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Volumn 4, Issue 12, 2004, Pages 953-964

War and peace at mucosal surfaces

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOKINE; CYTOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TOLL LIKE RECEPTOR; TUMOR NECROSIS FACTOR;

EID: 10244226689     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1499     Document Type: Review
Times cited : (564)

References (121)
  • 2
    • 0031461206 scopus 로고    scopus 로고
    • Epithelial cells as sensors for microbial infection
    • Kagnoff, M. F. & Eckmann, L. Epithelial cells as sensors for microbial infection. J. Clin. Invest. 100, 6-10 (1997).
    • (1997) J. Clin. Invest. , vol.100 , pp. 6-10
    • Kagnoff, M.F.1    Eckmann, L.2
  • 3
    • 0025068368 scopus 로고
    • Structure and function of the intestinal epithelial barrier in health and disease
    • Madara, J. L. Nash, S., Moore, R. & Atisook, K. Structure and function of the intestinal epithelial barrier in health and disease. Monogr. Pathol. 31, 306-324 (1990).
    • (1990) Monogr. Pathol. , vol.31 , pp. 306-324
    • Madara, J.L.1    Nash, S.2    Moore, R.3    Atisook, K.4
  • 4
    • 0014456576 scopus 로고
    • Freeze-etch appearance of the tight junctions in the epithelium of large and small intestine of mice
    • Staehelin, L. A., Mukherjee, T. M. & Williams, A. W. Freeze-etch appearance of the tight junctions in the epithelium of large and small intestine of mice. Protoplasma 67, 165-184 (1969).
    • (1969) Protoplasma , vol.67 , pp. 165-184
    • Staehelin, L.A.1    Mukherjee, T.M.2    Williams, A.W.3
  • 5
  • 6
    • 0030669302 scopus 로고    scopus 로고
    • Physiological regulation of epithelial junctions is associated with myosin light-chain phosphorylation
    • Turner, J. R. et al. Physiological regulation of epithelial junctions is associated with myosin light-chain phosphorylation. Am. J. Physiol. 273, C1378-C1385 (1997).
    • (1997) Am. J. Physiol. , vol.273
    • Turner, J.R.1
  • 7
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2. Reconstitutes tight junction strands and recruits occludin in fibroblasts
    • Furuse, M., Sasaki, H., Fujimoto, K. & Tsukita, S. A single gene product, claudin-1 or -2. reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143, 391-401 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 8
    • 0030043414 scopus 로고    scopus 로고
    • Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures
    • Furuse, M., Fujimoto, K., Sato, N., Hirase, T. & Tsukita, S. Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures. J. Cell Sci. 109, 429-435 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 429-435
    • Furuse, M.1    Fujimoto, K.2    Sato, N.3    Hirase, T.4    Tsukita, S.5
  • 9
    • 0019309991 scopus 로고
    • Mechanisms of rapid mucus secretion in goblet cells stimulated by acetylcholine
    • Specian, R. D. & Neutra, M. R. Mechanisms of rapid mucus secretion in goblet cells stimulated by acetylcholine. J. Cell Biol. 85, 626-640 (1980).
    • (1980) J. Cell Biol. , vol.85 , pp. 626-640
    • Specian, R.D.1    Neutra, M.R.2
  • 10
    • 0029133784 scopus 로고
    • Trefoil peptide protection of intestinal epithelial barrier function: Cooperative interaction with mucin glycoprotein
    • Kindon, H., Pothoulakis, C., Trim, L., Lynch-Devaney, K. & Podolsky, D. K. Trefoil peptide protection of intestinal epithelial barrier function: cooperative interaction with mucin glycoprotein. Gastroenterology 109, 516-523 (1995).
    • (1995) Gastroenterology , vol.109 , pp. 516-523
    • Kindon, H.1    Pothoulakis, C.2    Trim, L.3    Lynch-Devaney, K.4    Podolsky, D.K.5
  • 11
    • 0023877734 scopus 로고
    • Colonization of the streptomycin-treated mouse large intestine by a human fecal Escherichia coli strain: Role of growth in mucus
    • Wadolkowsky, E. A., Laux, D. C. & Cohen, P. S. Colonization of the streptomycin-treated mouse large intestine by a human fecal Escherichia coli strain: role of growth in mucus. Infect. Immun. 56, 1030-1035 (1988).
    • (1988) Infect. Immun. , vol.56 , pp. 1030-1035
    • Wadolkowsky, E.A.1    Laux, D.C.2    Cohen, P.S.3
  • 12
    • 0020027857 scopus 로고
    • Purification and characterization of the mucinase of Vibrio cholerae
    • Schneider, D. R. & Parker, C. D. Purification and characterization of the mucinase of Vibrio cholerae. J. Infect. Dis. 145, 474-482 (1982).
    • (1982) J. Infect. Dis. , vol.145 , pp. 474-482
    • Schneider, D.R.1    Parker, C.D.2
  • 15
    • 0029097115 scopus 로고
    • Structure, function and membrane integration of defensins
    • White, S. H., Wimley, W. C. & Selsted, M. E. Structure, function and membrane integration of defensins. Curr. Opin. Struct. Biol. 5, 521-527 (1995).
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 16
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • Lehrer, R. I. & Ganz, T. Defensins of vertebrate animals. Curr. Opin. Immunol. 14, 96-102 (2002). An excellent review of defensins.
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 17
    • 0035024206 scopus 로고    scopus 로고
    • Paneth cell defensins and innate immunity of the small bowel
    • Ouelette, A. J. & Bevins, C. L. Paneth cell defensins and innate immunity of the small bowel. Inflamm. Bowel Dis. 7, 43-50 (2001).
    • (2001) Inflamm. Bowel Dis. , vol.7 , pp. 43-50
    • Ouelette, A.J.1    Bevins, C.L.2
  • 18
    • 0032734313 scopus 로고    scopus 로고
    • Expression and regulation of the human β-defensins hBD1 and hBD2 in intestinal epithelium
    • O'Neil, D. A. et al. Expression and regulation of the human β-defensins hBD1 and hBD2 in intestinal epithelium. J. Immunol. 163, 6718-6724 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 6718-6724
    • O'Neil, D.A.1
  • 19
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: A family of endogenous antimicrobial peptides
    • Lehrer, R. I. & Ganz, T. Cathelicidins: a family of endogenous antimicrobial peptides. Curr. Opin. Hematol. 9, 18-22 (2002).
