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Volumn 4, Issue DEC, 2013, Pages

Interactions between Nod-like receptors and intestinal bacteria

Author keywords

Inflammasome; Intestine; Microbiota; Nod like receptors; Pathogen

Indexed keywords


EID: 84892169538     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2013.00462     Document Type: Review
Times cited : (33)

References (131)
  • 1
    • 72949091232 scopus 로고    scopus 로고
    • Bacterial community variation in human body habitats across space and time
    • doi: 10.1126/science.1177486
    • Costello EK, Lauber CL, Hamady M, Fierer N, Gordon JI, Knight R. Bacterial community variation in human body habitats across space and time. Science (2009) 326(5960):1694-7. doi: 10.1126/science.1177486
    • (2009) Science , vol.326 , Issue.5960 , pp. 1694-1697
    • Costello, E.K.1    Lauber, C.L.2    Hamady, M.3    Fierer, N.4    Gordon, J.I.5    Knight, R.6
  • 2
    • 84866146940 scopus 로고    scopus 로고
    • Diversity, stability and resilience of the human gut microbiota
    • doi:10.1038/nature11550
    • Lozupone CA, Stombaugh JI, Gordon JI, Jansson JK, Knight R. Diversity, stability and resilience of the human gut microbiota. Nature (2012) 489(7415):220-30. doi:10.1038/nature11550
    • (2012) Nature , vol.489 , Issue.7415 , pp. 220-230
    • Lozupone, C.A.1    Stombaugh, J.I.2    Gordon, J.I.3    Jansson, J.K.4    Knight, R.5
  • 3
    • 84856098171 scopus 로고    scopus 로고
    • Role of mucus layers in gut infection and inflammation
    • doi:10.1016/j.mib.2011.11.002
    • Hansson GC. Role of mucus layers in gut infection and inflammation. Curr Opin Microbiol (2012) 15(1):57-62. doi:10.1016/j.mib.2011.11.002
    • (2012) Curr Opin Microbiol , vol.15 , Issue.1 , pp. 57-62
    • Hansson, G.C.1
  • 4
    • 83655181087 scopus 로고    scopus 로고
    • Bacteria and host interactions in the gut epithelial barrier
    • doi:10.1038/nchembio.741
    • Ashida H, Ogawa M, Kim M, Mimuro H, Sasakawa C. Bacteria and host interactions in the gut epithelial barrier. Nat Chem Biol (2011) 8(1):36-45. doi:10.1038/nchembio.741
    • (2011) Nat Chem Biol , vol.8 , Issue.1 , pp. 36-45
    • Ashida, H.1    Ogawa, M.2    Kim, M.3    Mimuro, H.4    Sasakawa, C.5
  • 5
    • 58049220365 scopus 로고    scopus 로고
    • Pattern recognition receptors and control of adaptive immunity
    • doi:10.1111/j.1600-065X.2008.00731.x
    • Palm NW, Medzhitov R. Pattern recognition receptors and control of adaptive immunity. Immunol Rev (2009) 227(1):221-33. doi:10.1111/j.1600-065X.2008.00731.x
    • (2009) Immunol Rev , vol.227 , Issue.1 , pp. 221-233
    • Palm, N.W.1    Medzhitov, R.2
  • 6
    • 64749104915 scopus 로고    scopus 로고
    • Life on the inside: the intracellular lifestyle of cytosolic bacteria
    • doi:10.1038/nrmicro2112
    • Ray K, Marteyn B, Sansonetti PJ, Tang CM. Life on the inside: the intracellular lifestyle of cytosolic bacteria. Nat Rev Microbiol (2009) 7(5):333-40. doi:10.1038/nrmicro2112
    • (2009) Nat Rev Microbiol , vol.7 , Issue.5 , pp. 333-340
    • Ray, K.1    Marteyn, B.2    Sansonetti, P.J.3    Tang, C.M.4
  • 7
    • 0038615855 scopus 로고    scopus 로고
    • Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan
    • doi:10.1126/science.1084677
    • Girardin SE, Boneca IG, Carneiro LA, Antignac A, Jéhanno M, Viala J, et al. Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan. Science (2003) 300(5625):1584-7. doi:10.1126/science.1084677
    • (2003) Science , vol.300 , Issue.5625 , pp. 1584-1587
    • Girardin, S.E.1    Boneca, I.G.2    Carneiro, L.A.3    Antignac, A.4    Jéhanno, M.5    Viala, J.6
  • 8
    • 0012722659 scopus 로고    scopus 로고
    • Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection
    • doi:10.1074/jbc.C200651200
    • Girardin SE, Boneca IG, Viala J, Chamaillard M, Labigne A, Thomas G, et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J Biol Chem (2003) 278(11):8869-72. doi:10.1074/jbc.C200651200
    • (2003) J Biol Chem , vol.278 , Issue.11 , pp. 8869-8872
    • Girardin, S.E.1    Boneca, I.G.2    Viala, J.3    Chamaillard, M.4    Labigne, A.5    Thomas, G.6
  • 9
    • 0037075551 scopus 로고    scopus 로고
    • RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems
    • doi:10.1038/416194a
    • Kobayashi K, Inohara N, Hernandez LD, Galán JE, Núñez G, Janeway CA, et al. RICK/Rip2/CARDIAK mediates signalling for receptors of the innate and adaptive immune systems. Nature (2002) 416(6877):194-9. doi:10.1038/416194a
    • (2002) Nature , vol.416 , Issue.6877 , pp. 194-199
    • Kobayashi, K.1    Inohara, N.2    Hernandez, L.D.3    Galán, J.E.4    Núñez, G.5    Janeway, C.A.6
  • 10
    • 84874216392 scopus 로고    scopus 로고
    • NOD1 and NOD2 signaling in infection and inflammation
    • doi:10.3389/fimmu.2012.00328
    • Moreira LO, Zamboni DS. NOD1 and NOD2 signaling in infection and inflammation. Front Immunol (2012) 3:328. doi:10.3389/fimmu.2012.00328
    • (2012) Front Immunol , vol.3 , pp. 328
    • Moreira, L.O.1    Zamboni, D.S.2
  • 11
    • 64249098607 scopus 로고    scopus 로고
    • Evaluation of Nod-like receptor (NLR) effector domain interactions
    • doi:10.1371/journal.pone.0004931
    • Wagner RN, Proell M, Kufer TA, Schwarzenbacher R. Evaluation of Nod-like receptor (NLR) effector domain interactions. PLoS One (2009) 4(4):e4931. doi:10.1371/journal.pone.0004931
    • (2009) PLoS One , vol.4 , Issue.4
    • Wagner, R.N.1    Proell, M.2    Kufer, T.A.3    Schwarzenbacher, R.4
  • 12
    • 73849121209 scopus 로고    scopus 로고
    • Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry
    • doi:10.1038/ni.1823
    • Travassos LH, Carneiro LA, Ramjeet M, Hussey S, Kim Y-G, Magalhães JG, et al. Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry. Nat Immunol (2009) 11(1):55-62. doi:10.1038/ni.1823
    • (2009) Nat Immunol , vol.11 , Issue.1 , pp. 55-62
    • Travassos, L.H.1    Carneiro, L.A.2    Ramjeet, M.3    Hussey, S.4    Kim, Y.-G.5    Magalhães, J.G.6
  • 13
    • 84876282419 scopus 로고    scopus 로고
    • Manipulation of small Rho GTPases is a pathogen-induced process detected by NOD1
    • doi:10.1038/nature12025
    • Keestra AM, Winter MG, Auburger JJ, Fräßle SP, Xavier MN, Winter SE, et al. Manipulation of small Rho GTPases is a pathogen-induced process detected by NOD1. Nature (2013) 496(7444):233-7. doi:10.1038/nature12025
    • (2013) Nature , vol.496 , Issue.7444 , pp. 233-237
    • Keestra, A.M.1    Winter, M.G.2    Auburger, J.J.3    Fräßle, S.P.4    Xavier, M.N.5    Winter, S.E.6
  • 14
    • 84880280093 scopus 로고    scopus 로고
    • Crystal structure of NLRC4 reveals its autoinhibition mechanism
    • doi:10.1126/science.1236381
    • Hu Z, Yan C, Liu P, Huang Z, Ma R, Zhang C, et al. Crystal structure of NLRC4 reveals its autoinhibition mechanism. Science (2013) 341(6142):172-5. doi:10.1126/science.1236381
    • (2013) Science , vol.341 , Issue.6142 , pp. 172-175
    • Hu, Z.1    Yan, C.2    Liu, P.3    Huang, Z.4    Ma, R.5    Zhang, C.6
  • 15
    • 84867861468 scopus 로고    scopus 로고
    • Phosphorylation of NLRC4 is critical for inflammasome activation
    • doi:10.1038/nature11429
    • Qu Y, Misaghi S, Izrael-Tomasevic A, Newton K, Gilmour LL, Lamkanfi M, et al. Phosphorylation of NLRC4 is critical for inflammasome activation. Nature (2012) 490(7421):539-42. doi:10.1038/nature11429
    • (2012) Nature , vol.490 , Issue.7421 , pp. 539-542
    • Qu, Y.1    Misaghi, S.2    Izrael-Tomasevic, A.3    Newton, K.4    Gilmour, L.L.5    Lamkanfi, M.6
  • 16
    • 33744464740 scopus 로고    scopus 로고
    • Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1β in Salmonella-infected macrophages
    • doi:10.1038/ni1346
    • Franchi L, Amer A, Body-Malapel M, Kanneganti T-D, Özören N, Jagirdar R, et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1β in Salmonella-infected macrophages. Nat Immunol (2006) 7(6):576-82. doi:10.1038/ni1346
    • (2006) Nat Immunol , vol.7 , Issue.6 , pp. 576-582
    • Franchi, L.1    Amer, A.2    Body-Malapel, M.3    Kanneganti, T.-D.4    Özören, N.5    Jagirdar, R.6
  • 17
    • 33744493091 scopus 로고    scopus 로고
    • Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf
    • doi:10.1038/ni1344
    • Miao EA, Alpuche-Aranda CM, Dors M, Clark AE, Bader MW, Miller SI, et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf. Nat Immunol (2006) 7(6):569-75. doi:10.1038/ni1344
    • (2006) Nat Immunol , vol.7 , Issue.6 , pp. 569-575
    • Miao, E.A.1    Alpuche-Aranda, C.M.2    Dors, M.3    Clark, A.E.4    Bader, M.W.5    Miller, S.I.6
  • 18
    • 33645843633 scopus 로고    scopus 로고
    • Cytosolic recognition of flagellin by mouse macrophages restricts Legionella pneumophila infection
    • doi:10.1084/jem.20051659
