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Volumn 182, Issue 11, 2009, Pages 6690-6696

Induction of distinct TLR2-mediated proinflammatory and proadhesive signaling pathways in response to Porphyromonas gingivalis fimbriae

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; BETA2 INTEGRIN; CYTOHESIN 1; INTERCELLULAR ADHESION MOLECULE 1; INTERLEUKIN 1 RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE 13; MYELOID DIFFERENTIATION FACTOR 88; PROTEIN SERINE THREONINE KINASE; TOLL LIKE RECEPTOR 2; MEMBRANE PROTEIN; MYD88 PROTEIN, HUMAN; PHOSPHATIDYLINOSITOL 3 KINASE; TIRAP PROTEIN, HUMAN;

EID: 67449116290     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0900524     Document Type: Article
Times cited : (80)

References (61)
  • 1
    • 0035524488 scopus 로고    scopus 로고
    • Toll-like receptors and innate immunity
    • Medzhitov, R. 2001. Toll-like receptors and innate immunity. Nat. Rev. Immunol. 1: 135-145.
    • (2001) Nat. Rev. Immunol. , vol.1 , pp. 135-145
    • Medzhitov, R.1
  • 3
    • 34447645301 scopus 로고    scopus 로고
    • How important are Toll-like receptors for antimicrobial responses?
    • Carpenter, S., and L. A. O'Neill. 2007. How important are Toll-like receptors for antimicrobial responses? Cell. Microbiol. 9: 1891-1901.
    • (2007) Cell. Microbiol. , vol.9 , pp. 1891-1901
    • Carpenter, S.1    O'Neill, L.A.2
  • 4
    • 33744823520 scopus 로고    scopus 로고
    • Innate immune signaling and Porphyromonas gingivalis-accelerated atherosclerosis
    • Gibson, F. C., 3rd, H. Yumoto, Y. Takahashi, H. H. Chou, and C. A. Genco. 2006. Innate immune signaling and Porphyromonas gingivalis-accelerated atherosclerosis. J. Dent. Res. 85: 106-121.
    • (2006) J. Dent. Res. , vol.85 , pp. 106-121
    • Gibson III, F.C.1    Yumoto, H.2    Takahashi, Y.3    Chou, H.H.4    Genco, C.A.5
  • 5
    • 33845462504 scopus 로고    scopus 로고
    • Cutting edge: TLR2 is required for the innate response to Porphyromonas gingivalis: Activation leads to bacterial persistence and TLR2 deficiency attenuates induced alveolar bone resorption
    • Burns, E., G. Bachrach, L. Shapira, and G. Nussbaum. 2006. Cutting edge: TLR2 is required for the innate response to Porphyromonas gingivalis: Activation leads to bacterial persistence and TLR2 deficiency attenuates induced alveolar bone resorption. J. Immunol. 177: 8296-8300. (Pubitemid 44893789)
    • (2006) Journal of Immunology , vol.177 , Issue.12 , pp. 8296-8300
    • Burns, E.1    Bachrach, G.2    Shapira, L.3    Nussbaum, G.4
  • 7
    • 12844264795 scopus 로고    scopus 로고
    • Cytokine profiling of macrophages exposed to Porphyromonas gingivalis, its lipopolysaccharide, or its FimA protein
    • Zhou, Q., T. Desta, M. Fenton, D. T. Graves, and S. Amar. 2005. Cytokine profiling of macrophages exposed to Porphyromonas gingivalis, its lipopolysaccharide, or its FimA protein. Infect. Immun. 73: 935-943.
    • (2005) Infect. Immun. , vol.73 , pp. 935-943
    • Zhou, Q.1    Desta, T.2    Fenton, M.3    Graves, D.T.4    Amar, S.5
  • 8
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • O'Neill, L. A., and A. G. Bowie. 2007. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nat. Rev. Immunol. 7: 353-364.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 10
    • 2942544238 scopus 로고    scopus 로고
    • Innate immune recognition of invasive bacteria accelerates atherosclerosis in apolipoprotein E-deficient mice
    • Gibson, F. C., 3rd, C. Hong, H. H. Chou, H. Yumoto, J. Chen, E. Lien, J. Wong, and C. A. Genco. 2004. Innate immune recognition of invasive bacteria accelerates atherosclerosis in apolipoprotein E-deficient mice. Circulation 109: 2801-2806.
