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Volumn 9, Issue 1, 2013, Pages

Erratum: Fine Tuning Inflammation at the Front Door: Macrophage Complement Receptor 3-mediates Phagocytosis and Immune Suppression for Francisella tularensis (PLoS Pathogens (2013) 9:1 (e1003114) DOI: 10.1371/journal.ppat.1003114);Fine Tuning Inflammation at the Front Door: Macrophage Complement Receptor 3-mediates Phagocytosis and Immune Suppression for Francisella tularensis

Author keywords

[No Author keywords available]

Indexed keywords

CD11B ANTIGEN; COMPLEMENT COMPONENT C3 RECEPTOR; GENTAMICIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; INTERLEUKIN 6; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; MYELOID DIFFERENTIATION FACTOR 88; PROTEIN KINASE B; PROTEIN KINASE LYN; SMALL INTERFERING RNA; TOLL LIKE RECEPTOR 2; TUMOR NECROSIS FACTOR ALPHA;

EID: 84875066771     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005504     Document Type: Erratum
Times cited : (71)

References (95)
  • 5
    • 77955595585 scopus 로고    scopus 로고
    • Objections to the transfer of Francisella novicida to the subspecies rank of Francisella tularensis
    • Johansson A, Celli J, Conlan W, Elkins KL, Forsman M, et al. (2010) Objections to the transfer of Francisella novicida to the subspecies rank of Francisella tularensis. Int J Syst Evol Microbiol 60: 1717-1718.
    • (2010) Int J Syst Evol Microbiol , vol.60 , pp. 1717-1718
    • Johansson, A.1    Celli, J.2    Conlan, W.3    Elkins, K.L.4    Forsman, M.5
  • 6
    • 57349174394 scopus 로고    scopus 로고
    • Infected-host-cell repertoire and cellular response in the lung following inhalation of Francisella tularensis Schu S4, LVS, or U112
    • Hall JD, Woolard MD, Gunn BM, Craven RR, Taft-Benz S, et al. (2008) Infected-host-cell repertoire and cellular response in the lung following inhalation of Francisella tularensis Schu S4, LVS, or U112. Infect Immun 76: 5843-5852.
    • (2008) Infect Immun , vol.76 , pp. 5843-5852
    • Hall, J.D.1    Woolard, M.D.2    Gunn, B.M.3    Craven, R.R.4    Taft-Benz, S.5
  • 7
    • 26844452231 scopus 로고    scopus 로고
    • Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis
    • Mariathasan S, Weiss DS, Dixit VM, Monack DM, (2005) Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J Exp Med 202: 1043-1049.
    • (2005) J Exp Med , vol.202 , pp. 1043-1049
    • Mariathasan, S.1    Weiss, D.S.2    Dixit, V.M.3    Monack, D.M.4
  • 9
    • 33646472970 scopus 로고    scopus 로고
    • Myeloid differentiation factor-88 (MyD88) is essential for control of primary in vivo Francisella tularensis LVS infection, but not for control of intra-macrophage bacterial replication
    • Collazo CM, Sher A, Meierovics AI, Elkins KL, (2006) Myeloid differentiation factor-88 (MyD88) is essential for control of primary in vivo Francisella tularensis LVS infection, but not for control of intra-macrophage bacterial replication. Microbes Infect 8: 779-790.
    • (2006) Microbes Infect , vol.8 , pp. 779-790
    • Collazo, C.M.1    Sher, A.2    Meierovics, A.I.3    Elkins, K.L.4
  • 10
    • 0029879149 scopus 로고    scopus 로고
    • Cytokine expression in the liver of mice infected with a highly virulent strain of Francisella tularensis
    • Golovliov I, Kuoppa K, Sjostedt A, Tarnvik A, Sandstrom G, (1996) Cytokine expression in the liver of mice infected with a highly virulent strain of Francisella tularensis. FEMS Immunol Med Microbiol 13: 239-244.
    • (1996) FEMS Immunol Med Microbiol , vol.13 , pp. 239-244
    • Golovliov, I.1    Kuoppa, K.2    Sjostedt, A.3    Tarnvik, A.4    Sandstrom, G.5
  • 11
  • 12
    • 0033002661 scopus 로고    scopus 로고
    • Rapid local expression of interleukin-12, tumor necrosis factor alpha, and gamma interferon after cutaneous Francisella tularensis infection in tularemia-immune mice
    • Stenmark S, Sunnemark D, Bucht A, Sjostedt A, (1999) Rapid local expression of interleukin-12, tumor necrosis factor alpha, and gamma interferon after cutaneous Francisella tularensis infection in tularemia-immune mice. Infect Immun 67: 1789-1797.
    • (1999) Infect Immun , vol.67 , pp. 1789-1797
    • Stenmark, S.1    Sunnemark, D.2    Bucht, A.3    Sjostedt, A.4
  • 13
    • 27744547036 scopus 로고    scopus 로고
    • Francisella tularensis induces aberrant activation of pulmonary dendritic cells
    • Bosio CM, Dow SW, (2005) Francisella tularensis induces aberrant activation of pulmonary dendritic cells. J Immunol 175: 6792-6801.
    • (2005) J Immunol , vol.175 , pp. 6792-6801
    • Bosio, C.M.1    Dow, S.W.2
  • 14
    • 0037243609 scopus 로고    scopus 로고
    • Francisella tularensis inhibits Toll-like receptor-mediated activation of intracellular signalling and secretion of TNF-alpha and IL-1 from murine macrophages
    • Telepnev M, Golovliov I, Grundstrom T, Tarnvik A, Sjostedt A, (2003) Francisella tularensis inhibits Toll-like receptor-mediated activation of intracellular signalling and secretion of TNF-alpha and IL-1 from murine macrophages. Cell Microbiol 5: 41-51.
