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Volumn 21, Issue 8, 2013, Pages 430-441

Subversion of trafficking, apoptosis, and innate immunity by type III secretion system effectors

Author keywords

Cell survival modulation; Enteropathogens; Inflammatory response manipulation; Phagocytosis remodeling; Subversion of cellular trafficking; T3SS

Indexed keywords

BACTERIAL PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 8; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 84881029343     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2013.06.008     Document Type: Review
Times cited : (112)

References (110)
  • 1
    • 77950259334 scopus 로고    scopus 로고
    • Bacterial guanine nucleotide exchange factors SopE-like and WxxxE effectors
    • Bulgin R., et al. Bacterial guanine nucleotide exchange factors SopE-like and WxxxE effectors. Infect. Immun. 2010, 78:1417-1425.
    • (2010) Infect. Immun. , vol.78 , pp. 1417-1425
    • Bulgin, R.1
  • 2
    • 84878127508 scopus 로고    scopus 로고
    • Vesicle coats: structure, function, and general principles of assembly
    • Faini M., et al. Vesicle coats: structure, function, and general principles of assembly. Trends Cell Biol. 2013, 23:279-288.
    • (2013) Trends Cell Biol. , vol.23 , pp. 279-288
    • Faini, M.1
  • 3
    • 36849055107 scopus 로고    scopus 로고
    • Biogenesis of γ-secretase early in the secretory pathway
    • Kim J., et al. Biogenesis of γ-secretase early in the secretory pathway. J. Cell Biol. 2007, 179:951-963.
    • (2007) J. Cell Biol. , vol.179 , pp. 951-963
    • Kim, J.1
  • 4
    • 84864022938 scopus 로고    scopus 로고
    • Sec24 interaction is essential for localization and virulence-associated function of the bacterial effector protein NleA
    • Thanabalasuriar A., et al. Sec24 interaction is essential for localization and virulence-associated function of the bacterial effector protein NleA. Cell. Microbiol. 2012, 14:1206-1218.
    • (2012) Cell. Microbiol. , vol.14 , pp. 1206-1218
    • Thanabalasuriar, A.1
  • 5
    • 11144231319 scopus 로고    scopus 로고
    • Distribution of espI among clinical enterohaemorrhagic and enteropathogenic Escherichia coli isolates
    • Mundy R., et al. Distribution of espI among clinical enterohaemorrhagic and enteropathogenic Escherichia coli isolates. J. Med. Microbiol. 2004, 53:1145-1149.
    • (2004) J. Med. Microbiol. , vol.53 , pp. 1145-1149
    • Mundy, R.1
  • 6
    • 77649211841 scopus 로고    scopus 로고
    • The bacterial virulence factor NleA is required for the disruption of intestinal tight junctions by enteropathogenic Escherichia coli
    • Thanabalasuriar A., et al. The bacterial virulence factor NleA is required for the disruption of intestinal tight junctions by enteropathogenic Escherichia coli. Cell. Microbiol. 2010, 12:31-41.
    • (2010) Cell. Microbiol. , vol.12 , pp. 31-41
    • Thanabalasuriar, A.1
  • 7
    • 84875856252 scopus 로고    scopus 로고
    • The enterohemorrhagic Escherichia coli effector protein NleF binds mammalian Tmp21
    • Olsen R.L., et al. The enterohemorrhagic Escherichia coli effector protein NleF binds mammalian Tmp21. Vet. Microbiol. 2013, 64:164-170.
    • (2013) Vet. Microbiol. , vol.64 , pp. 164-170
    • Olsen, R.L.1
  • 8
    • 78650973579 scopus 로고    scopus 로고
    • The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold
    • Selyunin A.S., et al. The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold. Nature 2011, 469:107-111.
    • (2011) Nature , vol.469 , pp. 107-111
    • Selyunin, A.S.1
  • 9
    • 80051808365 scopus 로고    scopus 로고
    • EspG of enteropathogenic and enterohemorrhagic E. coli binds the Golgi matrix protein GM130 and disrupts the Golgi structure and function
    • Clements A., et al. EspG of enteropathogenic and enterohemorrhagic E. coli binds the Golgi matrix protein GM130 and disrupts the Golgi structure and function. Cell. Microbiol. 2011, 13:1429-1439.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1429-1439
    • Clements, A.1
  • 10
    • 84865693202 scopus 로고    scopus 로고
    • Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses
    • Dong N., et al. Structurally distinct bacterial TBC-like GAPs link Arf GTPase to Rab1 inactivation to counteract host defenses. Cell 2012, 150:1029-1041.
    • (2012) Cell , vol.150 , pp. 1029-1041
    • Dong, N.1
  • 11
    • 79851474020 scopus 로고    scopus 로고
    • Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase
    • Germane K.L., Spiller B.W. Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase. Biochemistry 2011, 50:917-919.
    • (2011) Biochemistry , vol.50 , pp. 917-919
    • Germane, K.L.1    Spiller, B.W.2
  • 12
    • 84875899190 scopus 로고    scopus 로고
    • Proteolytic elimination of N-myristoylmodifications by the Shigella virulence factor IpaJ
    • Burnaevskiy N., et al. Proteolytic elimination of N-myristoylmodifications by the Shigella virulence factor IpaJ. Nature 2013, 496:106-109.
    • (2013) Nature , vol.496 , pp. 106-109
    • Burnaevskiy, N.1
  • 13
    • 77957852451 scopus 로고    scopus 로고
    • Salmonella-directed recruitment of new membrane to invasion foci via the host exocyst complex
    • Nichols C.D., Casanova J.E. Salmonella-directed recruitment of new membrane to invasion foci via the host exocyst complex. Curr. Biol. 2010, 20:1316-1320.
