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Volumn 6, Issue 1, 2009, Pages 10-21

Patterns of Pathogenesis: Discrimination of Pathogenic and Nonpathogenic Microbes by the Innate Immune System

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BETA INTERFERON; CYTOTOXIN; FLAGELLIN; PATTERN RECOGNITION RECEPTOR; TOLL LIKE RECEPTOR 4;

EID: 67651091732     PISSN: 19313128     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chom.2009.06.007     Document Type: Review
Times cited : (409)

References (154)
  • 1
    • 0038687121 scopus 로고    scopus 로고
    • Phagocytosis and the inflammatory response
    • Aderem A. Phagocytosis and the inflammatory response. J. Infect. Dis. 187 (2003) S340-S345
    • (2003) J. Infect. Dis. , vol.187
    • Aderem, A.1
  • 2
    • 43249114465 scopus 로고    scopus 로고
    • Positive and negative regulation of the Drosophila immune response
    • Aggarwal K., and Silverman N. Positive and negative regulation of the Drosophila immune response. BMB Rep. 41 (2008) 267-277
    • (2008) BMB Rep. , vol.41 , pp. 267-277
    • Aggarwal, K.1    Silverman, N.2
  • 3
    • 0036318851 scopus 로고    scopus 로고
    • Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments
    • Ahmad-Nejad P., Hacker H., Rutz M., Bauer S., Vabulas R.M., and Wagner H. Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments. Eur. J. Immunol. 32 (2002) 1958-1968
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1958-1968
    • Ahmad-Nejad, P.1    Hacker, H.2    Rutz, M.3    Bauer, S.4    Vabulas, R.M.5    Wagner, H.6
  • 4
    • 0028962035 scopus 로고
    • Ectopic expression of the flagellar regulon alters development of the Bordetella-host interaction
    • Akerley B.J., Cotter P.A., and Miller J.F. Ectopic expression of the flagellar regulon alters development of the Bordetella-host interaction. Cell 80 (1995) 611-620
    • (1995) Cell , vol.80 , pp. 611-620
    • Akerley, B.J.1    Cotter, P.A.2    Miller, J.F.3
  • 5
    • 0024584734 scopus 로고
    • The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3
    • Aktories K., Braun U., Rosener S., Just I., and Hall A. The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3. Biochem. Biophys. Res. Commun. 158 (1989) 209-213
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 209-213
    • Aktories, K.1    Braun, U.2    Rosener, S.3    Just, I.4    Hall, A.5
  • 7
    • 33846829776 scopus 로고    scopus 로고
    • Pore-forming toxins and cellular non-immune defenses (CNIDs)
    • Aroian R., and van der Goot F.G. Pore-forming toxins and cellular non-immune defenses (CNIDs). Curr. Opin. Microbiol. 10 (2007) 57-61
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 57-61
    • Aroian, R.1    van der Goot, F.G.2
  • 8
    • 38849133044 scopus 로고    scopus 로고
    • A calculated response: control of inflammation by the innate immune system
    • Barton G.M. A calculated response: control of inflammation by the innate immune system. J. Clin. Invest. 118 (2008) 413-420
    • (2008) J. Clin. Invest. , vol.118 , pp. 413-420
    • Barton, G.M.1
  • 9
    • 51849103168 scopus 로고    scopus 로고
    • The microbial and danger signals that activate Nod-like receptors
    • Benko S., Philpott D.J., and Girardin S.E. The microbial and danger signals that activate Nod-like receptors. Cytokine 43 (2008) 368-373
    • (2008) Cytokine , vol.43 , pp. 368-373
    • Benko, S.1    Philpott, D.J.2    Girardin, S.E.3
  • 10
    • 37349046671 scopus 로고    scopus 로고
    • Macrophage activation redirects yersinia-infected host cell death from apoptosis to caspase-1-dependent pyroptosis
    • Bergsbaken T., and Cookson B.T. Macrophage activation redirects yersinia-infected host cell death from apoptosis to caspase-1-dependent pyroptosis. PLoS Pathog. 3 (2007) e161
    • (2007) PLoS Pathog. , vol.3
    • Bergsbaken, T.1    Cookson, B.T.2
  • 13
    • 35348992048 scopus 로고    scopus 로고
    • Manipulation of host-cell pathways by bacterial pathogens
    • Bhavsar A.P., Guttman J.A., and Finlay B.B. Manipulation of host-cell pathways by bacterial pathogens. Nature 449 (2007) 827-834
    • (2007) Nature , vol.449 , pp. 827-834
    • Bhavsar, A.P.1    Guttman, J.A.2    Finlay, B.B.3
  • 14
    • 0033861270 scopus 로고    scopus 로고
    • The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence
    • Black D.S., and Bliska J.B. The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence. Mol. Microbiol. 37 (2000) 515-527
    • (2000) Mol. Microbiol. , vol.37 , pp. 515-527
    • Black, D.S.1    Bliska, J.B.2
  • 16
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • Boyden E.D., and Dietrich W.F. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat. Genet. 38 (2006) 240-244
    • (2006) Nat. Genet. , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 19
    • 33645236166 scopus 로고    scopus 로고
    • Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor
    • Chang C.I., Chelliah Y., Borek D., Mengin-Lecreulx D., and Deisenhofer J. Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor. Science 311 (2006) 1761-1764
    • (2006) Science , vol.311 , pp. 1761-1764
    • Chang, C.I.1    Chelliah, Y.2    Borek, D.3    Mengin-Lecreulx, D.4    Deisenhofer, J.5
  • 20
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin P., Boquet P., Madaule P., Popoff M.R., Rubin E.J., and Gill D.M. The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8 (1989) 1087-1092
