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10.1016/j.ijbiomac.2021.08.054 http://scihub22266oqcxt.onion/10.1016/j.ijbiomac.2021.08.054 34389387!ä!34389387 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34389387&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Biol+Macromol 2021 ; 189 (ä): 279-291 Nephropedia Template TP {{tp|p=34389387|t=2021. Brilliant glycans and glycosylation: Seq and ye shall find |pdf=|usr=}}{{34389387}} gab.com Text Brilliant glycans and glycosylation: Seq and ye shall find JO: Int J Biol Macromol http://www.kidney.de/pget.php?&tw=1&pmid=34389387 #FOAvip Proteoglycosylation is the addition of monosaccharides or glycans to the protein peptide chain. This is a common post-translational modification of proteins with a variety of biological functions. At present, more than half of all biopharmaceuticals in clinic are modified by glycosylation. Most glycoproteins are potential drug targets and biomarkers for disease diagnosis. Therefore, in-depth study of glycan structure of glycoproteins will ultimately improve the sensitivity and specificity of glycoproteins for clinical disease detection. With the deepening of research, the function and application value of glycans and glycosylation has gradually emerged. This review systematically introduces the latest research progress of glycans and glycosylation. It encompasses six cancers, four viruses, and their latest discoveries in Alzheimer's disease, allergic diseases, congenital diseases, gastrointestinal diseases, inflammation, and aging. Twit Text FOAVip Brilliant glycans and glycosylation: Seq and ye shall find ????Int J Biol Macromol http://www.kidney.de/pget.php?&tw=1&pmid=34389387 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34389387 #FOAvip English Wikipedia <ref>{{Cite pmid|34389387}}</ref> Brilliant glycans and glycosylation: Seq and ye shall find #MMPMID34389387 Gao G; Li C; Fan W; Zhang M; Li X; Chen W; Li W; Liang R; Li Z; Zhu X Int J Biol Macromol 2021[Oct]; 189 (ä): 279-291 PMID34389387show ga Proteoglycosylation is the addition of monosaccharides or glycans to the protein peptide chain. This is a common post-translational modification of proteins with a variety of biological functions. At present, more than half of all biopharmaceuticals in clinic are modified by glycosylation. Most glycoproteins are potential drug targets and biomarkers for disease diagnosis. Therefore, in-depth study of glycan structure of glycoproteins will ultimately improve the sensitivity and specificity of glycoproteins for clinical disease detection. With the deepening of research, the function and application value of glycans and glycosylation has gradually emerged. This review systematically introduces the latest research progress of glycans and glycosylation. It encompasses six cancers, four viruses, and their latest discoveries in Alzheimer's disease, allergic diseases, congenital diseases, gastrointestinal diseases, inflammation, and aging. |Glycoproteins/*chemistry/metabolism[MESH] |Glycosylation[MESH] |Humans[MESH] |Monosaccharides[MESH] |Polysaccharides/*chemistry/metabolism[MESH] |Protein Processing, Post-Translational[MESH]Brilliant glycans and glycosylation: Seq and ye shall find (epmc).pdf DeepDyve Pubget Overpricing