    • (2010) Curr. Biol. , vol.20 , pp. 1316-1320
    • Nichols, C.D.1    Casanova, J.E.2
  • 14
    • 0040611104 scopus 로고    scopus 로고
    • Controlling the maturation of pathogen-containing vacuoles: a matter of life and death
    • Meresse S., et al. Controlling the maturation of pathogen-containing vacuoles: a matter of life and death. Nat. Cell Biol. 1999, 1:E183-E188.
    • (1999) Nat. Cell Biol. , vol.1
    • Meresse, S.1
  • 15
    • 0242485924 scopus 로고    scopus 로고
    • The rab7 GTPase controls the maturation of Salmonella typhimurium-containing vacuoles in HeLa cells
    • Meresse S., et al. The rab7 GTPase controls the maturation of Salmonella typhimurium-containing vacuoles in HeLa cells. EMBO J. 1999, 18:4394-4403.
    • (1999) EMBO J. , vol.18 , pp. 4394-4403
    • Meresse, S.1
  • 16
    • 84869108479 scopus 로고    scopus 로고
    • Salmonella inhibits retrograde trafficking of mannose-6-phosphate receptors and lysosome function
    • McGourty K., et al. Salmonella inhibits retrograde trafficking of mannose-6-phosphate receptors and lysosome function. Science 2012, 338:963-967.
    • (2012) Science , vol.338 , pp. 963-967
    • McGourty, K.1
  • 17
    • 33947130097 scopus 로고    scopus 로고
    • Salmonella trafficking is defined by continuous dynamic interactions with the endolysosomal system
    • Drecktrah D., et al. Salmonella trafficking is defined by continuous dynamic interactions with the endolysosomal system. Traffic 2007, 8:212-225.
    • (2007) Traffic , vol.8 , pp. 212-225
    • Drecktrah, D.1
  • 18
    • 56149122681 scopus 로고    scopus 로고
    • Dynamic behavior of Salmonella-induced membrane tubules in epithelial cells
    • Drecktrah D., et al. Dynamic behavior of Salmonella-induced membrane tubules in epithelial cells. Traffic 2008, 9:2117-2129.
    • (2008) Traffic , vol.9 , pp. 2117-2129
    • Drecktrah, D.1
  • 19
    • 56149100817 scopus 로고    scopus 로고
    • Dynamic remodeling of the endosomal system during formation of Salmonella-induced filaments by intracellular Salmonella enterica
    • Rajashekar R., et al. Dynamic remodeling of the endosomal system during formation of Salmonella-induced filaments by intracellular Salmonella enterica. Traffic 2008, 9:2100-2116.
    • (2008) Traffic , vol.9 , pp. 2100-2116
    • Rajashekar, R.1
  • 20
    • 0033230438 scopus 로고    scopus 로고
    • The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes
    • Blocker A., et al. The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J. Cell Biol. 1999, 147:683-693.
    • (1999) J. Cell Biol. , vol.147 , pp. 683-693
    • Blocker, A.1
  • 21
    • 0026534213 scopus 로고
    • IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole
    • High N., et al. IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole. EMBO J. 1992, 11:1991-1999.
    • (1992) EMBO J. , vol.11 , pp. 1991-1999
    • High, N.1
  • 22
    • 0034110502 scopus 로고    scopus 로고
    • Shigella flexneri IpaH(7.8) facilitates escape of virulent bacteria from the endocytic vacuoles of mouse and human macrophages
    • Fernandez-Prada C.M., et al. Shigella flexneri IpaH(7.8) facilitates escape of virulent bacteria from the endocytic vacuoles of mouse and human macrophages. Infect. Immun. 2000, 68:3608-3619.
    • (2000) Infect. Immun. , vol.68 , pp. 3608-3619
    • Fernandez-Prada, C.M.1
  • 23
    • 0032839369 scopus 로고    scopus 로고
    • Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility
    • Mounier J., et al. Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility. J. Cell Sci. 1999, 112:2069-2080.
    • (1999) J. Cell Sci. , vol.112 , pp. 2069-2080
    • Mounier, J.1
  • 24
    • 0035675043 scopus 로고    scopus 로고
    • Salmonella entry into host cells: the work in concert of type III secreted effector proteins
    • Zhou D., Galan J. Salmonella entry into host cells: the work in concert of type III secreted effector proteins. Microbes Infect. 2001, 3:1293-1298.
    • (2001) Microbes Infect. , vol.3 , pp. 1293-1298
    • Zhou, D.1    Galan, J.2
  • 25
    • 0036319223 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium effector SigD/SopB is membrane-associated and ubiquitinated inside host cells
    • Marcus S.L., et al. Salmonella enterica serovar Typhimurium effector SigD/SopB is membrane-associated and ubiquitinated inside host cells. Cell. Microbiol. 2002, 4:435-446.
    • (2002) Cell. Microbiol. , vol.4 , pp. 435-446
    • Marcus, S.L.1
  • 26
    • 80053111626 scopus 로고    scopus 로고
    • Shigella flexneri infection generates the lipid PI5P to alter endocytosis and prevent termination of EGFR signaling
    • Ramel D., et al. Shigella flexneri infection generates the lipid PI5P to alter endocytosis and prevent termination of EGFR signaling. Sci. Signal. 2011, 4:ra61.
    • (2011) Sci. Signal. , vol.4
    • Ramel, D.1
  • 27
    • 18644379244 scopus 로고    scopus 로고
    • Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology
    • Niebuhr K., et al. Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology. EMBO J. 2002, 21:5069-5078.
