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10.1128/MCB.00775-14 http://scihub22266oqcxt.onion/10.1128/MCB.00775-14 C4285429!4285429 !25452302     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25452302 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Cell+Biol 2015 ; 35 (3 ): 582-97 Nephropedia Template TP {{tp|p=25452302 |t=2015. Nedd8 regulates inflammasome-dependent caspase-1 activation |pdf=|usr=}}{{25452302 }} gab.com Text Nedd8 regulates inflammasome-dependent caspase-1 activation JO: Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=25452302 #FOAvip Caspase-1 is activated by the inflammasome complex to process cytokines like interleukin-1? (IL-1?). Pro-caspase-1 consists of three domains, CARD, p20, and p10. Association of pro-caspase-1 with the inflammasome results in initiation of its autocatalytic activity, culminating in self-cleavage that generates catalytically active subunits (p10 and p20). In the current study, we show that Nedd8 is required for efficient self-cleavage of pro-caspase-1 to generate its catalytically active subunits. Nedd8 silencing or treating cells with the neddylation inhibitor MLN4924 led to diminished caspase-1 processing and reduced IL-1? maturation following inflammasome activation. Coimmunoprecipitation and mass spectrometric analysis of 293 cells overexpressing pro-caspase-1 (and CARD) and Nedd8 suggested possible neddylation of caspase-1 CARD. Following inflammasome activation in primary macrophages, we observed colocalization of endogenous Nedd8 with caspase-1. Similarly, interaction of endogenous Nedd8 with caspase-1 CARD was detected in inflammasome-activated macrophages. Furthermore, enhanced autocatalytic activity of pro-caspase-1 was observed following Nedd8 overexpression in 293 cells, and such activity in inflammasome-activated macrophages was drastically diminished upon treatment of cells with MLN4924. Thus, our studies demonstrate a role of Nedd8 in regulating caspase-1 activation following inflammasome activation, presumably via augmenting autoprocessing/cleavage of pro-caspase-1 into its corresponding catalytically active subunits. Twit Text FOAVip Nedd8 regulates inflammasome-dependent caspase-1 activation ????Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=25452302 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25452302 #FOAvip English Wikipedia <ref>{{Cite pmid|25452302 }}</ref> Nedd8 regulates inflammasome-dependent caspase-1 activation #MMPMID25452302 Segovia JA ; Tsai SY ; Chang TH ; Shil NK ; Weintraub ST ; Short JD ; Bose S Mol Cell Biol 2015[Feb]; 35 (3 ): 582-97 PMID25452302 show ga Caspase-1 is activated by the inflammasome complex to process cytokines like interleukin-1? (IL-1?). Pro-caspase-1 consists of three domains, CARD, p20, and p10. Association of pro-caspase-1 with the inflammasome results in initiation of its autocatalytic activity, culminating in self-cleavage that generates catalytically active subunits (p10 and p20). In the current study, we show that Nedd8 is required for efficient self-cleavage of pro-caspase-1 to generate its catalytically active subunits. Nedd8 silencing or treating cells with the neddylation inhibitor MLN4924 led to diminished caspase-1 processing and reduced IL-1? maturation following inflammasome activation. Coimmunoprecipitation and mass spectrometric analysis of 293 cells overexpressing pro-caspase-1 (and CARD) and Nedd8 suggested possible neddylation of caspase-1 CARD. Following inflammasome activation in primary macrophages, we observed colocalization of endogenous Nedd8 with caspase-1. Similarly, interaction of endogenous Nedd8 with caspase-1 CARD was detected in inflammasome-activated macrophages. Furthermore, enhanced autocatalytic activity of pro-caspase-1 was observed following Nedd8 overexpression in 293 cells, and such activity in inflammasome-activated macrophages was drastically diminished upon treatment of cells with MLN4924. Thus, our studies demonstrate a role of Nedd8 in regulating caspase-1 activation following inflammasome activation, presumably via augmenting autoprocessing/cleavage of pro-caspase-1 into its corresponding catalytically active subunits. |Animals [MESH] |Carrier Proteins [MESH] |Caspase 1/*metabolism [MESH] |Enzyme Activation [MESH] |Humans [MESH] |Inflammasomes/*metabolism [MESH] |Influenza A virus/*isolation & purification [MESH] |Interleukin-1beta/biosynthesis [MESH] |Macrophages/metabolism/virology [MESH] |Mice, Inbred C57BL [MESH] |NEDD8 Protein [MESH]Nedd8 regulates inflammasome-dependent caspase-1 activation (epmc).pdf DeepDyve Pubget Overpricing