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10.3389/fimmu.2017.00884 http://scihub22266oqcxt.onion/10.3389/fimmu.2017.00884 C5566574!5566574!28871249     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 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=28871249|t=2017. Neutralization of Human Interleukin 23 by Multivalent Nanobodies Explained by the Structure of Cytokine?Nanobody Complex |pdf=|usr=}}{{28871249}} gab.com Text Neutralization of Human Interleukin 23 by Multivalent Nanobodies Explained by the Structure of Cytokine Nanobody Complex JO: Front Immunol http://www.kidney.de/pget.php?&tw=1&pmid=28871249 #FOAvip The heterodimeric cytokine interleukin (IL) 23 comprises the IL12-shared p40 subunit and an IL23-specific subunit, p19. Together with IL12 and IL27, IL23 sits at the apex of the regulatory mechanisms shaping adaptive immune responses. IL23, together with IL17, plays an important role in the development of chronic inflammation and autoimmune inflammatory diseases. In this context, we generated monovalent antihuman IL23 variable heavy chain domain of llama heavy chain antibody (VHH) domains (Nanobodies®) with low nanomolar affinity for human interleukin (hIL) 23. The crystal structure of a quaternary complex assembling hIL23 and several nanobodies against p19 and p40 subunits allowed identification of distinct epitopes and enabled rational design of a multivalent IL23-specific blocking nanobody. Taking advantage of the ease of nanobody formatting, multivalent IL23 nanobodies were assembled with properly designed linkers flanking an antihuman serum albumin nanobody, with improved hIL23 neutralization capacity in vitro and in vivo, as compared to the monovalent nanobodies. These constructs with long exposure time are excellent candidates for further developments targeting Crohn?s disease, rheumatoid arthritis, and psoriasis. Twit Text FOAVip Neutralization of Human Interleukin 23 by Multivalent Nanobodies Explained by the Structure of Cytokine Nanobody Complex ????Front Immunol http://www.kidney.de/pget.php?&tw=1&pmid=28871249 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28871249 #FOAvip English Wikipedia <ref>{{Cite pmid|28871249}}</ref> Neutralization of Human Interleukin 23 by Multivalent Nanobodies Explained by the Structure of Cytokine?Nanobody Complex #MMPMID28871249 Desmyter A; Spinelli S; Boutton C; Saunders M; Blachetot C; de Haard H; Denecker G; Van Roy M; Cambillau C; Rommelaere H Front Immunol 2017[]; 8 (ä): ä PMID28871249show ga The heterodimeric cytokine interleukin (IL) 23 comprises the IL12-shared p40 subunit and an IL23-specific subunit, p19. Together with IL12 and IL27, IL23 sits at the apex of the regulatory mechanisms shaping adaptive immune responses. IL23, together with IL17, plays an important role in the development of chronic inflammation and autoimmune inflammatory diseases. In this context, we generated monovalent antihuman IL23 variable heavy chain domain of llama heavy chain antibody (VHH) domains (Nanobodies®) with low nanomolar affinity for human interleukin (hIL) 23. The crystal structure of a quaternary complex assembling hIL23 and several nanobodies against p19 and p40 subunits allowed identification of distinct epitopes and enabled rational design of a multivalent IL23-specific blocking nanobody. Taking advantage of the ease of nanobody formatting, multivalent IL23 nanobodies were assembled with properly designed linkers flanking an antihuman serum albumin nanobody, with improved hIL23 neutralization capacity in vitro and in vivo, as compared to the monovalent nanobodies. These constructs with long exposure time are excellent candidates for further developments targeting Crohn?s disease, rheumatoid arthritis, and psoriasis. äNeutralization of Human Interleukin 23 by Multivalent Nanobodies Expla(epmc).pdf DeepDyve Pubget Overpricing