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10.1093/nar/gkx1307 http://scihub22266oqcxt.onion/10.1093/nar/gkx1307 C5887321!5887321!29346611     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nucleic+Acids+Res 2018 ; 46 (6): 3169-86 Nephropedia Template TP {{tp|p=29346611|t=2018. Combined roles of ATP and small hairpin RNA in the activation of RIG-I revealed by solution-based analysis |pdf=|usr=}}{{29346611}} gab.com Text Combined roles of ATP and small hairpin RNA in the activation of RIG-I revealed by solution-based analysis JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=29346611 #FOAvip RIG-I (retinoic acid inducible gene-I) is a cytosolic innate immune protein that senses viral dsRNA with a 5?-triphosphate overhang. Upon interaction with dsRNA a de-repression of the RIG-I CARD domains takes place that ultimately leads to the production of type I interferons and pro-inflammatory cytokines. Here we investigate the RIG-I conformational rearrangement upon interaction with an activating 5?-triphosphate-10-base pair dsRNA hairpin loop (10bp) compared with a less active 5?-triphosphate-8-base pair dsRNA hairpin loop (8bp). We use size-exclusion chromatography?coupled small-angle X-ray scattering (SAXS) and limited tryptic digest experiments to show that that upon binding to 10 bp, but not 8 bp, RIG-I becomes extended and shows greater flexibility, reflecting the release of its CARDs. We also examined the effect of different ATP analogues on the conformational changes of RIG-I/dsRNA complexes. Of the analogues tested, the addition of ATP transition state analogue ADP-AlFx further assisted in the complete activation of RIG-I in complex with 10bp and also to some extent RIG-I bound to 8bp. Together these data provide solution-based evidence for the molecular mechanism of innate immune signaling by RIG-I as stimulated by short hairpin RNA and ATP. Twit Text FOAVip Combined roles of ATP and small hairpin RNA in the activation of RIG-I revealed by solution-based analysis ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=29346611 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29346611 #FOAvip English Wikipedia <ref>{{Cite pmid|29346611}}</ref> Combined roles of ATP and small hairpin RNA in the activation of RIG-I revealed by solution-based analysis #MMPMID29346611 Shah N; Beckham SA; Wilce JA; Wilce M Nucleic Acids Res 2018[Apr]; 46 (6): 3169-86 PMID29346611show ga RIG-I (retinoic acid inducible gene-I) is a cytosolic innate immune protein that senses viral dsRNA with a 5?-triphosphate overhang. Upon interaction with dsRNA a de-repression of the RIG-I CARD domains takes place that ultimately leads to the production of type I interferons and pro-inflammatory cytokines. Here we investigate the RIG-I conformational rearrangement upon interaction with an activating 5?-triphosphate-10-base pair dsRNA hairpin loop (10bp) compared with a less active 5?-triphosphate-8-base pair dsRNA hairpin loop (8bp). We use size-exclusion chromatography?coupled small-angle X-ray scattering (SAXS) and limited tryptic digest experiments to show that that upon binding to 10 bp, but not 8 bp, RIG-I becomes extended and shows greater flexibility, reflecting the release of its CARDs. We also examined the effect of different ATP analogues on the conformational changes of RIG-I/dsRNA complexes. Of the analogues tested, the addition of ATP transition state analogue ADP-AlFx further assisted in the complete activation of RIG-I in complex with 10bp and also to some extent RIG-I bound to 8bp. Together these data provide solution-based evidence for the molecular mechanism of innate immune signaling by RIG-I as stimulated by short hairpin RNA and ATP. äCombined roles of ATP and small hairpin RNA in the activation of RIG-I(epmc).pdf DeepDyve Pubget Overpricing