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10.1038/nchembio.2358 http://scihub22266oqcxt.onion/10.1038/nchembio.2358 C5438047!5438047 !28346405     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28346405 &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 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28346405 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Chem+Biol 2017 ; 13 (6 ): 610-612 Nephropedia Template TP {{tp|p=28346405 |t=2017. Structural and functional insight into human O-GlcNAcase |pdf=|usr=}}{{28346405 }} gab.com Text Structural and functional insight into human O-GlcNAcase JO: Nat Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=28346405 #FOAvip O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value. Twit Text FOAVip Structural and functional insight into human O-GlcNAcase ????Nat Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=28346405 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28346405 #FOAvip English Wikipedia <ref>{{Cite pmid|28346405 }}</ref> Structural and functional insight into human O-GlcNAcase #MMPMID28346405 Roth C ; Chan S ; Offen WA ; Hemsworth GR ; Willems LI ; King DT ; Varghese V ; Britton R ; Vocadlo DJ ; Davies GJ Nat Chem Biol 2017[Jun]; 13 (6 ): 610-612 PMID28346405 show ga O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value. |*Models, Molecular [MESH] |Acetylglucosamine/metabolism [MESH] |Binding Sites [MESH] |Enzyme Activation/drug effects [MESH] |Enzyme Inhibitors/pharmacology [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Ligands [MESH] |Protein Binding [MESH] |Protein Isoforms/chemistry/genetics [MESH] |Protein Structure, Tertiary [MESH]Structural and functional insight into human O-GlcNAcase (epmc).pdf DeepDyve Pubget Overpricing