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10.1007/s13238-010-0030-1 http://scihub22266oqcxt.onion/10.1007/s13238-010-0030-1 C4875083!4875083!21203974     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=21203974&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 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Protein+Cell 2010 ; 1 (3): 275-83 Nephropedia Template TP {{tp|p=21203974|t=2010. SUMOylation of RIG-I positively regulates the type I interferon signaling |pdf=|usr=}}{{21203974}} gab.com Text SUMOylation of RIG-I positively regulates the type I interferon signaling JO: Protein Cell http://www.kidney.de/pget.php?&tw=1&pmid=21203974 #FOAvip Retinoic acid-inducible gene-I (RIG-I) functions as an intracellular pattern recognition receptor (PRR) that recognizes the 5?-triphosphate moiety of single-stranded RNA viruses to initiate the innate immune response. Previous studies have shown that Lys63-linked ubiquitylation is required for RIG-I activation and the downstream anti-viral type I interferon (IFN-I) induction. Herein we reported that, RIG-I was also modified by small ubiquitin-like modifier-1 (SUMO-1). Functional analysis showed that RIG-I SUMOylation enhanced IFN-I production through increased ubiquitylation and the interaction with its downstream adaptor molecule Cardif. Our results therefore suggested that SUMOylation might serve as an additional regulatory tier for RIG-I activation and IFN-I signaling.Electronic Supplementary Material: Supplementary material is available for this article at 10.1007/s13238-010-0030-1 and is accessible for authorized users. Twit Text FOAVip SUMOylation of RIG-I positively regulates the type I interferon signaling ????Protein Cell http://www.kidney.de/pget.php?&tw=1&pmid=21203974 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21203974 #FOAvip English Wikipedia <ref>{{Cite pmid|21203974}}</ref> SUMOylation of RIG-I positively regulates the type I interferon signaling #MMPMID21203974 Mi Z; Fu J; Xiong Y; Tang H Protein Cell 2010[Mar]; 1 (3): 275-83 PMID21203974show ga Retinoic acid-inducible gene-I (RIG-I) functions as an intracellular pattern recognition receptor (PRR) that recognizes the 5?-triphosphate moiety of single-stranded RNA viruses to initiate the innate immune response. Previous studies have shown that Lys63-linked ubiquitylation is required for RIG-I activation and the downstream anti-viral type I interferon (IFN-I) induction. Herein we reported that, RIG-I was also modified by small ubiquitin-like modifier-1 (SUMO-1). Functional analysis showed that RIG-I SUMOylation enhanced IFN-I production through increased ubiquitylation and the interaction with its downstream adaptor molecule Cardif. Our results therefore suggested that SUMOylation might serve as an additional regulatory tier for RIG-I activation and IFN-I signaling.Electronic Supplementary Material: Supplementary material is available for this article at 10.1007/s13238-010-0030-1 and is accessible for authorized users. äSUMOylation of RIG-I positively regulates the type I interferon signal(epmc).pdf DeepDyve Pubget Overpricing