메뉴 건너뛰기




Volumn 4, Issue NOV, 2013, Pages

The interplay between NLRs and autophagy in immunity and inflammation

Author keywords

Autophagy; Crohn's disease; Infection; Inflammasomes; Inflammation; Innate immunity; NLR proteins

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; CASPASE RECRUITMENT DOMAIN PROTEIN 4; CRYOPYRIN; INFLAMMASOME; INTERLEUKIN 18; INTERLEUKIN 1BETA; NEURONAL APOPTOSIS INHIBITORY PROTEIN; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; REACTIVE OXYGEN METABOLITE; UBIQUITIN;

EID: 84890335338     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2013.00361     Document Type: Review
Times cited : (47)

References (159)
  • 1
    • 0034661989 scopus 로고    scopus 로고
    • Invasive Shigella flexneri activates NF-kappa B through a lipopolysaccharide-dependent innate intracellular response and leads to IL-8 expression in epithelial cells
    • Philpott DJ, Yamaoka S, Israel A, Sansonetti PJ. Invasive Shigella flexneri activates NF-kappa B through a lipopolysaccharide-dependent innate intracellular response and leads to IL-8 expression in epithelial cells. J Immunol (2000) 165:903-14.
    • (2000) J Immunol , vol.165 , pp. 903-914
    • Philpott, D.J.1    Yamaoka, S.2    Israel, A.3    Sansonetti, P.J.4
  • 2
    • 33846330896 scopus 로고    scopus 로고
    • Nod-like proteins in immunity, inflammation and disease
    • doi: 10.1038/ni1412
    • Fritz JH, Ferrero RL, Philpott DJ, Girardin SE. Nod-like proteins in immunity, inflammation and disease. Nat Immunol (2006) 7:1250-7. doi: 10.1038/ni1412
    • (2006) Nat Immunol , vol.7 , pp. 1250-1257
    • Fritz, J.H.1    Ferrero, R.L.2    Philpott, D.J.3    Girardin, S.E.4
  • 3
    • 84857062410 scopus 로고    scopus 로고
    • A new eye on NLR proteins: focused on clarity or diffused by complexity?
    • doi:10.1016/j.coi.2011.12.006
    • Bonardi V, Cherkis K, Nishimura MT, Dangl JL. A new eye on NLR proteins: focused on clarity or diffused by complexity? Curr Opin Immunol (2012) 24:41-50. doi:10.1016/j.coi.2011.12.006
    • (2012) Curr Opin Immunol , vol.24 , pp. 41-50
    • Bonardi, V.1    Cherkis, K.2    Nishimura, M.T.3    Dangl, J.L.4
  • 4
    • 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) 278:8869-72. doi:10.1074/jbc.C200651200
    • (2003) J Biol Chem , vol.278 , pp. 8869-8872
    • Girardin, S.E.1    Boneca, I.G.2    Viala, J.3    Chamaillard, M.4    Labigne, A.5    Thomas, G.6
  • 5
    • 0037458665 scopus 로고    scopus 로고
    • Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease
    • doi:10.1074/jbc.C200673200
    • Inohara N, Ogura Y, Fontalba A, Gutierrez O, Pons F, Crespo J, et al. Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease. J Biol Chem (2003) 278:5509-12. doi:10.1074/jbc.C200673200
    • (2003) J Biol Chem , vol.278 , pp. 5509-5512
    • Inohara, N.1    Ogura, Y.2    Fontalba, A.3    Gutierrez, O.4    Pons, F.5    Crespo, J.6
  • 7
    • 27744606975 scopus 로고    scopus 로고
    • Nod1 participates in the innate immune response to Pseudomonas aeruginosa
    • doi:10.1074/jbc.M501649200
    • Travassos LH, Carneiro LAM, Girardin SE, Boneca IG, Lemos R, Bozza MT, et al. Nod1 participates in the innate immune response to Pseudomonas aeruginosa. J Biol Chem (2005) 280:36714-8. doi:10.1074/jbc.M501649200
    • (2005) J Biol Chem , vol.280 , pp. 36714-36718
    • Travassos, L.H.1    Carneiro, L.A.M.2    Girardin, S.E.3    Boneca, I.G.4    Lemos, R.5    Bozza, M.T.6
  • 8
    • 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 LAM, Antignac A, Jéhanno M, Viala J, et al. Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan. Science (2003) 300:1584-7. doi:10.1126/science.1084677
    • (2003) Science , vol.300 , pp. 1584-1587
    • Girardin, S.E.1    Boneca, I.G.2    Carneiro, L.A.M.3    Antignac, A.4    Jéhanno, M.5    Viala, J.6
  • 9
    • 0038824980 scopus 로고    scopus 로고
    • An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
    • doi:10.1038/ni945
    • Chamaillard M, Hashimoto M, Horie Y, Masumoto J, Qiu S, Saab L, et al. An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nat Immunol (2003) 4:702-7. doi:10.1038/ni945
    • (2003) Nat Immunol , vol.4 , pp. 702-707
    • Chamaillard, M.1    Hashimoto, M.2    Horie, Y.3    Masumoto, J.4    Qiu, S.5    Saab, L.6
  • 10
    • 12444259829 scopus 로고    scopus 로고
    • Muramyldipeptide and diaminopimelic acid-containing desmuramylpeptides in combination with chemically synthesized toll-like receptor agonists synergistically induced production of interleukin-8 in a NOD2-and NOD1-dependent manner, respectively, in human monocytic cells in culture
    • doi:10.1111/j.1462-5822.2004.00433.x
    • Uehara A, Yang S, Fujimoto Y, Fukase K, Kusumoto S, Shibata K, et al. Muramyldipeptide and diaminopimelic acid-containing desmuramylpeptides in combination with chemically synthesized toll-like receptor agonists synergistically induced production of interleukin-8 in a NOD2-and NOD1-dependent manner, respectively, in human monocytic cells in culture. Cell Microbiol (2005) 7:53-61. doi:10.1111/j.1462-5822.2004.00433.x
    • (2005) Cell Microbiol , vol.7 , pp. 53-61
    • Uehara, A.1    Yang, S.2    Fujimoto, Y.3    Fukase, K.4    Kusumoto, S.5    Shibata, K.6
  • 11
    • 28544434876 scopus 로고    scopus 로고
    • Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin
    • doi:10.1038/sj.embor.7400552
    • Magalhaes JG, Philpott DJ, Nahori M-A, Jéhanno M, Fritz J, Bourhis LL, et al. Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin. EMBO Rep (2005) 6:1201-7. doi:10.1038/sj.embor.7400552
    • (2005) EMBO Rep , vol.6 , pp. 1201-1207
    • Magalhaes, J.G.1    Philpott, D.J.2    Nahori, M.-A.3    Jéhanno, M.4    Fritz, J.5    Bourhis, L.L.6
  • 12
    • 33746210219 scopus 로고    scopus 로고
    • Meso-diaminopimelic acid and meso-lanthionine, amino acids specific to bacterial peptidoglycans, activate human epithelial cells through NOD1
    • Uehara A, Fujimoto Y, Kawasaki A, Kusumoto S, Fukase K, Takada H. Meso-diaminopimelic acid and meso-lanthionine, amino acids specific to bacterial peptidoglycans, activate human epithelial cells through NOD1. J Immunol (2006) 177:1796-804.
    • (2006) J Immunol , vol.177 , pp. 1796-1804
    • Uehara, A.1    Fujimoto, Y.2    Kawasaki, A.3    Kusumoto, S.4    Fukase, K.5    Takada, H.6
  • 13
    • 33749384363 scopus 로고    scopus 로고
    • Differential release and distribution of Nod1 and Nod2 immunostimulatory molecules among bacterial species and environments
    • doi:10.1074/jbc.M602638200
    • Hasegawa M, Yang K, Hashimoto M, Park J-H, Kim Y-G, Fujimoto Y, et al. Differential release and distribution of Nod1 and Nod2 immunostimulatory molecules among bacterial species and environments. J Biol Chem (2006) 281:29054-63. doi:10.1074/jbc.M602638200
    • (2006) J Biol Chem , vol.281 , pp. 29054-29063
    • Hasegawa, M.1    Yang, K.2    Hashimoto, M.3    Park, J.-H.4    Kim, Y.-G.5    Fujimoto, Y.6
  • 14
    • 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) 77:4480-6. doi:10.1128/IAI.00519-09
    • (2009) Infect Immun , vol.77 , 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
  • 15
    • 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) 5:1166-74. doi:10.1038/ni1131
    • (2004) Nat Immunol , vol.5 , pp. 1166-1174
    • Viala, J.1    Chaput, C.2    Boneca, I.G.3    Cardona, A.4    Girardin, S.E.5    Moran, A.P.6
  • 16
    • 84874099046 scopus 로고    scopus 로고
    • Nod1, but not the ASC inflammasome, contributes to induction of IL-1β secretion in human trophoblasts after sensing of Chlamydia trachomatis
    • doi:10.1038/mi.2012.63
    • Kavathas PB, Boeras CM, Mulla MJ, Abrahams VM. Nod1, but not the ASC inflammasome, contributes to induction of IL-1β secretion in human trophoblasts after sensing of Chlamydia trachomatis. Mucosal Immunol (2013) 6:235-43. doi:10.1038/mi.2012.63
    • (2013) Mucosal Immunol , vol.6 , pp. 235-243
    • Kavathas, P.B.1    Boeras, C.M.2    Mulla, M.J.3    Abrahams, V.M.4
  • 17
    • 46449093146 scopus 로고    scopus 로고
    • The cytosolic pattern recognition receptor NOD1 induces inflammatory interleukin-8 during Chlamydia trachomatis infection
    • doi:10.1128/IAI.00104-08
    • Buchholz KR, Stephens RS. The cytosolic pattern recognition receptor NOD1 induces inflammatory interleukin-8 during Chlamydia trachomatis infection. Infect Immun (2008) 76:3150-5. doi:10.1128/IAI.00104-08
    • (2008) Infect Immun , vol.76 , pp. 3150-3155
    • Buchholz, K.R.1    Stephens, R.S.2
  • 18
    • 33646382812 scopus 로고    scopus 로고
    • Stimulation of the cytosolic receptor for peptidoglycan, Nod1, by infection with Chlamydia trachomatis or Chlamydia muridarum
    • doi:10.1111/j.1462-5822.2006.00686.x
    • Welter-Stahl L, Ojcius DM, Viala J, Girardin S, Liu W, Delarbre C, et al. Stimulation of the cytosolic receptor for peptidoglycan, Nod1, by infection with Chlamydia trachomatis or Chlamydia muridarum. Cell Microbiol (2006) 8:1047-57. doi:10.1111/j.1462-5822.2006.00686.x
    • (2006) Cell Microbiol , vol.8 , pp. 1047-1057
    • Welter-Stahl, L.1    Ojcius, D.M.2    Viala, J.3    Girardin, S.4    Liu, W.5    Delarbre, C.6
  • 19
    • 14044268789 scopus 로고    scopus 로고
    • Nod1-mediated endothelial cell activation by Chlamydophila pneumoniae
    • doi:10.1161/01.RES.0000155721.83594.2c
    • Opitz B. Nod1-mediated endothelial cell activation by Chlamydophila pneumoniae. Circ Res (2005) 96:319-26. doi:10.1161/01.RES.0000155721.83594.2c
    • (2005) Circ Res , vol.96 , pp. 319-326
    • Opitz, B.1
  • 20
    • 34250888664 scopus 로고    scopus 로고
    • Nod1/RICK and TLR signaling regulate chemokine and antimicrobial innate immune responses in mesothelial cells
    • Park J-H, Kim Y-G, Shaw M, Kanneganti T-D, Fujimoto Y, Fukase K, et al. Nod1/RICK and TLR signaling regulate chemokine and antimicrobial innate immune responses in mesothelial cells. J Immunol (2007) 179:514-21.
