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10.1093/glycob/cwx065 http://scihub22266oqcxt.onion/10.1093/glycob/cwx065 C5881768!5881768!28810662     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Glycobiology 2017 ; 27 (9): 878-87 Nephropedia Template TP {{tp|p=28810662|t=2017. Galectin-9 binds to O-glycans on protein disulfide isomerase |pdf=|usr=}}{{28810662}} gab.com Text Galectin-9 binds to O-glycans on protein disulfide isomerase JO: Glycobiology http://www.kidney.de/pget.php?&tw=1&pmid=28810662 #FOAvip Changes in the T cell surface redox environment regulate critical cell functions, such as cell migration, viral entry and cytokine production. Cell surface protein disulfide isomerase (PDI) contributes to the regulation of T cell surface redox status. Cell surface PDI can be released into the extracellular milieu or can be internalized by T cells. We have found that galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface. While endogenous galectin-9 is not required for basal cell surface PDI expression, exogenous galectin-9 mediated retention of cell surface PDI shifted the disulfide/thiol equilibrium on the T cell surface. O-glycans on PDI are required for galectin-9 binding, and PDI recognition appears to be specific for galectin-9, as galectin-1 and galectin-3 do not bind PDI. Galectin-9 is widely expressed by immune and endothelial cells in inflamed tissues, suggesting that T cells would be exposed to abundant galectin-9, in cis and in trans, in infectious or autoimmune conditions. Twit Text FOAVip Galectin-9 binds to O-glycans on protein disulfide isomerase ????Glycobiology http://www.kidney.de/pget.php?&tw=1&pmid=28810662 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28810662 #FOAvip English Wikipedia <ref>{{Cite pmid|28810662}}</ref> Galectin-9 binds to O-glycans on protein disulfide isomerase #MMPMID28810662 Schaefer K; Webb NE; Pang M; Hernandez-Davies JE; Lee KP; Gonzalez P; Douglass MV; Lee B; Baum LG Glycobiology 2017[Sep]; 27 (9): 878-87 PMID28810662show ga Changes in the T cell surface redox environment regulate critical cell functions, such as cell migration, viral entry and cytokine production. Cell surface protein disulfide isomerase (PDI) contributes to the regulation of T cell surface redox status. Cell surface PDI can be released into the extracellular milieu or can be internalized by T cells. We have found that galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface. While endogenous galectin-9 is not required for basal cell surface PDI expression, exogenous galectin-9 mediated retention of cell surface PDI shifted the disulfide/thiol equilibrium on the T cell surface. O-glycans on PDI are required for galectin-9 binding, and PDI recognition appears to be specific for galectin-9, as galectin-1 and galectin-3 do not bind PDI. Galectin-9 is widely expressed by immune and endothelial cells in inflamed tissues, suggesting that T cells would be exposed to abundant galectin-9, in cis and in trans, in infectious or autoimmune conditions. äGalectin-9 binds to O-glycans on protein disulfide isomerase (epmc).pdf DeepDyve Pubget Overpricing