    • Molofsky AB, Byrne BG, Whitfield NN, Madigan CA, Fuse ET, Tateda K, et al. Cytosolic recognition of flagellin by mouse macrophages restricts Legionella pneumophila infection. J Exp Med (2006) 203(4):1093-104. doi:10.1084/jem.20051659
    • (2006) J Exp Med , vol.203 , Issue.4 , pp. 1093-1104
    • Molofsky, A.B.1    Byrne, B.G.2    Whitfield, N.N.3    Madigan, C.A.4    Fuse, E.T.5    Tateda, K.6
  • 19
    • 77649241461 scopus 로고    scopus 로고
    • Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome
    • doi:10.1073/pnas.0913087107
    • Miao EA, Mao DP, Yudkovsky N, Bonneau R, Lorang CG, Warren SE, et al. Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome. Proc Natl Acad Sci U S A (2010) 107(7):3076-80. doi:10.1073/pnas.0913087107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.7 , pp. 3076-3080
    • Miao, E.A.1    Mao, D.P.2    Yudkovsky, N.3    Bonneau, R.4    Lorang, C.G.5    Warren, S.E.6
  • 20
    • 80053349020 scopus 로고    scopus 로고
    • The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
    • doi:10.1038/nature10510
    • Zhao Y, Yang J, Shi J, Gong Y-N, Lu Q, Xu H, et al. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature (2011) 477(7366):596-600. doi:10.1038/nature10510
    • (2011) Nature , vol.477 , Issue.7366 , pp. 596-600
    • Zhao, Y.1    Yang, J.2    Shi, J.3    Gong, Y.-N.4    Lu, Q.5    Xu, H.6
  • 21
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • doi:10.1038/nature10394
    • Kofoed EM, Vance RE. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature (2011) 477(7366):592-5. doi:10.1038/nature10394
    • (2011) Nature , vol.477 , Issue.7366 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 22
    • 84869044838 scopus 로고    scopus 로고
    • Formation and structure of a NAIP5-NLRC4 inflammasome induced by direct interactions with conserved N-and C-terminal regions of flagellin
    • doi:10.1074/jbc.M112.393512
    • Halff EF, Diebolder CA, Versteeg M, Schouten A, Brondijk THC, Huizinga EG. Formation and structure of a NAIP5-NLRC4 inflammasome induced by direct interactions with conserved N-and C-terminal regions of flagellin. J Biol Chem (2012) 287(46):38460-72. doi:10.1074/jbc.M112.393512
    • (2012) J Biol Chem , vol.287 , Issue.46 , pp. 38460-38472
    • Halff, E.F.1    Diebolder, C.A.2    Versteeg, M.3    Schouten, A.4    Brondijk, T.H.C.5    Huizinga, E.G.6
  • 23
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • doi:10.1038/ng756
    • Hoffman HM, Mueller JL, Broide DH, Wanderer AA, Kolodner RD. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat Genet (2001) 29(3):301-5. doi:10.1038/ng756
    • (2001) Nat Genet , vol.29 , Issue.3 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 24
    • 84858677223 scopus 로고    scopus 로고
    • Sensing and reacting to microbes through the inflammasomes
    • doi:10.1038/ni.2231
    • Franchi L, Muñoz-Planillo R, Núñez G. Sensing and reacting to microbes through the inflammasomes. Nat Immunol (2012) 13(4):325-32. doi:10.1038/ni.2231
    • (2012) Nat Immunol , vol.13 , Issue.4 , pp. 325-332
    • Franchi, L.1    Muñoz-Planillo, R.2    Núñez, G.3
  • 25
    • 84862777872 scopus 로고    scopus 로고
    • Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
    • doi:10.1016/j.immuni.2012.01.009
    • Shimada K, Crother TR, Karlin J, Dagvadorj J, Chiba N, Chen S, et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity (2012) 36(3):401-14. doi:10.1016/j.immuni.2012.01.009
    • (2012) Immunity , vol.36 , Issue.3 , pp. 401-414
    • Shimada, K.1    Crother, T.R.2    Karlin, J.3    Dagvadorj, J.4    Chiba, N.5    Chen, S.6
  • 26
    • 75649096002 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein links oxidative stress to inflammasome activation
    • doi:10.1038/ni.1831
    • Zhou R, Tardivel A, Thorens B, Choi I, Tschopp J. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat Immunol (2009) 11(2):136-40. doi:10.1038/ni.1831
    • (2009) Nat Immunol , vol.11 , Issue.2 , pp. 136-140
    • Zhou, R.1    Tardivel, A.2    Thorens, B.3    Choi, I.4    Tschopp, J.5
  • 27
    • 84863978096 scopus 로고    scopus 로고
    • Critical role for calcium mobilization in activation of the NLRP3 inflammasome
    • doi:10.1073/pnas.1117765109
    • Murakami T, Ockinger J, Yu J, Byles V, McColl A, Hofer AM, et al. Critical role for calcium mobilization in activation of the NLRP3 inflammasome. Proc Natl Acad Sci U S A (2012) 109(28):11282-7. doi:10.1073/pnas.1117765109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.28 , pp. 11282-11287
    • Murakami, T.1    Ockinger, J.2    Yu, J.3    Byles, V.4    McColl, A.5    Hofer, A.M.6
  • 28
    • 84882614243 scopus 로고    scopus 로고
    • Mitochondrial cardiolipin is required for Nlrp3 inflammasome activation
    • doi:10.1016/j.immuni.2013.08.001
    • Iyer SS, He Q, Janczy JR, Elliott EI, Zhong Z, Olivier AK, et al. Mitochondrial cardiolipin is required for Nlrp3 inflammasome activation. Immunity (2013) 39(2):311-23. doi:10.1016/j.immuni.2013.08.001
    • (2013) Immunity , vol.39 , Issue.2 , pp. 311-323
    • Iyer, S.S.1    He, Q.2    Janczy, J.R.3    Elliott, E.I.4    Zhong, Z.5    Olivier, A.K.6
  • 29
    • 84866512376 scopus 로고    scopus 로고
    • Cell volume regulation modulates NLRP3 inflammasome activation
    • doi:10.1016/j.immuni.2012.06.013
    • Compan V, Baroja-Mazo A, López-Castejón G, Gomez AI, Martínez CM, Angosto D, et al. Cell volume regulation modulates NLRP3 inflammasome activation. Immunity (2012) 37(3):487-500. doi:10.1016/j.immuni.2012.06.013
    • (2012) Immunity , vol.37 , Issue.3 , pp. 487-500
    • Compan, V.1    Baroja-Mazo, A.2    López-Castejón, G.3    Gomez, A.I.4    Martínez, C.M.5    Angosto, D.6
  • 30
    • 84879596906 scopus 로고    scopus 로고
    • K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • doi:10.1016/j.immuni.2013.05.016
    • Munoz-Planillo R, Kuffa P, Martinez-Colon G, Smith BL, Rajendiran TM, Nunez G. K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity (2013) 38(6):1142-53. doi:10.1016/j.immuni.2013.05.016
    • (2013) Immunity , vol.38 , Issue.6 , pp. 1142-1153
    • Munoz-Planillo, R.1    Kuffa, P.2    Martinez-Colon, G.3    Smith, B.L.4    Rajendiran, T.M.5    Nunez, G.6
  • 31
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • doi:10.1038/nature10558
    • Kayagaki N, Warming S, Lamkanfi M, Walle LV, Louie S, Dong J, et al. Non-canonical inflammasome activation targets caspase-11. Nature (2011) 479(7371):117-21. doi:10.1038/nature10558
    • (2011) Nature , vol.479 , Issue.7371 , pp. 117-121
    • Kayagaki, N.1    Warming, S.2    Lamkanfi, M.3    Walle, L.V.4    Louie, S.5    Dong, J.6
  • 32
    • 84864600268 scopus 로고    scopus 로고
    • TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gram-negative bacteria
    • doi:10.1016/j.cell.2012.07.007
    • Rathinam VA, Vanaja SK, Waggoner L, Sokolovska A, Becker C, Stuart LM, et al. TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gram-negative bacteria. Cell (2012) 150(3):606-19. doi:10.1016/j.cell.2012.07.007
    • (2012) Cell , vol.150 , Issue.3 , pp. 606-619
    • Rathinam, V.A.1    Vanaja, S.K.2    Waggoner, L.3    Sokolovska, A.4    Becker, C.5    Stuart, L.M.6
  • 33
    • 84883775365 scopus 로고    scopus 로고
    • Noncanonical inflammasome activation by intracellular LPS independent of TLR4
    • doi:10.1126/science.1240248
    • Kayagaki N, Wong MT, Stowe IB, Ramani SR, Gonzalez LC, Akashi-Takamura S, et al. Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science (2013) 341(6151):1246-9. doi:10.1126/science.1240248
    • (2013) Science , vol.341 , Issue.6151 , pp. 1246-1249
    • Kayagaki, N.1    Wong, M.T.2    Stowe, I.B.3    Ramani, S.R.4    Gonzalez, L.C.5    Akashi-Takamura, S.6
  • 34
    • 18644368579 scopus 로고    scopus 로고
    • Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-κB and caspase-1
    • doi:10.1016/S0014-5793(02)03416-6
    • Grenier JM, Wang L, Manji GA, Huang W-J, Al-Garawi A, Kelly R, et al. Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-κB and caspase-1. FEBS Lett (2002) 530(1):73-8. doi:10.1016/S0014-5793(02)03416-6
    • (2002) FEBS Lett , vol.530 , Issue.1 , pp. 73-78
    • Grenier, J.M.1    Wang, L.2    Manji, G.A.3    Huang, W.-J.4    Al-Garawi, A.5    Kelly, R.6
  • 35
    • 77956103055 scopus 로고    scopus 로고
    • Quantitative expression of RIG-like helicase, NOD-like receptor and inflammasome-related mRNAs in humans and mice
    • doi:10.1093/intimm/dxq058
    • Lech M, Avila-Ferrufino A, Skuginna V, Susanti HE, Anders H-J. Quantitative expression of RIG-like helicase, NOD-like receptor and inflammasome-related mRNAs in humans and mice. Int Immunol (2010) 22(9):717-28. doi:10.1093/intimm/dxq058
    • (2010) Int Immunol , vol.22 , Issue.9 , pp. 717-728
    • Lech, M.1    Avila-Ferrufino, A.2    Skuginna, V.3    Susanti, H.E.4    Anders, H.-J.5
  • 36
    • 79957576718 scopus 로고    scopus 로고
    • NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis
    • doi:10.1016/j.cell.2011.04.022
    • Elinav E, Strowig T, Kau AL, Henao-Mejia J, Thaiss CA, Booth CJ, et al. NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis. Cell (2011) 145(5):745-57. doi:10.1016/j.cell.2011.04.022
    • (2011) Cell , vol.145 , Issue.5 , pp. 745-757
    • Elinav, E.1    Strowig, T.2    Kau, A.L.3    Henao-Mejia, J.4    Thaiss, C.A.5    Booth, C.J.6
  • 37
    • 84876713274 scopus 로고    scopus 로고
    • Stress-induced corticotropin-releasing hormone-mediated NLRP6 inflammasome inhibition and transmissible enteritis in mice
    • doi:10.1053/j.gastro.2013.02.038
    • Sun Y, Zhang M, Chen CC, Gillilland M, III, Sun X, El-Zaatari M, et al. Stress-induced corticotropin-releasing hormone-mediated NLRP6 inflammasome inhibition and transmissible enteritis in mice. Gastroenterology (2013). 144(7):1478-87.e8. doi:10.1053/j.gastro.2013.02.038
    • (2013) Gastroenterology , vol.144 , Issue.7
    • Sun, Y.1    Zhang, M.2    Chen, C.C.3    Gillilland I.I.I, M.4    Sun, X.5    El-Zaatari, M.6
  • 38
    • 84865130689 scopus 로고    scopus 로고
    • NLRP6 negatively regulates innate immunity and host defence against bacterial pathogens
    • doi:10.1038/nature11250
    • Anand PK, Malireddi RS, Lukens JR, Vogel P, Bertin J, Lamkanfi M, et al. NLRP6 negatively regulates innate immunity and host defence against bacterial pathogens. Nature (2012) 488(7411):389-93. doi:10.1038/nature11250
    • (2012) Nature , vol.488 , Issue.7411 , pp. 389-393
    • Anand, P.K.1    Malireddi, R.S.2    Lukens, J.R.3    Vogel, P.4    Bertin, J.5    Lamkanfi, M.6
  • 39
    • 79959369355 scopus 로고    scopus 로고
    • Nod-like receptor pyrin domain-containing protein 6 (NLRP6) controls epithelial self-renewal and colorectal carcinogenesis upon injury
    • doi:10.1073/pnas.1100981108
    • Normand S, Delanoye-Crespin A, Bressenot A, Huot L, Grandjean T, Peyrin-Biroulet L, et al. Nod-like receptor pyrin domain-containing protein 6 (NLRP6) controls epithelial self-renewal and colorectal carcinogenesis upon injury. Proc Natl Acad Sci U S A (2011) 108(23):9601-6. doi:10.1073/pnas.1100981108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.23 , pp. 9601-9606
    • Normand, S.1    Delanoye-Crespin, A.2    Bressenot, A.3    Huot, L.4    Grandjean, T.5    Peyrin-Biroulet, L.6
  • 40
    • 79959540809 scopus 로고    scopus 로고
    • A functional role for Nlrp6 in intestinal inflammation and tumorigenesis
    • doi:10.4049/jimmunol.1100412
    • Chen GY, Liu M, Wang F, Bertin J, Núñez G. A functional role for Nlrp6 in intestinal inflammation and tumorigenesis. J Immunol (2011) 186(12):7187-94. doi:10.4049/jimmunol.1100412
    • (2011) J Immunol , vol.186 , Issue.12 , pp. 7187-7194
    • Chen, G.Y.1    Liu, M.2    Wang, F.3    Bertin, J.4    Núñez, G.5
  • 41
    • 0010464874 scopus 로고    scopus 로고
    • PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-κB and caspase-1-dependent cytokine processing
    • doi:10.1074/jbc.M203915200
    • Wang L, Manji GA, Grenier JM, Al-Garawi A, Merriam S, Lora JM, et al. PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-κB and caspase-1-dependent cytokine processing. J Biol Chem (2002) 277(33):29874-80. doi:10.1074/jbc.M203915200
    • (2002) J Biol Chem , vol.277 , Issue.33 , pp. 29874-29880
    • Wang, L.1    Manji, G.A.2    Grenier, J.M.3    Al-Garawi, A.4    Merriam, S.5    Lora, J.M.6
  • 42
    • 0037852184 scopus 로고    scopus 로고
    • Cutting edge: monarch-1: a pyrin/nucleotide-binding domain/leucine-rich repeat protein that controls classical and nonclassical MHC class I genes
    • Williams KL, Taxman DJ, Linhoff MW, Reed W, Ting JP-Y. Cutting edge: monarch-1: a pyrin/nucleotide-binding domain/leucine-rich repeat protein that controls classical and nonclassical MHC class I genes. J Immunol (2003) 170(11):5354-8.
    • (2003) J Immunol , vol.170 , Issue.11 , pp. 5354-5358
    • Williams, K.L.1    Taxman, D.J.2    Linhoff, M.W.3    Reed, W.4    Ting, J.P.-Y.5
  • 43
    • 33846473862 scopus 로고    scopus 로고
    • Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes
    • Lich JD, Williams KL, Moore CB, Arthur JC, Davis BK, Taxman DJ, et al. Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes. J Immunol (2007) 178(3):1256-60.
    • (2007) J Immunol , vol.178 , Issue.3 , pp. 1256-1260
    • Lich, J.D.1    Williams, K.L.2    Moore, C.B.3    Arthur, J.C.4    Davis, B.K.5    Taxman, D.J.6
  • 44
    • 28844494900 scopus 로고    scopus 로고
    • The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor alpha-, and Mycobacterium tuberculosis-induced pro-inflammatory signals
    • doi:10.1074/jbc.M502820200
    • Williams KL, Lich JD, Duncan JA, Reed W, Rallabhandi P, Moore C, et al. The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor alpha-, and Mycobacterium tuberculosis-induced pro-inflammatory signals. J Biol Chem (2005) 280(48):39914-24. doi:10.1074/jbc.M502820200
    • (2005) J Biol Chem , vol.280 , Issue.48 , pp. 39914-39924
    • Williams, K.L.1    Lich, J.D.2    Duncan, J.A.3    Reed, W.4    Rallabhandi, P.5    Moore, C.6
  • 45
    • 78049489590 scopus 로고    scopus 로고
    • Cutting edge: NLRP12 controls dendritic and myeloid cell migration to affect contact hypersensitivity
    • doi:10.4049/jimmunol.1002227
    • Arthur JC, Lich JD, Ye Z, Allen IC, Gris D, Wilson JE, et al. Cutting edge: NLRP12 controls dendritic and myeloid cell migration to affect contact hypersensitivity. J Immunol (2010) 185(8):4515-9. doi:10.4049/jimmunol.1002227
    • (2010) J Immunol , vol.185 , Issue.8 , pp. 4515-4519
    • Arthur, J.C.1    Lich, J.D.2    Ye, Z.3    Allen, I.C.4    Gris, D.5    Wilson, J.E.6
  • 46
    • 81255189478 scopus 로고    scopus 로고
    • The NOD-like receptor NLRP12 attenuates colon inflammation and tumorigenesis
    • doi:10.1016/j.ccr.2011.10.022
    • Zaki MH, Vogel P, Malireddi R, Body-Malapel M, Anand PK, Bertin J, et al. The NOD-like receptor NLRP12 attenuates colon inflammation and tumorigenesis. Cancer Cell (2011) 20(5):649-60. doi:10.1016/j.ccr.2011.10.022
    • (2011) Cancer Cell , vol.20 , Issue.5 , pp. 649-660
    • Zaki, M.H.1    Vogel, P.2    Malireddi, R.3    Body-Malapel, M.4    Anand, P.K.5    Bertin, J.6
  • 47
    • 84861460062 scopus 로고    scopus 로고
    • NLRP12 suppresses colon inflammation and tumorigenesis through the negative regulation of noncanonical NF-κB signaling
    • doi:10.1016/j.immuni.2012.03.012
    • Allen IC, Wilson JE, Schneider M, Lich JD, Roberts RA, Arthur JC, et al. NLRP12 suppresses colon inflammation and tumorigenesis through the negative regulation of noncanonical NF-κB signaling. Immunity (2012) 36(5):742-54. doi:10.1016/j.immuni.2012.03.012
    • (2012) Immunity , vol.36 , Issue.5 , pp. 742-754
    • Allen, I.C.1    Wilson, J.E.2    Schneider, M.3    Lich, J.D.4    Roberts, R.A.5    Arthur, J.C.6
  • 48
    • 0030775488 scopus 로고    scopus 로고
    • Cloning a novel member of the human interferon-inducible gene family associated with control of tumorigenicity in a model of human melanoma
    • doi:10.1038/sj.onc.1201206
    • DeYoung KL, Ray ME, Su YA, Anzick SL, Johnstone RW, Trapani JA, et al. Cloning a novel member of the human interferon-inducible gene family associated with control of tumorigenicity in a model of human melanoma. Oncogene (1997) 15(4):453. doi:10.1038/sj.onc.1201206
    • (1997) Oncogene , vol.15 , Issue.4 , pp. 453
    • DeYoung, K.L.1    Ray, M.E.2    Su, Y.A.3    Anzick, S.L.4    Johnstone, R.W.5    Trapani, J.A.6
  • 49
    • 60749104535 scopus 로고    scopus 로고
    • HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA
    • doi:10.1126/science.1169841
    • Roberts TL, Idris A, Dunn JA, Kelly GM, Burnton CM, Hodgson S, et al. HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science (2009) 323(5917):1057-60. doi:10.1126/science.1169841
    • (2009) Science , vol.323 , Issue.5917 , pp. 1057-1060
    • Roberts, T.L.1    Idris, A.2    Dunn, J.A.3    Kelly, G.M.4    Burnton, C.M.5    Hodgson, S.6
  • 50
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
    • doi:10.1038/nature07725
    • Hornung V, Ablasser A, Charrel-Dennis M, Bauernfeind F, Horvath G, Caffrey DR, et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature (2009) 458(7237):514-8. doi:10.1038/nature07725
    • (2009) Nature , vol.458 , Issue.7237 , pp. 514-518
    • Hornung, V.1    Ablasser, A.2    Charrel-Dennis, M.3    Bauernfeind, F.4    Horvath, G.5    Caffrey, D.R.6
  • 51
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • doi:10.1038/nature07710
    • Fernandes-Alnemri T, Yu J-W, Datta P, Wu J, Alnemri ES. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature (2009) 458(7237):509-13. doi:10.1038/nature07710
    • (2009) Nature , vol.458 , Issue.7237 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.-W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 52