    • (1989) EMBO J. , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 21
    • 57049171269 scopus 로고    scopus 로고
    • TLR-independent type I interferon induction in response to an extracellular bacterial pathogen via intracellular recognition of its DNA
    • Charrel-Dennis M., Latz E., Halmen K.A., Trieu-Cuot P., Fitzgerald K.A., Kasper D.L., and Golenbock D.T. TLR-independent type I interferon induction in response to an extracellular bacterial pathogen via intracellular recognition of its DNA. Cell Host Microbe 4 (2008) 543-554
    • (2008) Cell Host Microbe , vol.4 , pp. 543-554
    • Charrel-Dennis, M.1    Latz, E.2    Halmen, K.A.3    Trieu-Cuot, P.4    Fitzgerald, K.A.5    Kasper, D.L.6    Golenbock, D.T.7
  • 22
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance F.F., and Hughes K.T. Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol. 6 (2008) 455-465
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 455-465
    • Chevance, F.F.1    Hughes, K.T.2
  • 23
    • 32944479048 scopus 로고    scopus 로고
    • Host-microbe interactions: shaping the evolution of the plant immune response
    • Chisholm S.T., Coaker G., Day B., and Staskawicz B.J. Host-microbe interactions: shaping the evolution of the plant immune response. Cell 124 (2006) 803-814
    • (2006) Cell , vol.124 , pp. 803-814
    • Chisholm, S.T.1    Coaker, G.2    Day, B.3    Staskawicz, B.J.4
  • 25
    • 50249175927 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae uses two lytic transglycosylases to produce cytotoxic peptidoglycan monomers
    • Cloud-Hansen K.A., Hackett K.T., Garcia D.L., and Dillard J.P. Neisseria gonorrhoeae uses two lytic transglycosylases to produce cytotoxic peptidoglycan monomers. J. Bacteriol. 190 (2008) 5989-5994
    • (2008) J. Bacteriol. , vol.190 , pp. 5989-5994
    • Cloud-Hansen, K.A.1    Hackett, K.T.2    Garcia, D.L.3    Dillard, J.P.4
  • 26
    • 34047262709 scopus 로고    scopus 로고
    • Antagonistic lipopolysaccharides block E. coli lipopolysaccharide function at human TLR4 via interaction with the human MD-2 lipopolysaccharide binding site
    • Coats S.R., Do C.T., Karimi-Naser L.M., Braham P.H., and Darveau R.P. Antagonistic lipopolysaccharides block E. coli lipopolysaccharide function at human TLR4 via interaction with the human MD-2 lipopolysaccharide binding site. Cell. Microbiol. 9 (2007) 1191-1202
    • (2007) Cell. Microbiol. , vol.9 , pp. 1191-1202
    • Coats, S.R.1    Do, C.T.2    Karimi-Naser, L.M.3    Braham, P.H.4    Darveau, R.P.5
  • 28
  • 29
    • 43249125839 scopus 로고    scopus 로고
    • Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
    • Dostert C., Petrilli V., Van Bruggen R., Steele C., Mossman B.T., and Tschopp J. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 320 (2008) 674-677
    • (2008) Science , vol.320 , pp. 674-677
    • Dostert, C.1    Petrilli, V.2    Van Bruggen, R.3    Steele, C.4    Mossman, B.T.5    Tschopp, J.6
  • 30
    • 45749111446 scopus 로고    scopus 로고
    • Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants
    • Eisenbarth S.C., Colegio O.R., O'Connor W., Sutterwala F.S., and Flavell R.A. Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants. Nature 453 (2008) 1122-1126
    • (2008) Nature , vol.453 , pp. 1122-1126
    • Eisenbarth, S.C.1    Colegio, O.R.2    O'Connor, W.3    Sutterwala, F.S.4    Flavell, R.A.5
  • 31
    • 0016200846 scopus 로고
    • Minimal structural requirements for adjuvant activity of bacterial peptidoglycan derivatives
    • Ellouz F., Adam A., Ciorbaru R., and Lederer E. Minimal structural requirements for adjuvant activity of bacterial peptidoglycan derivatives. Biochem. Biophys. Res. Commun. 59 (1974) 1317-1325
    • (1974) Biochem. Biophys. Res. Commun. , vol.59 , pp. 1317-1325
    • Ellouz, F.1    Adam, A.2    Ciorbaru, R.3    Lederer, E.4
  • 32
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri T., Yu J.W., Datta P., Wu J., and Alnemri E.S. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 458 (2009) 509-513
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 34
    • 16244362671 scopus 로고    scopus 로고
    • Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells
    • Fink S.L., and Cookson B.T. Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect. Immun. 73 (2005) 1907-1916
    • (2005) Infect. Immun. , vol.73 , pp. 1907-1916
    • Fink, S.L.1    Cookson, B.T.2
  • 35
    • 0030790687 scopus 로고    scopus 로고
    • Common themes in microbial pathogenicity revisited
    • Finlay B.B., and Falkow S. Common themes in microbial pathogenicity revisited. Microbiol. Mol. Biol. Rev. 61 (1997) 136-169
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 136-169
    • Finlay, B.B.1    Falkow, S.2
  • 37
    • 60749104683 scopus 로고    scopus 로고
    • The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis
    • Franchi L., Eigenbrod T., Muñoz-Planillo R., and Nuñez G. The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis. Nat. Immunol. 10 (2009) 241-247
    • (2009) Nat. Immunol. , vol.10 , pp. 241-247
    • Franchi, L.1    Eigenbrod, T.2    Muñoz-Planillo, R.3    Nuñez, G.4
  • 38
    • 34548699677 scopus 로고    scopus 로고
    • The role of the inflammasome in cellular responses to toxins and bacterial effectors
    • Freche B., Reig N., and van der Goot F.G. The role of the inflammasome in cellular responses to toxins and bacterial effectors. Semin. Immunopathol. 29 (2007) 249-260