    • (2003) Cell Microbiol , vol.5 , pp. 41-51
    • Telepnev, M.1    Golovliov, I.2    Grundstrom, T.3    Tarnvik, A.4    Sjostedt, A.5
  • 15
    • 19544395035 scopus 로고    scopus 로고
    • Francisella tularensis LVS initially activates but subsequently down-regulates intracellular signaling and cytokine secretion in mouse monocytic and human peripheral blood mononuclear cells
    • Telepnev M, Golovliov I, Sjostedt A, (2005) Francisella tularensis LVS initially activates but subsequently down-regulates intracellular signaling and cytokine secretion in mouse monocytic and human peripheral blood mononuclear cells. Microb Pathog 38: 239-247.
    • (2005) Microb Pathog , vol.38 , pp. 239-247
    • Telepnev, M.1    Golovliov, I.2    Sjostedt, A.3
  • 16
    • 33947702199 scopus 로고    scopus 로고
    • Active suppression of the pulmonary immune response by Francisella tularensis Schu4
    • Bosio CM, Bielefeldt-Ohmann H, Belisle JT, (2007) Active suppression of the pulmonary immune response by Francisella tularensis Schu4. J Immunol 178: 4538-4547.
    • (2007) J Immunol , vol.178 , pp. 4538-4547
    • Bosio, C.M.1    Bielefeldt-Ohmann, H.2    Belisle, J.T.3
  • 17
    • 51449099913 scopus 로고    scopus 로고
    • Microarray analysis of human monocytes infected with Francisella tularensis identifies new targets of host response subversion
    • Butchar JP, Cremer TJ, Clay CD, Gavrilin MA, Wewers MD, et al. (2008) Microarray analysis of human monocytes infected with Francisella tularensis identifies new targets of host response subversion. PLoS One 3: e2924.
    • (2008) PLoS One , vol.3
    • Butchar, J.P.1    Cremer, T.J.2    Clay, C.D.3    Gavrilin, M.A.4    Wewers, M.D.5
  • 18
    • 84875064452 scopus 로고    scopus 로고
    • Francisella Subverts Innate Immune Signaling: Focus On PI3K/Akt
    • Cremer TJ, Butchar JP, Tridandapani S, (2011) Francisella Subverts Innate Immune Signaling: Focus On PI3K/Akt. Front Microbiol 5: 13.
    • (2011) Front Microbiol , vol.5 , pp. 13
    • Cremer, T.J.1    Butchar, J.P.2    Tridandapani, S.3
  • 19
    • 33748079800 scopus 로고    scopus 로고
    • Characterization of the receptor-ligand pathways important for entry and survival of Francisella tularensis in human macrophages
    • Balagopal A, MacFarlane AS, Mohapatra N, Soni S, Gunn JS, et al. (2006) Characterization of the receptor-ligand pathways important for entry and survival of Francisella tularensis in human macrophages. Infect Immun 74: 5114-5125.
    • (2006) Infect Immun , vol.74 , pp. 5114-5125
    • Balagopal, A.1    MacFarlane, A.S.2    Mohapatra, N.3    Soni, S.4    Gunn, J.S.5
  • 20
    • 33751501420 scopus 로고    scopus 로고
    • Differential infection of mononuclear phagocytes by Francisella tularensis: role of the macrophage mannose receptor
    • Schulert GS, Allen LA, (2006) Differential infection of mononuclear phagocytes by Francisella tularensis: role of the macrophage mannose receptor. J Leukoc Biol 80: 563-571.
    • (2006) J Leukoc Biol , vol.80 , pp. 563-571
    • Schulert, G.S.1    Allen, L.A.2
  • 21
    • 23944445646 scopus 로고    scopus 로고
    • Francisella tularensis enters macrophages via a novel process involving pseudopod loops
    • Clemens DL, Lee BY, Horwitz MA, (2005) Francisella tularensis enters macrophages via a novel process involving pseudopod loops. Infect Immun 73: 5892-5902.
    • (2005) Infect Immun , vol.73 , pp. 5892-5902
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 22
    • 79959484170 scopus 로고    scopus 로고
    • Phagocytic receptors dictate phagosomal escape and intracellular proliferation of Francisella tularensis
    • Geier H, Celli J, (2011) Phagocytic receptors dictate phagosomal escape and intracellular proliferation of Francisella tularensis. Infect Immun 79: 2204-2214.
    • (2011) Infect Immun , vol.79 , pp. 2204-2214
    • Geier, H.1    Celli, J.2
  • 23
    • 52649094980 scopus 로고    scopus 로고
    • A novel receptor - ligand pathway for entry of Francisella tularensis in monocyte-like THP-1 cells: interaction between surface nucleolin and bacterial elongation factor Tu
    • Barel M, Hovanessian AG, Meibom K, Briand JP, Dupuis M, et al. (2008) A novel receptor- ligand pathway for entry of Francisella tularensis in monocyte-like THP-1 cells: interaction between surface nucleolin and bacterial elongation factor Tu. BMC Microbiol 8: 145.