    • 60749136484 scopus 로고    scopus 로고
    • An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
    • doi:10.1038/ni.1702
    • Bürckstümmer T, Baumann C, Blüml S, Dixit E, Dürnberger G, Jahn H, et al. An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat Immunol (2009) 10(3):266-72. doi:10.1038/ni.1702
    • (2009) Nat Immunol , vol.10 , Issue.3 , pp. 266-272
    • Bürckstümmer, T.1    Baumann, C.2    Blüml, S.3    Dixit, E.4    Dürnberger, G.5    Jahn, H.6
  • 53
    • 77955294800 scopus 로고    scopus 로고
    • Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol
    • doi:10.1016/j.chom.2010.04.004
    • Sauer J-D, Witte CE, Zemansky J, Hanson B, Lauer P, Portnoy DA. Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol. Cell Host Microbe (2010) 7(5):412-9. doi:10.1016/j.chom.2010.04.004
    • (2010) Cell Host Microbe , vol.7 , Issue.5 , pp. 412-419
    • Sauer, J.-D.1    Witte, C.E.2    Zemansky, J.3    Hanson, B.4    Lauer, P.5    Portnoy, D.A.6
  • 54
    • 84874885642 scopus 로고    scopus 로고
    • Discordant results obtained with Francisella tularensis during in vitro and in vivo immunological studies are attributable to compromised bacterial structural integrity
    • doi:10.1371/journal.pone.0058513
    • Singh A, Rahman T, Malik M, Hickey AJ, Leifer CA, Hazlett KR, et al. Discordant results obtained with Francisella tularensis during in vitro and in vivo immunological studies are attributable to compromised bacterial structural integrity. PLoS One (2013) 8(3):e58513. doi:10.1371/journal.pone.0058513
    • (2013) PLoS One , vol.8 , Issue.3
    • Singh, A.1    Rahman, T.2    Malik, M.3    Hickey, A.J.4    Leifer, C.A.5    Hazlett, K.R.6
  • 55
    • 84859945146 scopus 로고    scopus 로고
    • Preventing bacterial DNA release and absent in melanoma 2 inflammasome activation by a Legionella effector functioning in membrane trafficking
    • doi:10.1073/pnas.1117490109
    • Ge J, Gong Y-N, Xu Y, Shao F. Preventing bacterial DNA release and absent in melanoma 2 inflammasome activation by a Legionella effector functioning in membrane trafficking. Proc Natl Acad Sci U S A (2012) 109(16):6193-8. doi:10.1073/pnas.1117490109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.16 , pp. 6193-6198
    • Ge, J.1    Gong, Y.-N.2    Xu, Y.3    Shao, F.4
  • 56
    • 84859986329 scopus 로고    scopus 로고
    • Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor
    • doi:10.1016/j.immuni.2012.02.014
    • Jin T, Perry A, Jiang J, Smith P, Curry JA, Unterholzner L, et al. Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor. Immunity (2012) 36(4):561-71. doi:10.1016/j.immuni.2012.02.014
    • (2012) Immunity , vol.36 , Issue.4 , pp. 561-571
    • Jin, T.1    Perry, A.2    Jiang, J.3    Smith, P.4    Curry, J.A.5    Unterholzner, L.6
  • 57
    • 84877692253 scopus 로고    scopus 로고
    • Structure of the absent in melanoma 2 (AIM2) Pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly
    • doi:10.1074/jbc.M113.468033
    • Jin T, Perry A, Smith P, Jiang J, Xiao TS. Structure of the absent in melanoma 2 (AIM2) Pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly. J Biol Chem (2013) 288(19):13225-35. doi:10.1074/jbc.M113.468033
    • (2013) J Biol Chem , vol.288 , Issue.19 , pp. 13225-13235
    • Jin, T.1    Perry, A.2    Smith, P.3    Jiang, J.4    Xiao, T.S.5
  • 58
    • 77952671243 scopus 로고    scopus 로고
    • Food-borne diseases-the challenges of 20 years ago still persist while new ones continue to emerge
    • doi:10.1016/j.ijfoodmicro.2010.01.021
    • Newell DG, Koopmans M, Verhoef L, Duizer E, Aidara-Kane A, Sprong H, et al. Food-borne diseases-the challenges of 20 years ago still persist while new ones continue to emerge. Int J Food Microbiol (2010) 139(Suppl 1):S3-15. doi:10.1016/j.ijfoodmicro.2010.01.021
    • (2010) Int J Food Microbiol , vol.139 , Issue.SUPPL. 1
    • Newell, D.G.1    Koopmans, M.2    Verhoef, L.3    Duizer, E.4    Aidara-Kane, A.5    Sprong, H.6
  • 59
    • 67651176112 scopus 로고    scopus 로고
    • A cluster-randomized effectiveness trial of Vi typhoid vaccine in India
    • doi:10.1056/NEJMoa0807521
    • Sur D, Ochiai RL, Bhattacharya SK, Ganguly NK, Ali M, Manna B, et al. A cluster-randomized effectiveness trial of Vi typhoid vaccine in India. N Engl J Med (2009) 361(4):335-44. doi:10.1056/NEJMoa0807521
    • (2009) N Engl J Med , vol.361 , Issue.4 , pp. 335-344
    • Sur, D.1    Ochiai, R.L.2    Bhattacharya, S.K.3    Ganguly, N.K.4    Ali, M.5    Manna, B.6
  • 60
  • 61
    • 42149167915 scopus 로고    scopus 로고
    • Motility allows S. typhimurium to benefit from the mucosal defence
    • doi:10.1111/j.1462-5822.2008.01118.x
    • Stecher B, Barthel M, Schlumberger MC, Haberli L, Rabsch W, Kremer M, et al. Motility allows S. typhimurium to benefit from the mucosal defence. Cell Microbiol (2008) 10(5):1166-80. doi:10.1111/j.1462-5822.2008.01118.x
    • (2008) Cell Microbiol , vol.10 , Issue.5 , pp. 1166-1180
    • Stecher, B.1    Barthel, M.2    Schlumberger, M.C.3    Haberli, L.4    Rabsch, W.5    Kremer, M.6
  • 62
    • 37349110158 scopus 로고    scopus 로고
    • Salmonellae interplay with host cells
    • doi:10.1038/nrmicro1788
    • Haraga A, Ohlson MB, Miller SI. Salmonellae interplay with host cells. Nat Rev Microbiol (2008) 6(1):53-66. doi:10.1038/nrmicro1788
    • (2008) Nat Rev Microbiol , vol.6 , Issue.1 , pp. 53-66
    • Haraga, A.1    Ohlson, M.B.2    Miller, S.I.3
  • 63
    • 84874688283 scopus 로고    scopus 로고
    • Microbiota restricts trafficking of bacteria to mesenteric lymph nodes by CX3CR1hi cells
    • doi:10.1038/nature11809
    • Diehl GE, Longman RS, Zhang J-X, Breart B, Galan C, Cuesta A, et al. Microbiota restricts trafficking of bacteria to mesenteric lymph nodes by CX3CR1hi cells. Nature (2013) 494(7435):116-20. doi:10.1038/nature11809
    • (2013) Nature , vol.494 , Issue.7435 , pp. 116-120
    • Diehl, G.E.1    Longman, R.S.2    Zhang, J.-X.3    Breart, B.4    Galan, C.5    Cuesta, A.6
  • 64
    • 83655193511 scopus 로고    scopus 로고
    • The streptomycin mouse model for Salmonella diarrhea: functional analysis of the microbiota, the pathogen's virulence factors, and the host's mucosal immune response
    • doi:10.1111/j.1600-065X.2011.01070.x
    • Kaiser P, Diard M, Stecher B, Hardt WD. The streptomycin mouse model for Salmonella diarrhea: functional analysis of the microbiota, the pathogen's virulence factors, and the host's mucosal immune response. Immunol Rev (2012) 245(1):56-83. doi:10.1111/j.1600-065X.2011.01070.x
    • (2012) Immunol Rev , vol.245 , Issue.1 , pp. 56-83
    • Kaiser, P.1    Diard, M.2    Stecher, B.3    Hardt, W.D.4
  • 65
    • 77957157893 scopus 로고    scopus 로고
    • Gut inflammation provides a respiratory electron acceptor for Salmonella
    • doi:10.1038/nature09415
    • Winter SE, Thiennimitr P, Winter MG, Butler BP, Huseby DL, Crawford RW, et al. Gut inflammation provides a respiratory electron acceptor for Salmonella. Nature (2010) 467(7314):426-9. doi:10.1038/nature09415
    • (2010) Nature , vol.467 , Issue.7314 , pp. 426-429
    • Winter, S.E.1    Thiennimitr, P.2    Winter, M.G.3    Butler, B.P.4    Huseby, D.L.5    Crawford, R.W.6
  • 66
    • 0037380969 scopus 로고    scopus 로고
    • CARD15/NOD2 functions as an antibacterial factor in human intestinal epithelial cells
    • doi:10.1053/gast.2003.50153
    • Hisamatsu T, Suzuki M, Reinecker HC, Nadeau WJ, McCormick BA, Podolsky DK. CARD15/NOD2 functions as an antibacterial factor in human intestinal epithelial cells. Gastroenterology (2003) 124(4):993-1000. doi:10.1053/gast.2003.50153
    • (2003) Gastroenterology , vol.124 , Issue.4 , pp. 993-1000
    • Hisamatsu, T.1    Suzuki, M.2    Reinecker, H.C.3    Nadeau, W.J.4    McCormick, B.A.5    Podolsky, D.K.6
  • 67
    • 84864094479 scopus 로고    scopus 로고
    • A dual role for receptor-interacting protein kinase 2 (RIP2) kinase activity in nucleotide-binding oligomerization domain 2 (NOD2)-dependent autophagy
    • doi:10.1074/jbc.M111.326835
    • Homer CR, Kabi A, Marina-Garcia N, Sreekumar A, Nesvizhskii AI, Nickerson KP, et al. A dual role for receptor-interacting protein kinase 2 (RIP2) kinase activity in nucleotide-binding oligomerization domain 2 (NOD2)-dependent autophagy. J Biol Chem (2012) 287(30):25565-76. doi:10.1074/jbc.M111.326835
    • (2012) J Biol Chem , vol.287 , Issue.30 , pp. 25565-25576
    • Homer, C.R.1    Kabi, A.2    Marina-Garcia, N.3    Sreekumar, A.4    Nesvizhskii, A.I.5    Nickerson, K.P.6
  • 68
    • 77950641148 scopus 로고    scopus 로고
    • MDP-NOD2 stimulation induces HNP-1 secretion, which contributes to NOD2 antibacterial function
    • doi:10.1002/ibd.21144
    • Yamamoto-Furusho JK, Barnich N, Hisamatsu T, Podolsky DK. MDP-NOD2 stimulation induces HNP-1 secretion, which contributes to NOD2 antibacterial function. Inflamm Bowel Dis (2010) 16(5):736-42. doi:10.1002/ibd.21144
