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10.3389/fimmu.2017.00592 http://scihub22266oqcxt.onion/10.3389/fimmu.2017.00592 C5442170!5442170!28596769     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Immunol 2017 ; 8 (ä): ä Nephropedia Template TP {{tp|p=28596769|t=2017. C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions |pdf=|usr=}}{{28596769}} gab.com Text C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions JO: Front Immunol http://www.kidney.de/pget.php?&tw=1&pmid=28596769 #FOAvip Complement C1 is the defining component of the classical pathway. Within the C1qC1r2C1s2 complex, C1q functions as a molecular scaffold for C1r2C1s2 and C1q binding to its ligands activates these two serine proteases. The classic C1q ligands are antigen-bound antibodies and activated C1s cleaves C4 and C2 to initiate the complement cascade. Recent studies suggest broad C1 functions beyond the complement system. C1q binds to the Frizzled receptors to activate C1s, which cleaves lipoprotein receptor-related protein 6 to trigger aging-associated Wnt receptor signaling. C1q binds to apoptotic cells and the activated C1 proteases cleave nuclear antigens. C1s also cleaves MHC class I molecule and potentially numerous other proteins. The diversity of C1q ligands and C1 protease substrates renders C1 complex versatile and modular so that it can adapt to multiple molecular and cellular processes besides the complement system. Twit Text FOAVip C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions ????Front Immunol http://www.kidney.de/pget.php?&tw=1&pmid=28596769 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28596769 #FOAvip English Wikipedia <ref>{{Cite pmid|28596769}}</ref> C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions #MMPMID28596769 Lu J; Kishore U Front Immunol 2017[]; 8 (ä): ä PMID28596769show ga Complement C1 is the defining component of the classical pathway. Within the C1qC1r2C1s2 complex, C1q functions as a molecular scaffold for C1r2C1s2 and C1q binding to its ligands activates these two serine proteases. The classic C1q ligands are antigen-bound antibodies and activated C1s cleaves C4 and C2 to initiate the complement cascade. Recent studies suggest broad C1 functions beyond the complement system. C1q binds to the Frizzled receptors to activate C1s, which cleaves lipoprotein receptor-related protein 6 to trigger aging-associated Wnt receptor signaling. C1q binds to apoptotic cells and the activated C1 proteases cleave nuclear antigens. C1s also cleaves MHC class I molecule and potentially numerous other proteins. The diversity of C1q ligands and C1 protease substrates renders C1 complex versatile and modular so that it can adapt to multiple molecular and cellular processes besides the complement system. äC1 Complex: An Adaptable Proteolytic Module for Complement and Non-Com(epmc).pdf DeepDyve Pubget Overpricing