    • (2007) Semin. Immunopathol. , vol.29 , pp. 249-260
    • Freche, B.1    Reig, N.2    van der Goot, F.G.3
  • 39
    • 0033575956 scopus 로고    scopus 로고
    • A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu Y., and Galán J.E. A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 401 (1999) 293-297
    • (1999) Nature , vol.401 , pp. 293-297
    • Fu, Y.1    Galán, J.E.2
  • 40
    • 0034676002 scopus 로고    scopus 로고
    • In vivo covalent cross-linking of cellular actin by the Vibrio cholerae RTX toxin
    • Fullner K.J., and Mekalanos J.J. In vivo covalent cross-linking of cellular actin by the Vibrio cholerae RTX toxin. EMBO J. 19 (2000) 5315-5323
    • (2000) EMBO J. , vol.19 , pp. 5315-5323
    • Fullner, K.J.1    Mekalanos, J.J.2
  • 41
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galán J.E., and Wolf-Watz H. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444 (2006) 567-573
    • (2006) Nature , vol.444 , pp. 567-573
    • Galán, J.E.1    Wolf-Watz, H.2
  • 42
    • 0037443403 scopus 로고    scopus 로고
    • Increased inflammation in lysozyme M-deficient mice in response to Micrococcus luteus and its peptidoglycan
    • Ganz T., Gabayan V., Liao H.I., Liu L., Oren A., Graf T., and Cole A.M. Increased inflammation in lysozyme M-deficient mice in response to Micrococcus luteus and its peptidoglycan. Blood 101 (2003) 2388-2392
    • (2003) Blood , vol.101 , pp. 2388-2392
    • Ganz, T.1    Gabayan, V.2    Liao, H.I.3    Liu, L.4    Oren, A.5    Graf, T.6    Cole, A.M.7
  • 43
    • 24144443517 scopus 로고    scopus 로고
    • The DNA damage pathway regulates innate immune system ligands of the NKG2D receptor
    • Gasser S., Orsulic S., Brown E.J., and Raulet D.H. The DNA damage pathway regulates innate immune system ligands of the NKG2D receptor. Nature 436 (2005) 1186-1190
    • (2005) Nature , vol.436 , pp. 1186-1190
    • Gasser, S.1    Orsulic, S.2    Brown, E.J.3    Raulet, D.H.4
  • 45
    • 0033579479 scopus 로고    scopus 로고
    • The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases
    • Goehring U.M., Schmidt G., Pederson K.J., Aktories K., and Barbieri J.T. The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases. J. Biol. Chem. 274 (1999) 36369-36372
    • (1999) J. Biol. Chem. , vol.274 , pp. 36369-36372
    • Goehring, U.M.1    Schmidt, G.2    Pederson, K.J.3    Aktories, K.4    Barbieri, J.T.5
  • 46
  • 47
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L., Abrami L., Girardin S., Tschopp J., and van der Goot F.G. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126 (2006) 1135-1145
    • (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
  • 48
    • 0032476602 scopus 로고    scopus 로고
    • CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation
    • Hacker H., Mischak H., Miethke T., Liptay S., Schmid R., Sparwasser T., Heeg K., Lipford G.B., and Wagner H. CpG-DNA-specific activation of antigen-presenting cells requires stress kinase activity and is preceded by non-specific endocytosis and endosomal maturation. EMBO J. 17 (1998) 6230-6240
    • (1998) EMBO J. , vol.17 , pp. 6230-6240
    • Hacker, H.1    Mischak, H.2    Miethke, T.3    Liptay, S.4    Schmid, R.5    Sparwasser, T.6    Heeg, K.7    Lipford, G.B.8    Wagner, H.9
  • 49
    • 33645065353 scopus 로고    scopus 로고
    • Natural transformation of Neisseria gonorrhoeae: from DNA donation to homologous recombination
    • Hamilton H.L., and Dillard J.P. Natural transformation of Neisseria gonorrhoeae: from DNA donation to homologous recombination. Mol. Microbiol. 59 (2006) 376-385
    • (2006) Mol. Microbiol. , vol.59 , pp. 376-385
    • Hamilton, H.L.1    Dillard, J.P.2
  • 50
    • 38549096234 scopus 로고    scopus 로고
    • Shaping and reshaping CD8+ T-cell memory
    • Harty J.T., and Badovinac V.P. Shaping and reshaping CD8+ T-cell memory. Nat. Rev. Immunol. 8 (2008) 107-119
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 107-119
    • Harty, J.T.1    Badovinac, V.P.2
  • 51
    • 0033567985 scopus 로고    scopus 로고
    • Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella
    • Hayward R.D., and Koronakis V. Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella. EMBO J. 18 (1999) 4926-4934
    • (1999) EMBO J. , vol.18 , pp. 4926-4934
    • Hayward, R.D.1    Koronakis, V.2
  • 52
    • 34248675516 scopus 로고    scopus 로고
    • Elicitation and suppression of microbe-associated molecular pattern-triggered immunity in plant-microbe interactions
    • He P., Shan L., and Sheen J. Elicitation and suppression of microbe-associated molecular pattern-triggered immunity in plant-microbe interactions. Cell. Microbiol. 9 (2007) 1385-1396
    • (2007) Cell. Microbiol. , vol.9 , pp. 1385-1396
    • He, P.1    Shan, L.2    Sheen, J.3
  • 53
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman S.J., and Ridley A.J. Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol. 9 (2008) 690-701
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 54
    • 8444249576 scopus 로고    scopus 로고
    • The acquired immune system: a vantage from beneath
    • Hedrick S.M. The acquired immune system: a vantage from beneath. Immunity 21 (2004) 607-615
    • (2004) Immunity , vol.21 , pp. 607-615
    • Hedrick, S.M.1
  • 55
    • 34249044447 scopus 로고    scopus 로고
    • Type I interferon signaling is required for activation of the inflammasome during Francisella infection