    • (2010) Inflamm Bowel Dis , vol.16 , Issue.5 , pp. 736-742
    • Yamamoto-Furusho, J.K.1    Barnich, N.2    Hisamatsu, T.3    Podolsky, D.K.4
  • 69
    • 70349433671 scopus 로고    scopus 로고
    • Role of Nod1 in mucosal dendritic cells during Salmonella pathogenicity island 1-independent Salmonella enterica serovar typhimurium infection
    • doi:10.1128/IAI.00519-09
    • Le Bourhis L, Magalhaes JG, Selvanantham T, Travassos LH, Geddes K, Fritz JH, et al. Role of Nod1 in mucosal dendritic cells during Salmonella pathogenicity island 1-independent Salmonella enterica serovar typhimurium infection. Infect Immun (2009) 77(10):4480-6. doi:10.1128/IAI.00519-09
    • (2009) Infect Immun , vol.77 , Issue.10 , pp. 4480-4486
    • Le Bourhis, L.1    Magalhaes, J.G.2    Selvanantham, T.3    Travassos, L.H.4    Geddes, K.5    Fritz, J.H.6
  • 70
    • 84855221528 scopus 로고    scopus 로고
    • A Salmonella virulence factor activates the NOD1/NOD2 signaling pathway
    • doi: 10.1128/mBio.00266-11
    • Keestra AM, Winter MG, Klein-Douwel D, Xavier MN, Winter SE, Kim A, et al. A Salmonella virulence factor activates the NOD1/NOD2 signaling pathway. MBio (2011) 2(6). doi:10.1128/mBio.00266-11
    • (2011) MBio , vol.2 , Issue.6
    • Keestra, A.M.1    Winter, M.G.2    Klein-Douwel, D.3    Xavier, M.N.4    Winter, S.E.5    Kim, A.6
  • 71
    • 84872705482 scopus 로고    scopus 로고
    • Salmonella downregulates Nod-like receptor family CARD domain containing protein 4 expression to promote its survival in B cells by preventing inflammasome activation and cell death
    • doi:10.4049/jimmunol.1200415
    • Perez-Lopez A, Rosales-Reyes R, Alpuche-Aranda CM, Ortiz-Navarrete V. Salmonella downregulates Nod-like receptor family CARD domain containing protein 4 expression to promote its survival in B cells by preventing inflammasome activation and cell death. J Immunol (2013) 190(3):1201-9. doi:10.4049/jimmunol.1200415
    • (2013) J Immunol , vol.190 , Issue.3 , pp. 1201-1209
    • Perez-Lopez, A.1    Rosales-Reyes, R.2    Alpuche-Aranda, C.M.3    Ortiz-Navarrete, V.4
  • 72
    • 84855954988 scopus 로고    scopus 로고
    • NLRC4 inflammasomes in dendritic cells regulate noncognate effector function by memory CD8+ T cells
    • doi:10.1038/ni.2195
    • Kupz A, Guarda G, Gebhardt T, Sander LE, Short KR, Diavatopoulos DA, et al. NLRC4 inflammasomes in dendritic cells regulate noncognate effector function by memory CD8+ T cells. Nat Immunol (2012) 13(2):162-9. doi:10.1038/ni.2195
    • (2012) Nat Immunol , vol.13 , Issue.2 , pp. 162-169
    • Kupz, A.1    Guarda, G.2    Gebhardt, T.3    Sander, L.E.4    Short, K.R.5    Diavatopoulos, D.A.6
  • 73
    • 84867333450 scopus 로고    scopus 로고
    • Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
    • doi:10.1038/nature11419
    • Broz P, Ruby T, Belhocine K, Bouley DM, Kayagaki N, Dixit VM, et al. Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1. Nature (2012) 490(7419):288-91. doi:10.1038/nature11419
    • (2012) Nature , vol.490 , Issue.7419 , pp. 288-291
    • Broz, P.1    Ruby, T.2    Belhocine, K.3    Bouley, D.M.4    Kayagaki, N.5    Dixit, V.M.6
  • 74
    • 78649957904 scopus 로고    scopus 로고
    • Nod1 and Nod2 regulation of inflammation in the Salmonella colitis model
    • doi:10.1128/IAI.00759-10
    • Geddes K, Rubino S, Streutker C, Cho JH, Magalhaes JG, Le Bourhis L, et al. Nod1 and Nod2 regulation of inflammation in the Salmonella colitis model. Infect Immun (2010) 78(12):5107-15. doi:10.1128/IAI.00759-10
    • (2010) Infect Immun , vol.78 , Issue.12 , pp. 5107-5115
    • Geddes, K.1    Rubino, S.2    Streutker, C.3    Cho, J.H.4    Magalhaes, J.G.5    Le Bourhis, L.6
  • 75
    • 79960131814 scopus 로고    scopus 로고
    • Identification of an innate T helper type 17 response to intestinal bacterial pathogens
    • doi:10.1038/nm.2391
    • Geddes K, Rubino SJ, Magalhaes JG, Streutker C, Le Bourhis L, Cho JH, et al. Identification of an innate T helper type 17 response to intestinal bacterial pathogens. Nat Med (2011) 17(7):837-44. doi:10.1038/nm.2391
    • (2011) Nat Med , vol.17 , Issue.7 , pp. 837-844
    • Geddes, K.1    Rubino, S.J.2    Magalhaes, J.G.3    Streutker, C.4    Le Bourhis, L.5    Cho, J.H.6
  • 76
    • 70049109028 scopus 로고    scopus 로고
    • Salmonella typhimurium type III secretion effectors stimulate innate immune responses in cultured epithelial cells
    • doi:10.1371/journal.ppat.1000538
    • Bruno VM, Hannemann S, Lara-Tejero M, Flavell RA, Kleinstein SH, Galán JE. Salmonella typhimurium type III secretion effectors stimulate innate immune responses in cultured epithelial cells. PLoS Pathog (2009) 5(8):e1000538. doi:10.1371/journal.ppat.1000538
    • (2009) PLoS Pathog , vol.5 , Issue.8
    • Bruno, V.M.1    Hannemann, S.2    Lara-Tejero, M.3    Flavell, R.A.4    Kleinstein, S.H.5    Galán, J.E.6
  • 77
    • 33745012076 scopus 로고    scopus 로고
    • Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis
    • doi:10.1084/jem.20060206
    • Lara-Tejero M, Sutterwala FS, Ogura Y, Grant EP, Bertin J, Coyle AJ, et al. Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis. J Exp Med (2006) 203(6):1407-12. doi:10.1084/jem.20060206
    • (2006) J Exp Med , vol.203 , Issue.6 , pp. 1407-1412
    • Lara-Tejero, M.1    Sutterwala, F.S.2    Ogura, Y.3    Grant, E.P.4    Bertin, J.5    Coyle, A.J.6
  • 78
    • 33746583965 scopus 로고    scopus 로고
    • Caspase-1-mediated activation of interleukin-1β (IL-1β) and IL-18 contributes to innate immune defenses against Salmonella enterica serovar typhimurium infection
    • doi:10.1128/IAI.00417-06
    • Raupach B, Peuschel S-K, Monack DM, Zychlinsky A. Caspase-1-mediated activation of interleukin-1β (IL-1β) and IL-18 contributes to innate immune defenses against Salmonella enterica serovar typhimurium infection. Infect Immun (2006) 74(8):4922-6. doi:10.1128/IAI.00417-06
    • (2006) Infect Immun , vol.74 , Issue.8 , pp. 4922-4926
    • Raupach, B.1    Peuschel, S.-K.2    Monack, D.M.3    Zychlinsky, A.4
  • 79
    • 77955390094 scopus 로고    scopus 로고
    • Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella
    • doi:10.1084/jem.20100257
    • Broz P, Newton K, Lamkanfi M, Mariathasan S, Dixit VM, Monack DM. Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella. J Exp Med (2010) 207(8):1745-55. doi:10.1084/jem.20100257
    • (2010) J Exp Med , vol.207 , Issue.8 , pp. 1745-1755
    • Broz, P.1    Newton, K.2    Lamkanfi, M.3    Mariathasan, S.4    Dixit, V.M.5    Monack, D.M.6
  • 80
    • 84859862381 scopus 로고    scopus 로고
    • Cytosolic flagellin receptor NLRC4 protects mice against mucosal and systemic challenges
    • doi:10.1038/mi.2012.8
    • Carvalho FA, Nalbantoglu I, Aitken JD, Uchiyama R, Su Y, Doho GH, et al. Cytosolic flagellin receptor NLRC4 protects mice against mucosal and systemic challenges. Mucosal Immunol (2012) 5(3):288-98. doi:10.1038/mi.2012.8
    • (2012) Mucosal Immunol , vol.5 , Issue.3 , pp. 288-298
    • Carvalho, F.A.1    Nalbantoglu, I.2    Aitken, J.D.3    Uchiyama, R.4    Su, Y.5    Doho, G.H.6
  • 81
    • 78449269290 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
    • doi:10.1038/ni.1960
    • Miao EA, Leaf IA, Treuting PM, Mao DP, Dors M, Sarkar A, et al. Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat Immunol (2010) 11(12):1136-42. doi:10.1038/ni.1960
    • (2010) Nat Immunol , vol.11 , Issue.12 , pp. 1136-1142
    • Miao, E.A.1    Leaf, I.A.2    Treuting, P.M.3    Mao, D.P.4    Dors, M.5    Sarkar, A.6
  • 82
    • 78649605448 scopus 로고    scopus 로고
    • TLR5 or NLRC4 is necessary and sufficient for promotion of humoral immunity by flagellin
    • doi:10.1002/eji.201040421
    • Vijay Kumar M, Carvalho FA, Aitken JD, Fifadara NH, Gewirtz AT. TLR5 or NLRC4 is necessary and sufficient for promotion of humoral immunity by flagellin. Eur J Immunol (2010) 40(12):3528-34. doi:10.1002/eji.201040421
    • (2010) Eur J Immunol , vol.40 , Issue.12 , pp. 3528-3534
    • Vijay Kumar, M.1    Carvalho, F.A.2    Aitken, J.D.3    Fifadara, N.H.4    Gewirtz, A.T.5
  • 83
    • 84874189388 scopus 로고    scopus 로고
    • Caspase-11 protects against bacteria that escape the vacuole
    • doi:10.1126/science.1230751
    • Aachoui Y, Leaf IA, Hagar JA, Fontana MF, Campos CG, Zak DE, et al. Caspase-11 protects against bacteria that escape the vacuole. Science (2013) 339(6122):975-8. doi:10.1126/science.1230751
    • (2013) Science , vol.339 , Issue.6122 , pp. 975-978
    • Aachoui, Y.1    Leaf, I.A.2    Hagar, J.A.3    Fontana, M.F.4    Campos, C.G.5    Zak, D.E.6
  • 84
    • 84859911615 scopus 로고    scopus 로고
    • NLRC4-driven production of IL-1 [beta] discriminates between pathogenic and commensal bacteria and promotes host intestinal defense