    • (2002) EMBO J. , vol.21 , pp. 5069-5078
    • Niebuhr, K.1
  • 28
    • 0034018021 scopus 로고    scopus 로고
    • Macrophage class A scavenger receptor-mediated phagocytosis of Escherichia coli: role of cell heterogeneity, microbial strain, and culture conditions in vitro
    • Peiser L., et al. Macrophage class A scavenger receptor-mediated phagocytosis of Escherichia coli: role of cell heterogeneity, microbial strain, and culture conditions in vitro. Infect. Immun. 2000, 68:1953-1963.
    • (2000) Infect. Immun. , vol.68 , pp. 1953-1963
    • Peiser, L.1
  • 29
    • 0025278076 scopus 로고
    • Phagocytosis mediated by three distinct Fcγ receptor classes on human leukocytes
    • Anderson C.L., et al. Phagocytosis mediated by three distinct Fcγ receptor classes on human leukocytes. J. Exp. Med. 1990, 171:1333-1345.
    • (1990) J. Exp. Med. , vol.171 , pp. 1333-1345
    • Anderson, C.L.1
  • 30
    • 0026773636 scopus 로고
    • Macrophage cytoskeleton association with CR3 and CR4 regulates receptor mobility and phagocytosis of iC3b-opsonized erythrocytes
    • Ross G.D., et al. Macrophage cytoskeleton association with CR3 and CR4 regulates receptor mobility and phagocytosis of iC3b-opsonized erythrocytes. J. Leukoc. Biol. 1992, 51:109-117.
    • (1992) J. Leukoc. Biol. , vol.51 , pp. 109-117
    • Ross, G.D.1
  • 31
    • 0025376298 scopus 로고
    • Pathways for the penetration of enteroinvasive Yersinia into mammalian cells
    • Isberg R.R. Pathways for the penetration of enteroinvasive Yersinia into mammalian cells. Mol. Biol. Med. 1990, 7:73-82.
    • (1990) Mol. Biol. Med. , vol.7 , pp. 73-82
    • Isberg, R.R.1
  • 32
    • 74549169867 scopus 로고    scopus 로고
    • The T3SS effector EspT defines a new category of invasive enteropathogenic E. coli (EPEC) which form intracellular actin pedestals
    • Bulgin R., et al. The T3SS effector EspT defines a new category of invasive enteropathogenic E. coli (EPEC) which form intracellular actin pedestals. PLoS Pathog. 2009, 5:e1000683.
    • (2009) PLoS Pathog. , vol.5
    • Bulgin, R.1
  • 33
    • 34248645977 scopus 로고    scopus 로고
    • Translocation of enteropathogenic Escherichia coli across an in vitro M cell model is regulated by its type III secretion system
    • Martinez-Argudo I., et al. Translocation of enteropathogenic Escherichia coli across an in vitro M cell model is regulated by its type III secretion system. Cell. Microbiol. 2007, 9:1538-1546.
    • (2007) Cell. Microbiol. , vol.9 , pp. 1538-1546
    • Martinez-Argudo, I.1
  • 34
    • 0032911257 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli inhibits phagocytosis
    • Goosney D.L., et al. Enteropathogenic Escherichia coli inhibits phagocytosis. Infect. Immun. 1999, 67:490-495.
    • (1999) Infect. Immun. , vol.67 , pp. 490-495
    • Goosney, D.L.1
  • 35
    • 0031689503 scopus 로고    scopus 로고
    • Identification of an amino-terminal substrate-binding domain in the Yersinia tyrosine phosphatase that is required for efficient recognition of focal adhesion targets
    • Black D.S., et al. Identification of an amino-terminal substrate-binding domain in the Yersinia tyrosine phosphatase that is required for efficient recognition of focal adhesion targets. Mol. Microbiol. 1998, 29:1263-1274.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1263-1274
    • Black, D.S.1
  • 36
    • 84887212578 scopus 로고    scopus 로고
    • Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH
    • de la Puerta M.L., et al. Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH. PLoS ONE 2009, 4:e4431.
    • (2009) PLoS ONE , vol.4
    • de la Puerta, M.L.1
  • 37
    • 0032841813 scopus 로고    scopus 로고
    • YopH dephosphorylates Cas and Fyn-binding protein in macrophages
    • Hamid N., et al. YopH dephosphorylates Cas and Fyn-binding protein in macrophages. Microb. Pathog. 1999, 27:231-242.
    • (1999) Microb. Pathog. , vol.27 , pp. 231-242
    • Hamid, N.1
  • 38
    • 0030978909 scopus 로고    scopus 로고
    • The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
    • Persson C., et al. The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions. EMBO J. 1997, 16:2307-2318.
    • (1997) EMBO J. , vol.16 , pp. 2307-2318
    • Persson, C.1
  • 39
    • 0034523546 scopus 로고    scopus 로고
    • CAS/Crk signalling mediates uptake of Yersinia into human epithelial cells
    • Weidow C.L., et al. CAS/Crk signalling mediates uptake of Yersinia into human epithelial cells. Cell. Microbiol. 2000, 2:549-560.
    • (2000) Cell. Microbiol. , vol.2 , pp. 549-560
    • Weidow, C.L.1
  • 40
    • 0034097414 scopus 로고    scopus 로고
    • GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure
    • Von Pawel-Rammingen U., et al. GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure. Mol. Microbiol. 2000, 36:737-748.