    • (2008) BMC Microbiol , vol.8 , pp. 145
    • Barel, M.1    Hovanessian, A.G.2    Meibom, K.3    Briand, J.P.4    Dupuis, M.5
  • 24
    • 33745762939 scopus 로고    scopus 로고
    • Uptake of serum-opsonized Francisella tularensis by macrophages can be mediated by class A scavenger receptors
    • Pierini LM, (2006) Uptake of serum-opsonized Francisella tularensis by macrophages can be mediated by class A scavenger receptors. Cell Microbiol 8: 1361-1370.
    • (2006) Cell Microbiol , vol.8 , pp. 1361-1370
    • Pierini, L.M.1
  • 25
    • 54049154653 scopus 로고    scopus 로고
    • Evasion of complement-mediated lysis and complement C3 deposition are regulated by Francisella tularensis lipopolysaccharide O antigen
    • Clay CD, Soni S, Gunn JS, Schlesinger LS, (2008) Evasion of complement-mediated lysis and complement C3 deposition are regulated by Francisella tularensis lipopolysaccharide O antigen. J Immunol 181: 5568-5578.
    • (2008) J Immunol , vol.181 , pp. 5568-5578
    • Clay, C.D.1    Soni, S.2    Gunn, J.S.3    Schlesinger, L.S.4
  • 26
    • 0021999634 scopus 로고
    • Ligated complement receptors do not activate the arachidonic acid cascade in resident peritoneal macrophages
    • Aderem AA, Wright SD, Silverstein SC, Cohn ZA, (1985) Ligated complement receptors do not activate the arachidonic acid cascade in resident peritoneal macrophages. J Exp Med 161: 617-622.
    • (1985) J Exp Med , vol.161 , pp. 617-622
    • Aderem, A.A.1    Wright, S.D.2    Silverstein, S.C.3    Cohn, Z.A.4
  • 27
    • 0021080912 scopus 로고
    • Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes
    • Wright SD, Silverstein SC, (1983) Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes. J Exp Med 158: 2016-2023.
    • (1983) J Exp Med , vol.158 , pp. 2016-2023
    • Wright, S.D.1    Silverstein, S.C.2
  • 28
    • 0025967507 scopus 로고
    • Regulation of tumor necrosis factor (TNF) release by murine peritoneal macrophages: role of cell stimulation and specific phagocytic plasma membrane receptors
    • Stein M, Gordon S, (1991) Regulation of tumor necrosis factor (TNF) release by murine peritoneal macrophages: role of cell stimulation and specific phagocytic plasma membrane receptors. Eur J Immunol 21: 431-437.
    • (1991) Eur J Immunol , vol.21 , pp. 431-437
    • Stein, M.1    Gordon, S.2
  • 29
    • 67650716492 scopus 로고    scopus 로고
    • The ins and outs of leukocyte integrin signaling
    • Abram CL, Lowell CA, (2009) The ins and outs of leukocyte integrin signaling. Annu Rev Immunol 27: 339-362.
    • (2009) Annu Rev Immunol , vol.27 , pp. 339-362
    • Abram, C.L.1    Lowell, C.A.2
  • 30
    • 77950187449 scopus 로고    scopus 로고
    • Crosstalk pathways between Toll-like receptors and the complement system
    • Hajishengallis G, Lambris JD, (2010) Crosstalk pathways between Toll-like receptors and the complement system. Trends Immunol 31: 154-163.
    • (2010) Trends Immunol , vol.31 , pp. 154-163
    • Hajishengallis, G.1    Lambris, J.D.2
  • 31
    • 79952123931 scopus 로고    scopus 로고
    • Microbial manipulation of receptor crosstalk in innate immunity
    • Hajishengallis G, Lambris JD, (2011) Microbial manipulation of receptor crosstalk in innate immunity. Nat Rev Immunol 11: 187-200.
    • (2011) Nat Rev Immunol , vol.11 , pp. 187-200
    • Hajishengallis, G.1    Lambris, J.D.2
  • 32
    • 62849123774 scopus 로고    scopus 로고
    • Cross-regulation of signaling by ITAM-associated receptors
    • Ivashkiv LB, (2009) Cross-regulation of signaling by ITAM-associated receptors. Nat Immunol 10: 340-347.
    • (2009) Nat Immunol , vol.10 , pp. 340-347
    • Ivashkiv, L.B.1
  • 33
    • 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, Hajishengallis G, (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
  • 34
    • 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, Reiner NE, Lee JS, Bourgoin S, Talal A, et al. (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.
    • (2005) J Immunol , vol.174 , pp. 4210-4219
    • Sendide, K.1    Reiner, N.E.2    Lee, J.S.3    Bourgoin, S.4    Talal, A.5
  • 35
    • 77951892594 scopus 로고    scopus 로고
    • Indirect inhibition of Toll-like receptor and type I interferon responses by ITAM-coupled receptors and integrins
    • Wang L, Gordon RA, Huynh L, Su X, Park Min KH, et al. (2010) Indirect inhibition of Toll-like receptor and type I interferon responses by ITAM-coupled receptors and integrins. Immunity 32: 518-530.
    • (2010) Immunity , vol.32 , pp. 518-530
    • Wang, L.1    Gordon, R.A.2    Huynh, L.3    Su, X.4    Park Min, K.H.5
  • 36
    • 77954946392 scopus 로고    scopus 로고
    • Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b
    • Han C, Jin J, Xu S, Liu H, Li N, et al. (2010) Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b. Nat Immunol 11: 734-742.
    • (2010) Nat Immunol , vol.11 , pp. 734-742
    • Han, C.1    Jin, J.2    Xu, S.3    Liu, H.4    Li, N.5
  • 37
    • 0030980385 scopus 로고    scopus 로고
    • Regulation of interleukin-12 by complement receptor 3 signaling
    • Marth T, Kelsall BL, (1997) Regulation of interleukin-12 by complement receptor 3 signaling. J Exp Med 185: 1987-1995.