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 18-22
    • Lehrer, R.I.1    Ganz, T.2
  • 20
    • 0031883544 scopus 로고    scopus 로고
    • Apical secretion of a pathogen-elicited epithelial chemoattractant (PEEC) activity in response to surface colonization of intestinal epithelia by Salmonella typhimurium
    • McCormick, B. A., Parkos, C. A., Colgan, S. P., Carnes, D. K. & Madara, J. L. Apical secretion of a pathogen-elicited epithelial chemoattractant (PEEC) activity in response to surface colonization of intestinal epithelia by Salmonella typhimurium. J. Immunol. 160, 455-456 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 455-456
    • McCormick, B.A.1    Parkos, C.A.2    Colgan, S.P.3    Carnes, D.K.4    Madara, J.L.5
  • 21
    • 0036081269 scopus 로고    scopus 로고
    • Host-pathogen interactions: Subversion and utilization of the NF-κB pathway during infection
    • Tato, C. M. & Hunter, C. A. Host-pathogen interactions: subversion and utilization of the NF-κB pathway during infection. Infect. Immun. 70, 3311-3317 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 3311-3317
    • Tato, C.M.1    Hunter, C.A.2
  • 23
    • 0032794570 scopus 로고    scopus 로고
    • Uptake and transport of intestinal macromolecules and microorganisms by M cells in Peyer's patches - A personal and historical perspective
    • Owen, R. Uptake and transport of intestinal macromolecules and microorganisms by M cells in Peyer's patches - a personal and historical perspective. Semin. Immunol. 11, 1-7 (1999).
    • (1999) Semin. Immunol. , vol.11 , pp. 1-7
    • Owen, R.1
  • 24
    • 0026642604 scopus 로고
    • Ultrastructural study of M cells from colonic lymphoid nodules obtained by colonoscopic biopsy
    • Fujimura, Y., Hosobe, M. & Kihara, T. Ultrastructural study of M cells from colonic lymphoid nodules obtained by colonoscopic biopsy. Dig. Dis. Sci. 37, 1089-1098 (1992).
    • (1992) Dig. Dis. Sci. , vol.37 , pp. 1089-1098
    • Fujimura, Y.1    Hosobe, M.2    Kihara, T.3
  • 25
    • 1542618118 scopus 로고    scopus 로고
    • Induction of protective IgA by intestinal dendritic cells carrying commensal bacteria
    • MacPherson, A. J. & Uhr, T. Induction of protective IgA by intestinal dendritic cells carrying commensal bacteria. Science 303, 1662-1665 (2004). A research article about T-cell independent generation of IgA specificity.
    • (2004) Science , vol.303 , pp. 1662-1665
    • MacPherson, A.J.1    Uhr, T.2
  • 26
    • 2342646956 scopus 로고    scopus 로고
    • Bacterial flagellin is a dominant antigen in Crohn disease
    • Lode, M. J. et al. Bacterial flagellin is a dominant antigen in Crohn disease. J. Clin Invest. 113, 1296-1306 (2004).
    • (2004) J. Clin Invest. , vol.113 , pp. 1296-1306
    • Lode, M.J.1
  • 27
    • 2942625911 scopus 로고    scopus 로고
    • Interactions between commensal intestinal bacteria and the immune system
    • Macpherson, A. J. & Harris, N. L. Interactions between commensal intestinal bacteria and the immune system. Nature Rev. Immunol. 4, 478-485 (2004).
    • (2004) Nature Rev. Immunol. , vol.4 , pp. 478-485
    • Macpherson, A.J.1    Harris, N.L.2
  • 28
    • 0035321325 scopus 로고    scopus 로고
    • Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria
    • Rescigno, M. et al. Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria. Nature Immunol. 2, 361-367 (2001). Unravels an original pathway of crossing the epithelium.
    • (2001) Nature Immunol. , vol.2 , pp. 361-367
    • Rescigno, M.1
  • 30
    • 0032792638 scopus 로고    scopus 로고
    • M cells as ports of entry for enteroinvasive pathogens: Mechanisms of interaction, consequences for the disease process
    • Sansonetti, P. J. & Phalipon, A. M cells as ports of entry for enteroinvasive pathogens: mechanisms of interaction, consequences for the disease process. Semin, Immunol. 11, 193-203 (1999).
    • (1999) Semin. Immunol. , vol.11 , pp. 193-203
    • Sansonetti, P.J.1    Phalipon, A.2
  • 33
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and non-self by the innate immune system
    • Medzhitov, R. & Janeway, C. A. Decoding the patterns of self and non-self by the innate immune system. Science 296, 298-300 (2002). An outstanding introduction to the concept of innate immunity.
    • (2002) Science , vol.296 , pp. 298-300
    • Medzhitov, R.1    Janeway, C.A.2
  • 34
    • 0034680145 scopus 로고    scopus 로고
    • Toll-like receptors in the induction of the innate immune response
    • Aderem, A. & Ulevitch, R. J. Toll-like receptors in the induction of the innate immune response. Nature 406, 782-787 (2000).
    • (2000) Nature , vol.406 , pp. 782-787
    • Aderem, A.1    Ulevitch, R.J.2
  • 35
    • 3242664636 scopus 로고    scopus 로고
    • Recognition of commensal microflora by Toll-like receptors is required for intestinal homeostasis
    • Rahoff-Nahoum, S., Paglino, J., Eslami-Varzaneh, F., Edberg, S. & Medzhitov, R. Recognition of commensal microflora by Toll-like receptors is required for intestinal homeostasis. Cell 118, 229-241 (2004).
    • (2004) Cell , vol.118 , pp. 229-241
    • Rahoff-Nahoum, S.1    Paglino, J.2    Eslami-Varzaneh, F.3    Edberg, S.4    Medzhitov, R.5
  • 36
    • 0033580949 scopus 로고    scopus 로고
    • Peptidoglycan- and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2
    • Schwandner, R., Dziarski, R., Wesche, H., Rothe, M. & Kirschning, C. J. Peptidoglycan- and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2. J. Biol. Chem. 274, 17406-17409 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 17406-17409
    • Schwandner, R.1    Dziarski, R.2    Wesche, H.3    Rothe, M.4    Kirschning, C.J.5
  • 37
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene
    • Poltorak, A. et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282, 2085-2088 (2001).