    • (2004) Circulation , vol.109 , pp. 2801-2806
    • Gibson III, F.C.1    Hong, C.2    Chou, H.H.3    Yumoto, H.4    Chen, J.5    Lien, E.6    Wong, J.7    Genco, C.A.8
  • 11
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: Pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont, R. J., and H. F. Jenkinson. 1998. Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev. 62: 1244-1263.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 12
    • 0037265493 scopus 로고    scopus 로고
    • Molecular interaction of Porphyromonas gingivalis with host cells: Implication for the microbial pathogenesis of periodontal disease
    • Amano, A. 2003. Molecular interaction of Porphyromonas gingivalis with host cells: implication for the microbial pathogenesis of periodontal disease. J. Periodontol. 74: 90-96.
    • (2003) J. Periodontol. , vol.74 , pp. 90-96
    • Amano, A.1
  • 13
    • 0035184263 scopus 로고    scopus 로고
    • Bacterial fimbriae and their peptides activate human gingival epithelial cells through Toll-like receptor 2
    • Asai, Y., Y. Ohyama, K. Gen, and T. Ogawa. 2001. Bacterial fimbriae and their peptides activate human gingival epithelial cells through Toll-like receptor 2. Infect. Immun. 69: 7387-7395.
    • (2001) Infect. Immun. , vol.69 , pp. 7387-7395
    • Asai, Y.1    Ohyama, Y.2    Gen, K.3    Ogawa, T.4
  • 14
    • 28244498667 scopus 로고    scopus 로고
    • Peptide mapping of bacterial fimbrial epitopes interacting with pattern recognition receptors
    • Hajishengallis, G., P. Ratti, and E. Harokopakis. 2005. Peptide mapping of bacterial fimbrial epitopes interacting with pattern recognition receptors. J. Biol. Chem. 280: 38902-38913.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38902-38913
    • Hajishengallis, G.1    Ratti, P.2    Harokopakis, E.3
  • 15
    • 1342302486 scopus 로고    scopus 로고
    • Fimbriated Porphyromonas gingivalis is more efficient than fimbria-deficient P. gingivalis in entering human dendritic cells in vitro and induces an inflammatory Th1 effector response
    • Jotwani, R., and C. W. Cutler. 2004. Fimbriated Porphyromonas gingivalis is more efficient than fimbria-deficient P. gingivalis in entering human dendritic cells in vitro and induces an inflammatory Th1 effector response. Infect. Immun. 72: 1725-1732.
    • (2004) Infect. Immun. , vol.72 , pp. 1725-1732
    • Jotwani, R.1    Cutler, C.W.2
  • 16
    • 33846805500 scopus 로고    scopus 로고
    • Differential activation of human gingival epithelial cells and monocytes by Porphyromonas gingivalis fimbriae
    • Eskan, M. A., G. Hajishengallis, and D. F. Kinane. 2007. Differential activation of human gingival epithelial cells and monocytes by Porphyromonas gingivalis fimbriae. Infect. Immun. 75: 892-898.
