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10.1016/j.bbrc.2014.05.115 http://scihub22266oqcxt.onion/10.1016/j.bbrc.2014.05.115 C4254162!4254162 !24909690     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24909690 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochem+Biophys+Res+Commun 2014 ; 453 (2 ): 235-42 Nephropedia Template TP {{tp|p=24909690 |t=2014. Significance of glycosylation in Notch signaling |pdf=|usr=}}{{24909690 }} gab.com Text Significance of glycosylation in Notch signaling JO: Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=24909690 #FOAvip Notch signaling is essential for cell-fate specification in metazoans, and dysregulation of the pathway leads to a variety of human diseases including heart and vascular defects as well as cancer. Glycosylation of the Notch extracellular domain has emerged as an elegant means for regulating Notch activity, especially since the discovery that Fringe is a glycosyltransferase that modifies O-fucose in 2000. Since then, several other O-glycans on the extracellular domain have been demonstrated to modulate Notch activity. Here we will describe recent results on the molecular mechanisms by which Fringe modulates Notch activity, summarize recent work on how O-glucose, O-GlcNAc, and O-GalNAc glycans affect Notch, and discuss several human genetic disorders resulting from defects in Notch glycosylation. Twit Text FOAVip Significance of glycosylation in Notch signaling ????Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=24909690 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24909690 #FOAvip English Wikipedia <ref>{{Cite pmid|24909690 }}</ref> Significance of glycosylation in Notch signaling #MMPMID24909690 Takeuchi H ; Haltiwanger RS Biochem Biophys Res Commun 2014[Oct]; 453 (2 ): 235-42 PMID24909690 show ga Notch signaling is essential for cell-fate specification in metazoans, and dysregulation of the pathway leads to a variety of human diseases including heart and vascular defects as well as cancer. Glycosylation of the Notch extracellular domain has emerged as an elegant means for regulating Notch activity, especially since the discovery that Fringe is a glycosyltransferase that modifies O-fucose in 2000. Since then, several other O-glycans on the extracellular domain have been demonstrated to modulate Notch activity. Here we will describe recent results on the molecular mechanisms by which Fringe modulates Notch activity, summarize recent work on how O-glucose, O-GlcNAc, and O-GalNAc glycans affect Notch, and discuss several human genetic disorders resulting from defects in Notch glycosylation. |Animals [MESH] |Congenital Disorders of Glycosylation/genetics/metabolism [MESH] |Fucose/chemistry [MESH] |Glucose/chemistry [MESH] |Glycosylation [MESH] |Glycosyltransferases/metabolism [MESH] |Humans [MESH] |Models, Molecular [MESH] |Polysaccharides/chemistry/metabolism [MESH] |Protein Interaction Domains and Motifs [MESH] |Protein Processing, Post-Translational [MESH] |Receptors, Notch/chemistry/genetics/*metabolism [MESH] |Repetitive Sequences, Amino Acid [MESH]Significance of glycosylation in Notch signaling (epmc).pdf DeepDyve Pubget Overpricing