    • Henry T., Brotcke A., Weiss D.S., Thompson L.J., and Monack D.M. Type I interferon signaling is required for activation of the inflammasome during Francisella infection. J. Exp. Med. 204 (2007) 987-994
    • (2007) J. Exp. Med. , vol.204 , pp. 987-994
    • Henry, T.1    Brotcke, A.2    Weiss, D.S.3    Thompson, L.J.4    Monack, D.M.5
  • 56
    • 34047196224 scopus 로고    scopus 로고
    • Bacterial ligands generated in a phagosome are targets of the cytosolic innate immune system
    • Herskovits A.A., Auerbuch V., and Portnoy D.A. Bacterial ligands generated in a phagosome are targets of the cytosolic innate immune system. PLoS Pathog. 3 (2007) e51
    • (2007) PLoS Pathog. , vol.3
    • Herskovits, A.A.1    Auerbuch, V.2    Portnoy, D.A.3
  • 57
    • 0035824794 scopus 로고    scopus 로고
    • Identification of (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate as a major activator for human gammadelta T cells in Escherichia coli
    • Hintz M., Reichenberg A., Altincicek B., Bahr U., Gschwind R.M., Kollas A.K., Beck E., Wiesner J., Eberl M., and Jomaa H. Identification of (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate as a major activator for human gammadelta T cells in Escherichia coli. FEBS Lett. 509 (2001) 317-322
    • (2001) FEBS Lett. , vol.509 , pp. 317-322
    • Hintz, M.1    Reichenberg, A.2    Altincicek, B.3    Bahr, U.4    Gschwind, R.M.5    Kollas, A.K.6    Beck, E.7    Wiesner, J.8    Eberl, M.9    Jomaa, H.10
  • 58
    • 17844380477 scopus 로고    scopus 로고
    • Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction
    • Honda K., Ohba Y., Yanai H., Negishi H., Mizutani T., Takaoka A., Taya C., and Taniguchi T. Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction. Nature 434 (2005) 1035-1040
    • (2005) Nature , vol.434 , pp. 1035-1040
    • Honda, K.1    Ohba, Y.2    Yanai, H.3    Negishi, H.4    Mizutani, T.5    Takaoka, A.6    Taya, C.7    Taniguchi, T.8
  • 59
    • 0036851306 scopus 로고    scopus 로고
    • Bacterial strategies for overcoming host innate and adaptive immune responses
    • Hornef M.W., Wick M.J., Rhen M., and Normark S. Bacterial strategies for overcoming host innate and adaptive immune responses. Nat. Immunol. 3 (2002) 1033-1040
    • (2002) Nat. Immunol. , vol.3 , pp. 1033-1040
    • Hornef, M.W.1    Wick, M.J.2    Rhen, M.3    Normark, S.4
  • 63
    • 60849098840 scopus 로고    scopus 로고
    • Bacterial peptidoglycan-degrading enzymes and their impact on host muropeptide detection
    • Humann J., and Lenz L.L. Bacterial peptidoglycan-degrading enzymes and their impact on host muropeptide detection. J. Innate Immun. 1 (2008) 88-97
    • (2008) J. Innate Immun. , vol.1 , pp. 88-97
    • Humann, J.1    Lenz, L.L.2
  • 65
    • 44649132540 scopus 로고    scopus 로고
    • Host innate immune receptors and beyond: making sense of microbial infections
    • Ishii K.J., Koyama S., Nakagawa A., Coban C., and Akira S. Host innate immune receptors and beyond: making sense of microbial infections. Cell Host Microbe 3 (2008) 352-363
    • (2008) Cell Host Microbe , vol.3 , pp. 352-363
    • Ishii, K.J.1    Koyama, S.2    Nakagawa, A.3    Coban, C.4    Akira, S.5
  • 66
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway Jr. C.A. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb. Symp. Quant. Biol. 54 (1989) 1-13
    • (1989) Cold Spring Harb. Symp. Quant. Biol. , vol.54 , pp. 1-13
    • Janeway Jr., C.A.1
  • 67
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones J.D., and Dangl J.L. The plant immune system. Nature 444 (2006) 323-329
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 71
    • 0036073290 scopus 로고    scopus 로고
    • Modification of the structure and activity of lipid A in Yersinia pestis lipopolysaccharide by growth temperature
    • Kawahara K., Tsukano H., Watanabe H., Lindner B., and Matsuura M. Modification of the structure and activity of lipid A in Yersinia pestis lipopolysaccharide by growth temperature. Infect. Immun. 70 (2002) 4092-4098
    • (2002) Infect. Immun. , vol.70 , pp. 4092-4098
    • Kawahara, K.1    Tsukano, H.2    Watanabe, H.3    Lindner, B.4    Matsuura, M.5
  • 72
    • 56549116047 scopus 로고    scopus 로고
    • Toll-like receptor and RIG-I-like receptor signaling
    • Kawai T., and Akira S. Toll-like receptor and RIG-I-like receptor signaling. Ann. N Y Acad. Sci. 1143 (2008) 1-20
    • (2008) Ann. N Y Acad. Sci. , vol.1143 , pp. 1-20
    • Kawai, T.1    Akira, S.2
  • 73
    • 0032109180 scopus 로고    scopus 로고
    • Legionnaires' disease: the pore macrophage and the legion of terror within
    • Kirby J.E., and Isberg R.R. Legionnaires' disease: the pore macrophage and the legion of terror within. Trends Microbiol. 6 (1998) 256-258
    • (1998) Trends Microbiol. , vol.6 , pp. 256-258
    • Kirby, J.E.1    Isberg, R.R.2
  • 74
    • 41149118513 scopus 로고    scopus 로고
    • How dying cells alert the immune system to danger
    • Kono H., and Rock K.L. How dying cells alert the immune system to danger. Nat. Rev. Immunol. 8 (2008) 279-289
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 279-289
    • Kono, H.1    Rock, K.L.2
  • 76
    • 0344393521 scopus 로고    scopus 로고
    • Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria
    • Koraimann G. Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria. Cell. Mol. Life Sci. 60 (2003) 2371-2388
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2371-2388