    • (2000) Mol. Microbiol. , vol.36 , pp. 737-748
    • Von Pawel-Rammingen, U.1
  • 41
    • 0035035193 scopus 로고    scopus 로고
    • YopE of Yersinia, a GAP for Rho GTPases, selectively modulates Rac-dependent actin structures in endothelial cells
    • Andor A., et al. YopE of Yersinia, a GAP for Rho GTPases, selectively modulates Rac-dependent actin structures in endothelial cells. Cell. Microbiol. 2001, 3:301-310.
    • (2001) Cell. Microbiol. , vol.3 , pp. 301-310
    • Andor, A.1
  • 42
    • 66149150664 scopus 로고    scopus 로고
    • Yersinia enterocolitica differentially modulates RhoG activity in host cells
    • Roppenser B., et al. Yersinia enterocolitica differentially modulates RhoG activity in host cells. J. Cell Sci. 2009, 122:696-705.
    • (2009) J. Cell Sci. , vol.122 , pp. 696-705
    • Roppenser, B.1
  • 43
    • 33748192535 scopus 로고    scopus 로고
    • Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors
    • Prehna G., et al. Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors. Cell 2006, 126:869-880.
    • (2006) Cell , vol.126 , pp. 869-880
    • Prehna, G.1
  • 44
    • 77950481822 scopus 로고    scopus 로고
    • Sequestering of Rac by the Yersinia effector YopO blocks Fcγ receptor-mediated phagocytosis
    • Groves E., et al. Sequestering of Rac by the Yersinia effector YopO blocks Fcγ receptor-mediated phagocytosis. J. Biol. Chem. 2010, 285:4087-4098.
    • (2010) J. Biol. Chem. , vol.285 , pp. 4087-4098
    • Groves, E.1
  • 45
    • 0037417878 scopus 로고    scopus 로고
    • Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases
    • Shao F., et al. Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:904-909.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 904-909
    • Shao, F.1
  • 46
    • 77951474502 scopus 로고    scopus 로고
    • A bacterial effector targets host DH-PH domain RhoGEFs and antagonizes macrophage phagocytosis
    • Dong N., et al. A bacterial effector targets host DH-PH domain RhoGEFs and antagonizes macrophage phagocytosis. EMBO J. 2010, 29:1363-1376.
    • (2010) EMBO J. , vol.29 , pp. 1363-1376
    • Dong, N.1
  • 47
    • 36749001580 scopus 로고    scopus 로고
    • The enteropathogenic E. coli effector EspB facilitates microvillus effacing and antiphagocytosis by inhibiting myosin function
    • Iizumi Y., et al. The enteropathogenic E. coli effector EspB facilitates microvillus effacing and antiphagocytosis by inhibiting myosin function. Cell Host Microbe 2007, 2:383-392.
    • (2007) Cell Host Microbe , vol.2 , pp. 383-392
    • Iizumi, Y.1
  • 48
    • 42149144665 scopus 로고    scopus 로고
    • EspJ of enteropathogenic and enterohaemorrhagic Escherichia coli inhibits opsono-phagocytosis
    • Marches O., et al. EspJ of enteropathogenic and enterohaemorrhagic Escherichia coli inhibits opsono-phagocytosis. Cell. Microbiol. 2008, 10:1104-1115.
    • (2008) Cell. Microbiol. , vol.10 , pp. 1104-1115
    • Marches, O.1
  • 49
    • 33646357752 scopus 로고    scopus 로고
    • The enteropathogenic Escherichia coli EspF effector molecule inhibits PI-3 kinase-mediated uptake independently of mitochondrial targeting
    • Quitard S., et al. The enteropathogenic Escherichia coli EspF effector molecule inhibits PI-3 kinase-mediated uptake independently of mitochondrial targeting. Cell. Microbiol. 2006, 8:972-981.
    • (2006) Cell. Microbiol. , vol.8 , pp. 972-981
    • Quitard, S.1
  • 50
    • 51949110637 scopus 로고    scopus 로고
    • EspF interacts with nucleation-promoting factors to recruit junctional proteins into pedestals for pedestal maturation and disruption of paracellular permeability
    • Peralta-Ramirez J., et al. EspF interacts with nucleation-promoting factors to recruit junctional proteins into pedestals for pedestal maturation and disruption of paracellular permeability. Infect. Immun. 2008, 76:3854-3868.
    • (2008) Infect. Immun. , vol.76 , pp. 3854-3868
    • Peralta-Ramirez, J.1
  • 51
    • 34748911856 scopus 로고    scopus 로고
    • The type III effector EspF coordinates membrane trafficking by the spatiotemporal activation of two eukaryotic signaling pathways
    • Alto N.M., et al. The type III effector EspF coordinates membrane trafficking by the spatiotemporal activation of two eukaryotic signaling pathways. J. Cell Biol. 2007, 178:1265-1278.
    • (2007) J. Cell Biol. , vol.178 , pp. 1265-1278
    • Alto, N.M.1
  • 52
    • 39749182234 scopus 로고    scopus 로고
    • Apoptosis: controlled demolition at the cellular level
    • Taylor R.C., et al. Apoptosis: controlled demolition at the cellular level. Nat. Rev. Mol. Cell Biol. 2008, 9:231-241.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 231-241
    • Taylor, R.C.1
  • 53
    • 77649260428 scopus 로고    scopus 로고
    • NleH effectors interact with Bax inhibitor-1 to block apoptosis during enteropathogenic Escherichia coli infection
    • Hemrajani C., et al. NleH effectors interact with Bax inhibitor-1 to block apoptosis during enteropathogenic Escherichia coli infection. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:3129-3134.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3129-3134
    • Hemrajani, C.1
  • 54
    • 34248348720 scopus 로고    scopus 로고
    • Shigella flexneri inhibits staurosporine-induced apoptosis in epithelial cells
    • Clark C.S., Maurelli A.T. Shigella flexneri inhibits staurosporine-induced apoptosis in epithelial cells. Infect. Immun. 2007, 75:2531-2539.
