbate Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV2)","authors":"A. Raghav, Renu Tomar, J. Ahmad","doi":"10.5772/intechopen.100740","DOIUrl":"https://doi.org/10.5772/intechopen.100740","url":null,"abstract":"Severe acute respiratory syndrome coronavirus 2 (SARS-CoV2) is severely affecting the worldwide population. It belongs to the coronavirus family which exhibit protein constituted enveloped single-stranded RNA. These viral proteins undergo post-translational modifications (PTMs) that reorganized covalent bonds and modify the polypeptides and in turn modulate the protein functions. Being viral machinery, it uses host cells system to replicate itself and make their copes, their proteins are also subject to PTMs. Glycosylation, palmitoylation of the spike and envelope proteins, phosphorylation, of the nucleocapsid protein are among the major PTMs responsible for the pathogenesis of the viral infection phase. The current knowledge of CoV proteins PTMs is limited and need to be exploring for to understand the viral pathogenesis mechanism and PTMs effect of infection phase.","PeriodicalId":183835,"journal":{"name":"Fundamentals of Glycosylation [Working Title]","volume":"2 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2021-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"128016942","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The Structure of Leukocyte Sialic Acid-Containing Membrane Glycoconjugates is a Differential Indicator of the Development of Diabetic Complications","authors":"I. Brodyak, N. Sybirna","doi":"10.5772/INTECHOPEN.97199","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.97199","url":null,"abstract":"Glycans, as potential prognostic biomarkers, deserve attention in clinical glycomics for diseases diagnosis. The variety of glycan chains, attached to proteins and lipids, makes it possible to form unique glycoconjugates with a wide range of cellular functions. Under leukocyte-endothelial interaction, not only the availability of glycoconjugates with sialic acids at the terminal position of glycans are informative, but also the type of glycosidic bond by which sialic acids links to subterminal carbohydrates in structure of glycans. The process of sialylation of leukocyte glycoconjugates undergoes considerable changes in type 1 diabetes mellitus. At early stage of disease without diabetic complications, the pathology is accompanied by the increase of α2,6-linked sialic acids. The quantity of sialic acid-containing glycoconjugates on leukocytes surface increases in condition of disease duration up to five years. However, the quantity of sialic acids linked by α2,6-glycosidic bonds decreases in patients with the disease duration over ten years. Therefore, sialoglycans as marker molecules determine the leukocyte function in patients with type 1 diabetes mellitus, depending on the disease duration. Changes in the glycans structure of membrane glycoconjugates of leukocytes allow understanding the mechanism of diabetic complications development.","PeriodicalId":183835,"journal":{"name":"Fundamentals of Glycosylation [Working Title]","volume":"1 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2021-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"130384036","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Advanced Glycation End Products and Oxidative Stress in a Hyperglycaemic Environment","authors":"A. Nakamura, Ritsuko Kawahrada","doi":"10.5772/INTECHOPEN.97234","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.97234","url":null,"abstract":"Protein glycation is the random, nonenzymatic reaction of sugar and protein induced by diabetes and ageing; this process is quite different from glycosylation mediated by the enzymatic reactions catalysed by glycosyltransferases. Schiff bases form advanced glycation end products (AGEs) via intermediates, such as Amadori compounds. Although these AGEs form various molecular species, only a few of their structures have been determined. AGEs bind to different AGE receptors on the cell membrane and transmit signals to the cell. Signal transduction via the receptor of AGEs produces reactive oxygen species in cells, and oxidative stress is responsible for the onset of diabetic complications. This chapter introduces the molecular mechanisms of disease onset due to oxidative stress, including reactive oxygen species, caused by AGEs generated by protein glycation in a hyperglycaemic environment.","PeriodicalId":183835,"journal":{"name":"Fundamentals of Glycosylation [Working Title]","volume":"174 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2021-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"131265288","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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