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Year Number of Results
2006 3
2007 6
2008 2
2009 4
2010 2
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2012 5
2013 8
2014 7
2015 5
2016 5
2017 5
2018 3
2019 3
2022 0
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56 results
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Page 1
The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus.
Zhao Y, Yang J, Shi J, Gong YN, Lu Q, Xu H, Liu L, Shao F. Zhao Y, et al. Nature. 2011 Sep 14;477(7366):596-600. doi: 10.1038/nature10510. Nature. 2011. PMID: 21918512
NAIP5 directly and specifically interacted with flagellin, which determined the inflammasome-stimulation activities of different bacterial flagellins. NAIP5 engagement by flagellin promoted a physical NAIP5-NLRC4 association, rendering fu
NAIP5 directly and specifically interacted with flagellin, which determined the inflammasome-stimulation activities of differe
Formation and structure of a NAIP5-NLRC4 inflammasome induced by direct interactions with conserved N- and C-terminal regions of flagellin.
Halff EF, Diebolder CA, Versteeg M, Schouten A, Brondijk TH, Huizinga EG. Halff EF, et al. J Biol Chem. 2012 Nov 9;287(46):38460-72. doi: 10.1074/jbc.M112.393512. Epub 2012 Sep 25. J Biol Chem. 2012. PMID: 23012363 Free PMC article.
The NOD-like receptors NAIP5 and NLRC4 play an essential role in the innate immune response to the bacterial tail protein flagellin. Upon flagellin detection, NAIP5 and NLRC4 form a hetero-oligomeric inflammasome that induces caspase-1-dependent cell d …
The NOD-like receptors NAIP5 and NLRC4 play an essential role in the innate immune response to the bacterial tail protein flagelli
Flagellin-induced NLRC4 phosphorylation primes the inflammasome for activation by NAIP5.
Matusiak M, Van Opdenbosch N, Vande Walle L, Sirard JC, Kanneganti TD, Lamkanfi M. Matusiak M, et al. Proc Natl Acad Sci U S A. 2015 Feb 3;112(5):1541-6. doi: 10.1073/pnas.1417945112. Epub 2015 Jan 20. Proc Natl Acad Sci U S A. 2015. PMID: 25605939 Free PMC article.
Here, we showed that Nlrc4 phosphorylation occurs independently of Naip5 detection of flagellin because Naip5 deletion in macrophages abolished caspase-1 activation, interleukin (IL)-1beta secretion, and pyroptosis, but not Nlrc4 phosphorylation by cytosolic …
Here, we showed that Nlrc4 phosphorylation occurs independently of Naip5 detection of flagellin because Naip5 deletion …
Structural basis for specific flagellin recognition by the NLR protein NAIP5.
Yang X, Yang F, Wang W, Lin G, Hu Z, Han Z, Qi Y, Zhang L, Wang J, Sui SF, Chai J. Yang X, et al. Cell Res. 2018 Jan;28(1):35-47. doi: 10.1038/cr.2017.148. Epub 2017 Nov 28. Cell Res. 2018. PMID: 29182158 Free PMC article.
Binding to NAIP5 results in a nearly complete burial of the flagellin derivative, thus stabilizing the active conformation of NAIP5. The extreme C-terminal side of the flagellin is anchored to a sterically constrained binding pocket of NAIP5, wh …
Binding to NAIP5 results in a nearly complete burial of the flagellin derivative, thus stabilizing the active conformation of …
Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity.
Ren T, Zamboni DS, Roy CR, Dietrich WF, Vance RE. Ren T, et al. PLoS Pathog. 2006 Mar;2(3):e18. doi: 10.1371/journal.ppat.0020018. Epub 2006 Mar 17. PLoS Pathog. 2006. PMID: 16552444 Free PMC article.
All mutants were deficient in expression of flagellin, the primary flagellar subunit, and failed to induce caspase-1-mediated macrophage death. ...Thus, flagellin itself, not flagella or motility, is required to initiate macrophage innate immunity. ...
All mutants were deficient in expression of flagellin, the primary flagellar subunit, and failed to induce caspase-1-mediated macroph …
The structural basis of flagellin detection by NAIP5: A strategy to limit pathogen immune evasion.