    • (2001) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1
  • 38
    • 0035881675 scopus 로고    scopus 로고
    • Bacterial flagellin activates baso-laterally expressed TLR5 to induce epithelial proinflammatory gene expression
    • Gewirtz, A. T., Navas, T. A., Lyons, S., Godowski, P. J. & Madara, J. L. Bacterial flagellin activates baso-laterally expressed TLR5 to induce epithelial proinflammatory gene expression. J. Immunol. 167, 1882-1885 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 1882-1885
    • Gewirtz, A.T.1    Navas, T.A.2    Lyons, S.3    Godowski, P.J.4    Madara, J.L.5
  • 39
    • 0035979192 scopus 로고    scopus 로고
    • Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition
    • Bauer, S. et al. Human TLR9 confers responsiveness to bacterial DNA via species-specific CpG motif recognition. Proc. Natl Acad Sci. USA 98, 9237-9242 (2001).
    • (2001) Proc. Natl Acad Sci. USA , vol.98 , pp. 9237-9242
    • Bauer, S.1
  • 40
    • 0038615855 scopus 로고    scopus 로고
    • Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan
    • Girardin, S. et al. Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science 300, 1584-1587 (2003).
    • (2003) Science , vol.300 , pp. 1584-1587
    • Girardin, S.1
  • 41
    • 0038824980 scopus 로고    scopus 로고
    • An essential role for Nod1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
    • Chamaillard, M. et al. An essential role for Nod1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nature Immunol. 4, 702-707 (2003). References 40 and 41 identify NOD1 as an intracellular sensor for bacteria that allows discrimination between Gram-positive and Gram-negative bacteria on the basis of differences in their PGN.
    • (2003) Nature Immunol. , vol.4 , pp. 702-707
    • Chamaillard, M.1
  • 42
    • 0012722659 scopus 로고    scopus 로고
    • Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection
    • Girardin, S. et al. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J. Biol. Chem. 278, 8869-8872 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 8869-8872
    • Girardin, S.1
  • 43
    • 0034623225 scopus 로고    scopus 로고
    • An induced proximity model for NF-κB activation of the Nod1/RICK and RIP signaling pathways
    • Inohara, N. et al. An induced proximity model for NF-κB activation of the Nod1/RICK and RIP signaling pathways. J. Biol. Chem. 275, 27823-27831 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 27823-27831
    • Inohara, N.1
  • 44
    • 17944380130 scopus 로고    scopus 로고
    • CARD4/Nod1 mediates NF-κB and JNK activation by invasive Shigella flexneri
    • Girardin, S. E. et al. CARD4/Nod1 mediates NF-κB and JNK activation by invasive Shigella flexneri. EMBO Rep. 2, 736-742 (2001).
    • (2001) EMBO Rep. , vol.2 , pp. 736-742
    • Girardin, S.E.1
  • 45
    • 0037018107 scopus 로고    scopus 로고
    • Toll-like receptor 4 resides in the Golgi apparatus and colocalizes with internalized lipopolysaccharide in intestinal epithelial cells
    • Hornef, M. W., Frisan, T., Vandewalle, A., Normark, S. & Richter-Dahlfors, A. Toll-like receptor 4 resides in the Golgi apparatus and colocalizes with internalized lipopolysaccharide in intestinal epithelial cells. J. Exp. Med. 195, 559-570 (2002).
    • (2002) J. Exp. Med. , vol.195 , pp. 559-570
    • Hornef, M.W.1    Frisan, T.2    Vandewalle, A.3    Normark, S.4    Richter-Dahlfors, A.5
  • 46
    • 0037446528 scopus 로고    scopus 로고
    • Strategic compartmentalization of Toll-like receptor 4 in the mouse gut
    • Ortega-Cava, C. F. et al. Strategic compartmentalization of Toll-like receptor 4 in the mouse gut. J. Immunol. 170, 3977-3985 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 3977-3985
    • Ortega-Cava, C.F.1
  • 47
    • 0035978651 scopus 로고    scopus 로고
    • Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
    • Hugot J. P. et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease. Nature 411, 599-603 (2001).
    • (2001) Nature , vol.411 , pp. 599-603
    • Hugot, J.P.1
  • 48
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
    • Ogura, Y. et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 411, 603-606 (2001).
    • (2001) Nature , vol.411 , pp. 603-606
    • Ogura, Y.1
  • 49
    • 0038109983 scopus 로고    scopus 로고
    • Crohn's disease and the NOD2 gene: A role for Paneth cells
    • Lala, S. et al. Crohn's disease and the NOD2 gene: a role for Paneth cells. Gastroenterology 125, 47-67 (2003).
    • (2003) Gastroenterology , vol.125 , pp. 47-67
    • Lala, S.1
  • 50
    • 0030297089 scopus 로고    scopus 로고
    • The indigenous gastrointestinal microflora
    • Berg, R. D. The indigenous gastrointestinal microflora. Trends Microbiol. 4, 430-435 (1996).
    • (1996) Trends Microbiol. , vol.4 , pp. 430-435
    • Berg, R.D.1
  • 51
    • 0036399823 scopus 로고    scopus 로고
    • How host-microbial interactions shape the nutrient environment of the mammalian intestine
    • Hooper, L. V., Midtvedt, T. & Gordon, J. I. How host-microbial interactions shape the nutrient environment of the mammalian intestine. Annu. Rev. Nutr. 22, 283-307 (2002).
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 283-307
    • Hooper, L.V.1    Midtvedt, T.2    Gordon, J.I.3
  • 52
    • 0024321629 scopus 로고
    • Structural characterization of the lipid A component of Bacteroides fragilis strain NCTC 9343 lipopolysaccharide
    • Weintraub, A., Zahninger, U., Wollenweber, H. W., Seydel, U. & Rietschel, E. Structural characterization of the lipid A component of Bacteroides fragilis strain NCTC 9343 lipopolysaccharide. Eur. J. Biochem. 183, 425-431 (1989).