    • (2007) Infect. Immun. , vol.75 , pp. 2531-2539
    • Clark, C.S.1    Maurelli, A.T.2
  • 55
    • 84858411647 scopus 로고    scopus 로고
    • Calpain activation by the Shigella flexneri effector VirA regulates key steps in the formation and life of the bacterium's epithelial niche
    • Bergounioux J., et al. Calpain activation by the Shigella flexneri effector VirA regulates key steps in the formation and life of the bacterium's epithelial niche. Cell Host Microbe 2012, 11:240-252.
    • (2012) Cell Host Microbe , vol.11 , pp. 240-252
    • Bergounioux, J.1
  • 56
    • 84875022980 scopus 로고    scopus 로고
    • The E. coli effector protein NleF is a caspase inhibitor
    • Blasche S., et al. The E. coli effector protein NleF is a caspase inhibitor. PLoS ONE 2013, 8:e58937.
    • (2013) PLoS ONE , vol.8
    • Blasche, S.1
  • 57
    • 15744385951 scopus 로고    scopus 로고
    • The Salmonella effector protein SopB protects epithelial cells from apoptosis by sustained activation of Akt
    • Knodler L.A., et al. The Salmonella effector protein SopB protects epithelial cells from apoptosis by sustained activation of Akt. J. Biol. Chem. 2005, 280:9058-9064.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9058-9064
    • Knodler, L.A.1
  • 58
    • 41849151481 scopus 로고    scopus 로고
    • Salmonella AvrA coordinates suppression of host immune and apoptotic defenses via JNK pathway blockade
    • Jones R.M., et al. Salmonella AvrA coordinates suppression of host immune and apoptotic defenses via JNK pathway blockade. Cell Host Microbe 2008, 3:233-244.
    • (2008) Cell Host Microbe , vol.3 , pp. 233-244
    • Jones, R.M.1
  • 59
    • 6344235634 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli EspF is targeted to mitochondria and is required to initiate the mitochondrial death pathway
    • Nougayrede J.P., Donnenberg M.S. Enteropathogenic Escherichia coli EspF is targeted to mitochondria and is required to initiate the mitochondrial death pathway. Cell. Microbiol. 2004, 6:1097-1111.
    • (2004) Cell. Microbiol. , vol.6 , pp. 1097-1111
    • Nougayrede, J.P.1    Donnenberg, M.S.2
  • 60
    • 72449156546 scopus 로고    scopus 로고
    • The enteropathogenic Escherichia coli effector Cif induces delayed apoptosis in epithelial cells
    • Samba-Louaka A., et al. The enteropathogenic Escherichia coli effector Cif induces delayed apoptosis in epithelial cells. Infect. Immun. 2009, 77:5471-5477.
    • (2009) Infect. Immun. , vol.77 , pp. 5471-5477
    • Samba-Louaka, A.1
  • 61
    • 84857885364 scopus 로고    scopus 로고
    • The interplay between the Escherichia coli Rho guanine nucleotide exchange factor effectors and the mammalian RhoGEF inhibitor EspH
    • e00250-11
    • Wong A.R., et al. The interplay between the Escherichia coli Rho guanine nucleotide exchange factor effectors and the mammalian RhoGEF inhibitor EspH. mBio 2012, 3. e00250-11, http://dx.doi.org/10.1128/mBio.00250-11.
    • (2012) mBio , vol.3
    • Wong, A.R.1
  • 62
    • 0034596826 scopus 로고    scopus 로고
    • Salmonella-induced caspase-2 activation in macrophages: a novel mechanism in pathogen-mediated apoptosis
    • Jesenberger V., et al. Salmonella-induced caspase-2 activation in macrophages: a novel mechanism in pathogen-mediated apoptosis. J. Exp. Med. 2000, 192:1035-1046.
    • (2000) J. Exp. Med. , vol.192 , pp. 1035-1046
    • Jesenberger, V.1
  • 63
    • 77649216223 scopus 로고    scopus 로고
    • The type III secretion effector NleE inhibits NF-κB activation
    • Nadler C., et al. The type III secretion effector NleE inhibits NF-κB activation. PLoS Pathog. 2010, 6:e1000743.
    • (2010) PLoS Pathog. , vol.6
    • Nadler, C.1
  • 64
    • 77954066144 scopus 로고    scopus 로고
    • The type III effectors NleE and NleB from enteropathogenic E. coli and OspZ from Shigella block nuclear translocation of NF-κB p65
    • Newton H.J., et al. The type III effectors NleE and NleB from enteropathogenic E. coli and OspZ from Shigella block nuclear translocation of NF-κB p65. PLoS Pathog. 2010, 6:e1000898.
    • (2010) PLoS Pathog. , vol.6
    • Newton, H.J.1
  • 65
    • 77958133862 scopus 로고    scopus 로고
    • Inhibition of NF-κB signaling in human dendritic cells by the enteropathogenic Escherichia coli effector protein NleE
    • Vossenkamper A., et al. Inhibition of NF-κB signaling in human dendritic cells by the enteropathogenic Escherichia coli effector protein NleE. J. Immunol. 2010, 185:4118-4127.
    • (2010) J. Immunol. , vol.185 , pp. 4118-4127
    • Vossenkamper, A.1
  • 66
    • 84872566186 scopus 로고    scopus 로고
    • NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-κB activation
    • Gao X., et al. NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-κB activation. Cell Host Microbe 2013, 13:87-99.