    • (1997) J Exp Med , vol.185 , pp. 1987-1995
    • Marth, T.1    Kelsall, B.L.2
  • 38
    • 25444513110 scopus 로고    scopus 로고
    • Immunological consequences of macrophage-mediated clearance of apoptotic cells
    • Kim S, Chung EY, Ma X, (2005) Immunological consequences of macrophage-mediated clearance of apoptotic cells. Cell Cycle 4: 231-234.
    • (2005) Cell Cycle , vol.4 , pp. 231-234
    • Kim, S.1    Chung, E.Y.2    Ma, X.3
  • 39
    • 8444251663 scopus 로고    scopus 로고
    • Transcriptional suppression of interleukin-12 gene expression following phagocytosis of apoptotic cells
    • Kim S, Elkon KB, Ma X, (2004) Transcriptional suppression of interleukin-12 gene expression following phagocytosis of apoptotic cells. Immunity 21: 643-653.
    • (2004) Immunity , vol.21 , pp. 643-653
    • Kim, S.1    Elkon, K.B.2    Ma, X.3
  • 40
    • 69549098037 scopus 로고    scopus 로고
    • CD14-Mac-1 interactions in Bacillus anthracis spore internalization by macrophages
    • Oliva C, Turnbough CL Jr, Kearney JF, (2009) CD14-Mac-1 interactions in Bacillus anthracis spore internalization by macrophages. Proc Natl Acad Sci U S A 106: 13957-13962.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13957-13962
    • Oliva, C.1    Turnbough Jr., C.L.2    Kearney, J.F.3
  • 41
    • 77949500446 scopus 로고    scopus 로고
    • MiR-155 induction by F. novicida but not the virulent F. tularensis results in SHIP down-regulation and enhanced pro-inflammatory cytokine response
    • Cremer TJ, Ravneberg DH, Clay CD, Piper-Hunter MG, Marsh CB, et al. (2009) MiR-155 induction by F. novicida but not the virulent F. tularensis results in SHIP down-regulation and enhanced pro-inflammatory cytokine response. PLoS One 4: e8508.
    • (2009) PLoS One , vol.4
    • Cremer, T.J.1    Ravneberg, D.H.2    Clay, C.D.3    Piper-Hunter, M.G.4    Marsh, C.B.5
  • 42
    • 79960675331 scopus 로고    scopus 로고
    • Host-adaptation of Francisella tularensis alters the bacterium's surface-carbohydrates to hinder effectors of innate and adaptive immunity
    • Zarrella TM, Singh A, Bitsaktsis C, Rahman T, Sahay B, et al. (2011) Host-adaptation of Francisella tularensis alters the bacterium's surface-carbohydrates to hinder effectors of innate and adaptive immunity. PLoS One 6: e22335.
    • (2011) PLoS One , vol.6
    • Zarrella, T.M.1    Singh, A.2    Bitsaktsis, C.3    Rahman, T.4    Sahay, B.5
  • 43
    • 34748816297 scopus 로고    scopus 로고
    • The structure and function of Francisella lipopolysaccharide
    • Gunn JS, Ernst RK, (2007) The structure and function of Francisella lipopolysaccharide. Ann N Y Acad Sci 1105: 202-218.
    • (2007) Ann N Y Acad Sci , vol.1105 , pp. 202-218
    • Gunn, J.S.1    Ernst, R.K.2
  • 44
    • 34547636340 scopus 로고    scopus 로고
    • Toll-like receptor 2-mediated signaling requirements for Francisella tularensis live vaccine strain infection of murine macrophages
    • Cole LE, Shirey KA, Barry E, Santiago A, Rallabhandi P, et al. (2007) Toll-like receptor 2-mediated signaling requirements for Francisella tularensis live vaccine strain infection of murine macrophages. Infect Immun 75: 4127-4137.
    • (2007) Infect Immun , vol.75 , pp. 4127-4137
    • Cole, L.E.1    Shirey, K.A.2    Barry, E.3    Santiago, A.4    Rallabhandi, P.5
  • 45
    • 35648963645 scopus 로고    scopus 로고
    • Toll-like receptor 2 controls the gamma interferon response to Francisella tularensis by mouse liver lymphocytes
    • Hong KJ, Wickstrum JR, Yeh HW, Parmely MJ, (2007) Toll-like receptor 2 controls the gamma interferon response to Francisella tularensis by mouse liver lymphocytes. Infect Immun 75: 5338-5345.
    • (2007) Infect Immun , vol.75 , pp. 5338-5345
    • Hong, K.J.1    Wickstrum, J.R.2    Yeh, H.W.3    Parmely, M.J.4
  • 46
    • 79959221587 scopus 로고    scopus 로고
    • TLR2 Signaling Contributes to Rapid Inflammasome Activation during F. novicida Infection
    • Jones CL, Weiss DS, (2011) TLR2 Signaling Contributes to Rapid Inflammasome Activation during F. novicida Infection. PLoS One 6: e20609.
    • (2011) PLoS One , vol.6
    • Jones, C.L.1    Weiss, D.S.2
  • 47
    • 33646357470 scopus 로고    scopus 로고
    • Toll-like receptor 2 is required for inflammatory responses to Francisella tularensis LVS
    • Katz J, Zhang P, Martin M, Vogel SN, Michalek SM, (2006) Toll-like receptor 2 is required for inflammatory responses to Francisella tularensis LVS. Infect Immun 74: 2809-2816.