    • Koraimann, G.1
  • 78
    • 38049177193 scopus 로고    scopus 로고
    • The pattern-recognition molecule Nod1 is localized at the plasma membrane at sites of bacterial interaction
    • Kufer T.A., Kremmer E., Adam A.C., Philpott D.J., and Sansonetti P.J. The pattern-recognition molecule Nod1 is localized at the plasma membrane at sites of bacterial interaction. Cell. Microbiol. 10 (2008) 477-486
    • (2008) Cell. Microbiol. , vol.10 , pp. 477-486
    • Kufer, T.A.1    Kremmer, E.2    Adam, A.C.3    Philpott, D.J.4    Sansonetti, P.J.5
  • 79
    • 54249085295 scopus 로고    scopus 로고
    • Actin cytoskeleton differentially modulates NF-kappaB-mediated IL-8 expression in myelomonocytic cells
    • Kustermans G., El Mjiyad N., Horion J., Jacobs N., Piette J., and Legrand-Poels S. Actin cytoskeleton differentially modulates NF-kappaB-mediated IL-8 expression in myelomonocytic cells. Biochem. Pharmacol. 76 (2008) 1214-1228
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1214-1228
    • Kustermans, G.1    El Mjiyad, N.2    Horion, J.3    Jacobs, N.4    Piette, J.5    Legrand-Poels, S.6
  • 80
    • 58049202273 scopus 로고    scopus 로고
    • Inflammasomes: guardians of cytosolic sanctity
    • Lamkanfi M., and Dixit V.M. Inflammasomes: guardians of cytosolic sanctity. Immunol. Rev. 227 (2009) 95-105
    • (2009) Immunol. Rev. , vol.227 , pp. 95-105
    • Lamkanfi, M.1    Dixit, V.M.2
  • 82
    • 0344234277 scopus 로고    scopus 로고
    • Helicobacter pylori flagellins have very low intrinsic activity to stimulate human gastric epithelial cells via TLR5
    • Lee S.K., Stack A., Katzowitsch E., Aizawa S.I., Suerbaum S., and Josenhans C. Helicobacter pylori flagellins have very low intrinsic activity to stimulate human gastric epithelial cells via TLR5. Microbes Infect. 5 (2003) 1345-1356
    • (2003) Microbes Infect. , vol.5 , pp. 1345-1356
    • Lee, S.K.1    Stack, A.2    Katzowitsch, E.3    Aizawa, S.I.4    Suerbaum, S.5    Josenhans, C.6
  • 84
    • 47849087075 scopus 로고    scopus 로고
    • Cutting edge: inflammasome activation by alum and alum's adjuvant effect are mediated by NLRP3
    • Li H., Willingham S.B., Ting J.P., and Re F. Cutting edge: inflammasome activation by alum and alum's adjuvant effect are mediated by NLRP3. J. Immunol. 181 (2008) 17-21
    • (2008) J. Immunol. , vol.181 , pp. 17-21
    • Li, H.1    Willingham, S.B.2    Ting, J.P.3    Re, F.4
  • 86
    • 0029018206 scopus 로고
    • Tracheal cytotoxin structural requirements for respiratory epithelial damage in pertussis
    • Luker K.E., Tyler A.N., Marshall G.R., and Goldman W.E. Tracheal cytotoxin structural requirements for respiratory epithelial damage in pertussis. Mol. Microbiol. 16 (1995) 733-743
    • (1995) Mol. Microbiol. , vol.16 , pp. 733-743
    • Luker, K.E.1    Tyler, A.N.2    Marshall, G.R.3    Goldman, W.E.4
  • 87
    • 33748494269 scopus 로고    scopus 로고
    • MAMPs and MIMPs: proposed classifications for inducers of innate immunity
    • Mackey D., and McFall A.J. MAMPs and MIMPs: proposed classifications for inducers of innate immunity. Mol. Microbiol. 61 (2006) 1365-1371
    • (2006) Mol. Microbiol. , vol.61 , pp. 1365-1371
    • Mackey, D.1    McFall, A.J.2
  • 88
    • 0035846909 scopus 로고    scopus 로고
    • Cytolysin-mediated translocation (CMT): a functional equivalent of type III secretion in gram-positive bacteria
    • Madden J.C., Ruiz N., and Caparon M. Cytolysin-mediated translocation (CMT): a functional equivalent of type III secretion in gram-positive bacteria. Cell 104 (2001) 143-152
    • (2001) Cell , vol.104 , pp. 143-152
    • Madden, J.C.1    Ruiz, N.2    Caparon, M.3
  • 94
    • 44849136632 scopus 로고    scopus 로고
    • Pannexin-1-mediated intracellular delivery of muramyl dipeptide induces caspase-1 activation via cryopyrin/NLRP3 independently of Nod2
    • Marina-García N., Franchi L., Kim Y.G., Miller D., McDonald C., Boons G.J., and Nuñez G. Pannexin-1-mediated intracellular delivery of muramyl dipeptide induces caspase-1 activation via cryopyrin/NLRP3 independently of Nod2. J. Immunol. 180 (2008) 4050-4057
    • (2008) J. Immunol. , vol.180 , pp. 4050-4057
    • Marina-García, N.1    Franchi, L.2    Kim, Y.G.3    Miller, D.4    McDonald, C.5    Boons, G.J.6    Nuñez, G.7
  • 95
    • 7944232105 scopus 로고    scopus 로고
    • Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome
    • Martinon F., Agostini L., Meylan E., and Tschopp J. Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome. Curr. Biol. 14 (2004) 1929-1934
    • (2004) Curr. Biol. , vol.14 , pp. 1929-1934
    • Martinon, F.1    Agostini, L.2    Meylan, E.3    Tschopp, J.4
  • 96
    • 0028201732 scopus 로고
    • Tolerance, danger, and the extended family
    • Matzinger P. Tolerance, danger, and the extended family. Annu. Rev. Immunol. 12 (1994) 991-1045
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 98
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • Medzhitov R. Recognition of microorganisms and activation of the immune response. Nature 449 (2007) 819-826
    • (2007) Nature , vol.449 , pp. 819-826
    • Medzhitov, R.1
  • 100
    • 33748588915 scopus 로고    scopus 로고
    • Disruption-induced mucus secretion: repair and protection
    • Miyake K., Tanaka T., and McNeil P.L. Disruption-induced mucus secretion: repair and protection. PLoS Biol. 4 (2006) e276
    • (2006) PLoS Biol. , vol.4
