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10.1038/ncomms14654 http://scihub22266oqcxt.onion/10.1038/ncomms14654 C5355826!5355826!28287082     free     free     free 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       Nat+Commun 2017 ; 8 (ä): ä Nephropedia Template TP {{tp|p=28287082|t=2017. E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses |pdf=|usr=}}{{28287082}} gab.com Text E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28287082 #FOAvip Viruses can escape from host recognition by degradation of RIG-I or interference with the RIG-I signalling to establish persistent infections. However, the mechanisms by which host cells stabilize RIG-I protein for avoiding its degradation are largely unknown. We report here that, upon virus infection, the E3 ubiquitin ligase FBXW7 translocates from the nucleus into the cytoplasm and stabilizes RIG-I. FBXW7 interacts with SHP2 and mediates the degradation and ubiquitination of SHP2, thus disrupting the SHP2/c-Cbl complex, which mediates RIG-I degradation. When infected with VSV or influenza A virus, FBXW7 conditional knockout mice (Lysm+FBXW7f/f) show impaired antiviral immunity. FBXW7-deficient macrophages have decreased RIG-I protein levels and type-I interferon signalling. Furthermore, PBMCs from RSV-infected children have reduced FBXW7 mRNA levels. Our results identify FBXW7 as an important interacting partner for RIG-I. These findings provide insights into the function of FBXW7 in antiviral immunity and its related clinical significance. Twit Text FOAVip E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28287082 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28287082 #FOAvip English Wikipedia <ref>{{Cite pmid|28287082}}</ref> E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses #MMPMID28287082 Song Y; Lai L; Chong Z; He J; Zhang Y; Xue Y; Xie Y; Chen S; Dong P; Chen L; Chen Z; Dai F; Wan X; Xiao P; Cao X; Liu Y; Wang Q Nat Commun 2017[]; 8 (ä): ä PMID28287082show ga Viruses can escape from host recognition by degradation of RIG-I or interference with the RIG-I signalling to establish persistent infections. However, the mechanisms by which host cells stabilize RIG-I protein for avoiding its degradation are largely unknown. We report here that, upon virus infection, the E3 ubiquitin ligase FBXW7 translocates from the nucleus into the cytoplasm and stabilizes RIG-I. FBXW7 interacts with SHP2 and mediates the degradation and ubiquitination of SHP2, thus disrupting the SHP2/c-Cbl complex, which mediates RIG-I degradation. When infected with VSV or influenza A virus, FBXW7 conditional knockout mice (Lysm+FBXW7f/f) show impaired antiviral immunity. FBXW7-deficient macrophages have decreased RIG-I protein levels and type-I interferon signalling. Furthermore, PBMCs from RSV-infected children have reduced FBXW7 mRNA levels. Our results identify FBXW7 as an important interacting partner for RIG-I. These findings provide insights into the function of FBXW7 in antiviral immunity and its related clinical significance. äE3 ligase FBXW7 is critical for RIG-I stabilization during antiviral r(epmc).pdf DeepDyve Pubget Overpricing