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10.15698/mic2017.11.600 http://scihub22266oqcxt.onion/10.15698/mic2017.11.600 C5695857!5695857!29167802     free     free     free 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       Microb+Cell ä ; 4 (11): 387-9 Nephropedia Template TP {{tp|p=29167802|t=ä. Shutdown of interferon signaling by a viral-hijacked E3 ubiquitin ligase |pdf=|usr=}}{{29167802}} gab.com Text Shutdown of interferon signaling by a viral-hijacked E3 ubiquitin ligase JO: Microb Cell http://www.kidney.de/pget.php?&tw=1&pmid=29167802 #FOAvip Viruses manipulate cellular processes to create an environment favorable to replication. For most viruses, this includes subverting the expression of interferon (IFN), a signaling molecule that can stimulate production of a vast array of antiviral gene products. Rotavirus, a segmented double-stranded RNA virus that causes acute gastroenteritis in infants and young children, inhibits IFN expression through its nonstructural protein NSP1. This viral protein stifles IFN expression by inducing the degradation of host factors that are necessary for upregulating the activity of IFN genes. In the case of nearly all human and porcine rotavirus strains, NSP1 induces the ubiquitination-dependent proteasomal degradation of ?-transducin repeat containing protein (?-TrCP), a host factor that plays an essential role in activating the IFN-transcription factor, NF-?B. Key to the process is the presence of a decoy sequence (degron) at the C-terminus of NSP1 that causes ?-TrCP to mistakenly bind NSP1 instead of its natural target, inhibitor-of-?B (I?B). In a recent report published by Davis et al [2017; mBio 8(4): e01213-17], we describe molecular requirements that govern NSP1 recognition of ?-TrCP, including an essential degron phosphorylation event, and the step-wise incorporation of NSP1 into hijacked cullin-RING E3 ligases (CRLs) that ubiquitinate and tag ?-TrCP for degradation. Notably, although ?-TrCP is chiefly recognized for its role as a master regulator of NF-?B signaling and IFN expression, ?-TrCP also controls the stability of checkpoint proteins implicated in numerous other cellular pathways with antiviral activities, including autophagy and apoptosis. Thus, the impact of NSP1 on creating an intracellular environment favorable to virus replication may extend well beyond the IFN signaling pathway. Twit Text FOAVip Shutdown of interferon signaling by a viral-hijacked E3 ubiquitin ligase ????Microb Cell http://www.kidney.de/pget.php?&tw=1&pmid=29167802 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29167802 #FOAvip English Wikipedia <ref>{{Cite pmid|29167802}}</ref> Shutdown of interferon signaling by a viral-hijacked E3 ubiquitin ligase #MMPMID29167802 Davis KA; Patton JT Microb Cell ä[]; 4 (11): 387-9 PMID29167802show ga Viruses manipulate cellular processes to create an environment favorable to replication. For most viruses, this includes subverting the expression of interferon (IFN), a signaling molecule that can stimulate production of a vast array of antiviral gene products. Rotavirus, a segmented double-stranded RNA virus that causes acute gastroenteritis in infants and young children, inhibits IFN expression through its nonstructural protein NSP1. This viral protein stifles IFN expression by inducing the degradation of host factors that are necessary for upregulating the activity of IFN genes. In the case of nearly all human and porcine rotavirus strains, NSP1 induces the ubiquitination-dependent proteasomal degradation of ?-transducin repeat containing protein (?-TrCP), a host factor that plays an essential role in activating the IFN-transcription factor, NF-?B. Key to the process is the presence of a decoy sequence (degron) at the C-terminus of NSP1 that causes ?-TrCP to mistakenly bind NSP1 instead of its natural target, inhibitor-of-?B (I?B). In a recent report published by Davis et al [2017; mBio 8(4): e01213-17], we describe molecular requirements that govern NSP1 recognition of ?-TrCP, including an essential degron phosphorylation event, and the step-wise incorporation of NSP1 into hijacked cullin-RING E3 ligases (CRLs) that ubiquitinate and tag ?-TrCP for degradation. Notably, although ?-TrCP is chiefly recognized for its role as a master regulator of NF-?B signaling and IFN expression, ?-TrCP also controls the stability of checkpoint proteins implicated in numerous other cellular pathways with antiviral activities, including autophagy and apoptosis. Thus, the impact of NSP1 on creating an intracellular environment favorable to virus replication may extend well beyond the IFN signaling pathway. äShutdown of interferon signaling by a viral-hijacked E3 ubiquitin liga(epmc).pdf DeepDyve Pubget Overpricing