    • (1989) Eur. J. Biochem. , vol.183 , pp. 425-431
    • Weintraub, A.1    Zahninger, U.2    Wollenweber, H.W.3    Seydel, U.4    Rietschel, E.5
  • 53
    • 0026088437 scopus 로고
    • Lipid A-like molecules that antagonize the effects of endotoxins on human monocytes
    • Golenbock, D. T., Hampton, R. Y., Qureshi, N., Takayama, K. & Raetz, C. R. Lipid A-like molecules that antagonize the effects of endotoxins on human monocytes. J. Biol. Chem. 266, 19490-19498 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 19490-19498
    • Golenbock, D.T.1    Hampton, R.Y.2    Qureshi, N.3    Takayama, K.4    Raetz, C.R.5
  • 54
    • 0035451799 scopus 로고    scopus 로고
    • Intestinal macrophages lack CD14 and CD89 and consequently are down-regulated for LPS- and IgA-mediated activities
    • Smith, P. D. et al. Intestinal macrophages lack CD14 and CD89 and consequently are down-regulated for LPS- and IgA-mediated activities. J. Immunol. 167, 2651-2656 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 2651-2656
    • Smith, P.D.1
  • 55
    • 0035424901 scopus 로고    scopus 로고
    • Decreased expression of Toll-like receptor-4 and MD- 2 correlates with intestinal epithelial cell protection against dysregulated proinflammatory gene expression in response to bacterial lipopolysaccharide
    • Abreu, M. T. et al. Decreased expression of Toll-like receptor-4 and MD-2 correlates with intestinal epithelial cell protection against dysregulated proinflammatory gene expression in response to bacterial lipopolysaccharide. J. Immunol. 167, 1609-1616 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 1609-1616
    • Abreu, M.T.1
  • 56
    • 0035000687 scopus 로고    scopus 로고
    • Absence of Toll-like receptor- 4 explains endotoxin hyporesponsiveness in human intestinal epithelium
    • Naik, S., Kelly, E. J., Meijer, L. Petterson, S. & Sanderson, I. R. Absence of Toll-like receptor-4 explains endotoxin hyporesponsiveness in human intestinal epithelium. J. Pediatr. Gastroenterol. Nutr. 32, 449-453 (2001).
    • (2001) J. Pediatr. Gastroenterol. Nutr. , vol.32 , pp. 449-453
    • Naik, S.1    Kelly, E.J.2    Meijer, L.3    Petterson, S.4    Sanderson, I.R.5
  • 57
    • 0035953543 scopus 로고    scopus 로고
    • The innate immune response to bacteria flagellin is mediated by Toll-like receptor 5
    • Hayashi, F. et al. The innate immune response to bacteria flagellin is mediated by Toll-like receptor 5. Nature 410, 1099-1103 (2001).
    • (2001) Nature , vol.410 , pp. 1099-1103
    • Hayashi, F.1
  • 58
    • 0035170239 scopus 로고    scopus 로고
    • Salmonella typhimurium translocates flagellin across intestinal epithelia, inducing a pro-inflammatory response
    • Gewirtz, A. T. et al. Salmonella typhimurium translocates flagellin across intestinal epithelia, inducing a pro-inflammatory response. J. Clin. Invest. 107, 99-109 (2001).
    • (2001) J. Clin. Invest. , vol.107 , pp. 99-109
    • Gewirtz, A.T.1
  • 59
    • 0035923513 scopus 로고    scopus 로고
    • Flagellin stimulation of intestinal epithelial cells triggers CCL20-mediated migration of dendritic cells
    • Sierra, F. et al. Flagellin stimulation of intestinal epithelial cells triggers CCL20-mediated migration of dendritic cells. Proc. Natl Acad. Sci. USA 98, 13722-13727 (2001). An important paper about transepithelial signalling by bacteria.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 13722-13727
    • Sierra, F.1
  • 60
    • 0344234277 scopus 로고    scopus 로고
    • Helicobacter pylori flagellins have very low intrinsic activity to stimulate human gastric epithelial cells via TLR5
    • Lee, S. K. et al. Helicobacter pylori flagellins have very low intrinsic activity to stimulate human gastric epithelial cells via TLR5. Microbes Infect. 5, 1345-1356 (2003).
    • (2003) Microbes Infect. , vol.5 , pp. 1345-1356
    • Lee, S.K.1
  • 61
    • 0037756822 scopus 로고    scopus 로고
    • Anti-inflammatory role for intracellular dimeric immunoglobulin A by neutralization of lipopolysaccharide in epithelial cells
    • Fernandez, M. I. et al. Anti-inflammatory role for intracellular dimeric immunoglobulin A by neutralization of lipopolysaccharide in epithelial cells. Immunity 18, 739-749 (2003).
    • (2003) Immunity , vol.18 , pp. 739-749
    • Fernandez, M.I.1
  • 62
    • 17344379177 scopus 로고    scopus 로고
    • Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion
    • Odenbreit, S. et al. Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion. Science 287, 1497-1500 (2000).
    • (2000) Science , vol.287 , pp. 1497-1500
    • Odenbreit, S.1
  • 63
    • 0036006290 scopus 로고    scopus 로고
    • Regulation of interleukin-1 and NF-κB activation by alternative splicing of MyD88
    • Janssens, S., Burns, K., Tschopp, R. & Beyaert, R. Regulation of interleukin-1 and NF-κB activation by alternative splicing of MyD88. Curr. Biol. 12, 467-471 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 467-471
    • Janssens, S.1    Burns, K.2    Tschopp, R.3    Beyaert, R.4
  • 64
    • 0037178785 scopus 로고    scopus 로고
    • IRAK-M is a negative regulator of Toll-like receptor signalling
    • Kobayashi, K. et al. IRAK-M is a negative regulator of Toll-like receptor signalling. Cell 110, 191-202 (2002).
    • (2002) Cell , vol.110 , pp. 191-202
    • Kobayashi, K.1
  • 65
    • 0032746173 scopus 로고    scopus 로고
    • A novel therapy for colitis utilizing PPAR-γ ligands to inhibit the epithelial inflammatory response
    • Su, C. G. et al. A novel therapy for colitis utilizing PPAR-γ ligands to inhibit the epithelial inflammatory response. J. Clin. Invest. 104, 383-389 (1999).