    • (2007) Infect. Immun. , vol.75 , pp. 892-898
    • Eskan, M.A.1    Hajishengallis, G.2    Kinane, D.F.3
  • 20
    • 33744903384 scopus 로고    scopus 로고
    • TLR2 transmodulates monocyte adhesion and transmigration via Rac1- And PI3K-mediated inside-out signaling in response to Porphyromonas gingivalis fimbriae
    • Harokopakis, E., M. H. Albzreh, M. H. Martin, and G. Hajishengallis. 2006. TLR2 transmodulates monocyte adhesion and transmigration via Rac1- and PI3K-mediated inside-out signaling in response to Porphyromonas gingivalis fimbriae. J. Immunol. 176: 7645-7656. (Pubitemid 43849065)
    • (2006) Journal of Immunology , vol.176 , Issue.12 , pp. 7645-7656
    • Harokopakis, E.1    Albzreh, M.H.2    Martin, M.H.3    Hajishengallis, G.4
  • 21
    • 17444394875 scopus 로고    scopus 로고
    • Integrin activation by bacterial fimbriae through a pathway involving CD14, Toll-like receptor 2, and phosphatidylinositol- 3-kinase
    • Harokopakis, E., and G. Hajishengallis. 2005. Integrin activation by bacterial fimbriae through a pathway involving CD14, Toll-like receptor 2, and phosphatidylinositol- 3-kinase. Eur. J. Immunol. 35: 1201-1210.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 1201-1210
    • Harokopakis, E.1    Hajishengallis, G.2
  • 22
    • 12844278116 scopus 로고    scopus 로고
    • Oral mucosal endotoxin tolerance induction in chronic periodontitis
    • Muthukuru, M., R. Jotwani, and C. W. Cutler. 2005. Oral mucosal endotoxin tolerance induction in chronic periodontitis. Infect. Immun. 73: 687-694.
    • (2005) Infect. Immun. , vol.73 , pp. 687-694
    • Muthukuru, M.1    Jotwani, R.2    Cutler, C.W.3
  • 23
    • 28644452355 scopus 로고    scopus 로고
    • The expression profile of lipopolysaccharide-binding protein, membrane-bound CD14, and toll-like receptors 2 and 4 in chronic periodontitis
    • Ren, L., W. K. Leung, R. P. Darveau, and L. Jin. 2005. The expression profile of lipopolysaccharide-binding protein, membrane-bound CD14, and toll-like receptors 2 and 4 in chronic periodontitis. J. Periodontol. 76: 1950-1959.
    • (2005) J. Periodontol. , vol.76 , pp. 1950-1959
    • Ren, L.1    Leung, W.K.2    Darveau, R.P.3    Jin, L.4
  • 24
    • 0347511008 scopus 로고    scopus 로고
    • Macrophages, inflammation, and atherosclerosis
    • Linton, M. F., and S. Fazio. 2003 Macrophages, inflammation, and atherosclerosis. Int. J. Obes. Relat. Metab. Disord. 27 Suppl 3: S35-S40.
    • (2003) Int. J. Obes. Relat. Metab. Disord. , vol.27 , Issue.SUPPL. 3
    • Linton, M.F.1    Fazio, S.2
  • 25
    • 34848855747 scopus 로고    scopus 로고
    • Complement receptor 3 blockade promotes IL-12-mediated clearance of Porphyromonas gingivalis and negates its virulence in vivo
    • Hajishengallis, G., M.-A. K. Shakhatreh, M. Wang, and S. Liang. 2007. Complement receptor 3 blockade promotes IL-12-mediated clearance of Porphyromonas gingivalis and negates its virulence in vivo. J. Immunol. 179: 2359-2367.
    • (2007) J. Immunol. , vol.179 , pp. 2359-2367
    • Hajishengallis, G.1    Shakhatreh, M.-A.K.2    Wang, M.3    Liang, S.4
  • 26
    • 34848908962 scopus 로고    scopus 로고
    • Fimbrial proteins of Porphyromonas gingivalis mediate in vivo virulence and exploit TLR2 and complement receptor 3 to persist in macrophages
    • Wang, M., M.-A. K. Shakhatreh, D. James, S. Liang, S.-i. Nishiyama, F. Yoshimura, D. R. Demuth, and G. Hajishengallis. 2007. Fimbrial proteins of Porphyromonas gingivalis mediate in vivo virulence and exploit TLR2 and complement receptor 3 to persist in macrophages. J. Immunol. 179: 2349-2358.
    • (2007) J. Immunol. , vol.179 , pp. 2349-2358
    • Wang, M.1    Shakhatreh, M.-A.K.2    James, D.3    Liang, S.4    Nishiyama, S.-I.5    Yoshimura, F.6    Demuth, D.R.7    Hajishengallis, G.8
  • 27
    • 0021678531 scopus 로고
    • Purification and characterization of a novel type of fimbriae from the oral anaerobe Bacteroides gingivalis
    • Yoshimura, F., K. Takahashi, Y. Nodasaka, and T. Suzuki. 1984. Purification and characterization of a novel type of fimbriae from the oral anaerobe Bacteroides gingivalis. J. Bacteriol. 160: 949-957.
