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10.1038/nrm.2017.22 http://scihub22266oqcxt.onion/10.1038/nrm.2017.22 C5667541!5667541 !28488703     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28488703 &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 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28488703 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Rev+Mol+Cell+Biol 2017 ; 18 (7 ): 452-465 Nephropedia Template TP {{tp|p=28488703 |t=2017. Protein O-GlcNAcylation: emerging mechanisms and functions |pdf=|usr=}}{{28488703 }} gab.com Text Protein O-GlcNAcylation: emerging mechanisms and functions JO: Nat Rev Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=28488703 #FOAvip O-GlcNAcylation - the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to cytoplasmic, nuclear and mitochondrial proteins - is a post-translational modification that regulates fundamental cellular processes in metazoans. A single pair of enzymes - O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) - controls the dynamic cycling of this protein modification in a nutrient- and stress-responsive manner. Recent years have seen remarkable advances in our understanding of O-GlcNAcylation at levels that range from structural and molecular biology to cell signalling and gene regulation to physiology and disease. New mechanisms and functions of O-GlcNAcylation that are emerging from these recent developments enable us to begin constructing a unified conceptual framework through which the significance of this modification in cellular and organismal physiology can be understood. Twit Text FOAVip Protein O-GlcNAcylation: emerging mechanisms and functions ????Nat Rev Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=28488703 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28488703 #FOAvip English Wikipedia <ref>{{Cite pmid|28488703 }}</ref> Protein O-GlcNAcylation: emerging mechanisms and functions #MMPMID28488703 Yang X ; Qian K Nat Rev Mol Cell Biol 2017[Jul]; 18 (7 ): 452-465 PMID28488703 show ga O-GlcNAcylation - the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to cytoplasmic, nuclear and mitochondrial proteins - is a post-translational modification that regulates fundamental cellular processes in metazoans. A single pair of enzymes - O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) - controls the dynamic cycling of this protein modification in a nutrient- and stress-responsive manner. Recent years have seen remarkable advances in our understanding of O-GlcNAcylation at levels that range from structural and molecular biology to cell signalling and gene regulation to physiology and disease. New mechanisms and functions of O-GlcNAcylation that are emerging from these recent developments enable us to begin constructing a unified conceptual framework through which the significance of this modification in cellular and organismal physiology can be understood. |Acetylglucosamine/metabolism [MESH] |Animals [MESH] |Humans [MESH] |N-Acetylglucosaminyltransferases/metabolism [MESH] |Protein Processing, Post-Translational/genetics/*physiology [MESH] |Proteins/chemistry/*metabolism [MESH]Protein O-GlcNAcylation: emerging mechanisms and functions (epmc).pdf DeepDyve Pubget Overpricing