    • (2006) Infect Immun , vol.74 , pp. 2809-2816
    • Katz, J.1    Zhang, P.2    Martin, M.3    Vogel, S.N.4    Michalek, S.M.5
  • 48
    • 33646911624 scopus 로고    scopus 로고
    • Toll-like receptor 2 is required for control of pulmonary infection with Francisella tularensis
    • Malik M, Bakshi CS, Sahay B, Shah A, Lotz SA, et al. (2006) Toll-like receptor 2 is required for control of pulmonary infection with Francisella tularensis. Infect Immun 74: 3657-3662.
    • (2006) Infect Immun , vol.74 , pp. 3657-3662
    • Malik, M.1    Bakshi, C.S.2    Sahay, B.3    Shah, A.4    Lotz, S.A.5
  • 49
    • 70949098358 scopus 로고    scopus 로고
    • TLR-dependent control of Francisella tularensis infection and host inflammatory responses
    • Abplanalp AL, Morris IR, Parida BK, Teale JM, Berton MT, (2009) TLR-dependent control of Francisella tularensis infection and host inflammatory responses. PLoS One 4: e7920.
    • (2009) PLoS One , vol.4
    • Abplanalp, A.L.1    Morris, I.R.2    Parida, B.K.3    Teale, J.M.4    Berton, M.T.5
  • 50
    • 0030448437 scopus 로고    scopus 로고
    • Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses
    • Chen LM, Hobbie S, Galan JE, (1996) Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses. Science 274: 2115-2118.
    • (1996) Science , vol.274 , pp. 2115-2118
    • Chen, L.M.1    Hobbie, S.2    Galan, J.E.3
  • 51
    • 76149116836 scopus 로고    scopus 로고
    • Phagosomal retention of Francisella tularensis results in TIRAP/Mal-independent TLR2 signaling
    • Cole LE, Laird MH, Seekatz A, Santiago A, Jiang Z, et al. (2010) Phagosomal retention of Francisella tularensis results in TIRAP/Mal-independent TLR2 signaling. J Leukoc Biol 87: 275-281.
    • (2010) J Leukoc Biol , vol.87 , pp. 275-281
    • Cole, L.E.1    Laird, M.H.2    Seekatz, A.3    Santiago, A.4    Jiang, Z.5
  • 52
    • 78149489515 scopus 로고    scopus 로고
    • Deletion of ripA alleviates suppression of the inflammasome and MAPK by Francisella tularensis
    • Huang MT, Mortensen BL, Taxman DJ, Craven RR, Taft-Benz S, et al. (2010) Deletion of ripA alleviates suppression of the inflammasome and MAPK by Francisella tularensis. J Immunol 185: 5476-5485.
    • (2010) J Immunol , vol.185 , pp. 5476-5485
    • Huang, M.T.1    Mortensen, B.L.2    Taxman, D.J.3    Craven, R.R.4    Taft-Benz, S.5
  • 53
    • 77955480359 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis activates human macrophage peroxisome proliferator-activated receptor gamma linking mannose receptor recognition to regulation of immune responses
    • Rajaram MV, Brooks MN, Morris JD, Torrelles JB, Azad AK, et al. (2010) Mycobacterium tuberculosis activates human macrophage peroxisome proliferator-activated receptor gamma linking mannose receptor recognition to regulation of immune responses. J Immunol 185: 929-942.
    • (2010) J Immunol , vol.185 , pp. 929-942
    • Rajaram, M.V.1    Brooks, M.N.2    Morris, J.D.3    Torrelles, J.B.4    Azad, A.K.5
  • 54
    • 79961038713 scopus 로고    scopus 로고
    • Multiscale simulations suggest a mechanism for integrin inside-out activation
    • Kalli AC, Campbell ID, Sansom MS, (2011) Multiscale simulations suggest a mechanism for integrin inside-out activation. Proc Natl Acad Sci U S A 108: 11890-11895.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 11890-11895
    • Kalli, A.C.1    Campbell, I.D.2    Sansom, M.S.3
  • 55
    • 0031183179 scopus 로고    scopus 로고
    • Outside-in signaling by lipopolysaccharide through a tailless integrin
    • Ingalls RR, Arnaout MA, Golenbock DT, (1997) Outside-in signaling by lipopolysaccharide through a tailless integrin. J Immunol 159: 433-438.
    • (1997) J Immunol , vol.159 , pp. 433-438
    • Ingalls, R.R.1    Arnaout, M.A.2    Golenbock, D.T.3
  • 56
    • 70350026642 scopus 로고    scopus 로고
    • A TIR domain variant of MyD88 adapter-like (Mal)/TIRAP results in loss of MyD88 binding and reduced TLR2/TLR4 signaling
    • Nagpal K, Plantinga TS, Wong J, Monks BG, Gay NJ, et al. (2009) A TIR domain variant of MyD88 adapter-like (Mal)/TIRAP results in loss of MyD88 binding and reduced TLR2/TLR4 signaling. J Biol Chem 284: 25742-25748.
    • (2009) J Biol Chem , vol.284 , pp. 25742-25748
    • Nagpal, K.1    Plantinga, T.S.2    Wong, J.3    Monks, B.G.4    Gay, N.J.5
  • 57
    • 42549107360 scopus 로고    scopus 로고
    • The diverse functions of Src family kinases in macrophages
    • Abram CL, Lowell CA, (2008) The diverse functions of Src family kinases in macrophages. Front Biosci 13: 4426-4450.