    • Miyake, K.1    Tanaka, T.2    McNeil, P.L.3
  • 103
    • 65249135027 scopus 로고    scopus 로고
    • Retinoic acid-induced gene-1 (RIG-I) associates with the actin cytoskeleton via caspase activation and recruitment domain-dependent interactions
    • Mukherjee A., Morosky S.A., Shen L., Weber C.R., Turner J.R., Kim K.S., Wang T., and Coyne C.B. Retinoic acid-induced gene-1 (RIG-I) associates with the actin cytoskeleton via caspase activation and recruitment domain-dependent interactions. J. Biol. Chem. 284 (2009) 6486-6494
    • (2009) J. Biol. Chem. , vol.284 , pp. 6486-6494
    • Mukherjee, A.1    Morosky, S.A.2    Shen, L.3    Weber, C.R.4    Turner, J.R.5    Kim, K.S.6    Wang, T.7    Coyne, C.B.8
  • 104
    • 33745712575 scopus 로고    scopus 로고
    • Shield as signal: lipopolysaccharides and the evolution of immunity to gram-negative bacteria
    • Munford R.S., and Varley A.W. Shield as signal: lipopolysaccharides and the evolution of immunity to gram-negative bacteria. PLoS Pathog. 2 (2006) e67
    • (2006) PLoS Pathog. , vol.2
    • Munford, R.S.1    Varley, A.W.2
  • 105
  • 108
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)
    • Park J.T., and Uehara T. How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol. Mol. Biol. Rev. 72 (2008) 211-227
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 211-227
    • Park, J.T.1    Uehara, T.2
  • 109
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • Pelegrin P., and Surprenant A. Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor. EMBO J. 25 (2006) 5071-5082
    • (2006) EMBO J. , vol.25 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 110
    • 34047270416 scopus 로고    scopus 로고
    • Pannexin-1 couples to maitotoxin- and nigericin-induced interleukin-1beta release through a dye uptake-independent pathway
    • Pelegrin P., and Surprenant A. Pannexin-1 couples to maitotoxin- and nigericin-induced interleukin-1beta release through a dye uptake-independent pathway. J. Biol. Chem. 282 (2007) 2386-2394
    • (2007) J. Biol. Chem. , vol.282 , pp. 2386-2394
    • Pelegrin, P.1    Surprenant, A.2
  • 111
    • 23944516870 scopus 로고    scopus 로고
    • The host type I interferon response to viral and bacterial infections
    • Perry A.K., Chen G., Zheng D., Tang H., and Cheng G. The host type I interferon response to viral and bacterial infections. Cell Res. 15 (2005) 407-422
    • (2005) Cell Res. , vol.15 , pp. 407-422
    • Perry, A.K.1    Chen, G.2    Zheng, D.3    Tang, H.4    Cheng, G.5
  • 112
    • 35348898443 scopus 로고    scopus 로고
    • Genetics-squared: combining host and pathogen genetics in the analysis of innate immunity and bacterial virulence
    • Persson J., and Vance R.E. Genetics-squared: combining host and pathogen genetics in the analysis of innate immunity and bacterial virulence. Immunogenetics 59 (2007) 761-778
    • (2007) Immunogenetics , vol.59 , pp. 761-778
    • Persson, J.1    Vance, R.E.2
  • 113
    • 36849045915 scopus 로고    scopus 로고
    • The inflammasome: a danger sensing complex triggering innate immunity
    • Petrilli V., Dostert C., Muruve D.A., and Tschopp J. The inflammasome: a danger sensing complex triggering innate immunity. Curr. Opin. Immunol. 19 (2007) 615-622
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 615-622
    • Petrilli, V.1    Dostert, C.2    Muruve, D.A.3    Tschopp, J.4
  • 114
    • 34548027736 scopus 로고    scopus 로고
    • Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration
    • Petrilli V., Papin S., Dostert C., Mayor A., Martinon F., and Tschopp J. Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration. Cell Death Differ. 14 (2007) 1583-1589
    • (2007) Cell Death Differ. , vol.14 , pp. 1583-1589
    • Petrilli, V.1    Papin, S.2    Dostert, C.3    Mayor, A.4    Martinon, F.5    Tschopp, J.6
  • 118
    • 32444440799 scopus 로고    scopus 로고
    • Characterization of late acyltransferase genes of Yersinia pestis and their role in temperature-dependent lipid A variation
    • Rebeil R., Ernst R.K., Jarrett C.O., Adams K.N., Miller S.I., and Hinnebusch B.J. Characterization of late acyltransferase genes of Yersinia pestis and their role in temperature-dependent lipid A variation. J. Bacteriol. 188 (2006) 1381-1388
    • (2006) J. Bacteriol. , vol.188 , pp. 1381-1388
    • Rebeil, R.1    Ernst, R.K.2    Jarrett, C.O.3    Adams, K.N.4    Miller, S.I.5    Hinnebusch, B.J.6
  • 119
    • 33645535833 scopus 로고    scopus 로고
    • Porphyromonas gingivalis lipopolysaccharide lipid A heterogeneity: differential activities of tetra- and penta-acylated lipid A structures on E-selectin expression and TLR4 recognition
    • Reife R.A., Coats S.R., Al-Qutub M., Dixon D.M., Braham P.A., Billharz R.J., Howald W.N., and Darveau R.P. Porphyromonas gingivalis lipopolysaccharide lipid A heterogeneity: differential activities of tetra- and penta-acylated lipid A structures on E-selectin expression and TLR4 recognition. Cell. Microbiol. 8 (2006) 857-868
    • (2006) Cell. Microbiol. , vol.8 , pp. 857-868
    • Reife, R.A.1    Coats, S.R.2    Al-Qutub, M.3    Dixon, D.M.4    Braham, P.A.5    Billharz, R.J.6    Howald, W.N.7    Darveau, R.P.8
  • 120
    • 33645791082 scopus 로고    scopus 로고
    • Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity
    • Ren T., Zamboni D.S., Roy C.R., Dietrich W.F., and Vance R.E. Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity. PLoS Pathog. 2 (2006) e18