    • (2013) Cell Host Microbe , vol.13 , pp. 87-99
    • Gao, X.1
  • 67
    • 78651257387 scopus 로고    scopus 로고
    • NleC, a type III secretion protease, compromises NF-κB activation by targeting p65/RelA
    • Yen H., et al. NleC, a type III secretion protease, compromises NF-κB activation by targeting p65/RelA. PLoS Pathog. 2010, 6:e1001231.
    • (2010) PLoS Pathog. , vol.6
    • Yen, H.1
  • 68
    • 85047686900 scopus 로고    scopus 로고
    • Functional differences and interactions between the Escherichia coli type III secretion system effectors NleH1 and NleH2
    • Pham T.H., et al. Functional differences and interactions between the Escherichia coli type III secretion system effectors NleH1 and NleH2. Infect. Immun. 2012, 80:2133-2140.
    • (2012) Infect. Immun. , vol.80 , pp. 2133-2140
    • Pham, T.H.1
  • 69
    • 74549206085 scopus 로고    scopus 로고
    • Bacterial effector binding to ribosomal protein s3 subverts NF-κB function
    • Gao X., et al. Bacterial effector binding to ribosomal protein s3 subverts NF-κB function. PLoS Pathog. 2009, 5:e1000708.
    • (2009) PLoS Pathog. , vol.5
    • Gao, X.1
  • 70
    • 84855263757 scopus 로고    scopus 로고
    • The enteropathogenic E. coli (EPEC) Tir effector inhibits NF-κB activity by targeting TNFα receptor-associated factors
    • Ruchaud-Sparagano M.H., et al. The enteropathogenic E. coli (EPEC) Tir effector inhibits NF-κB activity by targeting TNFα receptor-associated factors. PLoS Pathog. 2011, 7:e1002414.
    • (2011) PLoS Pathog. , vol.7
    • Ruchaud-Sparagano, M.H.1
  • 71
    • 84867746584 scopus 로고    scopus 로고
    • Inhibition of TLR signaling by a bacterial protein containing immunoreceptor tyrosine-based inhibitory motifs
    • Yan D., et al. Inhibition of TLR signaling by a bacterial protein containing immunoreceptor tyrosine-based inhibitory motifs. Nat. Immunol. 2012, 13:1063-1071.
    • (2012) Nat. Immunol. , vol.13 , pp. 1063-1071
    • Yan, D.1
  • 72
    • 25444461419 scopus 로고    scopus 로고
    • The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes
    • Kim D.W., et al. The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:14046-14051.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14046-14051
    • Kim, D.W.1
  • 73
    • 84874573643 scopus 로고    scopus 로고
    • The Shigella type three secretion system effector OspG directly and specifically binds to host ubiquitin for activation
    • Zhou Y., et al. The Shigella type three secretion system effector OspG directly and specifically binds to host ubiquitin for activation. PLoS ONE 2013, 8:e57558.
    • (2013) PLoS ONE , vol.8
    • Zhou, Y.1
  • 74
    • 57149105701 scopus 로고    scopus 로고
    • Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
    • Singer A.U., et al. Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases. Nat. Struct. Mol. Biol. 2008, 15:1293-1301.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1293-1301
    • Singer, A.U.1
  • 75
    • 77955109451 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKγ to dampen the host NF-κB-mediated inflammatory response
    • Ashida H., et al. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKγ to dampen the host NF-κB-mediated inflammatory response. Nat. Cell Biol. 2010, 12:66-73.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 66-73
    • Ashida, H.1
  • 76
    • 84862818454 scopus 로고    scopus 로고
    • The Shigella flexneri effector OspI deamidates UBC13 to dampen the inflammatory response
    • Sanada T., et al. The Shigella flexneri effector OspI deamidates UBC13 to dampen the inflammatory response. Nature 2012, 483:623-626.
    • (2012) Nature , vol.483 , pp. 623-626
    • Sanada, T.1
  • 77
    • 33746930289 scopus 로고    scopus 로고
    • Comparison of YopE and YopT activities in counteracting host signalling responses to Yersinia pseudotuberculosis infection
    • Viboud G.I., et al. Comparison of YopE and YopT activities in counteracting host signalling responses to Yersinia pseudotuberculosis infection. Cell. Microbiol. 2006, 8:1504-1515.
    • (2006) Cell. Microbiol. , vol.8 , pp. 1504-1515
    • Viboud, G.I.1
  • 78
    • 0034711403 scopus 로고    scopus 로고
    • Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease
    • Orth K., et al. Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease. Science 2000, 290:1594-1597.
    • (2000) Science , vol.290 , pp. 1594-1597
    • Orth, K.1
  • 79
    • 84864518388 scopus 로고    scopus 로고
    • Serine/threonine acetylation of TGFβ-activated kinase (TAK1) by Yersinia pestis YopJ inhibits innate immune signaling
    • Paquette N., et al. Serine/threonine acetylation of TGFβ-activated kinase (TAK1) by Yersinia pestis YopJ inhibits innate immune signaling. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:12710-12715.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 12710-12715
    • Paquette, N.1
  • 80
    • 44449107633 scopus 로고    scopus 로고
    • Salmonella secreted factor L deubiquitinase of Salmonella typhimurium inhibits NF-κB, suppresses IκBα ubiquitination and modulates innate immune responses
    • Le Negrate G., et al. Salmonella secreted factor L deubiquitinase of Salmonella typhimurium inhibits NF-κB, suppresses IκBα ubiquitination and modulates innate immune responses. J. Immunol. 2008, 180:5045-5056.