    • (1999) J. Clin. Invest. , vol.104 , pp. 383-389
    • Su, C.G.1
  • 66
    • 0035794293 scopus 로고    scopus 로고
    • Attenuation of colon inflammation through activators of the retinoid X receptor (RXR)/peroxisome proliferator-activated receptor γ(PPARγ) heterodimer. A basis for new therapeutic strategies
    • Desreumaux, P. et al. Attenuation of colon inflammation through activators of the retinoid X receptor (RXR)/peroxisome proliferator-activated receptor γ(PPARγ) heterodimer. A basis for new therapeutic strategies. J. Exp. Med. 193, 827-838 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 827-838
    • Desreumaux, P.1
  • 67
    • 0347756655 scopus 로고    scopus 로고
    • Commensal anaerobic gut bacteria attenuate inflammation by regulating nuclear-cytoplasmic shuttling of PPAR-γ and RelA
    • Kelly, D. et al. Commensal anaerobic gut bacteria attenuate inflammation by regulating nuclear-cytoplasmic shuttling of PPAR-γ and RelA. Nature Immunol. 5, 104-112 (2004).
    • (2004) Nature Immunol. , vol.5 , pp. 104-112
    • Kelly, D.1
  • 68
    • 0034284803 scopus 로고    scopus 로고
    • Prokaryotic regulation of epithelial responses by inhibition of IκB-α ubiquitination
    • Neish, A. S. Prokaryotic regulation of epithelial responses by inhibition of IκB-α ubiquitination. Science 289, 1560-1563 (2000). Coins the idea that non-pathogenic bacteria could mediate anti-inflammatory signals.
    • (2000) Science , vol.289 , pp. 1560-1563
    • Neish, A.S.1
  • 69
    • 2142810997 scopus 로고    scopus 로고
    • DNA from probiotic bacteria modulates murine and human epithelial and immune functions
    • Jijon, H. et al. DNA from probiotic bacteria modulates murine and human epithelial and immune functions. Gastroenterology 126, 1358-1373 (2004).
    • (2004) Gastroenterology , vol.126 , pp. 1358-1373
    • Jijon, H.1
  • 70
    • 0029993786 scopus 로고    scopus 로고
    • Tolerance towards resident intestinal flora in mice is abrogated in experimental colitis and restored by treatment with interleukin-10 or antibodies to interleukin-12
    • Duchmann, R., Schmitt, E., Knolle, P., Meyer zum Büschenfelde, K. H. & Neurath, M. Tolerance towards resident intestinal flora in mice is abrogated in experimental colitis and restored by treatment with interleukin-10 or antibodies to interleukin-12. Eur. J. Immunol. 26, 934-938 (1996).
    • (1996) Eur. J. Immunol. , vol.26 , pp. 934-938
    • Duchmann, R.1    Schmitt, E.2    Knolle, P.3    Meyer Zum Büschenfelde, K.H.4    Neurath, M.5
  • 71
    • 0030043855 scopus 로고    scopus 로고
    • Oral tolerance in myelin basic protein T cell receptor transgenic mice: Suppression of auto-immune encephalomyelitis and dose-dependent induction of regulatory cells
    • Chen, Y. et al. Oral tolerance in myelin basic protein T cell receptor transgenic mice: suppression of auto-immune encephalomyelitis and dose-dependent induction of regulatory cells. Proc. Natl Acad. Sci. USA 93, 388-391 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 388-391
    • Chen, Y.1
  • 72
    • 0029609870 scopus 로고
    • Breakdown of tolerance to the intestinal bacterial flora in inflammatory bowel disease (IBD)
    • MacDonald, T. M. Breakdown of tolerance to the intestinal bacterial flora in inflammatory bowel disease (IBD). Clin. Exp. Immunol. 102, 445-447 (1995).
    • (1995) Clin. Exp. Immunol. , vol.102 , pp. 445-447
    • MacDonald, T.M.1
  • 74
    • 1842430006 scopus 로고    scopus 로고
    • Bacterial invasion: The paradigms of enteroinvasive pathogens
    • Cossart, P. & Sansonetti P. J. Bacterial invasion: the paradigms of enteroinvasive pathogens. Science 304, 242-248 (2004).
    • (2004) Science , vol.304 , pp. 242-248
    • Cossart, P.1    Sansonetti, P.J.2
  • 75
    • 0020003681 scopus 로고
    • Involvement of a large plasmid in the invasive ability of Shigella flexneri
    • Sansonetti, P. J., Kopecko, D. J. & Formal, S. B. Involvement of a large plasmid in the invasive ability of Shigella flexneri. Infect. Immun. 35, 852-860 (1982).
    • (1982) Infect. Immun. , vol.35 , pp. 852-860
    • Sansonetti, P.J.1    Kopecko, D.J.2    Formal, S.B.3
  • 76
    • 0025755783 scopus 로고
    • Discrimination between intracellular uptake and surface adhesion of bacterial pathogens
    • Isberg, R. R. Discrimination between intracellular uptake and surface adhesion of bacterial pathogens. Science 252, 934-938 (1991).
    • (1991) Science , vol.252 , pp. 934-938
    • Isberg, R.R.1
  • 77
    • 0028332527 scopus 로고
    • Salmonella entry into mammalian cells: Different yet converging signal transduction pathways?
    • Galan, J. E. Salmonella entry into mammalian cells: different yet converging signal transduction pathways? Trends Cell Biol. 4, 196-199 (1994).
    • (1994) Trends Cell Biol. , vol.4 , pp. 196-199
    • Galan, J.E.1
  • 78
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacteria pathogens of animals and plants
    • Hueck, C. Type III protein secretion systems in bacteria pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62, 379-433 (1998).
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.1
  • 79
    • 0030031402 scopus 로고    scopus 로고
    • The Ipf fimbrial operon mediates adhesion of Salmonella typhimurium to murine Peyer's patches
    • Baumler, A. J., Tsolis, R. M. & Heffron, F. The Ipf fimbrial operon mediates adhesion of Salmonella typhimurium to murine Peyer's patches. Proc. Natl Acad. Sci. USA 93, 279-283 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 279-283
    • Baumler, A.J.1    Tsolis, R.M.2    Heffron, F.3
  • 80
    • 0030845121 scopus 로고    scopus 로고
    • Invasin-dependent and invasin-independent pathways for translocation of Yersinia pseudotuberculosis across the Peyer's patch intestinal epithelium
    • Marra, A. & Isberg, R. R. Invasin-dependent and invasin-independent pathways for translocation of Yersinia pseudotuberculosis across the Peyer's patch intestinal epithelium. Infect. Immun. 65, 3412-3421 (1997).