    • (2007) J Immunol , vol.179 , pp. 514-521
    • Park, J.-H.1    Kim, Y.-G.2    Shaw, M.3    Kanneganti, T.-D.4    Fujimoto, Y.5    Fukase, K.6
  • 21
    • 56149111709 scopus 로고    scopus 로고
    • Cross-tolerization between Nod1 and Nod2 signaling results in reduced refractoriness to bacterial infection in Nod2-deficient macrophages
    • Kim Y-G, Park J-H, Daignault S, Fukase K, Nuñez G. Cross-tolerization between Nod1 and Nod2 signaling results in reduced refractoriness to bacterial infection in Nod2-deficient macrophages. J Immunol (2008) 181:4340-6.
    • (2008) J Immunol , vol.181 , pp. 4340-4346
    • Kim, Y.-G.1    Park, J.-H.2    Daignault, S.3    Fukase, K.4    Nuñez, G.5
  • 22
    • 29644434743 scopus 로고    scopus 로고
    • Listeria monocytogenes activated p38 MAPK and induced IL-8 secretion in a nucleotide-binding oligomerization domain 1-dependent manner in endothelial cells
    • Opitz B, Püschel A, Beermann W, Hocke AC, Förster S, Schmeck B, et al. Listeria monocytogenes activated p38 MAPK and induced IL-8 secretion in a nucleotide-binding oligomerization domain 1-dependent manner in endothelial cells. J Immunol (2006) 176:484-90.
    • (2006) J Immunol , vol.176 , pp. 484-490
    • Opitz, B.1    Püschel, A.2    Beermann, W.3    Hocke, A.C.4    Förster, S.5    Schmeck, B.6
  • 23
    • 1342344961 scopus 로고    scopus 로고
    • Nod1 is an essential signal transducer in intestinal epithelial cells infected with bacteria that avoid recognition by toll-like receptors
    • doi:10.1128/IAI.72.3.1487-1495.2004
    • Kim JG, Lee SJ, Kagnoff MF. Nod1 is an essential signal transducer in intestinal epithelial cells infected with bacteria that avoid recognition by toll-like receptors. Infect Immun (2004) 72:1487-95. doi:10.1128/IAI.72.3.1487-1495.2004
    • (2004) Infect Immun , vol.72 , pp. 1487-1495
    • Kim, J.G.1    Lee, S.J.2    Kagnoff, M.F.3
  • 24
    • 17944380130 scopus 로고    scopus 로고
    • CARD4/Nod1 mediates NF-κB and JNK activation by invasive Shigella flexneri
    • doi:10.1093/embo-reports/kve155
    • Girardin SE, Tournebize R, Mavris M, Page AL, Li X. CARD4/Nod1 mediates NF-κB and JNK activation by invasive Shigella flexneri. EMBO Rep (2001) 2(8):736-42. doi:10.1093/embo-reports/kve155
    • (2001) EMBO Rep , vol.2 , Issue.8 , pp. 736-742
    • Girardin, S.E.1    Tournebize, R.2    Mavris, M.3    Page, A.L.4    Li, X.5
  • 25
    • 60649120752 scopus 로고    scopus 로고
    • Shigella induces mitochondrial dysfunction and cell death in nonmyleoid cells
    • doi:10.1016/j.chom.2008.12.011
    • Carneiro LAM, Travassos LH, Soares F, Tattoli I, Magalhaes JG, Bozza MT, et al. Shigella induces mitochondrial dysfunction and cell death in nonmyleoid cells. Cell Host Microbe (2009) 5:123-36. doi:10.1016/j.chom.2008.12.011
    • (2009) Cell Host Microbe , vol.5 , pp. 123-136
    • Carneiro, L.A.M.1    Travassos, L.H.2    Soares, F.3    Tattoli, I.4    Magalhaes, J.G.5    Bozza, M.T.6
  • 26
    • 77955424978 scopus 로고    scopus 로고
    • Campylobacter jejuni activates NF-kappaB independently of TLR2, TLR4, Nod1 and Nod2 receptors
    • doi:10.1016/j.micpath.2010.06.011
    • Al-Sayeqh AF, Loughlin MF, Dillon E, Mellits KH, Connerton IF. Campylobacter jejuni activates NF-kappaB independently of TLR2, TLR4, Nod1 and Nod2 receptors. Microb Pathog (2010) 49:294-304. doi:10.1016/j.micpath.2010.06.011
    • (2010) Microb Pathog , vol.49 , pp. 294-304
    • Al-Sayeqh, A.F.1    Loughlin, M.F.2    Dillon, E.3    Mellits, K.H.4    Connerton, I.F.5
  • 27
    • 34548425221 scopus 로고    scopus 로고
    • A major role for intestinal epithelial nucleotide oligomerization domain 1 (NOD1) in eliciting host bactericidal immune responses to Campylobacter jejuni
    • doi:10.1111/j.1462-5822.2007.01008.x
    • Zilbauer M, Dorrell N, Elmi A, Lindley KJ, Schüller S, Jones HE, et al. A major role for intestinal epithelial nucleotide oligomerization domain 1 (NOD1) in eliciting host bactericidal immune responses to Campylobacter jejuni. Cell Microbiol (2007) 9:2404-16. doi:10.1111/j.1462-5822.2007.01008.x
    • (2007) Cell Microbiol , vol.9 , pp. 2404-2416
    • Zilbauer, M.1    Dorrell, N.2    Elmi, A.3    Lindley, K.J.4    Schüller, S.5    Jones, H.E.6
  • 28
    • 77949326831 scopus 로고    scopus 로고
    • Cutting edge: nucleotide-binding oligomerization domain 1-dependent responses account for murine resistance against Trypanosoma cruzi infection
    • doi:10.4049/jimmunol.0902254
    • Silva GK, Gutierrez FRS, Guedes PMM, Horta CV, Cunha LD, Mineo TWP, et al. Cutting edge: nucleotide-binding oligomerization domain 1-dependent responses account for murine resistance against Trypanosoma cruzi infection. J Immunol (2010) 184:1148-52. doi:10.4049/jimmunol.0902254
    • (2010) J Immunol , vol.184 , pp. 1148-1152
    • Silva, G.K.1    Gutierrez, F.R.S.2    Guedes, P.M.M.3    Horta, C.V.4    Cunha, L.D.5    Mineo, T.W.P.6
  • 31
    • 77951073629 scopus 로고    scopus 로고
    • NOD2 and toll-like receptors are nonredundant recognition systems of Mycobacterium tuberculosis
    • doi:10.1371/journal.ppat.0010034
    • Ferwerda G, Girardin SE, Kullberg B-J, Le Bourhis L, de Jong DJ, Langenberg DML, et al. NOD2 and toll-like receptors are nonredundant recognition systems of Mycobacterium tuberculosis. PLoS Pathog (2005) 1:e34. doi:10.1371/journal.ppat.0010034
    • (2005) PLoS Pathog , vol.1
    • Ferwerda, G.1    Girardin, S.E.2    Kullberg, B.-J.3    Le Bourhis, L.4    de Jong, D.J.5    Langenberg, D.M.L.6
  • 32
    • 58149189054 scopus 로고    scopus 로고
    • NOD2-deficient mice have impaired resistance to Mycobacterium tuberculosis infection through defective innate and adaptive immunity
    • Divangahi M, Mostowy S, Coulombe F, Kozak R, Guillot L, Veyrier F, et al. NOD2-deficient mice have impaired resistance to Mycobacterium tuberculosis infection through defective innate and adaptive immunity. J Immunol (2008) 181:7157-65.