    • (2008) J. Immunol. , vol.180 , pp. 5045-5056
    • Le Negrate, G.1
  • 81
    • 0037972467 scopus 로고    scopus 로고
    • A Salmonella enterica serovar typhimurium translocated leucine-rich repeat effector protein inhibits NF-κB-dependent gene expression
    • Haraga A., Miller S.I. A Salmonella enterica serovar typhimurium translocated leucine-rich repeat effector protein inhibits NF-κB-dependent gene expression. Infect. Immun. 2003, 71:4052-4058.
    • (2003) Infect. Immun. , vol.71 , pp. 4052-4058
    • Haraga, A.1    Miller, S.I.2
  • 82
    • 0037105562 scopus 로고    scopus 로고
    • Cutting edge: Salmonella AvrA effector inhibits the key proinflammatory, anti-apoptotic NF-κB pathway
    • Collier-Hyams L.S., et al. Cutting edge: Salmonella AvrA effector inhibits the key proinflammatory, anti-apoptotic NF-κB pathway. J. Immunol. 2002, 169:2846-2850.
    • (2002) J. Immunol. , vol.169 , pp. 2846-2850
    • Collier-Hyams, L.S.1
  • 83
    • 33644976705 scopus 로고    scopus 로고
    • MAP kinases in immune responses
    • Zhang Y.L., Dong C. MAP kinases in immune responses. Cell. Mol. Immunol. 2005, 2:20-27.
    • (2005) Cell. Mol. Immunol. , vol.2 , pp. 20-27
    • Zhang, Y.L.1    Dong, C.2
  • 84
    • 78650875210 scopus 로고    scopus 로고
    • Metalloprotease type III effectors that specifically cleave JNK and NF-κB
    • Baruch K., et al. Metalloprotease type III effectors that specifically cleave JNK and NF-κB. EMBO J. 2011, 30:221-231.
    • (2011) EMBO J. , vol.30 , pp. 221-231
    • Baruch, K.1
  • 85
    • 80052305157 scopus 로고    scopus 로고
    • Attaching and effacing bacterial effector NleC suppresses epithelial inflammatory responses by inhibiting NF-κB and p38 mitogen-activated protein kinase activation
    • Sham H.P., et al. Attaching and effacing bacterial effector NleC suppresses epithelial inflammatory responses by inhibiting NF-κB and p38 mitogen-activated protein kinase activation. Infect. Immun. 2011, 79:3552-3562.
    • (2011) Infect. Immun. , vol.79 , pp. 3552-3562
    • Sham, H.P.1
  • 86
    • 33947727977 scopus 로고    scopus 로고
    • Type III secretion effectors of the IpaH family are E3 ubiquitin ligases
    • Rohde J.R., et al. Type III secretion effectors of the IpaH family are E3 ubiquitin ligases. Cell Host Microbe 2007, 1:77-83.
    • (2007) Cell Host Microbe , vol.1 , pp. 77-83
    • Rohde, J.R.1
  • 87
    • 33847154642 scopus 로고    scopus 로고
    • The phosphothreonine lyase activity of a bacterial type III effector family
    • Li H., et al. The phosphothreonine lyase activity of a bacterial type III effector family. Science 2007, 315:1000-1003.
    • (2007) Science , vol.315 , pp. 1000-1003
    • Li, H.1
  • 88
    • 33846958783 scopus 로고    scopus 로고
    • An injected bacterial effector targets chromatin access for transcription factor NF-κB to alter transcription of host genes involved in immune responses
    • Arbibe L., et al. An injected bacterial effector targets chromatin access for transcription factor NF-κB to alter transcription of host genes involved in immune responses. Nat. Immunol. 2007, 8:47-56.
    • (2007) Nat. Immunol. , vol.8 , pp. 47-56
    • Arbibe, L.1
  • 89
    • 0036366158 scopus 로고    scopus 로고
    • YopH prevents monocyte chemoattractant protein 1 expression in macrophages and T-cell proliferation through inactivation of the phosphatidylinositol 3-kinase pathway
    • Sauvonnet N., et al. YopH prevents monocyte chemoattractant protein 1 expression in macrophages and T-cell proliferation through inactivation of the phosphatidylinositol 3-kinase pathway. Mol. Microbiol. 2002, 45:805-815.
    • (2002) Mol. Microbiol. , vol.45 , pp. 805-815
    • Sauvonnet, N.1
  • 90
    • 0033578923 scopus 로고    scopus 로고
    • Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector
    • Orth K., et al. Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science 1999, 285:1920-1923.
    • (1999) Science , vol.285 , pp. 1920-1923
    • Orth, K.1
  • 91
    • 70049109028 scopus 로고    scopus 로고
    • Salmonella Typhimurium type III secretion effectors stimulate innate immune responses in cultured epithelial cells
    • Bruno V.M., et al. Salmonella Typhimurium type III secretion effectors stimulate innate immune responses in cultured epithelial cells. PLoS Pathog. 2009, 5:e1000538.
    • (2009) PLoS Pathog. , vol.5
    • Bruno, V.M.1
  • 92
    • 84876282419 scopus 로고    scopus 로고
    • Manipulation of small Rho GTPases is a pathogen-induced process detected by NOD1
    • Keestra A.M., et al. Manipulation of small Rho GTPases is a pathogen-induced process detected by NOD1. Nature 2013, 496:233-237.
    • (2013) Nature , vol.496 , pp. 233-237
    • Keestra, A.M.1
  • 93
    • 35649026345 scopus 로고    scopus 로고
    • Salmonella enterica serovar typhimurium exploits inflammation to compete with the intestinal microbiota
    • Stecher B., et al. Salmonella enterica serovar typhimurium exploits inflammation to compete with the intestinal microbiota. PLoS Biol. 2007, 5:2177-2189.
