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10.1007/s00018-016-2191-4

http://scihub22266oqcxt.onion/10.1007/s00018-016-2191-4
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C4887548!4887548!27066894
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suck abstract from ncbi

pmid27066894      Cell+Mol+Life+Sci 2016 ; 73 (ä): 2165-76
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  • Poly-ubiquitination in TNFR1-mediated necroptosis #MMPMID27066894
  • Dondelinger Y; Darding M; Bertrand MJM; Walczak H
  • Cell Mol Life Sci 2016[]; 73 (ä): 2165-76 PMID27066894show 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.
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