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10.1038/cmi.2015.19 http://scihub22266oqcxt.onion/10.1038/cmi.2015.19 C4856805!4856805!25942513     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Mol+Immunol 2016 ; 13 (3): 391-400 Nephropedia Template TP {{tp|p=25942513|t=2016. Development of an antibody that neutralizes soluble IgE and eliminates IgE expressing B cells |pdf=|usr=}}{{25942513}} gab.com Text Development of an antibody that neutralizes soluble IgE and eliminates IgE expressing B cells JO: Cell Mol Immunol http://www.kidney.de/pget.php?&tw=1&pmid=25942513 #FOAvip Immunoglobulin E (IgE) plays a key role in allergic asthma and is a clinically validated target for monoclonal antibodies. Therapeutic anti-IgE antibodies block the interaction between IgE and the Fc epsilon (Fc?) receptor, which eliminates or minimizes the allergic phenotype but does not typically curtail the ongoing production of IgE by B cells. We generated high-affinity anti-IgE antibodies (MEDI4212) that have the potential to both neutralize soluble IgE and eliminate IgE-expressing B-cells through antibody-dependent cell-mediated cytotoxicity. MEDI4212 variants were generated that contain mutations in the Fc region of the antibody or alterations in fucosylation in order to enhance the antibody's affinity for Fc?RIIIa. All MEDI4212 variants bound to human IgE with affinities comparable to the wild-type (WT) antibody. Each variant was shown to inhibit the interaction between IgE and Fc?RI, which translated into potent inhibition of Fc?RI-mediated function responses. Importantly, all variants bound similarly to IgE at the surface of membrane IgE expressing cells. However, MEDI4212 variants demonstrated enhanced affinity for Fc?RIIIa including the polymorphic variants at position 158. The improvement in Fc?RIIIa binding led to increased effector function in cell based assays using both engineered cell lines and class switched human IgE B cells. Through its superior suppression of IgE, we anticipate that effector function enhanced MEDI4212 may be able to neutralize high levels of soluble IgE and provide increased long-term benefit by eliminating the IgE expressing B cells before they differentiate and become IgE secreting plasma cells. Twit Text FOAVip Development of an antibody that neutralizes soluble IgE and eliminates IgE expressing B cells ????Cell Mol Immunol http://www.kidney.de/pget.php?&tw=1&pmid=25942513 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25942513 #FOAvip English Wikipedia <ref>{{Cite pmid|25942513}}</ref> Development of an antibody that neutralizes soluble IgE and eliminates IgE expressing B cells #MMPMID25942513 Nyborg AC; Zacco A; Ettinger R; Jack Borrok M; Zhu J; Martin T; Woods R; Kiefer C; Bowen MA; Suzanne Cohen E; Herbst R; Wu H; Coats S Cell Mol Immunol 2016[May]; 13 (3): 391-400 PMID25942513show ga Immunoglobulin E (IgE) plays a key role in allergic asthma and is a clinically validated target for monoclonal antibodies. Therapeutic anti-IgE antibodies block the interaction between IgE and the Fc epsilon (Fc?) receptor, which eliminates or minimizes the allergic phenotype but does not typically curtail the ongoing production of IgE by B cells. We generated high-affinity anti-IgE antibodies (MEDI4212) that have the potential to both neutralize soluble IgE and eliminate IgE-expressing B-cells through antibody-dependent cell-mediated cytotoxicity. MEDI4212 variants were generated that contain mutations in the Fc region of the antibody or alterations in fucosylation in order to enhance the antibody's affinity for Fc?RIIIa. All MEDI4212 variants bound to human IgE with affinities comparable to the wild-type (WT) antibody. Each variant was shown to inhibit the interaction between IgE and Fc?RI, which translated into potent inhibition of Fc?RI-mediated function responses. Importantly, all variants bound similarly to IgE at the surface of membrane IgE expressing cells. However, MEDI4212 variants demonstrated enhanced affinity for Fc?RIIIa including the polymorphic variants at position 158. The improvement in Fc?RIIIa binding led to increased effector function in cell based assays using both engineered cell lines and class switched human IgE B cells. Through its superior suppression of IgE, we anticipate that effector function enhanced MEDI4212 may be able to neutralize high levels of soluble IgE and provide increased long-term benefit by eliminating the IgE expressing B cells before they differentiate and become IgE secreting plasma cells. äDevelopment of an antibody that neutralizes soluble IgE and eliminates(epmc).pdf DeepDyve Pubget Overpricing