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10.1038/srep42989 http://scihub22266oqcxt.onion/10.1038/srep42989 C5322398!5322398!28230186     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2017 ; 7 (ä): ä Nephropedia Template TP {{tp|p=28230186|t=2017. Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor |pdf=|usr=}}{{28230186}} gab.com Text Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28230186 #FOAvip IgM is the first antibody to be produced in immune responses and plays an important role in the neutralization of bacteria and viruses. Human IgM is heavily glycosylated, featuring five N-linked glycan sites on the ? chain and one on the J-chain. Glycosylation of IgG is known to modulate the effector functions of Fc? receptors. In contrast, little is known about the effect of glycosylation on IgM binding to the human Fc? receptor (hFCMR). In this study, we identify the C?4 domain of IgM as the target of hFCMR, and show that binding and internalization of IgM by hFCMR is glycan-independent. We generated a homology-based structure for hFCMR and used molecular dynamic simulations to show how this interaction with IgM may occur. Finally, we reveal an inhibitory function for IgM in the proliferation of T cells. Twit Text FOAVip Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28230186 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28230186 #FOAvip English Wikipedia <ref>{{Cite pmid|28230186}}</ref> Glycan-independent binding and internalization of human IgM to FCMR, its cognate cellular receptor #MMPMID28230186 Lloyd KA; Wang J; Urban BC; Czajkowsky DM; Pleass RJ Sci Rep 2017[]; 7 (ä): ä PMID28230186show ga IgM is the first antibody to be produced in immune responses and plays an important role in the neutralization of bacteria and viruses. Human IgM is heavily glycosylated, featuring five N-linked glycan sites on the ? chain and one on the J-chain. Glycosylation of IgG is known to modulate the effector functions of Fc? receptors. In contrast, little is known about the effect of glycosylation on IgM binding to the human Fc? receptor (hFCMR). In this study, we identify the C?4 domain of IgM as the target of hFCMR, and show that binding and internalization of IgM by hFCMR is glycan-independent. We generated a homology-based structure for hFCMR and used molecular dynamic simulations to show how this interaction with IgM may occur. Finally, we reveal an inhibitory function for IgM in the proliferation of T cells. äGlycan-independent binding and internalization of human IgM to FCMR, i(epmc).pdf DeepDyve Pubget Overpricing