    • (1997) Infect. Immun. , vol.65 , pp. 3412-3421
    • Marra, A.1    Isberg, R.R.2
  • 81
    • 0029945905 scopus 로고    scopus 로고
    • Infection of rabbit Peyer's patches by Shigella flexneri: Effect of adhesive or invasive bacterial phenotypes on follicle-associated epithelium
    • Sansonetti, P. J., Arondel, J., Cantey, J. R., Prévost. M. C. & Huerre, M. Infection of rabbit Peyer's patches by Shigella flexneri: effect of adhesive or invasive bacterial phenotypes on follicle-associated epithelium. Infect. Immun. 64, 2752-2764 (1996).
    • (1996) Infect. Immun. , vol.64 , pp. 2752-2764
    • Sansonetti, P.J.1    Arondel, J.2    Cantey, J.R.3    Prévost, M.C.4    Huerre, M.5
  • 82
    • 0032802267 scopus 로고    scopus 로고
    • Molecular basis of the interaction of Salmonella with the intestinal mucosa
    • Darwin, K. H. & Miller, V. L. Molecular basis of the interaction of Salmonella with the intestinal mucosa. Clin. Microbiol. Rev. 12, 405-428 (1999).
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 405-428
    • Darwin, K.H.1    Miller, V.L.2
  • 83
    • 0030067796 scopus 로고    scopus 로고
    • Distinct populations of dendritic cells are present in the subepithelial dome and T cell regions of murine Peyer's patches
    • Kelsall, B. L. & Strober, W. Distinct populations of dendritic cells are present in the subepithelial dome and T cell regions of murine Peyer's patches. J. Exp. Med. 183, 237-247 (1996).
    • (1996) J. Exp. Med. , vol.183 , pp. 237-247
    • Kelsall, B.L.1    Strober, W.2
  • 84
    • 0036792393 scopus 로고    scopus 로고
    • The Yersinia Ysc-Yop 'type III' weaponry
    • Cornelis, G. R. The Yersinia Ysc-Yop 'type III' weaponry. Nature Rev. Mol. Cell Biol. 3, 742-752 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 742-752
    • Cornelis, G.R.1
  • 85
    • 0037622178 scopus 로고    scopus 로고
    • Interaction of Yersinia enterocolitica with epithelial cells: Invasin beyond invasion
    • Grassl, G. A., Bohn, E., Müller, Y., Bühler, O. T. & Autenrieth, I. B. Interaction of Yersinia enterocolitica with epithelial cells: invasin beyond invasion. Int. J. Med. Microbiol. 293, 41-54 (2003).
    • (2003) Int. J. Med. Microbiol. , vol.293 , pp. 41-54
    • Grassl, G.A.1    Bohn, E.2    Müller, Y.3    Bühler, O.T.4    Autenrieth, I.B.5
  • 87
    • 0029804189 scopus 로고    scopus 로고
    • In vivo apoptosis in Shigella flexneri infections
    • Zychlinsky, A. et al. In vivo apoptosis in Shigella flexneri infections. Infect Immun. 64, 5357-5365 (1996).
    • (1996) Infect Immun. , vol.64 , pp. 5357-5365
    • Zychlinsky, A.1
  • 88
    • 0036259826 scopus 로고    scopus 로고
    • Apoptosis in acute shigellosis is associated with increased production of Fas/Fas ligand, perforin, caspase-1, and caspase-3, but reduced production of Bcl-2 and interleukin-2
    • Raqib, R. et al. Apoptosis in acute shigellosis is associated with increased production of Fas/Fas ligand, perforin, caspase-1, and caspase-3, but reduced production of Bcl-2 and interleukin-2. Infect. Immun. 70, 3199-3207 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 3199-3207
    • Raqib, R.1
  • 89
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • Zychlinsky, A., Prevost, M. C. & Sansonetti, P. J. Shigella flexneri induces apoptosis in infected macrophages. Nature 358, 167-169 (1992).
    • (1992) Nature , vol.358 , pp. 167-169
    • Zychlinsky, A.1    Prevost, M.C.2    Sansonetti, P.J.3
  • 90
    • 15644374367 scopus 로고    scopus 로고
    • Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB
    • Hilby, H. et al. Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB. J. Biol. Chem. 273, 32895-32900 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 32895-32900
    • Hilby, H.1
  • 91
    • 0028203807 scopus 로고
    • Polymorphonuclear leukocyte transmigration promotes invasion of colonic epithelial monolayer by Shigella flexneri
    • Perdomo, J. J., Gounon, P. & Sansonetti, P. J. Polymorphonuclear leukocyte transmigration promotes invasion of colonic epithelial monolayer by Shigella flexneri. J. Clin. Invest. 93, 633-643 (1994).
    • (1994) J. Clin. Invest. , vol.93 , pp. 633-643
    • Perdomo, J.J.1    Gounon, P.2    Sansonetti, P.J.3
  • 92
    • 0028033311 scopus 로고
    • Acute inflammation causes epithelial invasion and mucosal destruction in experimental shigellosis
    • Perdomo, J. J. et al. Acute inflammation causes epithelial invasion and mucosal destruction in experimental shigellosis. J. Exp. Med. 180, 1307-1319 (1994). First evidence that inflammation disrupts the epithelial barrier and promotes bacterial invasion.
    • (1994) J. Exp. Med. , vol.180 , pp. 1307-1319
    • Perdomo, J.J.1
  • 94
    • 10244237710 scopus 로고    scopus 로고
    • Caspase-1 activation of IL-1β and IL-18 are essential for Shigela flexneri induced inflammation
    • Sansonetti, P. J. et al. Caspase-1 activation of IL-1β and IL-18 are essential for Shigela flexneri induced inflammation. Immunity 12, 681-590 (2000).