    • (1984) J. Bacteriol. , vol.160 , pp. 949-957
    • Yoshimura, F.1    Takahashi, K.2    Nodasaka, Y.3    Suzuki, T.4
  • 29
    • 0031913035 scopus 로고    scopus 로고
    • Cell activation mediated by glycosylphosphatidylinositol-anchored or transmembrane forms of CD14
    • Pugin, J., V. V. Kravchenko, J. D. Lee, L. Kline, R. J. Ulevitch, and P. S. Tobias. 1998. Cell activation mediated by glycosylphosphatidylinositol- anchored or transmembrane forms of CD14. Infect. Immun. 66: 1174-1180.
    • (1998) Infect. Immun. , vol.66 , pp. 1174-1180
    • Pugin, J.1    Kravchenko, V.V.2    Lee, J.D.3    Kline, L.4    Ulevitch, R.J.5    Tobias, P.S.6
  • 31
    • 18144362027 scopus 로고    scopus 로고
    • Peptide-mediated interference of TIR domain dimerization in MyD88 inhibits interleukin-1-dependent activation of NF-κB
    • Loiarro, M., C. Sette, G. Gallo, A. Ciacci, N. Fanto, D. Mastroianni, P. Carminati, and V. Ruggiero. 2005. Peptide-mediated interference of TIR domain dimerization in MyD88 inhibits interleukin-1-dependent activation of NF-κB. J. Biol. Chem. 280: 15809-15814.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15809-15814
    • Loiarro, M.1    Sette, C.2    Gallo, G.3    Ciacci, A.4    Fanto, N.5    Mastroianni, D.6    Carminati, P.7    Ruggiero, V.8
  • 33
    • 0035555301 scopus 로고    scopus 로고
    • TIRAP: An adapter molecule in the Toll signaling pathway
    • Horng, T., G. M. Barton, and R. Medzhitov. 2001. TIRAP: an adapter molecule in the Toll signaling pathway. Nat. Immunol. 2: 835-841.
    • (2001) Nat. Immunol. , vol.2 , pp. 835-841
    • Horng, T.1    Barton, G.M.2    Medzhitov, R.3
  • 34
    • 11144222174 scopus 로고    scopus 로고
    • Inhibition of Akt kinase activity by a peptide spanning the βA strand of the proto-oncogene TCL1
    • Hiromura, M., F. Okada, T. Obata, D. Auguin, T. Shibata, C. Roumestand, and M. Noguchi. 2004. Inhibition of Akt kinase activity by a peptide spanning the βA strand of the proto-oncogene TCL1. J. Biol. Chem. 279: 53407-53418.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53407-53418
    • Hiromura, M.1    Okada, F.2    Obata, T.3    Auguin, D.4    Shibata, T.5    Roumestand, C.6    Noguchi, M.7
  • 35
    • 0033534720 scopus 로고    scopus 로고
    • Monocyte adherence induced by lipopolysaccharide involves CD14, LFA-1, and cytohesin-1: Regulation by Rho and phosphatidylinositol 3-kinase
    • Hmama, Z., K. L. Knutson, P. Herrera-Velit, D. Nandan, and N. E. Reiner. 1999. Monocyte adherence induced by lipopolysaccharide involves CD14, LFA-1, and cytohesin-1: regulation by Rho and phosphatidylinositol 3-kinase. J. Biol. Chem. 274: 1050-1057.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1050-1057
    • Hmama, Z.1    Knutson, K.L.2    Herrera-Velit, P.3    Nandan, D.4    Reiner, N.E.5
  • 36
    • 15444365158 scopus 로고    scopus 로고
    • Cross-talk between CD14 and complement receptor 3 promotes phagocytosis of mycobacteria: Regulation by phosphatidylinositol 3-kinase and cytohesin-1
    • Sendide, K., N. E. Reiner, J. S. Lee, S. Bourgoin, A. Talal, and Z. Hmama. 2005. Cross-talk between CD14 and complement receptor 3 promotes phagocytosis of mycobacteria: regulation by phosphatidylinositol 3-kinase and cytohesin-1. J. Immunol. 174: 4210-4219. (Pubitemid 40396001)
    • (2005) Journal of Immunology , vol.174 , Issue.7 , pp. 4210-4219
    • Sendide, K.1    Reiner, N.E.2    Lee, J.S.I.3    Bourgoin, S.4    Talal, A.5    Hmama, Z.6
  • 37
    • 0027398448 scopus 로고
    • A subpopulation of Mac-1 (CD11b/ CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen
    • Diamond, M. S., and T. A. Springer. 1993. A subpopulation of Mac-1 (CD11b/ CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen. J. Cell Biol. 120: 545-556.