    • (2008) J Immunol , vol.181 , pp. 7157-7165
    • Divangahi, M.1    Mostowy, S.2    Coulombe, F.3    Kozak, R.4    Guillot, L.5    Veyrier, F.6
  • 33
    • 7944220803 scopus 로고    scopus 로고
    • Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition
    • doi:10.1038/sj.embor.7400248
    • Travassos LH, Girardin SE, Philpott DJ, Blanot D, Nahori M-A, Werts C, et al. Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition. EMBO Rep (2004) 5:1000-6. doi:10.1038/sj.embor.7400248
    • (2004) EMBO Rep , vol.5 , pp. 1000-1006
    • Travassos, L.H.1    Girardin, S.E.2    Philpott, D.J.3    Blanot, D.4    Nahori, M.-A.5    Werts, C.6
  • 34
    • 77952574671 scopus 로고    scopus 로고
    • NOD2 mediates inflammatory responses of primary murine glia to Streptococcus pneumoniae
    • doi:10.1002/glia.20968
    • Liu X, Chauhan VS, Young AB, Marriott I. NOD2 mediates inflammatory responses of primary murine glia to Streptococcus pneumoniae. Glia (2010) 58:839-47. doi:10.1002/glia.20968
    • (2010) Glia , vol.58 , pp. 839-847
    • Liu, X.1    Chauhan, V.S.2    Young, A.B.3    Marriott, I.4
  • 35
    • 33646941554 scopus 로고    scopus 로고
    • Role for erbin in bacterial activation of Nod2
    • doi:10.1128/IAI.00035-06
    • Kufer TA, Kremmer E, Banks DJ, Philpott DJ. Role for erbin in bacterial activation of Nod2. Infect Immun (2006) 74:3115-24. doi:10.1128/IAI.00035-06
    • (2006) Infect Immun , vol.74 , pp. 3115-3124
    • Kufer, T.A.1    Kremmer, E.2    Banks, D.J.3    Philpott, D.J.4
  • 36
    • 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):e00266-11. 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
  • 37
    • 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 H-C, Nadeau WJ, McCormick BA, Podolsky DK. CARD15/NOD2 functions as an antibacterial factor in human intestinal epithelial cells. Gastroenterology (2003) 124:993-1000. doi:10.1053/gast.2003.50153
    • (2003) Gastroenterology , vol.124 , 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
  • 38
    • 84864007849 scopus 로고    scopus 로고
    • Control of viral latency in neurons by axonal mTOR signaling and the 4E-BP translation repressor
    • doi:10.1101/gad.190157.112
    • Kobayashi M, Wilson AC, Chao MV, Mohr I. Control of viral latency in neurons by axonal mTOR signaling and the 4E-BP translation repressor. Genes Dev (2012) 26:1527-32. doi:10.1101/gad.190157.112
    • (2012) Genes Dev , vol.26 , pp. 1527-1532
    • Kobayashi, M.1    Wilson, A.C.2    Chao, M.V.3    Mohr, I.4
  • 39
    • 7944232105 scopus 로고    scopus 로고
    • Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome
    • doi:10.1016/j.cub.2004.10.027
    • Martinon F, Agostini L, Meylan E, Tschopp J. Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome. Curr Biol (2004) 14(21):1929-34. doi:10.1016/j.cub.2004.10.027
    • (2004) Curr Biol , vol.14 , Issue.21 , pp. 1929-1934
    • Martinon, F.1    Agostini, L.2    Meylan, E.3    Tschopp, J.4
  • 40
    • 32944462834 scopus 로고    scopus 로고
    • Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
    • doi:10.1038/nature04517
    • Kanneganti TD, Ozoren N, Body-Malapel M, Amer A. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature (2006) 440(7081):233-6. doi:10.1038/nature04517
    • (2006) Nature , vol.440 , Issue.7081 , pp. 233-236
    • Kanneganti, T.D.1    Ozoren, N.2    Body-Malapel, M.3    Amer, A.4
  • 41
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • doi:10.1038/nature04516
    • Martinon F, Pétrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nat Cell Biol (2006) 440:237-41. doi:10.1038/nature04516
    • (2006) Nat Cell Biol , vol.440 , pp. 237-241
    • Martinon, F.1    Pétrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 42
    • 77951800951 scopus 로고    scopus 로고
    • NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
    • doi:10.1038/nature08938
    • Duewell P, Kono H, Rayner KJ, Sirois CM, Vladimer G, Bauernfeind FG, et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature (2010) 464:1357-61. doi:10.1038/nature08938
    • (2010) Nature , vol.464 , pp. 1357-1361
    • Duewell, P.1    Kono, H.2    Rayner, K.J.3    Sirois, C.M.4    Vladimer, G.5    Bauernfeind, F.G.6
  • 43
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • doi:10.1038/ni.1631
    • Hornung V, Bauernfeind F, Halle A, Samstad EO, Kono H, Rock KL, et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol (2008) 9:847-56. doi:10.1038/ni.1631
    • (2008) Nat Immunol , vol.9 , pp. 847-856
    • Hornung, V.1    Bauernfeind, F.2    Halle, A.3    Samstad, E.O.4    Kono, H.5    Rock, K.L.6
  • 44
    • 79954587515 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts regulate the production of prostaglandin in macrophages via NALP3 inflammasome-independent mechanisms
    • doi:10.1016/j.immuni.2011.03.019
    • Kuroda E, Ishii KJ, Uematsu S, Ohata K, Coban C, Akira S, et al. Silica crystals and aluminum salts regulate the production of prostaglandin in macrophages via NALP3 inflammasome-independent mechanisms. Immunity (2011) 34:514-26. doi:10.1016/j.immuni.2011.03.019
    • (2011) Immunity , vol.34 , pp. 514-526
    • Kuroda, E.1    Ishii, K.J.2    Uematsu, S.3    Ohata, K.4    Coban, C.5    Akira, S.6
  • 46
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • doi:10.1038/ni.1636
    • Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, Reinheckel T, et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol (2008) 9:857-65. doi:10.1038/ni.1636
    • (2008) Nat Immunol , vol.9 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3    Stewart, C.R.4    Monks, B.G.5    Reinheckel, T.6
  • 47
    • 79955038882 scopus 로고    scopus 로고
    • Fatty acid-induced NLRP3-ASC inflammasome activation interferes with insulin signaling
    • doi:10.1038/ni.2022
    • Wen H, Gris D, Lei Y, Jha S, Zhang L, Huang MT-H, et al. Fatty acid-induced NLRP3-ASC inflammasome activation interferes with insulin signaling. Nat Immunol (2011) 12:408-15. doi:10.1038/ni.2022
    • (2011) Nat Immunol , vol.12 , pp. 408-415
    • Wen, H.1    Gris, D.2    Lei, Y.3    Jha, S.4    Zhang, L.5    Huang, M.T.-H.6
  • 48
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • doi:10.1038/ni.1980
    • Nakahira K, Haspel JA, Rathinam VAK, Lee S-J, Dolinay T, Lam HC, et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol (2011) 12:222-30. doi:10.1038/ni.1980
    • (2011) Nat Immunol , vol.12 , pp. 222-230
    • Nakahira, K.1    Haspel, J.A.2    Rathinam, V.A.K.3    Lee, S.-J.4    Dolinay, T.5    Lam, H.C.6
  • 49
    • 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) 36:401-14. doi:10.1016/j.immuni.2012.01.009
    • (2012) Immunity , vol.36 , pp. 401-414
    • Shimada, K.1    Crother, T.R.2    Karlin, J.3    Dagvadorj, J.4    Chiba, N.5    Chen, S.6
  • 50
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • doi:10.1016/j.cell.2006.07.033
    • Gurcel L, Abrami L, Girardin S, Tschopp J, van der Goot FG. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell (2006) 126:1135-45. doi:10.1016/j.cell.2006.07.033
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3    Tschopp, J.4    van der Goot, F.G.5
  • 51
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • doi:10.1038/nature04515
    • Mariathasan S, Weiss DS, Newton K, McBride J, O'Rourke K, Roose-Girma M, et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature (2006) 440:228-32. doi:10.1038/nature04515
    • (2006) Nature , vol.440 , pp. 228-232
    • Mariathasan, S.1    Weiss, D.S.2    Newton, K.3    McBride, J.4    O'Rourke, K.5    Roose-Girma, M.6
  • 52
    • 70449360107 scopus 로고    scopus 로고
    • Staphylococcus aureus α-hemolysin activates the NLRP3-inflammasome in human and mouse monocytic cells
    • doi:10.1371/journal.pone.0007446
    • Craven RR, Gao X, Allen IC, Gris D, Wardenburg JB. Staphylococcus aureus α-hemolysin activates the NLRP3-inflammasome in human and mouse monocytic cells. PLoS One (2009) 4(10):e7446. doi:10.1371/journal.pone.0007446
    • (2009) PLoS One , vol.4 , Issue.10
    • Craven, R.R.1    Gao, X.2    Allen, I.C.3    Gris, D.4    Wardenburg, J.B.5
  • 53
    • 77953305895 scopus 로고    scopus 로고
    • Listeria monocytogenes is sensed by the NLRP3 and AIM2 inflammasome
    • doi:10.1002/eji.201040425
    • Kim S, Bauernfeind F, Ablasser A. Listeria monocytogenes is sensed by the NLRP3 and AIM2 inflammasome. Eur J Immunol (2010) 40:1545-51. doi:10.1002/eji.201040425
    • (2010) Eur J Immunol , vol.40 , pp. 1545-1551
    • Kim, S.1    Bauernfeind, F.2    Ablasser, A.3
  • 54
    • 61449193203 scopus 로고    scopus 로고
    • Critical role of apoptotic speck protein containing a caspase recruitment domain (ASC) and NLRP3 in causing necrosis and ASC speck formation induced by Porphyromonas gingivalis in human cells
    • doi:10.4049/jimmunol.0800909
    • Huang MT-H, Taxman DJ, Holley-Guthrie EA, Moore CB, Willingham SB, Madden V, et al. Critical role of apoptotic speck protein containing a caspase recruitment domain (ASC) and NLRP3 in causing necrosis and ASC speck formation induced by Porphyromonas gingivalis in human cells. J Immunol (2009) 182:2395-404. doi:10.4049/jimmunol.0800909
    • (2009) J Immunol , vol.182 , pp. 2395-2404
    • Huang, M.T.-H.1    Taxman, D.J.2    Holley-Guthrie, E.A.3    Moore, C.B.4    Willingham, S.B.5    Madden, V.6
  • 55
    • 70350366890 scopus 로고    scopus 로고
    • Inflammasome-dependent caspase-1 activation in cervical epithelial cells stimulates growth of the intracellular pathogen Chlamydia trachomatis
    • doi:10.1074/jbc.M109.026823