    • (2000) Immunity , vol.12 , pp. 681-590
    • Sansonetti, P.J.1
  • 95
    • 0032037590 scopus 로고    scopus 로고
    • An essential role for γ interferon in innate resistance to Shigella flexneri infection
    • Way, S. S., Borczuk, A. C., Dominitz, R. & Goldberg, M. An essential role for γ interferon in innate resistance to Shigella flexneri infection. Infect. Immun. 66, 1342-1348 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 1342-1348
    • Way, S.S.1    Borczuk, A.C.2    Dominitz, R.3    Goldberg, M.4
  • 96
    • 0037007656 scopus 로고    scopus 로고
    • Neutrophil elastase targets virulence factors of enterobacteria
    • Weinrauch, Y., Drujan, D., Shapiro, S. D., Weiss, J. & Zychlinsky, A. Neutrophil elastase targets virulence factors of enterobacteria. Nature 417, 91-94 (2002). Shows that neutrophil elastase is essential for the degradation of bacterial virulence factors.
    • (2002) Nature , vol.417 , pp. 91-94
    • Weinrauch, Y.1    Drujan, D.2    Shapiro, S.D.3    Weiss, J.4    Zychlinsky, A.5
  • 97
    • 1542287347 scopus 로고    scopus 로고
    • Neutrophil extracellular traps kill bacteria
    • Brinkmann, V. et al. Neutrophil extracellular traps kill bacteria. Science 303, 1532-1535 (2004).
    • (2004) Science , vol.303 , pp. 1532-1535
    • Brinkmann, V.1
  • 98
    • 0035172569 scopus 로고    scopus 로고
    • Rupture, invasion and inflammatory destruction of the intestinal barrier by Shigella, making sense of prokaryote-eukaryote cross-talk
    • Sansonetti, P. J. Rupture, invasion and inflammatory destruction of the intestinal barrier by Shigella, making sense of prokaryote-eukaryote cross-talk. FEMS Microbiol. Rev. 25, 3-14 (2001).
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 3-14
    • Sansonetti, P.J.1
  • 99
    • 0142248435 scopus 로고    scopus 로고
    • The ShiA protein encoded by the Shigella flexneri SHI-2 pathogenicity island attenuates inflammation
    • Ingersoll, M. A. et al. The ShiA protein encoded by the Shigella flexneri SHI-2 pathogenicity island attenuates inflammation. Cell. Microbiol. 5, 797-807 (2003).
    • (2003) Cell. Microbiol. , vol.5 , pp. 797-807
    • Ingersoll, M.A.1
  • 100
    • 0035126317 scopus 로고    scopus 로고
    • Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
    • Islam, D. et al. Downregulation of bactericidal peptides in enteric infections: a novel immune escape mechanism with bacterial DNA as a potential regulator. Nature Med. 7, 180-185 (2001).
    • (2001) Nature Med. , vol.7 , pp. 180-185
    • Islam, D.1
  • 101
    • 0034679578 scopus 로고    scopus 로고
    • Salmonella exploits caspase-1 to colonize Peyer's patches in a murine typhoid model
    • Monack, D. M. et al. Salmonella exploits caspase-1 to colonize Peyer's patches in a murine typhoid model. J. Exp. Med. 192, 249-258 (2000).
    • (2000) J. Exp. Med. , vol.192 , pp. 249-258
    • Monack, D.M.1
  • 102
    • 0036112327 scopus 로고    scopus 로고
    • Trafficking of the Salmonella vacuole in macrophages
    • Holden, D. W. Trafficking of the Salmonella vacuole in macrophages. Traffics, 161-169 (2002).
    • (2002) Traffics , pp. 161-169
    • Holden, D.W.1
  • 103
    • 14444287535 scopus 로고    scopus 로고
    • Genes encoding putative effector proteins of the type III secretion system of Salmonella pathogenicity island 2 are required for bacterial virulence and proliferation in macrophages
    • Hensel, M., Shea, J. E. & Holden, D. Genes encoding putative effector proteins of the type III secretion system of Salmonella pathogenicity island 2 are required for bacterial virulence and proliferation in macrophages. Mol. Microbiol. 30, 163-174 (1998).
    • (1998) Mol. Microbiol. , vol.30 , pp. 163-174
    • Hensel, M.1    Shea, J.E.2    Holden, D.3
  • 104
    • 0242485924 scopus 로고    scopus 로고
    • The rab7 GTPase controls the maturation of Salmonella typhimurium-containing vacuoles in HeLa cells
    • Meresse, S., Steele-Mortimer, O., Finlay, B. B. & Gorvel, J.-P. The rab7 GTPase controls the maturation of Salmonella typhimurium-containing vacuoles in HeLa cells. EMBO J. 18, 4394-4403 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4394-4403
    • Meresse, S.1    Steele-Mortimer, O.2    Finlay, B.B.3    Gorvel, J.-P.4
  • 105
    • 0033157323 scopus 로고    scopus 로고
    • Biogenesis of Salmonella typhimurium-containing vacuoles in epithelial cells involves interactions with the early endocytic pathway
    • Steele-Mortimer, O., Méresse, S., Gorvel, J.-P., Toh, B. H. & Finlay, B. B. Biogenesis of Salmonella typhimurium-containing vacuoles in epithelial cells involves interactions with the early endocytic pathway. Cell. Microbiol. 1, 33-49 (1999).
    • (1999) Cell. Microbiol. , vol.1 , pp. 33-49
    • Steele-Mortimer, O.1    Méresse, S.2    Gorvel, J.-P.3    Toh, B.H.4    Finlay, B.B.5
  • 106
    • 0141642027 scopus 로고    scopus 로고
    • SseG, a virulence protein that targets Salmonella to the Golgi network
    • Salcedo, S. P. & Holden, D. SseG, a virulence protein that targets Salmonella to the Golgi network. EMBO J. 22, 5003-5014 (2003).
    • (2003) EMBO J. , vol.22 , pp. 5003-5014
    • Salcedo, S.P.1    Holden, D.2
  • 107
    • 0025739814 scopus 로고
    • Entry of Listeria monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from Gram-positive cocci
    • Gaillard, J.-L., Berche, P., Frehel, C., Gouin, E. & Cossart, P. Entry of Listeria monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from Gram-positive cocci. Cell 65, 1127-1141 (1991).