Tenthorey JL, Haloupek N, López-Blanco JR, Grob P, Adamson E, Hartenian E, Lind NA, Bourgeois NM, Chacón P, Nogales E, Vance RE. Tenthorey JL, et al. Science. 2017 Nov 17;358(6365):888-893. doi: 10.1126/science.aao1140. Science. 2017. PMID: 29146805 Free PMC article.
Here we report the cryo-electron microscopy structure of the assembled ~1.4-megadalton flagellin-NAIP5-NLRC4 inflammasome, revealing how a ligand activates an NLR. Six distinct NAIP5 domains contact multiple conserved regions of flagellin, prying NA
Here we report the cryo-electron microscopy structure of the assembled ~1.4-megadalton flagellin-NAIP5-NLRC4 inflammasome, rev …
Flagellin induces antibody responses through a TLR5- and inflammasome-independent pathway.
López-Yglesias AH, Zhao X, Quarles EK, Lai MA, VandenBos T, Strong RK, Smith KD. López-Yglesias AH, et al. J Immunol. 2014 Feb 15;192(4):1587-96. doi: 10.4049/jimmunol.1301893. Epub 2014 Jan 17. J Immunol. 2014. PMID: 24442437 Free PMC article.
Flagellin is a potent immunogen that activates the innate immune system via TLR5 and Naip5/6, and generates strong T and B cell responses. The adaptor protein MyD88 is critical for signaling by TLR5, as well as IL-1Rs and IL-18Rs, major downstream mediators of the
Flagellin is a potent immunogen that activates the innate immune system via TLR5 and Naip5/6, and generates strong T and B cel
Carboxyl-terminal fusion of E7 into Flagellin shifts TLR5 activation to NLRC4/NAIP5 activation and induces TLR5-independent anti-tumor immunity.
Lin KH, Chang LS, Tian CY, Yeh YC, Chen YJ, Chuang TH, Liu SJ, Leng CH. Lin KH, et al. Sci Rep. 2016 Apr 11;6:24199. doi: 10.1038/srep24199. Sci Rep. 2016. PMID: 27063435 Free PMC article.
Flagellin has the capacity to activate both Toll-like receptor 5 (TLR5) and Nod-like receptor C4 (NLRC4)/neuronal apoptosis inhibitory protein 5 (NAIP5) inflammasome signaling. We fused E7m (the inactivated E7 of human papillomavirus) to either end of the flagell
Flagellin has the capacity to activate both Toll-like receptor 5 (TLR5) and Nod-like receptor C4 (NLRC4)/neuronal apoptosis inhibitor
Restriction of Legionella pneumophila replication in macrophages requires concerted action of the transcriptional regulators Irf1 and Irf8 and nod-like receptors Naip5 and Nlrc4.
Fortier A, Doiron K, Saleh M, Grinstein S, Gros P. Fortier A, et al. Infect Immun. 2009 Nov;77(11):4794-805. doi: 10.1128/IAI.01546-08. Epub 2009 Aug 31. Infect Immun. 2009. PMID: 19720760 Free PMC article.
The unique permissiveness of A/J mouse macrophages for replication of Legionella pneumophila is caused by a deficiency in the Nod-like receptor (NLR) protein and intracellular sensor for L. pneumophila flagellin (Naip5). The signaling pathways and proteins activated …
The unique permissiveness of A/J mouse macrophages for replication of Legionella pneumophila is caused by a deficiency in the Nod-like recep …
Gasdermin-D and Caspase-7 are the key Caspase-1/8 substrates downstream of the NAIP5/NLRC4 inflammasome required for restriction of Legionella pneumophila.
Gonçalves AV, Margolis SR, Quirino GFS, Mascarenhas DPA, Rauch I, Nichols RD, Ansaldo E, Fontana MF, Vance RE, Zamboni DS. Gonçalves AV, et al. PLoS Pathog. 2019 Jun 28;15(6):e1007886. doi: 10.1371/journal.ppat.1007886. eCollection 2019 Jun. PLoS Pathog. 2019. PMID: 31251782 Free PMC article.
Inflammasomes are cytosolic multi-protein complexes that detect infection or cellular damage and activate the Caspase-1 (CASP1) protease. The NAIP5/NLRC4 inflammasome detects bacterial flagellin and is essential for resistance to the flagellated intracellular bacter …
Inflammasomes are cytosolic multi-protein complexes that detect infection or cellular damage and activate the Caspase-1 (CASP1) protease. Th …
56 results