    • doi:10.1038/ni.2263
    • Franchi L, Kamada N, Nakamura Y, Burberry A, Kuffa P, Suzuki S, et al. NLRC4-driven production of IL-1 [beta] discriminates between pathogenic and commensal bacteria and promotes host intestinal defense. Nat Immunol (2012) 13(5):449-56. doi:10.1038/ni.2263
    • (2012) Nat Immunol , vol.13 , Issue.5 , pp. 449-456
    • Franchi, L.1    Kamada, N.2    Nakamura, Y.3    Burberry, A.4    Kuffa, P.5    Suzuki, S.6
  • 85
    • 79951493901 scopus 로고    scopus 로고
    • LEEways: tales of EPEC, ATEC and EHEC
    • doi:10.1111/j.1462-5822.2010.01518.x
    • Schmidt MA. LEEways: tales of EPEC, ATEC and EHEC. Cell Microbiol (2010) 12(11):1544-52. doi:10.1111/j.1462-5822.2010.01518.x
    • (2010) Cell Microbiol , vol.12 , Issue.11 , pp. 1544-1552
    • Schmidt, M.A.1
  • 86
    • 28044461045 scopus 로고    scopus 로고
    • Citrobacter rodentium of mice and man
    • doi:10.1111/j.1462-5822.2005.00625.x
    • Mundy R, MacDonald TT, Dougan G, Frankel G, Wiles S. Citrobacter rodentium of mice and man. Cell Microbiol (2005) 7(12):1697-706. doi:10.1111/j.1462-5822.2005.00625.x
    • (2005) Cell Microbiol , vol.7 , Issue.12 , pp. 1697-1706
    • Mundy, R.1    MacDonald, T.T.2    Dougan, G.3    Frankel, G.4    Wiles, S.5
  • 87
    • 4544302531 scopus 로고    scopus 로고
    • Organ specificity, colonization and clearance dynamics in vivo following oral challenges with the murine pathogen Citrobacter rodentium
    • doi:10.1111/j.1462-5822.2004.00414.x
    • Wiles S, Clare S, Harker J, Huett A, Young D, Dougan G, et al. Organ specificity, colonization and clearance dynamics in vivo following oral challenges with the murine pathogen Citrobacter rodentium. Cell Microbiol (2004) 6(10):963-72. doi:10.1111/j.1462-5822.2004.00414.x
    • (2004) Cell Microbiol , vol.6 , Issue.10 , pp. 963-972
    • Wiles, S.1    Clare, S.2    Harker, J.3    Huett, A.4    Young, D.5    Dougan, G.6
  • 88
    • 35048845107 scopus 로고    scopus 로고
    • Cell attachment properties and infectivity of host-adapted and environmentally adapted Citrobacter rodentium
    • doi:10.1016/j.micinf.2007.06.006
    • Bishop AL, Wiles S, Dougan G, Frankel G. Cell attachment properties and infectivity of host-adapted and environmentally adapted Citrobacter rodentium. Microbes Infect (2007) 9(11):1316-24. doi:10.1016/j.micinf.2007.06.006
    • (2007) Microbes Infect , vol.9 , Issue.11 , pp. 1316-1324
    • Bishop, A.L.1    Wiles, S.2    Dougan, G.3    Frankel, G.4
  • 89
    • 77953583282 scopus 로고    scopus 로고
    • Virulence regulation in Citrobacter rodentium: the art of timing
    • doi:10.1111/j.1751-7915.2009.00114.x
    • Yang J, Tauschek M, Hart E, Hartland EL, Robins Browne RM. Virulence regulation in Citrobacter rodentium: the art of timing. Microb Biotechnol (2010) 3(3):259-68. doi:10.1111/j.1751-7915.2009.00114.x
    • (2010) Microb Biotechnol , vol.3 , Issue.3 , pp. 259-268
    • Yang, J.1    Tauschek, M.2    Hart, E.3    Hartland, E.L.4    Robins Browne, R.M.5
  • 90
    • 0034003289 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli (EPEC) attachment to epithelial cells: exploiting the host cell cytoskeleton from the outside
    • doi:10.1046/j.1462-5822.2000.00033.x
    • Celli J, Deng W, Finlay BB. Enteropathogenic Escherichia coli (EPEC) attachment to epithelial cells: exploiting the host cell cytoskeleton from the outside. Cell Microbiol (2000) 2(1):1-9. doi:10.1046/j.1462-5822.2000.00033.x
    • (2000) Cell Microbiol , vol.2 , Issue.1 , pp. 1-9
    • Celli, J.1    Deng, W.2    Finlay, B.B.3
  • 91
    • 40149084641 scopus 로고    scopus 로고
    • Caspase-12 modulates NOD signaling and regulates antimicrobial peptide production and mucosal immunity
    • doi:10.1016/j.chom.2008.02.004
    • LeBlanc PM, Yeretssian G, Rutherford N, Doiron K, Nadiri A, Zhu L, et al. Caspase-12 modulates NOD signaling and regulates antimicrobial peptide production and mucosal immunity. Cell Host Microbe (2008) 3(3):146-57. doi:10.1016/j.chom.2008.02.004
    • (2008) Cell Host Microbe , vol.3 , Issue.3 , pp. 146-157
    • LeBlanc, P.M.1    Yeretssian, G.2    Rutherford, N.3    Doiron, K.4    Nadiri, A.5    Zhu, L.6
  • 92
    • 79956319462 scopus 로고    scopus 로고
    • The Nod2 sensor promotes intestinal pathogen eradication via the chemokine CCL2-dependent recruitment of inflammatory monocytes
    • doi:10.1016/j.immuni.2011.04.013
    • Kim Y-G, Kamada N, Shaw MH, Warner N, Chen GY, Franchi L, et al. The Nod2 sensor promotes intestinal pathogen eradication via the chemokine CCL2-dependent recruitment of inflammatory monocytes. Immunity (2011) 34(5):769-80. doi:10.1016/j.immuni.2011.04.013
    • (2011) Immunity , vol.34 , Issue.5 , pp. 769-780
    • Kim, Y.-G.1    Kamada, N.2    Shaw, M.H.3    Warner, N.4    Chen, G.Y.5    Franchi, L.6
  • 93
    • 81355160488 scopus 로고    scopus 로고
    • The WxxxE effector EspT triggers expression of immune mediators in an Erk/JNK and NF-κB-dependent manner
    • doi:10.1111/j.1462-5822.2011.01666.x
    • Raymond B, Crepin VF, Collins JW, Frankel G. The WxxxE effector EspT triggers expression of immune mediators in an Erk/JNK and NF-κB-dependent manner. Cell Microbiol (2011) 13(12):1881-93. doi:10.1111/j.1462-5822.2011.01666.x
    • (2011) Cell Microbiol , vol.13 , Issue.12 , pp. 1881-1893
    • Raymond, B.1    Crepin, V.F.2    Collins, J.W.3    Frankel, G.4
  • 94
    • 84860859210 scopus 로고    scopus 로고
    • Role of inflammasomes in host defense against Citrobacter rodentium infection
    • doi:10.1074/jbc.M112.358705
    • Liu Z, Zaki MH, Vogel P, Gurung P, Finlay BB, Deng W, et al. Role of inflammasomes in host defense against Citrobacter rodentium infection. J Biol Chem (2012) 287(20):16955-64. doi:10.1074/jbc.M112.358705
    • (2012) J Biol Chem , vol.287 , Issue.20 , pp. 16955-16964
    • Liu, Z.1    Zaki, M.H.2    Vogel, P.3    Gurung, P.4    Finlay, B.B.5    Deng, W.6
  • 95
    • 60549106485 scopus 로고    scopus 로고
    • Interleukin-1 receptor signaling protects mice from lethal intestinal damage caused by the attaching and effacing pathogen Citrobacter rodentium
    • doi:10.1128/IAI.00907-08
    • Lebeis SL, Powell KR, Merlin D, Sherman MA, Kalman D. Interleukin-1 receptor signaling protects mice from lethal intestinal damage caused by the attaching and effacing pathogen Citrobacter rodentium. Infect Immun (2009) 77(2):604-14. doi:10.1128/IAI.00907-08
    • (2009) Infect Immun , vol.77 , Issue.2 , pp. 604-614
    • Lebeis, S.L.1    Powell, K.R.2    Merlin, D.3    Sherman, M.A.4    Kalman, D.5
  • 96
    • 84867241369 scopus 로고    scopus 로고
    • Toll or interleukin-1 receptor (TIR) domain-containing adaptor inducing interferon-β (TRIF)-mediated caspase-11 protease production integrates Toll-like receptor 4 (TLR4) protein-and Nlrp3 inflammasome-mediated host defense against enteropathogens
    • doi:10.1074/jbc.M112.401406
    • Gurung P, Malireddi RS, Anand PK, Demon D, Walle LV, Liu Z, et al. Toll or interleukin-1 receptor (TIR) domain-containing adaptor inducing interferon-β (TRIF)-mediated caspase-11 protease production integrates Toll-like receptor 4 (TLR4) protein-and Nlrp3 inflammasome-mediated host defense against enteropathogens. J Biol Chem (2012) 287(41):34474-83. doi:10.1074/jbc.M112.401406
    • (2012) J Biol Chem , vol.287 , Issue.41 , pp. 34474-34483
    • Gurung, P.1    Malireddi, R.S.2    Anand, P.K.3    Demon, D.4    Walle, L.V.5    Liu, Z.6
  • 97
    • 84883788152 scopus 로고    scopus 로고
    • Diagnosis and epidemiology of Helicobacter pylori infection
    • doi:10.1111/hel.12071
    • Calvet X, Ramírez Lázaro MJ, Lehours P, Mégraud F. Diagnosis and epidemiology of Helicobacter pylori infection. Helicobacter (2013) 18(s1):5-11. doi:10.1111/hel.12071
    • (2013) Helicobacter , vol.18 , Issue.S1 , pp. 5-11
    • Calvet, X.1    Ramírez Lázaro, M.J.2    Lehours, P.3    Mégraud, F.4
  • 98
    • 65449190100 scopus 로고    scopus 로고
    • Helicobacter pylori in health and disease
    • doi:10.1053/j.gastro.2009.01.073
    • Cover TL, Blaser MJ. Helicobacter pylori in health and disease. Gastroenterology (2009) 136(6):1863-73. doi:10.1053/j.gastro.2009.01.073
    • (2009) Gastroenterology , vol.136 , Issue.6 , pp. 1863-1873
    • Cover, T.L.1    Blaser, M.J.2
  • 99
    • 84878013732 scopus 로고    scopus 로고
    • Life in the human stomach: persistence strategies of the bacterial pathogen Helicobacter pylori
    • doi:10.1038/nrmicro3016
    • Salama NR, Hartung ML, Müller A. Life in the human stomach: persistence strategies of the bacterial pathogen Helicobacter pylori. Nat Rev Microbiol (2013) 11(6):385-99. doi:10.1038/nrmicro3016
    • (2013) Nat Rev Microbiol , vol.11 , Issue.6 , pp. 385-399
    • Salama, N.R.1    Hartung, M.L.2    Müller, A.3
  • 100
    • 78049354889 scopus 로고    scopus 로고
    • Helicobacter pylori and gastric cancer: factors that modulate disease risk