    • (2008) Front Biosci , vol.13 , pp. 4426-4450
    • Abram, C.L.1    Lowell, C.A.2
  • 58
    • 33746256896 scopus 로고    scopus 로고
    • Src kinase Lyn is crucial for Pseudomonas aeruginosa internalization into lung cells
    • Kannan S, Audet A, Knittel J, Mullegama S, Gao GF, et al. (2006) Src kinase Lyn is crucial for Pseudomonas aeruginosa internalization into lung cells. Eur J Immunol 36: 1739-1752.
    • (2006) Eur J Immunol , vol.36 , pp. 1739-1752
    • Kannan, S.1    Audet, A.2    Knittel, J.3    Mullegama, S.4    Gao, G.F.5
  • 59
    • 77954709866 scopus 로고    scopus 로고
    • Activation of murine macrophages via TLR2 and TLR4 is negatively regulated by a Lyn/PI3K module and promoted by SHIP1
    • Keck S, Freudenberg M, Huber M, (2010) Activation of murine macrophages via TLR2 and TLR4 is negatively regulated by a Lyn/PI3K module and promoted by SHIP1. J Immunol 184: 5809-5818.
    • (2010) J Immunol , vol.184 , pp. 5809-5818
    • Keck, S.1    Freudenberg, M.2    Huber, M.3
  • 60
    • 9144223047 scopus 로고    scopus 로고
    • Short interfering RNA (siRNA) targeting the Lyn kinase induces apoptosis in primary, and drug-resistant, BCR-ABL1(+) leukemia cells
    • Ptasznik A, Nakata Y, Kalota A, Emerson SG, Gewirtz AM, (2004) Short interfering RNA (siRNA) targeting the Lyn kinase induces apoptosis in primary, and drug-resistant, BCR-ABL1(+) leukemia cells. Nat Med 10: 1187-1189.
    • (2004) Nat Med , vol.10 , pp. 1187-1189
    • Ptasznik, A.1    Nakata, Y.2    Kalota, A.3    Emerson, S.G.4    Gewirtz, A.M.5
  • 61
    • 33746592575 scopus 로고    scopus 로고
    • Macrophage pro-inflammatory response to Francisella novicida infection is regulated by SHIP
    • Parsa KV, Ganesan LP, Rajaram MV, Gavrilin MA, Balagopal A, et al. (2006) Macrophage pro-inflammatory response to Francisella novicida infection is regulated by SHIP. PLoS Pathog 2: e71.
    • (2006) PLoS Pathog , vol.2
    • Parsa, K.V.1    Ganesan, L.P.2    Rajaram, M.V.3    Gavrilin, M.A.4    Balagopal, A.5
  • 62
    • 78650642949 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase activation attenuates the TLR2-mediated macrophage proinflammatory cytokine response to Francisella tularensis live vaccine strain
    • Medina EA, Morris IR, Berton MT, (2010) Phosphatidylinositol 3-kinase activation attenuates the TLR2-mediated macrophage proinflammatory cytokine response to Francisella tularensis live vaccine strain. J Immunol 185: 7562-7572.
    • (2010) J Immunol , vol.185 , pp. 7562-7572
    • Medina, E.A.1    Morris, I.R.2    Berton, M.T.3
  • 63
    • 0033553494 scopus 로고    scopus 로고
    • Nitric oxide inhibits thrombin receptor-activating peptide-induced phosphoinositide 3-kinase activity in human platelets
    • Pigazzi A, Heydrick S, Folli F, Benoit S, Michelson A, et al. (1999) Nitric oxide inhibits thrombin receptor-activating peptide-induced phosphoinositide 3-kinase activity in human platelets. J Biol Chem 274: 14368-14375.
    • (1999) J Biol Chem , vol.274 , pp. 14368-14375
    • Pigazzi, A.1    Heydrick, S.2    Folli, F.3    Benoit, S.4    Michelson, A.5
  • 64
    • 42149147975 scopus 로고    scopus 로고
    • Cholesterol-rich membrane rafts and Lyn are involved in phagocytosis during Pseudomonas aeruginosa infection
    • Kannan S, Audet A, Huang H, Chen LJ, Wu M, (2008) Cholesterol-rich membrane rafts and Lyn are involved in phagocytosis during Pseudomonas aeruginosa infection. J Immunol 180: 2396-2408.
    • (2008) J Immunol , vol.180 , pp. 2396-2408
    • Kannan, S.1    Audet, A.2    Huang, H.3    Chen, L.J.4    Wu, M.5
  • 65
    • 0034577944 scopus 로고    scopus 로고
    • Toll-like receptor 2-mediated NF-kappa B activation requires a Rac1-dependent pathway
    • Arbibe L, Mira JP, Teusch N, Kline L, Guha M, et al. (2000) Toll-like receptor 2-mediated NF-kappa B activation requires a Rac1-dependent pathway. Nat Immunol 1: 533-540.
    • (2000) Nat Immunol , vol.1 , pp. 533-540
    • Arbibe, L.1    Mira, J.P.2    Teusch, N.3    Kline, L.4    Guha, M.5
  • 66
    • 33847176551 scopus 로고    scopus 로고
    • MAPK phosphatases-regulating the immune response
    • Liu Y, Shepherd EG, Nelin LD, (2007) MAPK phosphatases-regulating the immune response. Nat Rev Immunol 7: 202-212.