    • Abdul-Sater AA, Koo E, Häcker G, Ojcius DM. Inflammasome-dependent caspase-1 activation in cervical epithelial cells stimulates growth of the intracellular pathogen Chlamydia trachomatis. J Biol Chem (2009) 284:26789-96. doi:10.1074/jbc.M109.026823
    • (2009) J Biol Chem , vol.284 , pp. 26789-26796
    • Abdul-Sater, A.A.1    Koo, E.2    Häcker, G.3    Ojcius, D.M.4
  • 56
    • 77954726266 scopus 로고    scopus 로고
    • Inflammation and fibrosis during Chlamydia pneumoniae infection is regulated by IL-1 and the NLRP3/ASC inflammasome
    • doi:10.4049/jimmunol.0903937
    • He X, Mekasha S, Mavrogiorgos N. Inflammation and fibrosis during Chlamydia pneumoniae infection is regulated by IL-1 and the NLRP3/ASC inflammasome. J Immunol (2010) 184:5743-54. doi:10.4049/jimmunol.0903937
    • (2010) J Immunol , vol.184 , pp. 5743-5754
    • He, X.1    Mekasha, S.2    Mavrogiorgos, N.3
  • 57
    • 64049096334 scopus 로고    scopus 로고
    • The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1
    • doi:10.1016/j.immuni.2009.02.006
    • Thomas PG, Dash P, Aldridge JR Jr, Ellebedy AH. The intracellular sensor NLRP3 mediates key innate and healing responses to influenza A virus via the regulation of caspase-1. Immunity (2009) 30(4):566-75. doi:10.1016/j.immuni.2009.02.006
    • (2009) Immunity , vol.30 , Issue.4 , pp. 566-575
    • Thomas, P.G.1    Dash, P.2    Aldridge Jr., J.R.3    Ellebedy, A.H.4
  • 58
    • 64049111768 scopus 로고    scopus 로고
    • The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA
    • doi:10.1016/j.immuni.2009.02.005
    • Allen IC, Scull MA, Moore CB, Holl EK. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity (2009) 30(4):556-65. doi:10.1016/j.immuni.2009.02.005
    • (2009) Immunity , vol.30 , Issue.4 , pp. 556-565
    • Allen, I.C.1    Scull, M.A.2    Moore, C.B.3    Holl, E.K.4
  • 59
    • 77954958602 scopus 로고    scopus 로고
    • Aspergillus fumigatus stimulates the NLRP3 inflammasome through a pathway requiring ROS production and the Syk tyrosine kinase
    • doi:10.1371/journal.pone.0010008
    • Saïd-Sadier N, Padilla E, Langsley G, Ojcius DM. Aspergillus fumigatus stimulates the NLRP3 inflammasome through a pathway requiring ROS production and the Syk tyrosine kinase. PLoS One (2010) 5:e10008. doi:10.1371/journal.pone.0010008
    • (2010) PLoS One , vol.5
    • Saïd-Sadier, N.1    Padilla, E.2    Langsley, G.3    Ojcius, D.M.4
  • 60
    • 84880255426 scopus 로고    scopus 로고
    • Inflammasome-derived IL-1β production induces nitric oxide-mediated resistance to Leishmania
    • doi:10.1038/nm.3221
    • Lima-Junior DS, Costa DL, Carregaro V, Cunha LD, Silva ALN, Mineo TWP, et al. Inflammasome-derived IL-1β production induces nitric oxide-mediated resistance to Leishmania. Nat Med (2013) 19:909-15. doi:10.1038/nm.3221
    • (2013) Nat Med , vol.19 , pp. 909-915
    • Lima-Junior, D.S.1    Costa, D.L.2    Carregaro, V.3    Cunha, L.D.4    Silva, A.L.N.5    Mineo, T.W.P.6
  • 61
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • doi:10.1038/nature09663
    • Zhou R, Yazdi AS, Menu P, Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature (2010) 469:221-5. doi:10.1038/nature09663
    • (2010) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 62
    • 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) 7:576-82. doi:10.1038/ni1346
    • (2006) Nat Immunol , vol.7 , pp. 576-582
    • Franchi, L.1    Amer, A.2    Body-Malapel, M.3    Kanneganti, T.-D.4    Özören, N.5    Jagirdar, R.6
  • 63
    • 65449134828 scopus 로고    scopus 로고
    • Asc and Ipaf inflammasomes direct distinct pathways for caspase-1 activation in response to Legionella pneumophila
    • doi:10.1128/IAI.01382-08
    • Case CL, Shin S, Roy CR. Asc and Ipaf inflammasomes direct distinct pathways for caspase-1 activation in response to Legionella pneumophila. Infect Immun (2009) 77:1981-91. doi:10.1128/IAI.01382-08
    • (2009) Infect Immun , vol.77 , pp. 1981-1991
    • Case, C.L.1    Shin, S.2    Roy, C.R.3
  • 64
    • 45549092412 scopus 로고    scopus 로고
    • NAIP and Ipaf control Legionella pneumophila replication in human cells
    • Vinzing M, Eitel J, Lippmann J, Hocke AC, Zahlten J, Slevogt H, et al. NAIP and Ipaf control Legionella pneumophila replication in human cells. J Immunol (2008) 180:6808-15.
    • (2008) J Immunol , vol.180 , pp. 6808-6815
    • Vinzing, M.1    Eitel, J.2    Lippmann, J.3    Hocke, A.C.4    Zahlten, J.5    Slevogt, H.6
  • 65
    • 34548406570 scopus 로고    scopus 로고
    • Restriction of Legionella pneumophila growth in macrophages requires the concerted action of cytokine and Naip5/Ipaf signalling pathways
    • doi:10.1111/j.1462-5822.2007.00963.x
    • Coers J, Vance RE, Fontana MF, Dietrich WF. Restriction of Legionella pneumophila growth in macrophages requires the concerted action of cytokine and Naip5/Ipaf signalling pathways. Cell Microbiol (2007) 9:2344-57. doi:10.1111/j.1462-5822.2007.00963.x
    • (2007) Cell Microbiol , vol.9 , pp. 2344-2357
    • Coers, J.1    Vance, R.E.2    Fontana, M.F.3    Dietrich, W.F.4
  • 66
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • doi:10.1038/nature02664
    • Mariathasan S, Newton K, Monack DM, Vucic D, French DM, Lee WP, et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature (2004) 430:213-8. doi:10.1038/nature02664
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1    Newton, K.2    Monack, D.M.3    Vucic, D.4    French, D.M.5    Lee, W.P.6
  • 67
    • 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) 207:1745-55. doi:10.1084/jem.20100257
    • (2010) J Exp Med , vol.207 , pp. 1745-1755
    • Broz, P.1    Newton, K.2    Lamkanfi, M.3    Mariathasan, S.4    Dixit, V.M.5    Monack, D.M.6
  • 68
    • 77649241461 scopus 로고    scopus 로고
    • From the cover: 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. From the cover: innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome. Proc Natl Acad Sci U S A (2010) 107:3076-80. doi:10.1073/pnas.0913087107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , 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
  • 69
    • 34548434775 scopus 로고    scopus 로고
    • Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages
    • doi:10.1371/journal.ppat.0030111
    • Suzuki T, Franchi L, Toma C, Ashida H, Ogawa M, Yoshikawa Y, et al. Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages. PLoS Pathog (2007) 3:e111. doi:10.1371/journal.ppat.0030111
    • (2007) PLoS Pathog , vol.3
    • Suzuki, T.1    Franchi, L.2    Toma, C.3    Ashida, H.4    Ogawa, M.5    Yoshikawa, Y.6
  • 70
    • 84875850500 scopus 로고    scopus 로고
    • Activation of inflammasome signaling mediates pathology of acute P. aeruginosa pneumonia
    • doi:10.1172/JCI66142
    • Cohen TS, Prince AS. Activation of inflammasome signaling mediates pathology of acute P. aeruginosa pneumonia. J Clin Invest (2013) 123:1630-7. doi:10.1172/JCI66142
    • (2013) J Clin Invest , vol.123 , pp. 1630-1637
    • Cohen, T.S.1    Prince, A.S.2
  • 71
    • 37549041954 scopus 로고    scopus 로고
    • Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome
    • doi:10.1084/jem.20071239
    • Sutterwala FS, Mijares LA, Li L, Ogura Y, Kazmierczak BI, Flavell RA. Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome. J Exp Med (2007) 204:3235-45. doi:10.1084/jem.20071239
    • (2007) J Exp Med , vol.204 , pp. 3235-3245
    • Sutterwala, F.S.1    Mijares, L.A.2    Li, L.3    Ogura, Y.4    Kazmierczak, B.I.5    Flavell, R.A.6
  • 72
    • 36248940773 scopus 로고    scopus 로고
    • Critical role for Ipaf in Pseudomonas aeruginosa-induced caspase-1 activation
    • doi:10.1002/eji.200737532
    • Franchi L, Stoolman J, Kanneganti T-D, Verma A, Ramphal R, Nuñez G. Critical role for Ipaf in Pseudomonas aeruginosa-induced caspase-1 activation. Eur J Immunol (2007) 37:3030-9. doi:10.1002/eji.200737532
    • (2007) Eur J Immunol , vol.37 , pp. 3030-3039
    • Franchi, L.1    Stoolman, J.2    Kanneganti, T.-D.3    Verma, A.4    Ramphal, R.5    Nuñez, G.6
  • 73
    • 33645770203 scopus 로고    scopus 로고
    • The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection
    • doi:10.1038/ni1305
    • Zamboni DS, Kobayashi KS, Kohlsdorf T, Ogura Y, Long EM, Vance RE, et al. The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection. Nat Immunol (2006) 7:318-25. doi:10.1038/ni1305
    • (2006) Nat Immunol , vol.7 , pp. 318-325
    • Zamboni, D.S.1    Kobayashi, K.S.2    Kohlsdorf, T.3    Ogura, Y.4    Long, E.M.5    Vance, R.E.6
  • 74
    • 79953315378 scopus 로고    scopus 로고
    • Differential requirements for NAIP5 in activation of the NLRC4 inflammasome
    • doi:10.1128/IAI.01187-10
    • Lightfield KL, Persson J, Trinidad NJ, Brubaker SW, Kofoed EM, Sauer J-D, et al. Differential requirements for NAIP5 in activation of the NLRC4 inflammasome. Infect Immun (2011) 79:1606-14. doi:10.1128/IAI.01187-10
    • (2011) Infect Immun , vol.79 , pp. 1606-1614
    • Lightfield, K.L.1    Persson, J.2    Trinidad, N.J.3    Brubaker, S.W.4    Kofoed, E.M.5    Sauer, J.-D.6
  • 75
    • 70449722759 scopus 로고    scopus 로고
    • T cell-intrinsic role of Nod2 in promoting type 1 immunity to Toxoplasma gondii
    • doi:10.1038/ni.1816
    • Shaw MH, Reimer T, Sánchez-Valdepeñas C, Warner N, Kim Y-G, Fresno M, et al. T cell-intrinsic role of Nod2 in promoting type 1 immunity to Toxoplasma gondii. Nat Immunol (2009) 10:1267-74. doi:10.1038/ni.1816
    • (2009) Nat Immunol , vol.10 , pp. 1267-1274
    • Shaw, M.H.1    Reimer, T.2    Sánchez-Valdepeñas, C.3    Warner, N.4    Kim, Y.-G.5    Fresno, M.6
  • 76
