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10.1111/cmi.12406 http://scihub22266oqcxt.onion/10.1111/cmi.12406 C4915744!4915744!25486861     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Microbiol 2015 ; 17 (6): 843-59 Nephropedia Template TP {{tp|p=25486861|t=2015. PERP, a host tetraspanning membrane protein, is required for Salmonella?induced inflammation |pdf=|usr=}}{{25486861}} gab.com Text PERP, a host tetraspanning membrane protein, is required for Salmonella induced inflammation JO: Cell Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=25486861 #FOAvip Salmonella enterica? Typhimurium induces intestinal inflammation through the activity of type III secreted effector (T3SE) proteins. Our prior results indicate that the secretion of the T3SE SipA and the ability of SipA to induce epithelial cell responses that lead to induction of polymorphonuclear transepithelial migration are not coupled to its direct delivery into epithelial cells from Salmonella. We therefore tested the hypothesis that SipA interacts with a membrane protein located at the apical surface of intestinal epithelial cells. Employing a split ubiquitin yeast?two?hybrid screen, we identified the tetraspanning membrane protein, p53 effector related to PMP?22 (PERP), as a SipA binding partner. SipA and PERP appear to have intersecting activities as we found PERP to be involved in proinflammatory pathways shown to be regulated by SipA. In sum, our studies reveal a critical role for PERP in the pathogenesis of S. Typhimurium, and for the first time demonstrate that SipA, a T3SE protein, can engage a host protein at the epithelial surface. Twit Text FOAVip PERP, a host tetraspanning membrane protein, is required for Salmonella induced inflammation ????Cell Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=25486861 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25486861 #FOAvip English Wikipedia <ref>{{Cite pmid|25486861}}</ref> PERP, a host tetraspanning membrane protein, is required for Salmonella?induced inflammation #MMPMID25486861 Hallstrom KN; Srikanth CV; Agbor TA; Dumont CM; Peters KN; Paraoan L; Casanova JE; Boll EJ; McCormick BA Cell Microbiol 2015[Jun]; 17 (6): 843-59 PMID25486861show ga Salmonella enterica? Typhimurium induces intestinal inflammation through the activity of type III secreted effector (T3SE) proteins. Our prior results indicate that the secretion of the T3SE SipA and the ability of SipA to induce epithelial cell responses that lead to induction of polymorphonuclear transepithelial migration are not coupled to its direct delivery into epithelial cells from Salmonella. We therefore tested the hypothesis that SipA interacts with a membrane protein located at the apical surface of intestinal epithelial cells. Employing a split ubiquitin yeast?two?hybrid screen, we identified the tetraspanning membrane protein, p53 effector related to PMP?22 (PERP), as a SipA binding partner. SipA and PERP appear to have intersecting activities as we found PERP to be involved in proinflammatory pathways shown to be regulated by SipA. In sum, our studies reveal a critical role for PERP in the pathogenesis of S. Typhimurium, and for the first time demonstrate that SipA, a T3SE protein, can engage a host protein at the epithelial surface. äPERP, a host tetraspanning membrane protein, is required for Salmonell(epmc).pdf DeepDyve Pubget Overpricing