    • (2007) Nat Rev Immunol , vol.7 , pp. 202-212
    • Liu, Y.1    Shepherd, E.G.2    Nelin, L.D.3
  • 67
    • 0026474423 scopus 로고
    • Rapid generation of specific protective immunity to Francisella tularensis
    • Elkins KL, Leiby DA, Winegar RK, Nacy CA, Fortier AH, (1992) Rapid generation of specific protective immunity to Francisella tularensis. Infect Immun 60: 4571-4577.
    • (1992) Infect Immun , vol.60 , pp. 4571-4577
    • Elkins, K.L.1    Leiby, D.A.2    Winegar, R.K.3    Nacy, C.A.4    Fortier, A.H.5
  • 68
    • 27844536449 scopus 로고    scopus 로고
    • Low dose aerosol infection of mice with virulent type A Francisella tularensis induces severe thymus atrophy and CD4+CD8+ thymocyte depletion
    • Chen W, Kuolee R, Austin JW, Shen H, Che Y, et al. (2005) Low dose aerosol infection of mice with virulent type A Francisella tularensis induces severe thymus atrophy and CD4+CD8+ thymocyte depletion. Microb Pathog 39: 189-196.
    • (2005) Microb Pathog , vol.39 , pp. 189-196
    • Chen, W.1    Kuolee, R.2    Austin, J.W.3    Shen, H.4    Che, Y.5
  • 69
    • 46449088249 scopus 로고    scopus 로고
    • Initial delay in the immune response to Francisella tularensis is followed by hypercytokinemia characteristic of severe sepsis and correlating with upregulation and release of damage-associated molecular patterns
    • Mares CA, Ojeda SS, Morris EG, Li Q, Teale JM, (2008) Initial delay in the immune response to Francisella tularensis is followed by hypercytokinemia characteristic of severe sepsis and correlating with upregulation and release of damage-associated molecular patterns. Infect Immun 76: 3001-3010.
    • (2008) Infect Immun , vol.76 , pp. 3001-3010
    • Mares, C.A.1    Ojeda, S.S.2    Morris, E.G.3    Li, Q.4    Teale, J.M.5
  • 70
    • 58449133177 scopus 로고    scopus 로고
    • Direct and indirect impairment of human dendritic cell function by virulent Francisella tularensis Schu S4
    • Chase JC, Celli J, Bosio CM, (2009) Direct and indirect impairment of human dendritic cell function by virulent Francisella tularensis Schu S4. Infect Immun 77: 180-195.
    • (2009) Infect Immun , vol.77 , pp. 180-195
    • Chase, J.C.1    Celli, J.2    Bosio, C.M.3
  • 71
    • 46949096670 scopus 로고    scopus 로고
    • Subversion of complement activation at the bacterial surface promotes serum resistance and opsonophagocytosis of Francisella tularensis
    • Ben Nasr A, Klimpel GR, (2008) Subversion of complement activation at the bacterial surface promotes serum resistance and opsonophagocytosis of Francisella tularensis. J Leukoc Biol 84: 77-85.
    • (2008) J Leukoc Biol , vol.84 , pp. 77-85
    • Ben Nasr, A.1    Klimpel, G.R.2
  • 72
    • 84870688032 scopus 로고    scopus 로고
    • A Mathematical Model of CR3/TLR2 Crosstalk in the Context of Francisella tularensis Infection
    • Leander R, Dai S, Schlesinger LS, Friedman A, (2012) A Mathematical Model of CR3/TLR2 Crosstalk in the Context of Francisella tularensis Infection. PLoS Comput Biol 8: e1002757.
    • (2012) PLoS Comput Biol , vol.8
    • Leander, R.1    Dai, S.2    Schlesinger, L.S.3    Friedman, A.4
  • 73
    • 0038446051 scopus 로고    scopus 로고
    • Role of the phosphatidylinositol 3 kinase-Akt pathway in the regulation of IL-10 and IL-12 by Porphyromonas gingivalis lipopolysaccharide
    • Martin M, Schifferle RE, Cuesta N, Vogel SN, Katz J, et al. (2003) Role of the phosphatidylinositol 3 kinase-Akt pathway in the regulation of IL-10 and IL-12 by Porphyromonas gingivalis lipopolysaccharide. J Immunol 171: 717-725.
    • (2003) J Immunol , vol.171 , pp. 717-725
    • Martin, M.1    Schifferle, R.E.2    Cuesta, N.3    Vogel, S.N.4    Katz, J.5
  • 74
    • 0037199972 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase-Akt pathway limits lipopolysaccharide activation of signaling pathways and expression of inflammatory mediators in human monocytic cells
    • Guha M, Mackman N, (2002) The phosphatidylinositol 3-kinase-Akt pathway limits lipopolysaccharide activation of signaling pathways and expression of inflammatory mediators in human monocytic cells. J Biol Chem 277: 32124-32132.
    • (2002) J Biol Chem , vol.277 , pp. 32124-32132
    • Guha, M.1    Mackman, N.2
  • 75
    • 0037629646 scopus 로고    scopus 로고
    • PI3K and negative regulation of TLR signaling
    • Fukao T, Koyasu S, (2003) PI3K and negative regulation of TLR signaling. Trends Immunol 24: 358-363.
    • (2003) Trends Immunol , vol.24 , pp. 358-363
    • Fukao, T.1    Koyasu, S.2
  • 76
    • 55949119669 scopus 로고    scopus 로고
    • A role of macrophage complement receptor CRIg in immune clearance and inflammation
    • He JQ, Wiesmann C, van Lookeren Campagne M, (2008) A role of macrophage complement receptor CRIg in immune clearance and inflammation. Mol Immunol 45: 4041-4047.
