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10.1002/pro.2729 http://scihub22266oqcxt.onion/10.1002/pro.2729 C4570538!4570538!26099203     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       Protein+Sci 2015 ; 24 (9): 1440-50 Nephropedia Template TP {{tp|p=26099203|t=2015. Structural basis of the broadly neutralizing anti-interferon-? antibody rontalizumab |pdf=|usr=}}{{26099203}} gab.com Text Structural basis of the broadly neutralizing anti-interferon- antibody rontalizumab JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=26099203 #FOAvip Interferons-alpha (IFN-?) are the expressed gene products comprising thirteen type I interferons with protein pairwise sequence similarities in the 77?96% range. Three other widely expressed human type I interferons, IFN-?, IFN-? and IFN-? have sequences 29?33%, 29?32% and 56?60% similar to the IFN-?s, respectively. Type I interferons act on immune cells by producing subtly different immune-modulatory effects upon binding to the extracellular domains of a heterodimeric cell-surface receptor composed of IFNAR1 and IFNAR2, most notably anti-viral effects. IFN-? has been used to treat infection by hepatitis-virus type C (HCV) and a correlation between hyperactivity of IFN-?-induced signaling and systemic lupus erythematosis (SLE), or lupus, has been noted. Anti-IFN-? antibodies including rontalizumab have been under clinical study for the treatment of lupus. To better understand the rontalizumab mechanism of action and specificity, we determined the X-ray crystal structure of the Fab fragment of rontalizumab bound to human IFN-?2 at 3Å resolution and find substantial overlap of the antibody and IFNA2 epitopes on IFN-?2. Twit Text FOAVip Structural basis of the broadly neutralizing anti-interferon- antibody rontalizumab ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=26099203 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26099203 #FOAvip English Wikipedia <ref>{{Cite pmid|26099203}}</ref> Structural basis of the broadly neutralizing anti-interferon-? antibody rontalizumab #MMPMID26099203 Maurer B; Bosanac I; Shia S; Kwong M; Corpuz R; Vandlen R; Schmidt K; Eigenbrot C Protein Sci 2015[Sep]; 24 (9): 1440-50 PMID26099203show ga Interferons-alpha (IFN-?) are the expressed gene products comprising thirteen type I interferons with protein pairwise sequence similarities in the 77?96% range. Three other widely expressed human type I interferons, IFN-?, IFN-? and IFN-? have sequences 29?33%, 29?32% and 56?60% similar to the IFN-?s, respectively. Type I interferons act on immune cells by producing subtly different immune-modulatory effects upon binding to the extracellular domains of a heterodimeric cell-surface receptor composed of IFNAR1 and IFNAR2, most notably anti-viral effects. IFN-? has been used to treat infection by hepatitis-virus type C (HCV) and a correlation between hyperactivity of IFN-?-induced signaling and systemic lupus erythematosis (SLE), or lupus, has been noted. Anti-IFN-? antibodies including rontalizumab have been under clinical study for the treatment of lupus. To better understand the rontalizumab mechanism of action and specificity, we determined the X-ray crystal structure of the Fab fragment of rontalizumab bound to human IFN-?2 at 3Å resolution and find substantial overlap of the antibody and IFNA2 epitopes on IFN-?2. äStructural basis of the broadly neutralizing anti-interferon-? antibod(epmc).pdf DeepDyve Pubget Overpricing