    • 82255194176 scopus 로고    scopus 로고
    • Intrinsic expression of Nod2 in CD4+ T lymphocytes is not necessary for the development of cell-mediated immunity and host resistance to Toxoplasma gondii
    • doi:10.1002/eji.201141876
    • Caetano BC, Biswas A, Lima DS, Benevides L, Mineo TWP, Horta CV, et al. Intrinsic expression of Nod2 in CD4+ T lymphocytes is not necessary for the development of cell-mediated immunity and host resistance to Toxoplasma gondii. Eur J Immunol (2011) 41:3627-31. doi:10.1002/eji.201141876
    • (2011) Eur J Immunol , vol.41 , pp. 3627-3631
    • Caetano, B.C.1    Biswas, A.2    Lima, D.S.3    Benevides, L.4    Mineo, T.W.P.5    Horta, C.V.6
  • 77
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
    • doi:10.1038/35079107
    • Hugot JP, Chamaillard M, Zouali H, Lesage S, Cezard JP, Belaiche J, et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature (2001) 411:599-603. doi:10.1038/35079107
    • (2001) Nature , vol.411 , pp. 599-603
    • Hugot, J.P.1    Chamaillard, M.2    Zouali, H.3    Lesage, S.4    Cezard, J.P.5    Belaiche, J.6
  • 78
    • 22244465576 scopus 로고    scopus 로고
    • Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition
    • doi:10.1083/jcb.200502153
    • Barnich N, Aguirre JE, Reinecker H-C, Xavier R, Podolsky DK. Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition. J Cell Biol (2005) 170:21-6. doi:10.1083/jcb.200502153
    • (2005) J Cell Biol , vol.170 , pp. 21-26
    • Barnich, N.1    Aguirre, J.E.2    Reinecker, H.-C.3    Xavier, R.4    Podolsky, D.K.5
  • 79
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • doi:10.1038/nri3452
    • Latz E, Xiao TS, Stutz A. Activation and regulation of the inflammasomes. Nat Rev Immunol (2013) 13:397-411. doi:10.1038/nri3452
    • (2013) Nat Rev Immunol , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 80
    • 77956958947 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes
    • doi:10.1038/ni.1935
    • Masters SL, Dunne A, Subramanian SL, Hull RL, Tannahill GM, Sharp FA, et al. Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. Nat Immunol (2010) 11:897-904. doi:10.1038/ni.1935
    • (2010) Nat Immunol , vol.11 , pp. 897-904
    • Masters, S.L.1    Dunne, A.2    Subramanian, S.L.3    Hull, R.L.4    Tannahill, G.M.5    Sharp, F.A.6
  • 81
    • 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) 341:172-5. doi:10.1126/science.1236381
    • (2013) Science , vol.341 , pp. 172-175
    • Hu, Z.1    Yan, C.2    Liu, P.3    Huang, Z.4    Ma, R.5    Zhang, C.6
  • 82
    • 84883441989 scopus 로고    scopus 로고
    • Cytosolic flagellin-induced lysosomal pathway regulates inflammasome-dependent and-independent macrophage responses
    • doi:10.1073/pnas.1305316110
    • Lage SL, Buzzo CL, Amaral EP, Matteucci KC, Massis LM, Icimoto MY, et al. Cytosolic flagellin-induced lysosomal pathway regulates inflammasome-dependent and-independent macrophage responses. Proc Natl Acad Sci U S A (2013) 110:E3321-30. doi:10.1073/pnas.1305316110
    • (2013) Proc Natl Acad Sci U S A , vol.110
    • Lage, S.L.1    Buzzo, C.L.2    Amaral, E.P.3    Matteucci, K.C.4    Massis, L.M.5    Icimoto, M.Y.6
  • 84
    • 70350365362 scopus 로고    scopus 로고
    • An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix
    • doi:10.1242/jcs.051193
    • Arnoult D, Soares F, Tattoli I, Castanier C, Philpott DJ, Girardin SE. An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix. J Cell Sci (2009) 122:3161-8. doi:10.1242/jcs.051193
    • (2009) J Cell Sci , vol.122 , pp. 3161-3168
    • Arnoult, D.1    Soares, F.2    Tattoli, I.3    Castanier, C.4    Philpott, D.J.5    Girardin, S.E.6
  • 86
    • 84862301902 scopus 로고    scopus 로고
    • Amino acid starvation induced by invasive bacterial pathogens triggers an innate host defense program
    • doi:10.1016/j.chom.2012.04.012
    • Tattoli I, Sorbara MT, Vuckovic D, Ling A, Soares F, Carneiro LAM, et al. Amino acid starvation induced by invasive bacterial pathogens triggers an innate host defense program. Cell Host Microbe (2012) 11:563-75. doi:10.1016/j.chom.2012.04.012
    • (2012) Cell Host Microbe , vol.11 , pp. 563-575
    • Tattoli, I.1    Sorbara, M.T.2    Vuckovic, D.3    Ling, A.4    Soares, F.5    Carneiro, L.A.M.6
  • 88
    • 84862815491 scopus 로고    scopus 로고
    • NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4
    • doi:10.1038/ni.2239
    • Cui J, Li Y, Zhu L, Liu D, Songyang Z, Wang HY, et al. NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4. Nat Immunol (2012) 13:387-95. doi:10.1038/ni.2239
    • (2012) Nat Immunol , vol.13 , pp. 387-395
    • Cui, J.1    Li, Y.2    Zhu, L.3    Liu, D.4    Songyang, Z.5    Wang, H.Y.6
  • 89
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: from phenomenology to molecular understanding in less than a decade
    • doi:10.1038/nrm2245
    • Klionsky DJ. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat Rev Mol Cell Biol (2007) 8:931-7. doi:10.1038/nrm2245
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 90
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: a history of macroautophagy
    • doi:10.1038/ncb0910-814
    • Yang Z, Klionsky DJ. Eaten alive: a history of macroautophagy. Nat Cell Biol (2010) 12:814-22. doi:10.1038/ncb0910-814
    • (2010) Nat Cell Biol , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 91
    • 84877628647 scopus 로고    scopus 로고
    • Autophagy in human health and disease
    • doi:10.1056/NEJMra1205406
    • Choi AMK, Ryter SW, Levine B. Autophagy in human health and disease. N Engl J Med (2013) 368:651-62. doi:10.1056/NEJMra1205406
    • (2013) N Engl J Med , vol.368 , pp. 651-662
    • Choi, A.M.K.1    Ryter, S.W.2    Levine, B.3
  • 92
    • 69949110579 scopus 로고    scopus 로고
    • Autophagy as an emerging dimension to adaptive and innate immunity
    • doi:10.1016/j.smim.2009.05.004
    • Hussey S, Travassos LH, Jones NL. Autophagy as an emerging dimension to adaptive and innate immunity. Semin Immunol (2009) 21:233-41. doi:10.1016/j.smim.2009.05.004
    • (2009) Semin Immunol , vol.21 , pp. 233-241
    • Hussey, S.1    Travassos, L.H.2    Jones, N.L.3
  • 93
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • doi:10.1038/nature06639
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature (2008) 451:1069-75. doi:10.1038/nature06639
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 94
    • 84855286487 scopus 로고    scopus 로고
    • Autophagy protein Atg3 is essential for maintaining mitochondrial integrity and for normal intracellular development of Toxoplasma gondii tachyzoites
    • doi:10.1371/journal.ppat.1002416
    • Besteiro S, Brooks CF, Striepen B, Dubremetz JF. Autophagy protein Atg3 is essential for maintaining mitochondrial integrity and for normal intracellular development of Toxoplasma gondii tachyzoites. PLoS Pathog (2011) 7(12):e1002416. doi:10.1371/journal.ppat.1002416
    • (2011) PLoS Pathog , vol.7 , Issue.12
    • Besteiro, S.1    Brooks, C.F.2    Striepen, B.3    Dubremetz, J.F.4
  • 95
  • 96
    • 84871581862 scopus 로고    scopus 로고
    • Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis
    • doi:10.1016/j.cell.2012.11.028
    • Ragusa MJ, Stanley RE, Hurley JH. Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis. Cell (2012) 151:1501-12. doi:10.1016/j.cell.2012.11.028
    • (2012) Cell , vol.151 , pp. 1501-1512
    • Ragusa, M.J.1    Stanley, R.E.2    Hurley, J.H.3
  • 97
    • 82855170846 scopus 로고    scopus 로고
    • Atg13 and FIP200 act independently of Ulk1 and Ulk2 in autophagy induction
    • doi:10.4161/auto.7.12.18027
    • Alers S, Löffler AS, Paasch F, Dieterle AM, Keppeler H, Lauber K, et al. Atg13 and FIP200 act independently of Ulk1 and Ulk2 in autophagy induction. Autophagy (2011) 7:1423-33. doi:10.4161/auto.7.12.18027
    • (2011) Autophagy , vol.7 , pp. 1423-1433
    • Alers, S.1    Löffler, A.S.2    Paasch, F.3    Dieterle, A.M.4    Keppeler, H.5    Lauber, K.6
  • 99
    • 70349687405 scopus 로고    scopus 로고
    • Discovery of Atg5/Atg7-independent alternative macroautophagy
    • doi:10.1038/nature08455
    • Nishida Y, Arakawa S, Fujitani K, Yamaguchi H, Mizuta T, Kanaseki T, et al. Discovery of Atg5/Atg7-independent alternative macroautophagy. Nature (2009) 461:654-8. doi:10.1038/nature08455
    • (2009) Nature , vol.461 , pp. 654-658
    • Nishida, Y.1    Arakawa, S.2    Fujitani, K.3    Yamaguchi, H.4    Mizuta, T.5    Kanaseki, T.6
  • 100
    • 0027311858 scopus 로고
    • Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression
    • doi:10.1016/0092-8674(93)90144-F
    • Kunz J, Henriquez R, Schneider U, Deuter-Reinhard M, Movva NR, Hall MN. Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression. Cell (1993) 73:585-96. doi:10.1016/0092-8674(93)90144-F
    • (1993) Cell , vol.73 , pp. 585-596
    • Kunz, J.1    Henriquez, R.2    Schneider, U.3    Deuter-Reinhard, M.4    Movva, N.R.5    Hall, M.N.6
  • 101
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • doi:10.1126/science.8385367
    • Schu PV, Takegawa K, Fry MJ, Stack JH, Waterfield MD, Emr SD. Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science (1993) 260:88-91. doi:10.1126/science.8385367
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 102
    • 0029831167 scopus 로고    scopus 로고
    • Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002
    • Brunn GJ, Williams J, Sabers C, Wiederrecht G, Lawrence JC, Abraham RT. Direct inhibition of the signaling functions of the mammalian target of rapamycin by the phosphoinositide 3-kinase inhibitors, wortmannin and LY294002. EMBO J (1996) 15:5256-67.