    • (2007) PLoS Biol. , vol.5 , pp. 2177-2189
    • Stecher, B.1
  • 94
    • 84863451084 scopus 로고    scopus 로고
    • Phage-mediated acquisition of a type III secreted effector protein boosts growth of salmonella by nitrate respiration
    • e00143-12
    • Lopez C.A., et al. Phage-mediated acquisition of a type III secreted effector protein boosts growth of salmonella by nitrate respiration. MBio 2012, 3. e00143-12, http://dx.doi.org/10.1128/mBio.00143-12.
    • (2012) MBio , vol.3
    • Lopez, C.A.1
  • 95
    • 77957157893 scopus 로고    scopus 로고
    • Gut inflammation provides a respiratory electron acceptor for Salmonella
    • Winter S.E., et al. Gut inflammation provides a respiratory electron acceptor for Salmonella. Nature 2010, 467:426-429.
    • (2010) Nature , vol.467 , pp. 426-429
    • Winter, S.E.1
  • 96
    • 81355160488 scopus 로고    scopus 로고
    • The WxxxE effector EspT triggers expression of immune mediators in an Erk/JNK and NF-κB-dependent manner
    • Raymond B., et al. The WxxxE effector EspT triggers expression of immune mediators in an Erk/JNK and NF-κB-dependent manner. Cell. Microbiol. 2011, 13:1881-1893.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1881-1893
    • Raymond, B.1
  • 97
    • 57149093623 scopus 로고    scopus 로고
    • GEF-H1 mediated control of NOD1 dependent NF-κB activation by Shigella effectors
    • Fukazawa A., et al. GEF-H1 mediated control of NOD1 dependent NF-κB activation by Shigella effectors. PLoS Pathog. 2008, 4:e1000228.
    • (2008) PLoS Pathog. , vol.4
    • Fukazawa, A.1
  • 98
    • 84855221528 scopus 로고    scopus 로고
    • A Salmonella virulence factor activates the NOD1/NOD2 signaling pathway
    • e00266-11
    • Keestra A.M., et al. A Salmonella virulence factor activates the NOD1/NOD2 signaling pathway. mBio 2011, 2. e00266-11, http://dx.doi.org/10.1128/mBio.00266-11.
    • (2011) mBio , vol.2
    • Keestra, A.M.1
  • 99
    • 58449083290 scopus 로고    scopus 로고
    • Pyroptosis: host cell death and inflammation
    • Bergsbaken T., et al. Pyroptosis: host cell death and inflammation. Nat. Rev. Microbiol. 2009, 7:99-109.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 99-109
    • Bergsbaken, T.1
  • 100
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan S., et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 2004, 430:213-218.
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1
  • 101
    • 68349131301 scopus 로고    scopus 로고
    • The S. Typhimurium effector SopE induces caspase-1 activation in stromal cells to initiate gut inflammation
    • Muller A.J., et al. The S. Typhimurium effector SopE induces caspase-1 activation in stromal cells to initiate gut inflammation. Cell Host Microbe 2009, 6:125-136.
    • (2009) Cell Host Microbe , vol.6 , pp. 125-136
    • Muller, A.J.1
  • 102
    • 77649241461 scopus 로고    scopus 로고
    • Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome
    • Miao E.A., et al. Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:3076-3080.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3076-3080
    • Miao, E.A.1
  • 103
    • 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
    • Perez-Lopez A., et al. 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, 190:1201-1209.
    • (2013) J. Immunol. , vol.190 , pp. 1201-1209
    • Perez-Lopez, A.1
  • 104
    • 0033515032 scopus 로고    scopus 로고
    • The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1
    • Hersh D., et al. The Salmonella invasin SipB induces macrophage apoptosis by binding to caspase-1. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:2396-2401.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2396-2401
    • Hersh, D.1
  • 105
    • 15644374367 scopus 로고    scopus 로고
    • Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB
    • Hilbi H., et al. Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB. J. Biol. Chem. 1998, 273:32895-32900.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32895-32900
    • Hilbi, H.1
  • 106
    • 20444413447 scopus 로고    scopus 로고
    • Inhibition of MAPK and NF-κB pathways is necessary for rapid apoptosis in macrophages infected with Yersinia
    • Zhang Y., et al. Inhibition of MAPK and NF-κB pathways is necessary for rapid apoptosis in macrophages infected with Yersinia. J. Immunol. 2005, 174:7939-7949.
    • (2005) J. Immunol. , vol.174 , pp. 7939-7949
    • Zhang, Y.1
  • 107
  • 108
    • 77953562208 scopus 로고    scopus 로고
    • A Yersinia effector protein promotes virulence by preventing inflammasome recognition of the type III secretion system
    • Brodsky I.E., et al. A Yersinia effector protein promotes virulence by preventing inflammasome recognition of the type III secretion system. Cell Host Microbe 2010, 7:376-387.
    • (2010) Cell Host Microbe , vol.7 , pp. 376-387
    • Brodsky, I.E.1
  • 109
    • 2942537824 scopus 로고    scopus 로고
    • Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1β
    • Schotte P., et al. Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1β. J. Biol. Chem. 2004, 279:25134-25142.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25134-25142
    • Schotte, P.1
  • 110
    • 84871001488 scopus 로고    scopus 로고
    • The Yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing
    • LaRock C.N., Cookson B.T. The Yersinia virulence effector YopM binds caspase-1 to arrest inflammasome assembly and processing. Cell Host Microbe 2012, 12:799-805.
    • (2012) Cell Host Microbe , vol.12 , pp. 799-805
    • LaRock, C.N.1    Cookson, B.T.2


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