    • (2006) PLoS Pathog. , vol.2
    • Ren, T.1    Zamboni, D.S.2    Roy, C.R.3    Dietrich, W.F.4    Vance, R.E.5
  • 123
    • 33947374647 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins: pleiotropic sensors and effectors of antimicrobial defences
    • Royet J., and Dziarski R. Peptidoglycan recognition proteins: pleiotropic sensors and effectors of antimicrobial defences. Nat. Rev. Microbiol. 5 (2007) 264-277
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 264-277
    • Royet, J.1    Dziarski, R.2
  • 124
    • 0030610785 scopus 로고    scopus 로고
    • Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • Schmidt G., Sehr P., Wilm M., Selzer J., Mann M., and Aktories K. Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature 387 (1997) 725-729
    • (1997) Nature , vol.387 , pp. 725-729
    • Schmidt, G.1    Sehr, P.2    Wilm, M.3    Selzer, J.4    Mann, M.5    Aktories, K.6
  • 125
    • 34548490518 scopus 로고    scopus 로고
    • Listeriolysin O: a phagosome-specific lysin
    • Schnupf P., and Portnoy D.A. Listeriolysin O: a phagosome-specific lysin. Microbes Infect. 9 (2007) 1176-1187
    • (2007) Microbes Infect. , vol.9 , pp. 1176-1187
    • Schnupf, P.1    Portnoy, D.A.2
  • 126
    • 0032539674 scopus 로고    scopus 로고
    • Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome
    • Segal G., Purcell M., and Shuman H.A. Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome. Proc. Natl. Acad. Sci. USA 95 (1998) 1669-1674
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1669-1674
    • Segal, G.1    Purcell, M.2    Shuman, H.A.3
  • 127
    • 33646254371 scopus 로고    scopus 로고
    • The MogR transcriptional repressor regulates nonhierarchal expression of flagellar motility genes and virulence in Listeria monocytogenes
    • Shen A., and Higgins D.E. The MogR transcriptional repressor regulates nonhierarchal expression of flagellar motility genes and virulence in Listeria monocytogenes. PLoS Pathog. 2 (2006) e30
    • (2006) PLoS Pathog. , vol.2
    • Shen, A.1    Higgins, D.E.2
  • 128
    • 34548675685 scopus 로고    scopus 로고
    • Type III secretion translocation pores of Yersinia enterocolitica trigger maturation and release of pro-inflammatory IL-1beta
    • Shin H., and Cornelis G.R. Type III secretion translocation pores of Yersinia enterocolitica trigger maturation and release of pro-inflammatory IL-1beta. Cell. Microbiol. 9 (2007) 2893-2902
    • (2007) Cell. Microbiol. , vol.9 , pp. 2893-2902
    • Shin, H.1    Cornelis, G.R.2
  • 129
    • 60049091769 scopus 로고    scopus 로고
    • ESX/type VII secretion systems and their role in host-pathogen interaction
    • Simeone R., Bottai D., and Brosch R. ESX/type VII secretion systems and their role in host-pathogen interaction. Curr. Opin. Microbiol. 12 (2009) 4-10
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 4-10
    • Simeone, R.1    Bottai, D.2    Brosch, R.3
  • 130
    • 32944471107 scopus 로고    scopus 로고
    • Pathogen-specific TLR signaling in mucosa: mutual contribution of microbial TLR agonists and virulence factors
    • Sirard J.C., Bayardo M., and Didierlaurent A. Pathogen-specific TLR signaling in mucosa: mutual contribution of microbial TLR agonists and virulence factors. Eur. J. Immunol. 36 (2006) 260-263
    • (2006) Eur. J. Immunol. , vol.36 , pp. 260-263
    • Sirard, J.C.1    Bayardo, M.2    Didierlaurent, A.3
  • 131
    • 39449133957 scopus 로고    scopus 로고
    • A mechanism for the initiation of allergen-induced T helper type 2 responses
    • Sokol C.L., Barton G.M., Farr A.G., and Medzhitov R. A mechanism for the initiation of allergen-induced T helper type 2 responses. Nat. Immunol. 9 (2008) 310-318
    • (2008) Nat. Immunol. , vol.9 , pp. 310-318
    • Sokol, C.L.1    Barton, G.M.2    Farr, A.G.3    Medzhitov, R.4
  • 132
    • 33847359299 scopus 로고    scopus 로고
    • The type I IFN response to infection with Mycobacterium tuberculosis requires ESX-1-mediated secretion and contributes to pathogenesis
    • Stanley S.A., Johndrow J.E., Manzanillo P., and Cox J.S. The type I IFN response to infection with Mycobacterium tuberculosis requires ESX-1-mediated secretion and contributes to pathogenesis. J. Immunol. 178 (2007) 3143-3152
    • (2007) J. Immunol. , vol.178 , pp. 3143-3152
    • Stanley, S.A.1    Johndrow, J.E.2    Manzanillo, P.3    Cox, J.S.4
  • 133
    • 30444450839 scopus 로고    scopus 로고
    • Recognition of cytosolic DNA activates an IRF3-dependent innate immune response
    • Stetson D.B., and Medzhitov R. Recognition of cytosolic DNA activates an IRF3-dependent innate immune response. Immunity 24 (2006) 93-103
    • (2006) Immunity , vol.24 , pp. 93-103
    • Stetson, D.B.1    Medzhitov, R.2
  • 134
    • 36348978900 scopus 로고    scopus 로고
    • Injection of flagellin into the host cell cytosol by Salmonella enterica serotype typhimurium
    • Sun Y.H., Rolan H.G., and Tsolis R.M. Injection of flagellin into the host cell cytosol by Salmonella enterica serotype typhimurium. J. Biol. Chem. 282 (2007) 33897-33901
    • (2007) J. Biol. Chem. , vol.282 , pp. 33897-33901
    • Sun, Y.H.1    Rolan, H.G.2    Tsolis, R.M.3
  • 139
    • 0035477848 scopus 로고    scopus 로고
    • A bacterial type III secretion system inhibits actin polymerization to prevent pore formation in host cell membranes