    • (1996) EMBO J , vol.15 , pp. 5256-5267
    • Brunn, G.J.1    Williams, J.2    Sabers, C.3    Wiederrecht, G.4    Lawrence, J.C.5    Abraham, R.T.6
  • 103
    • 2342472012 scopus 로고    scopus 로고
    • Towards an understanding of isoform specificity in phosphoinositide 3-kinase signalling in lymphocytes
    • doi:10.1042/BST0320315
    • Fruman DA. Towards an understanding of isoform specificity in phosphoinositide 3-kinase signalling in lymphocytes. Biochem Soc Trans (2004) 32:315-9. doi:10.1042/BST0320315
    • (2004) Biochem Soc Trans , vol.32 , pp. 315-319
    • Fruman, D.A.1
  • 106
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • doi:10.1101/gad.1212704
    • Hay N. Upstream and downstream of mTOR. Genes Dev (2004) 18:1926-45. doi:10.1101/gad.1212704
    • (2004) Genes Dev , vol.18 , pp. 1926-1945
    • Hay, N.1
  • 107
    • 17144427728 scopus 로고    scopus 로고
    • Synergistic augmentation of rapamycin-induced autophagy in malignant glioma cells by phosphatidylinositol 3-kinase/protein kinase B inhibitors
    • doi:10.1158/0008-5472.CAN-04-3640
    • Takeuchi H, Kondo Y, Fujiwara K, Kanzawa T, Aoki H, Mills GB, et al. Synergistic augmentation of rapamycin-induced autophagy in malignant glioma cells by phosphatidylinositol 3-kinase/protein kinase B inhibitors. Cancer Res (2005) 65:3336-46. doi:10.1158/0008-5472.CAN-04-3640
    • (2005) Cancer Res , vol.65 , pp. 3336-3346
    • Takeuchi, H.1    Kondo, Y.2    Fujiwara, K.3    Kanzawa, T.4    Aoki, H.5    Mills, G.B.6
  • 108
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • doi:10.1091/mbc.E08-12-1249
    • Jung CH, Jun CB, Ro SH, Kim YM, Otto NM, Cao J, et al. ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol Biol Cell (2009) 20:1992-2003. doi:10.1091/mbc.E08-12-1249
    • (2009) Mol Biol Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3    Kim, Y.M.4    Otto, N.M.5    Cao, J.6
  • 109
    • 84866426794 scopus 로고    scopus 로고
    • Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagy
    • doi:10.1038/emboj.2012.225
    • Kraft C, Kijanska M, Kalie E, Siergiejuk E, Lee SS, Semplicio G, et al. Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagy. EMBO J (2012) 31:3691-703. doi:10.1038/emboj.2012.225
    • (2012) EMBO J , vol.31 , pp. 3691-3703
    • Kraft, C.1    Kijanska, M.2    Kalie, E.3    Siergiejuk, E.4    Lee, S.S.5    Semplicio, G.6
  • 110
    • 84881553725 scopus 로고    scopus 로고
    • K63 polyubiquitination and activation of mTOR by the p62-TRAF6 complex in nutrient-activated cells
    • doi:10.1016/j.molcel.2013.06.020
    • Linares JF, Duran A, Yajima T, Pasparakis M, Moscat J, Diaz-Meco MT. K63 polyubiquitination and activation of mTOR by the p62-TRAF6 complex in nutrient-activated cells. Mol Cell (2013) 51:283-96. doi:10.1016/j.molcel.2013.06.020
    • (2013) Mol Cell , vol.51 , pp. 283-296
    • Linares, J.F.1    Duran, A.2    Yajima, T.3    Pasparakis, M.4    Moscat, J.5    Diaz-Meco, M.T.6
  • 111
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phosphoinositide 3-kinases
    • doi:10.1242/jcs.02855
    • Lindmo K. Regulation of membrane traffic by phosphoinositide 3-kinases. J Cell Sci (2006) 119:605-14. doi:10.1242/jcs.02855
    • (2006) J Cell Sci , vol.119 , pp. 605-614
    • Lindmo, K.1
  • 112
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • doi:10.1074/jbc.275.2.992
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P. Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem (2000) 275:992-8. doi:10.1074/jbc.275.2.992
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 113
    • 84866158316 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-phosphate clearance plays a key role in autophagosome completion
    • doi:10.1016/j.cub.2012.06.029
    • Cebollero E, van der Vaart A, Zhao M, Rieter E, Klionsky DJ, Helms JB, et al. Phosphatidylinositol-3-phosphate clearance plays a key role in autophagosome completion. Curr Biol (2012) 22:1545-53. doi:10.1016/j.cub.2012.06.029
    • (2012) Curr Biol , vol.22 , pp. 1545-1553
    • Cebollero, E.1    van der Vaart, A.2    Zhao, M.3    Rieter, E.4    Klionsky, D.J.5    Helms, J.B.6
  • 114
    • 84880376355 scopus 로고    scopus 로고
    • Emerging regulation and functions of autophagy
    • doi:10.1038/ncb2788
    • Boya P, Reggiori F, Codogno P. Emerging regulation and functions of autophagy. Nat Cell Biol (2013) 15:713-20. doi:10.1038/ncb2788
    • (2013) Nat Cell Biol , vol.15 , pp. 713-720
    • Boya, P.1    Reggiori, F.2    Codogno, P.3
  • 115
    • 84858016996 scopus 로고    scopus 로고
    • Autophagy and bacterial infectious diseases
    • doi:10.3858/emm.2012.44.2.032
    • Yuk JM, Yoshimori T, Jo E-K. Autophagy and bacterial infectious diseases. Exp Mol Med (2012) 44:99-108. doi:10.3858/emm.2012.44.2.032
    • (2012) Exp Mol Med , vol.44 , pp. 99-108
    • Yuk, J.M.1    Yoshimori, T.2    Jo, E.-K.3
  • 116
    • 8344247016 scopus 로고    scopus 로고
    • Autophagy defends cells against invading group A Streptococcus
    • doi:10.1126/science.1103966
    • Nakagawa I, Amano A, Mizushima N, Yamamoto A, Yamaguchi H, Kamimoto T, et al. Autophagy defends cells against invading group A Streptococcus. Science (2004) 306:1037-40. doi:10.1126/science.1103966
    • (2004) Science , vol.306 , pp. 1037-1040
    • Nakagawa, I.1    Amano, A.2    Mizushima, N.3    Yamamoto, A.4    Yamaguchi, H.5    Kamimoto, T.6
  • 117
    • 77958107375 scopus 로고    scopus 로고
    • Escape of intracellular Shigella from autophagy requires binding to cholesterol through the type III effector, IcsB
    • doi:10.1016/j.micinf.2010.06.006
    • Kayath CA, Hussey S, El Hajjami N, Nagra K, Philpott D, Allaoui A. Escape of intracellular Shigella from autophagy requires binding to cholesterol through the type III effector, IcsB. Microbes Infect (2010) 12:956-66. doi:10.1016/j.micinf.2010.06.006
    • (2010) Microbes Infect , vol.12 , pp. 956-966
    • Kayath, C.A.1    Hussey, S.2    El Hajjami, N.3    Nagra, K.4    Philpott, D.5    Allaoui, A.6
  • 118
  • 119
    • 68349143052 scopus 로고    scopus 로고
    • Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy
    • doi:10.1016/j.chom.2009.07.005
    • Dupont N, Lacas-Gervais S, Bertout J, Paz I, Freche B, Van Nhieu GT, et al. Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy. Cell Host Microbe (2009) 6:137-49. doi:10.1016/j.chom.2009.07.005
    • (2009) Cell Host Microbe , vol.6 , pp. 137-149
    • Dupont, N.1    Lacas-Gervais, S.2    Bertout, J.3    Paz, I.4    Freche, B.5    Van Nhieu, G.T.6
  • 120
    • 50249111985 scopus 로고    scopus 로고
    • Stimulation of autophagy suppresses the intracellular survival of Burkholderia pseudomallei in mammalian cell lines
    • Cullinane M, Gong L, Li X, Lazar-Adler N, Tra T, Wolvetang E, et al. Stimulation of autophagy suppresses the intracellular survival of Burkholderia pseudomallei in mammalian cell lines. Autophagy (2008) 4:744-53.
