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10.1007/s00018-016-2191-4 http://scihub22266oqcxt.onion/10.1007/s00018-016-2191-4 C4887548!4887548 !27066894     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27066894 &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\27066894 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Mol+Life+Sci 2016 ; 73 (11-12 ): 2165-76 Nephropedia Template TP {{tp|p=27066894 |t=2016. Poly-ubiquitination in TNFR1-mediated necroptosis |pdf=|usr=}}{{27066894 }} gab.com Text Poly-ubiquitination in TNFR1-mediated necroptosis JO: Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=27066894 #FOAvip Tumor necrosis factor (TNF) is a master pro-inflammatory cytokine, and inappropriate TNF signaling is implicated in the pathology of many inflammatory diseases. Ligation of TNF to its receptor TNFR1 induces the transient formation of a primary membrane-bound signaling complex, known as complex I, that drives expression of pro-survival genes. Defective complex I activation results in induction of cell death, in the form of apoptosis or necroptosis. This switch occurs via internalization of complex I components and assembly and activation of secondary cytoplasmic death complexes, respectively known as complex II and necrosome. In this review, we discuss the crucial regulatory functions of ubiquitination-a post-translational protein modification consisting of the covalent attachment of ubiquitin, and multiples thereof, to target proteins-to the various steps of TNFR1 signaling leading to necroptosis. Twit Text FOAVip Poly-ubiquitination in TNFR1-mediated necroptosis ????Cell Mol Life Sci http://www.kidney.de/pget.php?&tw=1&pmid=27066894 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27066894 #FOAvip English Wikipedia <ref>{{Cite pmid|27066894 }}</ref> Poly-ubiquitination in TNFR1-mediated necroptosis #MMPMID27066894 Dondelinger Y ; Darding M ; Bertrand MJ ; Walczak H Cell Mol Life Sci 2016[Jun]; 73 (11-12 ): 2165-76 PMID27066894 show ga Tumor necrosis factor (TNF) is a master pro-inflammatory cytokine, and inappropriate TNF signaling is implicated in the pathology of many inflammatory diseases. Ligation of TNF to its receptor TNFR1 induces the transient formation of a primary membrane-bound signaling complex, known as complex I, that drives expression of pro-survival genes. Defective complex I activation results in induction of cell death, in the form of apoptosis or necroptosis. This switch occurs via internalization of complex I components and assembly and activation of secondary cytoplasmic death complexes, respectively known as complex II and necrosome. In this review, we discuss the crucial regulatory functions of ubiquitination-a post-translational protein modification consisting of the covalent attachment of ubiquitin, and multiples thereof, to target proteins-to the various steps of TNFR1 signaling leading to necroptosis. |Animals [MESH] |Apoptosis/*physiology [MESH] |Mice [MESH] |Necrosis/*pathology [MESH] |Receptor-Interacting Protein Serine-Threonine Kinases/metabolism [MESH] |Receptors, Tumor Necrosis Factor, Type I/*metabolism [MESH] |Signal Transduction [MESH] |Tumor Necrosis Factor-alpha/*metabolism [MESH]Poly-ubiquitination in TNFR1-mediated necroptosis (epmc).pdf DeepDyve Pubget Overpricing