    • (1993) J. Cell Biol. , vol.120 , pp. 545-556
    • Diamond, M.S.1    Springer, T.A.2
  • 38
    • 0027530684 scopus 로고
    • The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands
    • Diamond, M. S., J. Garcia-Aguilar, J. K. Bickford, A. L. Corbi, and T. A. Springer. 1993. The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J. Cell Biol. 120: 1031-1043.
    • (1993) J. Cell Biol. , vol.120 , pp. 1031-1043
    • Diamond, M.S.1    Garcia-Aguilar, J.2    Bickford, J.K.3    Corbi, A.L.4    Springer, T.A.5
  • 39
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S., and K. Takeda. 2004. Toll-like receptor signalling. Nat. Rev. Immunol. 4: 499-511.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 42
    • 33646908228 scopus 로고    scopus 로고
    • Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling
    • Kagan, J. C., and R. Medzhitov. 2006. Phosphoinositide-mediated adaptor recruitment controls Toll-like receptor signaling. Cell 125: 943-955.
    • (2006) Cell , vol.125 , pp. 943-955
    • Kagan, J.C.1    Medzhitov, R.2
  • 44
    • 0345991221 scopus 로고    scopus 로고
    • TIR-containing adapter molecule (TICAM)-2, a bridging adapter recruiting to toll-like receptor 4 TICAM-1 that induces interferon-β
    • Oshiumi, H., M. Sasai, K. Shida, T. Fujita, M. Matsumoto, and T. Seya. 2003. TIR-containing adapter molecule (TICAM)-2, a bridging adapter recruiting to toll-like receptor 4 TICAM-1 that induces interferon-β. J. Biol. Chem. 278: 49751-49762.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49751-49762
    • Oshiumi, H.1    Sasai, M.2    Shida, K.3    Fujita, T.4    Matsumoto, M.5    Seya, T.6
  • 45
    • 0242624622 scopus 로고    scopus 로고
    • TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway
    • DOI 10.1038/ni986
    • Yamamoto, M., S. Sato, H. Hemmi, S. Uematsu, K. Hoshino, T. Kaisho, O. Takeuchi, K. Takeda, and S. Akira. 2003. TRAM is specifically involved in the Toll-like receptor 4-mediated MyD88-independent signaling pathway. Nat. Immunol. 4: 1144-1150. (Pubitemid 37428043)
    • (2003) Nature Immunology , vol.4 , Issue.11 , pp. 1144-1150
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3    Uematsu, S.4    Hoshino, K.5    Kaisho, T.6    Takeuchi, O.7    Takeda, K.8    Akira, S.9
  • 46
    • 38349188189 scopus 로고    scopus 로고
    • The role of Akt in the signaling pathway of the glycoprotein Ib-IX induced platelet activation
    • Yin, H., A. Stojanovic, N. Hay, and X. Du. 2008. The role of Akt in the signaling pathway of the glycoprotein Ib-IX induced platelet activation. Blood 111: 658-665.
    • (2008) Blood , vol.111 , pp. 658-665
    • Yin, H.1    Stojanovic, A.2    Hay, N.3    Du, X.4
  • 47
    • 0033604585 scopus 로고    scopus 로고
    • The regulation and activities of the multifunctional serine/threonine kinase Akt/PKB
    • Kandel, E. S., and N. Hay. 1999. The regulation and activities of the multifunctional serine/threonine kinase Akt/PKB. Exp. Cell Res. 253: 210-229.