    • (2008) Autophagy , vol.4 , pp. 744-753
    • Cullinane, M.1    Gong, L.2    Li, X.3    Lazar-Adler, N.4    Tra, T.5    Wolvetang, E.6
  • 121
    • 38349110486 scopus 로고    scopus 로고
    • Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles
    • doi:10.1038/nature06479
    • Birmingham CL, Canadien V, Kaniuk NA, Steinberg BE, Higgins DE, Brumell JH. Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles. Nature (2008) 451:350-4. doi:10.1038/nature06479
    • (2008) Nature , vol.451 , pp. 350-354
    • Birmingham, C.L.1    Canadien, V.2    Kaniuk, N.A.3    Steinberg, B.E.4    Higgins, D.E.5    Brumell, J.H.6
  • 122
    • 33744958258 scopus 로고    scopus 로고
    • Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole
    • doi:10.1074/jbc.M509157200
    • Birmingham CL. Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole. J Biol Chem (2006) 281:11374-83. doi:10.1074/jbc.M509157200
    • (2006) J Biol Chem , vol.281 , pp. 11374-11383
    • Birmingham, C.L.1
  • 123
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • doi:10.1016/j.cell.2004.11.038
    • Gutierrez MG, Master SS, Singh SB, Taylor GA, Colombo MI, Deretic V. Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell (2004) 119:1-14. doi:10.1016/j.cell.2004.11.038
    • (2004) Cell , vol.119 , pp. 1-14
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5    Deretic, V.6
  • 124
    • 33947715151 scopus 로고    scopus 로고
    • HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein
    • doi:10.1016/j.chom.2006.12.001
    • Orvedahl A, Alexander D, Tallóczy Z, Sun Q, Wei Y, Zhang W, et al. HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein. Cell Host Microbe (2007) 1:23-35. doi:10.1016/j.chom.2006.12.001
    • (2007) Cell Host Microbe , vol.1 , pp. 23-35
    • Orvedahl, A.1    Alexander, D.2    Tallóczy, Z.3    Sun, Q.4    Wei, Y.5    Zhang, W.6
  • 125
    • 33947134377 scopus 로고    scopus 로고
    • Autophagy-dependent viral recognition by plasmacytoid dendritic cells
    • doi:10.1126/science.1136880
    • Lee HK, Lund JM, Ramanathan B, Mizushima N, Iwasaki A. Autophagy-dependent viral recognition by plasmacytoid dendritic cells. Science (2007) 315:1398-401. doi:10.1126/science.1136880
    • (2007) Science , vol.315 , pp. 1398-1401
    • Lee, H.K.1    Lund, J.M.2    Ramanathan, B.3    Mizushima, N.4    Iwasaki, A.5
  • 126
    • 34447643958 scopus 로고    scopus 로고
    • Toll-like receptor 4 is a sensor for autophagy associated with innate immunity
    • doi:10.1016/j.immuni.2007.05.022
    • Xu Y, Jagannath C, Liu X-D, Sharafkhaneh A, Kolodziejska KE, Eissa NT. Toll-like receptor 4 is a sensor for autophagy associated with innate immunity. Immunity (2007) 27:135-44. doi:10.1016/j.immuni.2007.05.022
    • (2007) Immunity , vol.27 , pp. 135-144
    • Xu, Y.1    Jagannath, C.2    Liu, X.-D.3    Sharafkhaneh, A.4    Kolodziejska, K.E.5    Eissa, N.T.6
  • 127
    • 41949101594 scopus 로고    scopus 로고
    • Toll-like receptors control autophagy
    • doi:10.1038/emboj.2008.31
    • Delgado MA, Elmaoued RA, Davis AS, Kyei G, Deretic V. Toll-like receptors control autophagy. EMBO J (2008) 27:1110-21. doi:10.1038/emboj.2008.31
    • (2008) EMBO J , vol.27 , pp. 1110-1121
    • Delgado, M.A.1    Elmaoued, R.A.2    Davis, A.S.3    Kyei, G.4    Deretic, V.5
  • 128
    • 57749100267 scopus 로고    scopus 로고
    • MyD88 and Trif target Beclin 1 to trigger autophagy in macrophages
    • doi:10.1074/jbc.M804478200
    • Shi C-S, Kehrl JH. MyD88 and Trif target Beclin 1 to trigger autophagy in macrophages. J Biol Chem (2008) 283:33175-82. doi:10.1074/jbc.M804478200
    • (2008) J Biol Chem , vol.283 , pp. 33175-33182
    • Shi, C.-S.1    Kehrl, J.H.2
  • 129
    • 58149352480 scopus 로고    scopus 로고
    • Mammalian target of rapamycin (mTOR) orchestrates the defense program of innate immune cells
    • doi:10.1002/eji.200838761
    • Schmitz F, Heit A, Dreher S, Eisenächer K, Mages J, Haas T, et al. Mammalian target of rapamycin (mTOR) orchestrates the defense program of innate immune cells. Eur J Immunol (2008) 38:2981-92. doi:10.1002/eji.200838761
    • (2008) Eur J Immunol , vol.38 , pp. 2981-2992
    • Schmitz, F.1    Heit, A.2    Dreher, S.3    Eisenächer, K.4    Mages, J.5    Haas, T.6
  • 130
    • 47849094901 scopus 로고    scopus 로고
    • Autophagic control of listeria through intracellular innate immune recognition in Drosophila
    • doi:10.1038/ni.1634
    • Yano T, Mita S, Ohmori H, Oshima Y, Fujimoto Y, Ueda R, et al. Autophagic control of listeria through intracellular innate immune recognition in Drosophila. Nat Immunol (2008) 9:908-16. doi:10.1038/ni.1634
    • (2008) Nat Immunol , vol.9 , pp. 908-916
    • Yano, T.1    Mita, S.2    Ohmori, H.3    Oshima, Y.4    Fujimoto, Y.5    Ueda, R.6
  • 131
    • 73849151394 scopus 로고    scopus 로고
    • NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation
    • doi:10.1038/nm.2069
    • Cooney R, Baker J, Brain O, Danis B, Pichulik T, Allan P, et al. NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation. Nat Med (2009) 16:90-7. doi:10.1038/nm.2069
    • (2009) Nat Med , vol.16 , pp. 90-97
    • Cooney, R.1    Baker, J.2    Brain, O.3    Danis, B.4    Pichulik, T.5    Allan, P.6
  • 132
    • 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 LAM, Ramjeet M, Hussey S, Kim Y-G, Magalhaes JG, et al. Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry. Nat Immunol (2010) 11:55-62. doi:10.1038/ni.1823
    • (2010) Nat Immunol , vol.11 , pp. 55-62
    • Travassos, L.H.1    Carneiro, L.A.M.2    Ramjeet, M.3    Hussey, S.4    Kim, Y.-G.5    Magalhaes, J.G.6
  • 133
    • 34247554965 scopus 로고    scopus 로고
    • Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis
    • doi:10.1038/ng2032
    • Rioux JD, Xavier RJ, Taylor KD, Silverberg MS, Goyette P, Huett A, et al. Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis. Nat Genet (2007) 39:596-604. doi:10.1038/ng2032
    • (2007) Nat Genet , vol.39 , pp. 596-604
    • Rioux, J.D.1    Xavier, R.J.2    Taylor, K.D.3    Silverberg, M.S.4    Goyette, P.5    Huett, A.6
  • 134
    • 54849421128 scopus 로고    scopus 로고
    • Impaired autophagy of an intracellular pathogen induced by a Crohn's disease associated ATG16L1 variant
    • doi:10.1371/journal.pone.0003391
    • Kuballa P, Huett A, Rioux JD, Daly MJ, Xavier RJ. Impaired autophagy of an intracellular pathogen induced by a Crohn's disease associated ATG16L1 variant. PLoS One (2008) 3:e3391. doi:10.1371/journal.pone.0003391
    • (2008) PLoS One , vol.3
    • Kuballa, P.1    Huett, A.2    Rioux, J.D.3    Daly, M.J.4    Xavier, R.J.5
  • 135
    • 79959655886 scopus 로고    scopus 로고
    • NOD2 and ATG16L1 polymorphisms affect monocyte responses in Crohn's disease
    • doi:10.3748/wjg.v17.i23.2829
    • Glubb DM, Gearry RB, Barclay ML, Roberts RL, Pearson J, Keenan JI, et al. NOD2 and ATG16L1 polymorphisms affect monocyte responses in Crohn's disease. World J Gastroenterol (2011) 17:2829-37. doi:10.3748/wjg.v17.i23.2829
    • (2011) World J Gastroenterol , vol.17 , pp. 2829-2837
    • Glubb, D.M.1    Gearry, R.B.2    Barclay, M.L.3    Roberts, R.L.4    Pearson, J.5    Keenan, J.I.6
  • 136
    • 80052389178 scopus 로고    scopus 로고
    • ATG16L1 polymorphisms are associated with NOD2-induced hyperinflammation
    • doi:10.4161/auto.7.9.15867
    • Plantinga TS, Joosten LA, Netea MG. ATG16L1 polymorphisms are associated with NOD2-induced hyperinflammation. Autophagy (2011) 7:1074-5. doi:10.4161/auto.7.9.15867
    • (2011) Autophagy , vol.7 , pp. 1074-1075
    • Plantinga, T.S.1    Joosten, L.A.2    Netea, M.G.3
  • 138
    • 84874596968 scopus 로고    scopus 로고
    • Inflammasome components coordinate autophagy and pyroptosis as macrophage responses to infection
    • doi:10.1128/mBio.00620-12
    • Byrne BG, Dubuisson JF, Joshi AD, Persson JJ, Swanson MS. Inflammasome components coordinate autophagy and pyroptosis as macrophage responses to infection. MBio (2012) 4:e620-612. doi:10.1128/mBio.00620-12
    • (2012) MBio , vol.4
    • Byrne, B.G.1    Dubuisson, J.F.2    Joshi, A.D.3    Persson, J.J.4    Swanson, M.S.5
  • 139
    • 84863005844 scopus 로고    scopus 로고
    • The mitochondrial proteins NLRX1 and TUFM form a complex that regulates Type I interferon and autophagy
    • doi:10.1016/j.immuni.2012.03.025
    • Lei Y, Wen H, Yu Y, Taxman DJ, Zhang L, Widman DG, et al. The mitochondrial proteins NLRX1 and TUFM form a complex that regulates Type I interferon and autophagy. Immunity (2012) 36:933-46. doi:10.1016/j.immuni.2012.03.025
    • (2012) Immunity , vol.36 , pp. 933-946
