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10.1074/jbc.H117.800102 http://scihub22266oqcxt.onion/10.1074/jbc.H117.800102 C5612126!5612126 !28939751     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28939751 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28939751 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2017 ; 292 (38 ): 15974-15975 Nephropedia Template TP {{tp|p=28939751 |t=2017. A sweet development in Notch regulation |pdf=|usr=}}{{28939751 }} gab.com Text A sweet development in Notch regulation JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28939751 #FOAvip The transmembrane signaling protein Notch, which is crucial for embryonic cell fate decisions, has 36 extracellular EGF domains that are glycosylated in variable and complex ways. A new study shows that O-fucose and O-glucose stabilize the repeats but that extension of glucose by xylose weakens stability, explained by the binding of the glycan to a protein groove. This work shows how different types of glycosylation can distinctly influence protein stability and structure. Twit Text FOAVip A sweet development in Notch regulation ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=28939751 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28939751 #FOAvip English Wikipedia <ref>{{Cite pmid|28939751 }}</ref> A sweet development in Notch regulation #MMPMID28939751 Bakker H ; Gerardy-Schahn R J Biol Chem 2017[Sep]; 292 (38 ): 15974-15975 PMID28939751 show ga The transmembrane signaling protein Notch, which is crucial for embryonic cell fate decisions, has 36 extracellular EGF domains that are glycosylated in variable and complex ways. A new study shows that O-fucose and O-glucose stabilize the repeats but that extension of glucose by xylose weakens stability, explained by the binding of the glycan to a protein groove. This work shows how different types of glycosylation can distinctly influence protein stability and structure. |Glycosylation [MESH] |Models, Molecular [MESH] |Protein Conformation [MESH] |Protein Stability [MESH] |Receptors, Notch/*chemistry/*metabolism [MESH] |Repetitive Sequences, Amino Acid [MESH]A sweet development in Notch regulation (epmc).pdf DeepDyve Pubget Overpricing