    • (1999) Exp. Cell Res. , vol.253 , pp. 210-229
    • Kandel, E.S.1    Hay, N.2
  • 49
    • 0034122721 scopus 로고    scopus 로고
    • CR3: A general purpose adhesion-recognition receptor essential for innate immunity
    • Ehlers, M. R. W. 2000. CR3: a general purpose adhesion-recognition receptor essential for innate immunity. Microbes Infect. 2: 289-294.
    • (2000) Microbes Infect. , vol.2 , pp. 289-294
    • Ehlers, M.R.W.1
  • 50
    • 34247154495 scopus 로고    scopus 로고
    • Peptidoglycan increases firm adhesion of monocytes under flow conditions and primes monocyte chemotaxis
    • Nijhuis, M. M., G. Pasterkamp, N. I. Sluis, D. P. de Kleijn, J. D. Laman, and L. H. Ulfman. 2007. Peptidoglycan increases firm adhesion of monocytes under flow conditions and primes monocyte chemotaxis. J. Vasc. Res. 44: 214-222.
    • (2007) J. Vasc. Res. , vol.44 , pp. 214-222
    • Nijhuis, M.M.1    Pasterkamp, G.2    Sluis, N.I.3    De Kleijn, D.P.4    Laman, J.D.5    Ulfman, L.H.6
  • 52
    • 0035159327 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced activation of β2-integrin function in macrophages requires Irak kinase activity, p38 mitogen- Activated protein kinase, and the Rap1 GTPase
    • Schmidt, A., E. Caron, and A. Hall. 2001. Lipopolysaccharide-induced activation of β2-integrin function in macrophages requires Irak kinase activity, p38 mitogen- activated protein kinase, and the Rap1 GTPase. Mol. Cell Biol. 21: 438-448.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 438-448
    • Schmidt, A.1    Caron, E.2    Hall, A.3
  • 53
  • 54
    • 0035813130 scopus 로고    scopus 로고
    • Actin cytoskeletal association of cytohesin-1 is regulated by specific phosphorylation of its carboxyl-terminal polybasic domain
    • Dierks, H., J. Kolanus, and W. Kolanus. 2001. Actin cytoskeletal association of cytohesin-1 is regulated by specific phosphorylation of its carboxyl-terminal polybasic domain. J. Biol. Chem. 276: 37472-37481.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37472-37481
    • Dierks, H.1    Kolanus, J.2    Kolanus, W.3
  • 57
    • 0037180771 scopus 로고    scopus 로고
    • Inflammation in atherosclerosis
    • Libby, P. 2002. Inflammation in atherosclerosis. Nature 420: 868-874.
    • (2002) Nature , vol.420 , pp. 868-874
    • Libby, P.1
  • 58
    • 0032037616 scopus 로고    scopus 로고
    • Macrophage receptors for Mycobacterium tuberculosis
    • Ernst, J. D. 1998. Macrophage receptors for Mycobacterium tuberculosis. Infect. Immun. 66: 1277-1281.
    • (1998) Infect. Immun. , vol.66 , pp. 1277-1281
    • Ernst, J.D.1
  • 60
    • 0141533034 scopus 로고    scopus 로고
    • Roles of Rho-family GTPases in cell polarisation and directional migration
    • Fukata, M., M. Nakagawa, and K. Kaibuchi. 2003. Roles of Rho-family GTPases in cell polarisation and directional migration. Curr. Opin. Cell Biol. 15: 590-597.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 590-597
    • Fukata, M.1    Nakagawa, M.2    Kaibuchi, K.3
  • 61
    • 0037374815 scopus 로고    scopus 로고
    • The role of PI3K in immune cells
    • Koyasu, S. 2003. The role of PI3K in immune cells. Nat. Immunol. 4: 313-319.
    • (2003) Nat. Immunol. , vol.4 , pp. 313-319
    • Koyasu, S.1


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