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10.1084/jem.20132234 http://scihub22266oqcxt.onion/10.1084/jem.20132234 C4886354!4886354 !27139490     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27139490 &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 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27139490 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Exp+Med 2016 ; 213 (6 ): 877-85 Nephropedia Template TP {{tp|p=27139490 |t=2016. NLRP3 recruitment by NLRC4 during Salmonella infection |pdf=|usr=}}{{27139490 }} gab.com Text NLRP3 recruitment by NLRC4 during Salmonella infection JO: J Exp Med http://www.kidney.de/pget.php?&tw=1&pmid=27139490 #FOAvip NLRC4 and NLRP3, of the NOD-like receptor (NLR) family of intracellular proteins, are expressed in innate immune cells and are thought to nucleate distinct inflammasome complexes that promote caspase-1 activation, secretion of the proinflammatory cytokines IL-1? and IL-18, and a form of cell death termed pyroptosis. We show that NLRP3 associates with NLRC4 in macrophages infected with Salmonella typhimurium or transfected with flagellin. The significance of the interaction between the NLRC4 NACHT domain and NLRP3 was revealed when Nlrc4(S533A/S533A) bone marrow-derived macrophages (BMDMs) expressing phosphorylation site mutant NLRC4 S533A had only a mild defect in caspase-1 activation when compared with NLRC4-deficient BMDMs. NLRC4 S533A activated caspase-1 by recruiting NLRP3 and its adaptor protein ASC. Thus, Nlrc4(S533A/S533A) Nlrp3(-/-) BMDMs more closely resembled Nlrc4(-/-) BMDMs in their response to S. typhimurium or flagellin. The interplay between NLRP3 and NLRC4 reveals an unexpected overlap between what had been considered distinct inflammasome scaffolds. Twit Text FOAVip NLRP3 recruitment by NLRC4 during Salmonella infection ????J Exp Med http://www.kidney.de/pget.php?&tw=1&pmid=27139490 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27139490 #FOAvip English Wikipedia <ref>{{Cite pmid|27139490 }}</ref> NLRP3 recruitment by NLRC4 during Salmonella infection #MMPMID27139490 Qu Y ; Misaghi S ; Newton K ; Maltzman A ; Izrael-Tomasevic A ; Arnott D ; Dixit VM J Exp Med 2016[May]; 213 (6 ): 877-85 PMID27139490 show ga NLRC4 and NLRP3, of the NOD-like receptor (NLR) family of intracellular proteins, are expressed in innate immune cells and are thought to nucleate distinct inflammasome complexes that promote caspase-1 activation, secretion of the proinflammatory cytokines IL-1? and IL-18, and a form of cell death termed pyroptosis. We show that NLRP3 associates with NLRC4 in macrophages infected with Salmonella typhimurium or transfected with flagellin. The significance of the interaction between the NLRC4 NACHT domain and NLRP3 was revealed when Nlrc4(S533A/S533A) bone marrow-derived macrophages (BMDMs) expressing phosphorylation site mutant NLRC4 S533A had only a mild defect in caspase-1 activation when compared with NLRC4-deficient BMDMs. NLRC4 S533A activated caspase-1 by recruiting NLRP3 and its adaptor protein ASC. Thus, Nlrc4(S533A/S533A) Nlrp3(-/-) BMDMs more closely resembled Nlrc4(-/-) BMDMs in their response to S. typhimurium or flagellin. The interplay between NLRP3 and NLRC4 reveals an unexpected overlap between what had been considered distinct inflammasome scaffolds. |Amino Acid Substitution [MESH] |Animals [MESH] |Apoptosis Regulatory Proteins/genetics/*immunology [MESH] |Bone Marrow Cells/*metabolism/microbiology [MESH] |Calcium-Binding Proteins/genetics/*immunology [MESH] |Flagellin/genetics/immunology [MESH] |Macrophages/*immunology/microbiology [MESH] |Mice [MESH] |Mice, Knockout [MESH] |Mutation, Missense [MESH] |NLR Family, Pyrin Domain-Containing 3 Protein/genetics/*immunology [MESH] |Protein Domains [MESH] |Salmonella Infections/genetics/*immunology [MESH]NLRP3 recruitment by NLRC4 during Salmonella infection (epmc).pdf DeepDyve Pubget Overpricing