    • Viboud G.I., and Bliska J.B. A bacterial type III secretion system inhibits actin polymerization to prevent pore formation in host cell membranes. EMBO J. 20 (2001) 5373-5382
    • (2001) EMBO J. , vol.20 , pp. 5373-5382
    • Viboud, G.I.1    Bliska, J.B.2
  • 140
    • 25444476788 scopus 로고    scopus 로고
    • Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis
    • Viboud G.I., and Bliska J.B. Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis. Annu. Rev. Microbiol. 59 (2005) 69-89
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 69-89
    • Viboud, G.I.1    Bliska, J.B.2
  • 141
    • 0032488861 scopus 로고    scopus 로고
    • Conjugative transfer by the virulence system of Legionella pneumophila
    • Vogel J.P., Andrews H.L., Wong S.K., and Isberg R.R. Conjugative transfer by the virulence system of Legionella pneumophila. Science 279 (1998) 873-876
    • (1998) Science , vol.279 , pp. 873-876
    • Vogel, J.P.1    Andrews, H.L.2    Wong, S.K.3    Isberg, R.R.4
  • 143
    • 0020324198 scopus 로고
    • Failure of killed Listeria monocytogenes vaccine to produce protective immunity
    • von Koenig C.H., Finger H., and Hof H. Failure of killed Listeria monocytogenes vaccine to produce protective immunity. Nature 297 (1982) 233-234
    • (1982) Nature , vol.297 , pp. 233-234
    • von Koenig, C.H.1    Finger, H.2    Hof, H.3
  • 144
    • 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., Telepnev M.V., Schmidt G., Aktories K., Wolf-Watz H., and Rosqvist R. GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure. Mol. Microbiol. 36 (2000) 737-748
    • (2000) Mol. Microbiol. , vol.36 , pp. 737-748
    • Von Pawel-Rammingen, U.1    Telepnev, M.V.2    Schmidt, G.3    Aktories, K.4    Wolf-Watz, H.5    Rosqvist, R.6
  • 146
    • 4444253690 scopus 로고    scopus 로고
    • NOD2 is a negative regulator of Toll-like receptor 2-mediated T helper type 1 responses
    • Watanabe T., Kitani A., Murray P.J., and Strober W. NOD2 is a negative regulator of Toll-like receptor 2-mediated T helper type 1 responses. Nat. Immunol. 5 (2004) 800-808
    • (2004) Nat. Immunol. , vol.5 , pp. 800-808
    • Watanabe, T.1    Kitani, A.2    Murray, P.J.3    Strober, W.4
  • 147
    • 33748493563 scopus 로고    scopus 로고
    • Nucleotide binding oligomerization domain 2 deficiency leads to dysregulated TLR2 signaling and induction of antigen-specific colitis
    • Watanabe T., Kitani A., Murray P.J., Wakatsuki Y., Fuss I.J., and Strober W. Nucleotide binding oligomerization domain 2 deficiency leads to dysregulated TLR2 signaling and induction of antigen-specific colitis. Immunity 25 (2006) 473-485
    • (2006) Immunity , vol.25 , pp. 473-485
    • Watanabe, T.1    Kitani, A.2    Murray, P.J.3    Wakatsuki, Y.4    Fuss, I.J.5    Strober, W.6
  • 148
    • 2342630062 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa regulates flagellin expression as part of a global response to airway fluid from cystic fibrosis patients
    • Wolfgang M.C., Jyot J., Goodman A.L., Ramphal R., and Lory S. Pseudomonas aeruginosa regulates flagellin expression as part of a global response to airway fluid from cystic fibrosis patients. Proc. Natl. Acad. Sci. USA 101 (2004) 6664-6668
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6664-6668
    • Wolfgang, M.C.1    Jyot, J.2    Goodman, A.L.3    Ramphal, R.4    Lory, S.5
  • 149
    • 35648995482 scopus 로고    scopus 로고
    • NOD2 transgenic mice exhibit enhanced MDP-mediated down-regulation of TLR2 responses and resistance to colitis induction
    • Yang Z., Fuss I.J., Watanabe T., Asano N., Davey M.P., Rosenbaum J.T., Strober W., and Kitani A. NOD2 transgenic mice exhibit enhanced MDP-mediated down-regulation of TLR2 responses and resistance to colitis induction. Gastroenterology 133 (2007) 1510-1521
    • (2007) Gastroenterology , vol.133 , pp. 1510-1521
    • Yang, Z.1    Fuss, I.J.2    Watanabe, T.3    Asano, N.4    Davey, M.P.5    Rosenbaum, J.T.6    Strober, W.7    Kitani, A.8
  • 150
    • 58149400542 scopus 로고    scopus 로고
    • AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling
    • Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., and Orth K. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323 (2009) 269-272
    • (2009) Science , vol.323 , pp. 269-272
    • Yarbrough, M.L.1    Li, Y.2    Kinch, L.N.3    Grishin, N.V.4    Ball, H.L.5    Orth, K.6
  • 151
    • 48949094095 scopus 로고    scopus 로고
    • Structural mechanism of RNA recognition by the RIG-I-like receptors
    • Yoneyama M., and Fujita T. Structural mechanism of RNA recognition by the RIG-I-like receptors. Immunity 29 (2008) 178-181
    • (2008) Immunity , vol.29 , pp. 178-181
    • Yoneyama, M.1    Fujita, T.2
  • 152
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: receptor binding, internalization, pore formation, and translocation
    • Young J.A., and Collier R.J. Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76 (2007) 243-265
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 153
    • 0033621058 scopus 로고    scopus 로고
    • An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
    • Zhou D., Mooseker M.S., and Galán J.E. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proc. Natl. Acad. Sci. USA 96 (1999) 10176-10181
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10176-10181
    • Zhou, D.1    Mooseker, M.S.2    Galán, J.E.3
  • 154


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