Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1096/fj.14-258533 http://scihub22266oqcxt.onion/10.1096/fj.14-258533 C4415009!4415009!25667218     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 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 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 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       FASEB+J 2015 ; 29 (5): 1869-78 Nephropedia Template TP {{tp|p=25667218|t=2015. A20 suppresses vascular inflammation by recruiting proinflammatory signaling molecules to intracellular aggresomes |pdf=|usr=}}{{25667218}} gab.com Text A20 suppresses vascular inflammation by recruiting proinflammatory signaling molecules to intracellular aggresomes JO: FASEB J http://www.kidney.de/pget.php?&tw=1&pmid=25667218 #FOAvip A20 protects against pathologic vascular remodeling by inhibiting the inflammatory transcription factor NF-?B. A20?s function has been attributed to ubiquitin editing of receptor-interacting protein 1 (RIP1) to influence activity/stability. The validity of this mechanism was tested using a murine model of transplant vasculopathy and human cells. Mouse C57BL/6 aortae transduced with adenoviruses containing A20 (or ?-galactosidase as a control) were allografted into major histocompatibility complex-mismatched BALB/c mice. Primary endothelial cells, smooth muscle cells, or transformed epithelial cells (all human) were transfected with wild-type A20 or with catalytically inactive mutants as a control. NF-?B activity and intracellular localization of RIP1 was monitored by reporter gene assay, immunofluorescent staining, and Western blotting. Native and catalytically inactive versions of A20 had similar inhibitory effects on NF-?B activity (?70% vs. ?76%; P > 0.05). A20 promoted localization of RIP1 to insoluble aggresomes in murine vascular allografts and in human cells (53% vs. 0%) without altering RIP1 expression, and this process was increased by the assembly of polyubiquitin chains (87% vs. 28%; P < 0.05). A20 captures polyubiquitinated signaling intermediaries in insoluble aggresomes, thus reducing their bioavailability for downstream NF-?B signaling. This novel mechanism contributes to protection from vasculopathy in transplanted organs treated with exogenous A20.?Enesa, K., Moll, H. P., Luong, L., Ferran, C., Evans, P. C. A20 suppresses vascular inflammation by recruiting proinflammatory signaling molecules to intracellular aggresomes. Twit Text FOAVip A20 suppresses vascular inflammation by recruiting proinflammatory signaling molecules to intracellular aggresomes ????FASEB J http://www.kidney.de/pget.php?&tw=1&pmid=25667218 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25667218 #FOAvip English Wikipedia <ref>{{Cite pmid|25667218}}</ref> A20 suppresses vascular inflammation by recruiting proinflammatory signaling molecules to intracellular aggresomes #MMPMID25667218 Enesa K; Moll HP; Luong L; Ferran C; Evans PC FASEB J 2015[May]; 29 (5): 1869-78 PMID25667218show ga A20 protects against pathologic vascular remodeling by inhibiting the inflammatory transcription factor NF-?B. A20?s function has been attributed to ubiquitin editing of receptor-interacting protein 1 (RIP1) to influence activity/stability. The validity of this mechanism was tested using a murine model of transplant vasculopathy and human cells. Mouse C57BL/6 aortae transduced with adenoviruses containing A20 (or ?-galactosidase as a control) were allografted into major histocompatibility complex-mismatched BALB/c mice. Primary endothelial cells, smooth muscle cells, or transformed epithelial cells (all human) were transfected with wild-type A20 or with catalytically inactive mutants as a control. NF-?B activity and intracellular localization of RIP1 was monitored by reporter gene assay, immunofluorescent staining, and Western blotting. Native and catalytically inactive versions of A20 had similar inhibitory effects on NF-?B activity (?70% vs. ?76%; P > 0.05). A20 promoted localization of RIP1 to insoluble aggresomes in murine vascular allografts and in human cells (53% vs. 0%) without altering RIP1 expression, and this process was increased by the assembly of polyubiquitin chains (87% vs. 28%; P < 0.05). A20 captures polyubiquitinated signaling intermediaries in insoluble aggresomes, thus reducing their bioavailability for downstream NF-?B signaling. This novel mechanism contributes to protection from vasculopathy in transplanted organs treated with exogenous A20.?Enesa, K., Moll, H. P., Luong, L., Ferran, C., Evans, P. C. A20 suppresses vascular inflammation by recruiting proinflammatory signaling molecules to intracellular aggresomes. äA20 suppresses vascular inflammation by recruiting proinflammatory sig(epmc).pdf DeepDyve Pubget Overpricing