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10.1038/cdd.2017.26 http://scihub22266oqcxt.onion/10.1038/cdd.2017.26 C5520165!5520165 !28282038     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28282038 &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\28282038 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Death+Differ 2017 ; 24 (7 ): 1142-1147 Nephropedia Template TP {{tp|p=28282038 |t=2017. SPATA2: more than a missing link |pdf=|usr=}}{{28282038 }} gab.com Text SPATA2: more than a missing link JO: Cell Death Differ http://www.kidney.de/pget.php?&tw=1&pmid=28282038 #FOAvip The assembly of the TNFR1 signalling complex (TNF-RSC) depends on K63- and M1-linked ubiquitylation, promoting the recruitment of complex constituents and the stability of the complex. Ubiquitylation is a dynamic process, controlled by E3 ubiquitin ligases as well as deubiquitinases, such as CYLD and OTULIN. A novel molecule, SPATA2, which is crucial for recruiting and activating the deubiquitinase CYLD within the TNF-RSC, has now been identified by four different studies. Loss of SPATA2 was shown to result in increased TNF-, but also NOD2-mediated proinflammatory signalling. Importantly, SPATA2 is instrumental for TNF-induced cell death, and a closer look at these findings suggests that SPATA2 possibly has functions beyond promoting the activity of CYLD. Twit Text FOAVip SPATA2: more than a missing link ????Cell Death Differ http://www.kidney.de/pget.php?&tw=1&pmid=28282038 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28282038 #FOAvip English Wikipedia <ref>{{Cite pmid|28282038 }}</ref> SPATA2: more than a missing link #MMPMID28282038 Schlicher L ; Brauns-Schubert P ; Schubert F ; Maurer U Cell Death Differ 2017[Jul]; 24 (7 ): 1142-1147 PMID28282038 show ga The assembly of the TNFR1 signalling complex (TNF-RSC) depends on K63- and M1-linked ubiquitylation, promoting the recruitment of complex constituents and the stability of the complex. Ubiquitylation is a dynamic process, controlled by E3 ubiquitin ligases as well as deubiquitinases, such as CYLD and OTULIN. A novel molecule, SPATA2, which is crucial for recruiting and activating the deubiquitinase CYLD within the TNF-RSC, has now been identified by four different studies. Loss of SPATA2 was shown to result in increased TNF-, but also NOD2-mediated proinflammatory signalling. Importantly, SPATA2 is instrumental for TNF-induced cell death, and a closer look at these findings suggests that SPATA2 possibly has functions beyond promoting the activity of CYLD. |Animals [MESH] |Humans [MESH] |Models, Biological [MESH] |Protein Binding [MESH] |Proteins/*metabolism [MESH] |Receptors, Tumor Necrosis Factor, Type I/metabolism [MESH] |Signal Transduction [MESH]SPATA2: more than a missing link (epmc).pdf DeepDyve Pubget Overpricing