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10.1194/jlr.R063032 http://scihub22266oqcxt.onion/10.1194/jlr.R063032 C4808780!4808780!26593072     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Lipid+Res 2016 ; 57 (4): 538-45 Nephropedia Template TP {{tp|p=26593072|t=2016. GPI-AP release in cellular, developmental, and reproductive biology |pdf=|usr=}}{{26593072}} gab.com Text GPI-AP release in cellular, developmental, and reproductive biology JO: J Lipid Res http://www.kidney.de/pget.php?&tw=1&pmid=26593072 #FOAvip Glycosylphosphatidylinositol-anchored proteins (GPI-APs) contain a covalently linked GPI anchor located on outer cell membranes. GPI-APs are ubiquitously conserved from protozoa to vertebrates and are critical for physiological events such as development, immunity, and neurogenesis in vertebrates. Both membrane-anchored and soluble GPI-APs play a role in regulating their protein conformation and functional properties. Several pathways mediate the release of GPI-APs from the plasma membrane by vesiculation or cleavage. Phospholipases and putative substrate-specific GPI-AP-releasing enzymes, such as NOTUM, glycerophosphodiesterase 2, and angiotensin-converting enzyme, have been characterized in mammals. Here, the protein modifications resulting from the cleavage of the GPI anchor are discussed in the context of its physiological functions. Twit Text FOAVip GPI-AP release in cellular, developmental, and reproductive biology ????J Lipid Res http://www.kidney.de/pget.php?&tw=1&pmid=26593072 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26593072 #FOAvip English Wikipedia <ref>{{Cite pmid|26593072}}</ref> GPI-AP release in cellular, developmental, and reproductive biology #MMPMID26593072 Fujihara Y; Ikawa M J Lipid Res 2016[Apr]; 57 (4): 538-45 PMID26593072show ga Glycosylphosphatidylinositol-anchored proteins (GPI-APs) contain a covalently linked GPI anchor located on outer cell membranes. GPI-APs are ubiquitously conserved from protozoa to vertebrates and are critical for physiological events such as development, immunity, and neurogenesis in vertebrates. Both membrane-anchored and soluble GPI-APs play a role in regulating their protein conformation and functional properties. Several pathways mediate the release of GPI-APs from the plasma membrane by vesiculation or cleavage. Phospholipases and putative substrate-specific GPI-AP-releasing enzymes, such as NOTUM, glycerophosphodiesterase 2, and angiotensin-converting enzyme, have been characterized in mammals. Here, the protein modifications resulting from the cleavage of the GPI anchor are discussed in the context of its physiological functions. äGPI-AP release in cellular, developmental, and reproductive biology (epmc).pdf DeepDyve Pubget Overpricing