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10.1073/pnas.1718172115 http://scihub22266oqcxt.onion/10.1073/pnas.1718172115 C5789950!5789950!29311294     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2018 ; 115 (4): 720-5 Nephropedia Template TP {{tp|p=29311294|t=2018. Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation |pdf=|usr=}}{{29311294}} gab.com Text Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29311294 #FOAvip The carbohydrate components of glycoproteins are known to affect the structure and function of glycoproteins, and thus it is important to develop effective tools to manipulate and optimize the glycan components of glycoproteins with therapeutic significance. This study demonstrates the discovery of endoglycosidases for the remodeling of glycans on Herceptin, a monoclonal antibody used in the treatment of breast cancer, to optimize its effector functions, especially the antibody-dependent cellular cytotoxicity (ADCC). In addition, a method has been developed for the expression of antibodies from yeast to enable the large-scale synthesis of antibodies for further manipulation of the glycan moiety, using endoglycosidases and stable transglycosylation donors to prepare a homogeneous glycoform with optimized effector functions. Twit Text FOAVip Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=29311294 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29311294 #FOAvip English Wikipedia <ref>{{Cite pmid|29311294}}</ref> Glycoengineering of antibody (Herceptin) through yeast expression and in vitro enzymatic glycosylation #MMPMID29311294 Liu CP; Tsai TI; Cheng T; Shivatare VS; Wu CY; Wu CY; Wong CH Proc Natl Acad Sci U S A 2018[Jan]; 115 (4): 720-5 PMID29311294show ga The carbohydrate components of glycoproteins are known to affect the structure and function of glycoproteins, and thus it is important to develop effective tools to manipulate and optimize the glycan components of glycoproteins with therapeutic significance. This study demonstrates the discovery of endoglycosidases for the remodeling of glycans on Herceptin, a monoclonal antibody used in the treatment of breast cancer, to optimize its effector functions, especially the antibody-dependent cellular cytotoxicity (ADCC). In addition, a method has been developed for the expression of antibodies from yeast to enable the large-scale synthesis of antibodies for further manipulation of the glycan moiety, using endoglycosidases and stable transglycosylation donors to prepare a homogeneous glycoform with optimized effector functions. äGlycoengineering of antibody (Herceptin) through yeast expression and (epmc).pdf DeepDyve Pubget Overpricing