    • doi:10.1128/CMR.00011-10
    • Wroblewski LE, Peek RM, Wilson KT. Helicobacter pylori and gastric cancer: factors that modulate disease risk. Clin Microbiol Rev (2010) 23(4):713-39. doi:10.1128/CMR.00011-10
    • (2010) Clin Microbiol Rev , vol.23 , Issue.4 , pp. 713-739
    • Wroblewski, L.E.1    Peek, R.M.2    Wilson, K.T.3
  • 101
    • 70149122145 scopus 로고    scopus 로고
    • Helicobacter pylori moves through mucus by reducing mucin viscoelasticity
    • doi:10.1073/pnas.0903438106
    • Celli JP, Turner BS, Afdhal NH, Keates S, Ghiran I, Kelly CP, et al. Helicobacter pylori moves through mucus by reducing mucin viscoelasticity. Proc Natl Acad Sci U S A (2009) 106(34):14321-6. doi:10.1073/pnas.0903438106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.34 , pp. 14321-14326
    • Celli, J.P.1    Turner, B.S.2    Afdhal, N.H.3    Keates, S.4    Ghiran, I.5    Kelly, C.P.6
  • 102
    • 84855288788 scopus 로고    scopus 로고
    • Helicobacter pylori versus the host: remodeling of the bacterial outer membrane is required for survival in the gastric mucosa
    • doi:10.1371/journal.ppat.1002454
    • Cullen TW, Giles DK, Wolf LN, Ecobichon C, Boneca IG, Trent MS. Helicobacter pylori versus the host: remodeling of the bacterial outer membrane is required for survival in the gastric mucosa. PLoS Pathog (2011) 7(12):e1002454. doi:10.1371/journal.ppat.1002454
    • (2011) PLoS Pathog , vol.7 , Issue.12
    • Cullen, T.W.1    Giles, D.K.2    Wolf, L.N.3    Ecobichon, C.4    Boneca, I.G.5    Trent, M.S.6
  • 103
    • 2442678870 scopus 로고    scopus 로고
    • Helicobacter pylori flagellin evades toll-like receptor 5-mediated innate immunity
    • doi:10.1086/386289
    • Gewirtz AT, Yu Y, Krishna US, Israel DA, Lyons SL, Peek RM. Helicobacter pylori flagellin evades toll-like receptor 5-mediated innate immunity. J Infect Dis (2004) 189(10):1914-20. doi:10.1086/386289
    • (2004) J Infect Dis , vol.189 , Issue.10 , pp. 1914-1920
    • Gewirtz, A.T.1    Yu, Y.2    Krishna, U.S.3    Israel, D.A.4    Lyons, S.L.5    Peek, R.M.6
  • 104
    • 84874286760 scopus 로고    scopus 로고
    • Vacuolating cytotoxin A (VacA), a key toxin for Helicobacter pylori pathogenesis
    • doi:10.3389/fcimb.2012.00092
    • Palframan SL, Kwok T, Gabriel K. Vacuolating cytotoxin A (VacA), a key toxin for Helicobacter pylori pathogenesis. Front Cell Infect Microbiol (2012) 2:92. doi:10.3389/fcimb.2012.00092
    • (2012) Front Cell Infect Microbiol , vol.2 , pp. 92
    • Palframan, S.L.1    Kwok, T.2    Gabriel, K.3
  • 105
    • 33745033287 scopus 로고    scopus 로고
    • Influence of polymorphisms in the NOD1/CARD4 and NOD2/CARD15 genes on the clinical outcome of Helicobacter pylori infection
    • doi:10.1111/j.1462-5822.2006.00701.x
    • Rosenstiel P, Hellmig S, Hampe J, Ott S, Till A, Fischbach W, et al. Influence of polymorphisms in the NOD1/CARD4 and NOD2/CARD15 genes on the clinical outcome of Helicobacter pylori infection. Cell Microbiol (2006) 8(7):1188-98. doi:10.1111/j.1462-5822.2006.00701.x
    • (2006) Cell Microbiol , vol.8 , Issue.7 , pp. 1188-1198
    • Rosenstiel, P.1    Hellmig, S.2    Hampe, J.3    Ott, S.4    Till, A.5    Fischbach, W.6
  • 106
    • 33847063192 scopus 로고    scopus 로고
    • Genetic polymorphisms of NOD1 and IL-8, but not polymorphisms of TLR4 genes, are associated with Helicobacter pylori-induced duodenal ulcer and gastritis
    • doi:10.1111/j.1523-5378.2007.00481.x
    • Hofner P, Gyulai Z, Kiss ZF, Tiszai A, Tiszlavicz L, Toth G, et al. Genetic polymorphisms of NOD1 and IL-8, but not polymorphisms of TLR4 genes, are associated with Helicobacter pylori-induced duodenal ulcer and gastritis. Helicobacter (2007) 12(2):124-31. doi:10.1111/j.1523-5378.2007.00481.x
    • (2007) Helicobacter , vol.12 , Issue.2 , pp. 124-131
    • Hofner, P.1    Gyulai, Z.2    Kiss, Z.F.3    Tiszai, A.4    Tiszlavicz, L.5    Toth, G.6
  • 107
    • 77950183851 scopus 로고    scopus 로고
    • Influence of interleukin polymorphisms on development of gastric cancer and peptic ulcer
    • doi:10.3748/wjg.v16.i10.1188
    • Sugimoto M, Yamaoka Y, Furuta T. Influence of interleukin polymorphisms on development of gastric cancer and peptic ulcer. World J Gastroenterol (2010) 16(10):1188. doi:10.3748/wjg.v16.i10.1188
    • (2010) World J Gastroenterol , vol.16 , Issue.10 , pp. 1188
    • Sugimoto, M.1    Yamaoka, Y.2    Furuta, T.3
  • 108
    • 9244245293 scopus 로고    scopus 로고
    • Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island
    • doi:10.1038/ni1131
    • Viala J, Chaput C, Boneca IG, Cardona A, Girardin SE, Moran AP, et al. Nod1 responds to peptidoglycan delivered by the Helicobacter pylori cag pathogenicity island. Nat Immunol (2004) 5(11):1166-74. doi:10.1038/ni1131
    • (2004) Nat Immunol , vol.5 , Issue.11 , pp. 1166-1174
    • Viala, J.1    Chaput, C.2    Boneca, I.G.3    Cardona, A.4    Girardin, S.E.5    Moran, A.P.6
  • 109
    • 77950621399 scopus 로고    scopus 로고
    • Bacterial membrane vesicles deliver peptidoglycan to NOD1 in epithelial cells
    • doi:10.1111/j.1462-5822.2009.01404.x
    • Kaparakis M, Turnbull L, Carneiro L, Firth S, Coleman HA, Parkington HC, et al. Bacterial membrane vesicles deliver peptidoglycan to NOD1 in epithelial cells. Cell Microbiol (2010) 12(3):372-85. doi:10.1111/j.1462-5822.2009.01404.x
    • (2010) Cell Microbiol , vol.12 , Issue.3 , pp. 372-385
    • Kaparakis, M.1    Turnbull, L.2    Carneiro, L.3    Firth, S.4    Coleman, H.A.5    Parkington, H.C.6
  • 110
    • 84860342710 scopus 로고    scopus 로고
    • Caspase-1 has both proinflammatory and regulatory properties in Helicobacter infections, which are differentially mediated by its substrates IL-1β and IL-18
    • doi:10.4049/jimmunol.1103212
    • Hitzler I, Sayi A, Kohler E, Engler DB, Koch KN, Hardt W-D, et al. Caspase-1 has both proinflammatory and regulatory properties in Helicobacter infections, which are differentially mediated by its substrates IL-1β and IL-18. J Immunol (2012) 188(8):3594-602. doi:10.4049/jimmunol.1103212
    • (2012) J Immunol , vol.188 , Issue.8 , pp. 3594-3602
    • Hitzler, I.1    Sayi, A.2    Kohler, E.3    Engler, D.B.4    Koch, K.N.5    Hardt, W.-D.6
  • 111
    • 84885742487 scopus 로고    scopus 로고
    • The Cag pathogenicity island and interaction between TLR2/NOD2 and NLRP3 regulate IL-1β production in Helicobacter pylori infected dendritic cells
    • doi:10.1002/eji.201243281
    • Kim DJ, Park JH, Franchi L, Backert S, Núñez G. The Cag pathogenicity island and interaction between TLR2/NOD2 and NLRP3 regulate IL-1β production in Helicobacter pylori infected dendritic cells. Eur J Immunol (2013) 43(10):2650-8. doi:10.1002/eji.201243281
    • (2013) Eur J Immunol , vol.43 , Issue.10 , pp. 2650-2658
    • Kim, D.J.1    Park, J.H.2    Franchi, L.3    Backert, S.4    Núñez, G.5
  • 112
    • 84857885765 scopus 로고    scopus 로고
    • DC-derived IL-18 drives Treg differentiation, murine Helicobacter pylori-specific immune tolerance, and asthma protection
    • doi:10.1172/JCI61029
    • Oertli M, Sundquist M, Hitzler I, Engler DB, Arnold IC, Reuter S, et al. DC-derived IL-18 drives Treg differentiation, murine Helicobacter pylori-specific immune tolerance, and asthma protection. J Clin Invest (2012) 122(3):1082. doi:10.1172/JCI61029
    • (2012) J Clin Invest , vol.122 , Issue.3 , pp. 1082
    • Oertli, M.1    Sundquist, M.2    Hitzler, I.3    Engler, D.B.4    Arnold, I.C.5    Reuter, S.6
  • 113
    • 63849275746 scopus 로고    scopus 로고
    • Role of ASC in the mouse model of Helicobacter pylori infection
    • doi:10.1369/jhc.2008.952366
    • Benoit BN, Kobayashi M, Kawakubo M, Takeoka M, Sano K, Zou J, et al. Role of ASC in the mouse model of Helicobacter pylori infection. J Histochem Cytochem (2009) 57(4):327-38. doi:10.1369/jhc.2008.952366
    • (2009) J Histochem Cytochem , vol.57 , Issue.4 , pp. 327-338
    • Benoit, B.N.1    Kobayashi, M.2    Kawakubo, M.3    Takeoka, M.4    Sano, K.5    Zou, J.6
  • 114
    • 70449377200 scopus 로고    scopus 로고
    • Influence of inflammatory cytokine polymorphisms on eradication rates of Helicobacter pylori
    • doi:10.1111/j.1440-1746.2009.06047.x
    • Sugimoto M, Furuta T, Yamaoka Y. Influence of inflammatory cytokine polymorphisms on eradication rates of Helicobacter pylori. J Gastroenterol Hepatol (2009) 24(11):1725-32. doi:10.1111/j.1440-1746.2009.06047.x
    • (2009) J Gastroenterol Hepatol , vol.24 , Issue.11 , pp. 1725-1732
    • Sugimoto, M.1    Furuta, T.2    Yamaoka, Y.3
  • 116
    • 84878971321 scopus 로고    scopus 로고
    • Microbiota-induced activation of epithelial IL-6 signaling links inflammasome-driven inflammation with transmissible cancer
    • doi:10.1073/pnas.1307575110