    • (1991) Cell , vol.65 , pp. 1127-1141
    • Gaillard, J.-L.1    Berche, P.2    Frehel, C.3    Gouin, E.4    Cossart, P.5
  • 108
    • 0031883480 scopus 로고    scopus 로고
    • Comprehensive study of the intestinal stage of listeriosis in a rat ligated ileal-loop system
    • Pron, B. et al. Comprehensive study of the intestinal stage of listeriosis in a rat ligated ileal-loop system. Infect. Immun. 66, 747-755 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 747-755
    • Pron, B.1
  • 109
    • 0035368519 scopus 로고    scopus 로고
    • A transgenic model for listeriosis: Role of internalin in crossing the intestinal barrier
    • Lecuit, M. et al. A transgenic model for listeriosis: role of internalin in crossing the intestinal barrier. Science 292, 1722-1725 (2001). Example of a rational switch of species specificity that allows the modelling of a human disease in mice.
    • (2001) Science , vol.292 , pp. 1722-1725
    • Lecuit, M.1
  • 110
    • 0029889947 scopus 로고    scopus 로고
    • Listeriolysin O activates mitogen-activated protein kinase in eukaryotic cells
    • Tang, P., Rosenshine, I., Cossart, P. & Finlay, B. B. Listeriolysin O activates mitogen-activated protein kinase in eukaryotic cells. Infect. Immun. 6, 2359-2361 (1996).
    • (1996) Infect. Immun. , vol.6 , pp. 2359-2361
    • Tang, P.1    Rosenshine, I.2    Cossart, P.3    Finlay, B.B.4
  • 111
    • 0035013827 scopus 로고    scopus 로고
    • Regulated MIP-3α/CCL20 production by human intestinal epithelium: Mechanisms for modulating mucosal immunity
    • Izadpanah, A., Dwinnel, M. B., Eckmann, L., Varki, N. M. & Kagnoff, M. F. Regulated MIP-3α/CCL20 production by human intestinal epithelium: mechanisms for modulating mucosal immunity. Am. J. Physiol. 280, G710-G719 (2001).
    • (2001) Am. J. Physiol. , vol.280
    • Izadpanah, A.1    Dwinnel, M.B.2    Eckmann, L.3    Varki, N.M.4    Kagnoff, M.F.5
  • 112
    • 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 430, 213-218 (2004).
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1
  • 113
    • 0027428365 scopus 로고
    • Salmonella typhimurium attachment to human intestinal monolayers: Transcellular signaling to subepithelial neutrophils
    • McCormick, B. A., Colgan, S. P., Archer, C. D., Miller, S. I. & Madara, J. L. Salmonella typhimurium attachment to human intestinal monolayers: transcellular signaling to subepithelial neutrophils. J. Cell Biol. 123, 895-907 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 895-907
    • McCormick, B.A.1    Colgan, S.P.2    Archer, C.D.3    Miller, S.I.4    Madara, J.L.5
  • 114
    • 2442572098 scopus 로고    scopus 로고
    • Identification of hepoxilin A3 in inflammatory events: A required role in neutrophil migration across intestinal epithelia
    • Mrsny, R. J. et al. Identification of hepoxilin A3 in inflammatory events: a required role in neutrophil migration across intestinal epithelia. Proc. Natl Acad. Sci. USA 101, 7421-7426 (2004). Identifies the first transepithelial chemoattractant.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7421-7426
    • Mrsny, R.J.1
  • 116
    • 0013826738 scopus 로고
    • Experimental bacillary dysentery: An electron microscopic study of the response of intestinal mucosa to bacterial invasion
    • Takeuchi, A., Spring, H., Labrec, E. H. & Formal, S. B. Experimental bacillary dysentery: an electron microscopic study of the response of intestinal mucosa to bacterial invasion. Am. J. Pathol. 4, 1011-1044 (1965).
    • (1965) Am. J. Pathol. , vol.4 , pp. 1011-1044
    • Takeuchi, A.1    Spring, H.2    Labrec, E.H.3    Formal, S.B.4
  • 117
    • 4644226513 scopus 로고    scopus 로고
    • IL-8 is a key chemokine regulating neutrophil recruitment in a new mouse model of Shigella-induced colitis
    • Singer, M. & Sansonetti, P. J. IL-8 is a key chemokine regulating neutrophil recruitment in a new mouse model of Shigella-induced colitis. J. Immunol. 173, 4197-4206 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 4197-4206
    • Singer, M.1    Sansonetti, P.J.2
  • 118
    • 0033052681 scopus 로고    scopus 로고
    • Interleukin-8 controls bacterial transepithelial translocation at the cost of epithelial destruction in experimental shigellosis
    • Sansonetti, P. J., Arondel, J., Huerre, M., Harada, A. & Katsushima, K. Interleukin-8 controls bacterial transepithelial translocation at the cost of epithelial destruction in experimental shigellosis. Infect. Immun. 67, 1471-1480 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 1471-1480
    • Sansonetti, P.J.1    Arondel, J.2    Huerre, M.3    Harada, A.4    Katsushima, K.5
  • 119
    • 0033592595 scopus 로고    scopus 로고
    • Extraintestinal dissemination of Salmonella by CD18-expressing phagocytes
    • Vazquez-Torres, A. et al. Extraintestinal dissemination of Salmonella by CD18-expressing phagocytes. Nature 401, 804-808 (1999).
    • (1999) Nature , vol.401 , pp. 804-808
    • Vazquez-Torres, A.1
  • 120
    • 0842312142 scopus 로고    scopus 로고
    • Immunity to Salmonella from a dendritic point of view
    • Sundquist, M., Rydstrom, A. & Wick, M. J. Immunity to Salmonella from a dendritic point of view. Cell. Microbiol. 6, 1-11 (2004).
    • (2004) Cell. Microbiol. , vol.6 , pp. 1-11
    • Sundquist, M.1    Rydstrom, A.2    Wick, M.J.3
  • 121
    • 0345303939 scopus 로고    scopus 로고
    • Lessons from Nod2 studies: Towards a link between Crohn's disease and bacterial sensing
    • Girardin, S. E., Hugot, J.-P. & Sansonetti, P. J. Lessons from Nod2 studies: towards a link between Crohn's disease and bacterial sensing. Trends Immunol. 24, 652-658 (2003).
    • (2003) Trends Immunol. , vol.24 , pp. 652-658
    • Girardin, S.E.1    Hugot, J.-P.2    Sansonetti, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.