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10.3109/07388551.2013.834293 http://scihub22266oqcxt.onion/10.3109/07388551.2013.834293 C4876602!4876602!24156398     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       Crit+Rev+Biotechnol 2015 ; 35 (2): 235-54 Nephropedia Template TP {{tp|p=24156398|t=2015. Fc-fusion proteins and FcRn: structural insights for longer-lasting and more effective therapeutics |pdf=|usr=}}{{24156398}} gab.com Text Fc-fusion proteins and FcRn: structural insights for longer-lasting and more effective therapeutics JO: Crit Rev Biotechnol http://www.kidney.de/pget.php?&tw=1&pmid=24156398 #FOAvip Nearly 350 IgG-based therapeutics are approved for clinical use or are under development for many diseases lacking adequate treatment options. These include molecularly engineered biologicals comprising the IgG Fc-domain fused to various effector molecules (so-called Fc-fusion proteins) that confer the advantages of IgG, including binding to the neonatal Fc receptor (FcRn) to facilitate in vivo stability, and the therapeutic benefit of the specific effector functions. Advances in IgG structure-function relationships and an understanding of FcRn biology have provided therapeutic opportunities for previously unapproachable diseases. This article discusses approved Fc-fusion therapeutics, novel Fc-fusion proteins and FcRn-dependent delivery approaches in development, and how engineering of the FcRn?Fc interaction can generate longer-lasting and more effective therapeutics. Twit Text FOAVip Fc-fusion proteins and FcRn: structural insights for longer-lasting and more effective therapeutics ????Crit Rev Biotechnol http://www.kidney.de/pget.php?&tw=1&pmid=24156398 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24156398 #FOAvip English Wikipedia <ref>{{Cite pmid|24156398}}</ref> Fc-fusion proteins and FcRn: structural insights for longer-lasting and more effective therapeutics #MMPMID24156398 Rath T; Baker K; Dumont JA; Peters RT; Jiang H; Qiao SW; Lencer WI; Pierce GF; Blumberg RS Crit Rev Biotechnol 2015[Jun]; 35 (2): 235-54 PMID24156398show ga Nearly 350 IgG-based therapeutics are approved for clinical use or are under development for many diseases lacking adequate treatment options. These include molecularly engineered biologicals comprising the IgG Fc-domain fused to various effector molecules (so-called Fc-fusion proteins) that confer the advantages of IgG, including binding to the neonatal Fc receptor (FcRn) to facilitate in vivo stability, and the therapeutic benefit of the specific effector functions. Advances in IgG structure-function relationships and an understanding of FcRn biology have provided therapeutic opportunities for previously unapproachable diseases. This article discusses approved Fc-fusion therapeutics, novel Fc-fusion proteins and FcRn-dependent delivery approaches in development, and how engineering of the FcRn?Fc interaction can generate longer-lasting and more effective therapeutics. äFc-fusion proteins and FcRn: structural insights for longer-lasting an(epmc).pdf DeepDyve Pubget Overpricing