    • Hu B, Elinav E, Huber S, Strowig T, Hao L, Hafemann A, et al. Microbiota-induced activation of epithelial IL-6 signaling links inflammasome-driven inflammation with transmissible cancer. Proc Natl Acad Sci U S A (2013) 110(24):9862-7. doi:10.1073/pnas.1307575110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.24 , pp. 9862-9867
    • Hu, B.1    Elinav, E.2    Huber, S.3    Strowig, T.4    Hao, L.5    Hafemann, A.6
  • 117
    • 84856957894 scopus 로고    scopus 로고
    • Inflammasome-mediated dysbiosis regulates progression of NAFLD and obesity
    • doi:10.1038/nature10809
    • Henao-Mejia J, Elinav E, Jin C, Hao L, Mehal WZ, Strowig T, et al. Inflammasome-mediated dysbiosis regulates progression of NAFLD and obesity. Nature (2012) 482(7384):179-85. doi:10.1038/nature10809
    • (2012) Nature , vol.482 , Issue.7384 , pp. 179-185
    • Henao-Mejia, J.1    Elinav, E.2    Jin, C.3    Hao, L.4    Mehal, W.Z.5    Strowig, T.6
  • 118
    • 56749146467 scopus 로고    scopus 로고
    • Lymphoid tissue genesis induced by commensals through NOD1 regulates intestinal homeostasis
    • doi:10.1038/nature07450
    • Bouskra D, Brézillon C, Bérard M, Werts C, Varona R, Boneca IG, et al. Lymphoid tissue genesis induced by commensals through NOD1 regulates intestinal homeostasis. Nature (2008) 456(7221):507-10. doi:10.1038/nature07450
    • (2008) Nature , vol.456 , Issue.7221 , pp. 507-510
    • Bouskra, D.1    Brézillon, C.2    Bérard, M.3    Werts, C.4    Varona, R.5    Boneca, I.G.6
  • 119
    • 84877292277 scopus 로고    scopus 로고
    • Nod1 and Nod2 signaling does not alter the composition of intestinal bacterial communities at homeostasis
    • doi:10.4161/gmic.24373
    • Robertson SJ, Zhou JY, Geddes K, Rubino SJ, Cho JH, Philpott DJ, et al. Nod1 and Nod2 signaling does not alter the composition of intestinal bacterial communities at homeostasis. Gut Microbes (2013) 4(3):222-31. doi:10.4161/gmic.24373
    • (2013) Gut Microbes , vol.4 , Issue.3 , pp. 222-231
    • Robertson, S.J.1    Zhou, J.Y.2    Geddes, K.3    Rubino, S.J.4    Cho, J.H.5    Philpott, D.J.6
  • 120
    • 84863987697 scopus 로고    scopus 로고
    • Commensal and probiotic bacteria influence intestinal barrier function and susceptibility to colitis in Nod1-/-; Nod2-/- mice
    • doi:10.1002/ibd.22848
    • Natividad JM, Petit V, Huang X, de Palma G, Jury J, Sanz Y, et al. Commensal and probiotic bacteria influence intestinal barrier function and susceptibility to colitis in Nod1-/-; Nod2-/- mice. Inflamm Bowel Dis (2012) 18(8):1434-46. doi:10.1002/ibd.22848
    • (2012) Inflamm Bowel Dis , vol.18 , Issue.8 , pp. 1434-1446
    • Natividad, J.M.1    Petit, V.2    Huang, X.3    de Palma, G.4    Jury, J.5    Sanz, Y.6
  • 121
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
    • doi:10.1038/35079107
    • Hugot J-P, Chamaillard M, Zouali H, Lesage S, Cézard J-P, Belaiche J, et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature (2001) 411(6837):599-603. doi:10.1038/35079107
    • (2001) Nature , vol.411 , Issue.6837 , pp. 599-603
    • Hugot, J.-P.1    Chamaillard, M.2    Zouali, H.3    Lesage, S.4    Cézard, J.-P.5    Belaiche, J.6
  • 122
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
    • doi:10.1038/35079114
    • Ogura Y, Bonen DK, Inohara N, Nicolae DL, Chen FF, Ramos R, et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature (2001) 411(6837):603-6. doi:10.1038/35079114
    • (2001) Nature , vol.411 , Issue.6837 , pp. 603-606
    • Ogura, Y.1    Bonen, D.K.2    Inohara, N.3    Nicolae, D.L.4    Chen, F.F.5    Ramos, R.6
  • 123
    • 77957588986 scopus 로고    scopus 로고
    • Association of NOD1 (CARD4) insertion/deletion polymorphism with susceptibility to IBD: a meta-analysis
    • doi:10.3748/wjg.v16.i34.4348
    • Lu W-G, Zou Y-F, Feng X-L, Yuan F-L, Gu Y-L, Li X, et al. Association of NOD1 (CARD4) insertion/deletion polymorphism with susceptibility to IBD: a meta-analysis. World J Gastroenterol (2010) 16(34):4348. doi:10.3748/wjg.v16.i34.4348
    • (2010) World J Gastroenterol , vol.16 , Issue.34 , pp. 4348
    • Lu, W.-G.1    Zou, Y.-F.2    Feng, X.-L.3    Yuan, F.-L.4    Gu, Y.-L.5    Li, X.6
  • 124
    • 79955846705 scopus 로고    scopus 로고
    • NLRP3 inflammasome plays a key role in the regulation of intestinal homeostasis
    • doi:10.1002/ibd.21478
    • Hirota SA, Ng J, Lueng A, Khajah M, Parhar K, Li Y, et al. NLRP3 inflammasome plays a key role in the regulation of intestinal homeostasis. Inflamm Bowel Dis (2011) 17(6):1359-72. doi:10.1002/ibd.21478
    • (2011) Inflamm Bowel Dis , vol.17 , Issue.6 , pp. 1359-1372
    • Hirota, S.A.1    Ng, J.2    Lueng, A.3    Khajah, M.4    Parhar, K.5    Li, Y.6
  • 125
    • 77950002937 scopus 로고    scopus 로고
    • The NLRP3 inflammasome protects against loss of epithelial integrity and mortality during experimental colitis
    • doi:10.1016/j.immuni.2010.03.003
    • Zaki MH, Boyd KL, Vogel P, Kastan MB, Lamkanfi M, Kanneganti T-D. The NLRP3 inflammasome protects against loss of epithelial integrity and mortality during experimental colitis. Immunity (2010) 32(3):379-91. doi:10.1016/j.immuni.2010.03.003
    • (2010) Immunity , vol.32 , Issue.3 , pp. 379-391
    • Zaki, M.H.1    Boyd, K.L.2    Vogel, P.3    Kastan, M.B.4    Lamkanfi, M.5    Kanneganti, T.-D.6
  • 126
    • 77952303410 scopus 로고    scopus 로고
    • The NLRP3 inflammasome functions as a negative regulator of tumorigenesis during colitis-associated cancer
    • doi:10.1084/jem.20100050
    • Allen IC, TeKippe EM, Woodford R-MT, Uronis JM, Holl EK, Rogers AB, et al. The NLRP3 inflammasome functions as a negative regulator of tumorigenesis during colitis-associated cancer. J Exp Med (2010) 207(5):1045-56. doi:10.1084/jem.20100050
    • (2010) J Exp Med , vol.207 , Issue.5 , pp. 1045-1056
    • Allen, I.C.1    TeKippe, E.M.2    Woodford, R.-M.T.3    Uronis, J.M.4    Holl, E.K.5    Rogers, A.B.6
  • 127
    • 77956128040 scopus 로고    scopus 로고
    • Colitis induced in mice with dextran sulfate sodium (DSS) is mediated by the NLRP3 inflammasome
    • doi:10.1136/gut.2009.197822
    • Bauer C, Duewell P, Mayer C, Lehr HA, Fitzgerald KA, Dauer M, et al. Colitis induced in mice with dextran sulfate sodium (DSS) is mediated by the NLRP3 inflammasome. Gut (2010) 59(9):1192-9. doi:10.1136/gut.2009.197822
    • (2010) Gut , vol.59 , Issue.9 , pp. 1192-1199
    • Bauer, C.1    Duewell, P.2    Mayer, C.3    Lehr, H.A.4    Fitzgerald, K.A.5    Dauer, M.6
  • 128
    • 84867716442 scopus 로고    scopus 로고
    • Protective and aggravating effects of NLRP3 inflammasome activation in IBD models: influence of genetic and environmental factors
    • doi:10.1159/000341681
    • Bauer C, Duewell P, Lehr H-A, Endres S, Schnurr M. Protective and aggravating effects of NLRP3 inflammasome activation in IBD models: influence of genetic and environmental factors. Dig Dis (2012) 30(Suppl 1):82-90. doi:10.1159/000341681
    • (2012) Dig Dis , vol.30 , Issue.SUPPL. 1 , pp. 82-90
    • Bauer, C.1    Duewell, P.2    Lehr, H.-A.3    Endres, S.4    Schnurr, M.5
  • 129
    • 58149159542 scopus 로고    scopus 로고
    • Common variants in the NLRP3 region contribute to Crohn's disease susceptibility
    • doi:10.1038/ng.285
    • Villani A-C, Lemire M, Fortin G, Louis E, Silverberg MS, Collette C, et al. Common variants in the NLRP3 region contribute to Crohn's disease susceptibility. Nat Genet (2008) 41(1):71-6. doi:10.1038/ng.285
    • (2008) Nat Genet , vol.41 , Issue.1 , pp. 71-76
    • Villani, A.-C.1    Lemire, M.2    Fortin, G.3    Louis, E.4    Silverberg, M.S.5    Collette, C.6
  • 130
    • 66949174089 scopus 로고    scopus 로고
    • Combined polymorphisms in genes encoding the inflammasome components NALP3 and CARD8 confer susceptibility to Crohn's disease in Swedish men
    • doi:10.1038/ajg.2009.29
    • Schoultz I, Verma D, Halfvarsson J, Törkvist L, Fredrikson M, Sjöqvist U, et al. Combined polymorphisms in genes encoding the inflammasome components NALP3 and CARD8 confer susceptibility to Crohn's disease in Swedish men. Am J Gastroenterol (2009) 104(5):1180-8. doi:10.1038/ajg.2009.29
    • (2009) Am J Gastroenterol , vol.104 , Issue.5 , pp. 1180-1188
    • Schoultz, I.1    Verma, D.2    Halfvarsson, J.3    Törkvist, L.4    Fredrikson, M.5    Sjöqvist, U.6
  • 131
    • 79955825352 scopus 로고    scopus 로고
    • Genetic association between NLRP3 variants and Crohn's disease does not replicate in a large UK panel
    • doi:10.1002/ibd.21499
    • Lewis GJ, Massey DC, Zhang H, Bredin F, Tremelling M, Lee JC, et al. Genetic association between NLRP3 variants and Crohn's disease does not replicate in a large UK panel. Inflamm Bowel Dis (2011) 17(6):1387-91. doi:10.1002/ibd.21499
    • (2011) Inflamm Bowel Dis , vol.17 , Issue.6 , pp. 1387-1391
    • Lewis, G.J.1    Massey, D.C.2    Zhang, H.3    Bredin, F.4    Tremelling, M.5    Lee, J.C.6


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