    • Lei, Y.1    Wen, H.2    Yu, Y.3    Taxman, D.J.4    Zhang, L.5    Widman, D.G.6
  • 140
    • 64049114864 scopus 로고    scopus 로고
    • Autophagy is an essential component of Drosophila immunity against vesicular stomatitis virus
    • doi:10.1016/j.immuni.2009.02.009
    • Shelly S, Lukinova N, Bambina S, Berman A, Cherry S. Autophagy is an essential component of Drosophila immunity against vesicular stomatitis virus. Immunity (2009) 30:588-98. doi:10.1016/j.immuni.2009.02.009
    • (2009) Immunity , vol.30 , pp. 588-598
    • Shelly, S.1    Lukinova, N.2    Bambina, S.3    Berman, A.4    Cherry, S.5
  • 143
    • 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) 36:742-54. doi:10.1016/j.immuni.2012.03.012
    • (2012) Immunity , vol.36 , 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
  • 144
    • 79251588741 scopus 로고    scopus 로고
    • NLRP4 negatively regulates autophagic processes through an association with Beclin1
    • doi:10.4049/jimmunol.1001654
    • Jounai N, Kobiyama K, Shiina M, Ogata K, Ishii KJ, Takeshita F. NLRP4 negatively regulates autophagic processes through an association with Beclin1. J Immunol (2011) 186:1646-55. doi:10.4049/jimmunol.1001654
    • (2011) J Immunol , vol.186 , pp. 1646-1655
    • Jounai, N.1    Kobiyama, K.2    Shiina, M.3    Ogata, K.4    Ishii, K.J.5    Takeshita, F.6
  • 145
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • doi:10.1038/nature09782
    • Levine B, Mizushima N, Virgin HW. Autophagy in immunity and inflammation. Nature (2011) 469:323-35. doi:10.1038/nature09782
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 146
    • 35348921764 scopus 로고    scopus 로고
    • The Atg5 Atg12 conjugate associates with innate antiviral immune responses
    • doi:10.1073/pnas.0704014104
    • Jounai N, Takeshita F, Kobiyama K, Sawano A, Miyawaki A, Xin KQ, et al. The Atg5 Atg12 conjugate associates with innate antiviral immune responses. Proc Natl Acad Sci U S A (2007) 104:14050-5. doi:10.1073/pnas.0704014104
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14050-14055
    • Jounai, N.1    Takeshita, F.2    Kobiyama, K.3    Sawano, A.4    Miyawaki, A.5    Xin, K.Q.6
  • 147
    • 62449110463 scopus 로고    scopus 로고
    • Absence of autophagy results in reactive oxygen species-dependent amplification of RLR signaling
    • doi:10.1073/pnas.0807694106
    • Tal MC, Sasai M, Lee HK, Yordy B, Shadel GS, Iwasaki A. Absence of autophagy results in reactive oxygen species-dependent amplification of RLR signaling. Proc Natl Acad Sci U S A (2009) 106:2770-5. doi:10.1073/pnas.0807694106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2770-2775
    • Tal, M.C.1    Sasai, M.2    Lee, H.K.3    Yordy, B.4    Shadel, G.S.5    Iwasaki, A.6
  • 148
    • 84876685141 scopus 로고    scopus 로고
    • Receptor interacting protein kinase 2-mediated mitophagy regulates inflammasome activation during virus infection
    • doi:10.1038/ni.2563
    • Lupfer C, Thomas PG, Anand PK, Vogel P, Milasta S, Martinez J, et al. Receptor interacting protein kinase 2-mediated mitophagy regulates inflammasome activation during virus infection. Nat Immunol (2013) 14:480-8. doi:10.1038/ni.2563
    • (2013) Nat Immunol , vol.14 , pp. 480-488
    • Lupfer, C.1    Thomas, P.G.2    Anand, P.K.3    Vogel, P.4    Milasta, S.5    Martinez, J.6
  • 149
    • 79953176280 scopus 로고    scopus 로고
    • Autophagy controls IL-1 secretion by targeting pro-IL-1 for degradation
    • doi:10.1074/jbc.M110.202911
    • Harris J, Hartman M, Roche C, Zeng SG, O'Shea A, Sharp FA, et al. Autophagy controls IL-1 secretion by targeting pro-IL-1 for degradation. J Biol Chem (2011) 286:9587-97. doi:10.1074/jbc.M110.202911
    • (2011) J Biol Chem , vol.286 , pp. 9587-9597
    • Harris, J.1    Hartman, M.2    Roche, C.3    Zeng, S.G.4    O'Shea, A.5    Sharp, F.A.6
  • 150
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production
    • doi:10.1038/nature07383
    • Saitoh T, Fujita N, Jang MH, Uematsu S, Yang B-G, Satoh T, et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production. Nature (2008) 456:264-8. doi:10.1038/nature07383
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1    Fujita, N.2    Jang, M.H.3    Uematsu, S.4    Yang, B.-G.5    Satoh, T.6
  • 151
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction
    • doi:10.1038/ni.2215
    • Shi C-S, Shenderov K, Huang N-N, Kabat J, Abu-Asab M, Fitzgerald KA, et al. Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction. Nat Immunol (2012) 13:255-63. doi:10.1038/ni.2215
    • (2012) Nat Immunol , vol.13 , pp. 255-263
    • Shi, C.-S.1    Shenderov, K.2    Huang, N.-N.3    Kabat, J.4    Abu-Asab, M.5    Fitzgerald, K.A.6
  • 152
    • 79960542894 scopus 로고    scopus 로고
    • Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome
    • doi:10.4049/jimmunol.1100613
    • Bauernfeind F, Bartok E, Rieger A, Franchi L, Nuñez G, Hornung V. Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol (2011) 187:613-7. doi:10.4049/jimmunol.1100613
    • (2011) J Immunol , vol.187 , pp. 613-617
    • Bauernfeind, F.1    Bartok, E.2    Rieger, A.3    Franchi, L.4    Nuñez, G.5    Hornung, V.6
  • 153
    • 43249125839 scopus 로고    scopus 로고
    • Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
    • doi:10.1126/science.1156995
    • Dostert C, Pétrilli V, van Bruggen R, Steele C, Mossman BT, Tschopp J. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science (2008) 320:674-7. doi:10.1126/science.1156995
    • (2008) Science , vol.320 , pp. 674-677
    • Dostert, C.1    Pétrilli, V.2    van Bruggen, R.3    Steele, C.4    Mossman, B.T.5    Tschopp, J.6
  • 154
    • 77956574503 scopus 로고    scopus 로고
    • NOX-free inflammasome activation
    • doi:10.1182/blood-2010-06-287342
    • Latz E. NOX-free inflammasome activation. Blood (2010) 116:1393-4. doi:10.1182/blood-2010-06-287342
    • (2010) Blood , vol.116 , pp. 1393-1394
    • Latz, E.1
  • 155
    • 77956601381 scopus 로고    scopus 로고
    • Inflammasome activation in NADPH oxidase defective mononuclear phagocytes from patients with chronic granulomatous disease
    • doi:10.1182/blood-2010-01-264218
    • Meissner F, Seger RA, Moshous D, Fischer A, Reichenbach J, Zychlinsky A. Inflammasome activation in NADPH oxidase defective mononuclear phagocytes from patients with chronic granulomatous disease. Blood (2010) 116:1570-3. doi:10.1182/blood-2010-01-264218
    • (2010) Blood , vol.116 , pp. 1570-1573
    • Meissner, F.1    Seger, R.A.2    Moshous, D.3    Fischer, A.4    Reichenbach, J.5    Zychlinsky, A.6
  • 156
    • 79953046719 scopus 로고    scopus 로고
    • The inflammasome NLRs in immunity, inflammation, and associated diseases
    • doi:10.1146/annurev-immunol-031210-101405
    • Davis BK, Wen H, Ting JP. The inflammasome NLRs in immunity, inflammation, and associated diseases. Annu Rev Immunol (2011) 29:707-35. doi:10.1146/annurev-immunol-031210-101405
    • (2011) Annu Rev Immunol , vol.29 , pp. 707-735
    • Davis, B.K.1    Wen, H.2    Ting, J.P.3
  • 157
    • 82455210868 scopus 로고    scopus 로고
    • Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β
    • doi:10.1038/emboj.2011.398
    • Dupont N, Jiang S, Pilli M, Ornatowski W, Bhattacharya D, Deretic V. Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β. EMBO J (2011) 30:4701-11. doi:10.1038/emboj.2011.398
    • (2011) EMBO J , vol.30 , pp. 4701-4711
    • Dupont, N.1    Jiang, S.2    Pilli, M.3    Ornatowski, W.4    Bhattacharya, D.5    Deretic, V.6
  • 158
    • 84867770402 scopus 로고    scopus 로고
    • Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation
    • doi:10.1074/jbc.M112.407130
    • Juliana C, Fernandes-Alnemri T, Kang S, Farias A, Qin F, Alnemri ES. Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem (2012) 287:36617-22. doi:10.1074/jbc.M112.407130
    • (2012) J Biol Chem , vol.287 , pp. 36617-36622
    • Juliana, C.1    Fernandes-Alnemri, T.2    Kang, S.3    Farias, A.4    Qin, F.5    Alnemri, E.S.6
  • 159
    • 0142180157 scopus 로고    scopus 로고
    • Peptidoglycan molecular requirements allowing detection by Nod1 and Nod2
    • doi:10.1074/jbc.M307198200
    • Girardin SE, Travassos LH, Hervé M, Blanot D, Boneca IG, Philpott DJ, et al. Peptidoglycan molecular requirements allowing detection by Nod1 and Nod2. J Biol Chem (2003) 278:41702-8. doi:10.1074/jbc.M307198200
    • (2003) J Biol Chem , vol.278 , pp. 41702-41708
    • Girardin, S.E.1    Travassos, L.H.2    Hervé, M.3    Blanot, D.4    Boneca, I.G.5    Philpott, D.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.