    • (2008) Mol Immunol , vol.45 , pp. 4041-4047
    • He, J.Q.1    Wiesmann, C.2    van Lookeren Campagne, M.3
  • 77
    • 9144224761 scopus 로고    scopus 로고
    • Complement C1q regulates LPS-induced cytokine production in bone marrow-derived dendritic cells
    • Yamada M, Oritani K, Kaisho T, Ishikawa J, Yoshida H, et al. (2004) Complement C1q regulates LPS-induced cytokine production in bone marrow-derived dendritic cells. Eur J Immunol 34: 221-230.
    • (2004) Eur J Immunol , vol.34 , pp. 221-230
    • Yamada, M.1    Oritani, K.2    Kaisho, T.3    Ishikawa, J.4    Yoshida, H.5
  • 78
    • 34147187173 scopus 로고    scopus 로고
    • Generation of inhibitory NFkappaB complexes and phosphorylated cAMP response element-binding protein correlates with the anti-inflammatory activity of complement protein C1q in human monocytes
    • Fraser DA, Arora M, Bohlson SS, Lozano E, Tenner AJ, (2007) Generation of inhibitory NFkappaB complexes and phosphorylated cAMP response element-binding protein correlates with the anti-inflammatory activity of complement protein C1q in human monocytes. J Biol Chem 282: 7360-7367.
    • (2007) J Biol Chem , vol.282 , pp. 7360-7367
    • Fraser, D.A.1    Arora, M.2    Bohlson, S.S.3    Lozano, E.4    Tenner, A.J.5
  • 79
    • 33750429108 scopus 로고    scopus 로고
    • C1q and MBL, components of the innate immune system, influence monocyte cytokine expression
    • Fraser DA, Bohlson SS, Jasinskiene N, Rawal N, Palmarini G, et al. (2006) C1q and MBL, components of the innate immune system, influence monocyte cytokine expression. J Leukoc Biol 80: 107-116.
    • (2006) J Leukoc Biol , vol.80 , pp. 107-116
    • Fraser, D.A.1    Bohlson, S.S.2    Jasinskiene, N.3    Rawal, N.4    Palmarini, G.5
  • 80
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden CA, deCathelineau A, Hoffmann PR, Bratton D, Ghebrehiwet B, et al. (2001) C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J Exp Med 194: 781-795.
    • (2001) J Exp Med , vol.194 , pp. 781-795
    • Ogden, C.A.1    deCathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5
  • 81
    • 77950187399 scopus 로고    scopus 로고
    • Microbial hijacking of complement-toll-like receptor crosstalk
    • Wang M, Krauss JL, Domon H, Hosur KB, Liang S, et al. (2010) Microbial hijacking of complement-toll-like receptor crosstalk. Sci Signal 3: ra11.
    • (2010) Sci Signal , vol.3
    • Wang, M.1    Krauss, J.L.2    Domon, H.3    Hosur, K.B.4    Liang, S.5
  • 82
    • 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, Shakhatreh MA, Wang M, Liang S, (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.2    Wang, M.3    Liang, S.4
  • 83
    • 58149334966 scopus 로고    scopus 로고
    • Subversion of innate immunity by periodontopathic bacteria via exploitation of complement receptor-3
    • Hajishengallis G, Wang M, Liang S, Shakhatreh MA, James D, et al. (2008) Subversion of innate immunity by periodontopathic bacteria via exploitation of complement receptor-3. Adv Exp Med Biol 632: 203-219.
    • (2008) Adv Exp Med Biol , vol.632 , pp. 203-219
    • Hajishengallis, G.1    Wang, M.2    Liang, S.3    Shakhatreh, M.A.4    James, D.5
  • 84
    • 10344263399 scopus 로고    scopus 로고
    • Exploiting type 3 complement receptor for TNF-alpha suppression, immune evasion, and progressive pulmonary fungal infection
    • Brandhorst TT, Wuthrich M, Finkel-Jimenez B, Warner T, Klein BS, (2004) Exploiting type 3 complement receptor for TNF-alpha suppression, immune evasion, and progressive pulmonary fungal infection. J Immunol 173: 7444-7453.
    • (2004) J Immunol , vol.173 , pp. 7444-7453
    • Brandhorst, T.T.1    Wuthrich, M.2    Finkel-Jimenez, B.3    Warner, T.4    Klein, B.S.5
  • 85
    • 77955883153 scopus 로고    scopus 로고
    • Complement: a key system for immune surveillance and homeostasis
    • Ricklin D, Hajishengallis G, Yang K, Lambris JD, (2010) Complement: a key system for immune surveillance and homeostasis. Nat Immunol 11: 785-797.
    • (2010) Nat Immunol , vol.11 , pp. 785-797
    • Ricklin, D.1    Hajishengallis, G.2    Yang, K.3    Lambris, J.D.4
  • 86
    • 34248174388 scopus 로고    scopus 로고
    • Complement receptor 3 ligation of dendritic cells suppresses their stimulatory capacity
    • Behrens EM, Sriram U, Shivers DK, Gallucci M, Ma Z, et al. (2007) Complement receptor 3 ligation of dendritic cells suppresses their stimulatory capacity. J Immunol 178: 6268-6279.
    • (2007) J Immunol , vol.178 , pp. 6268-6279
    • Behrens, E.M.1    Sriram, U.2    Shivers, D.K.3    Gallucci, M.4    Ma, Z.5
  • 87
    • 16844382768 scopus 로고    scopus 로고
    • Inhibition of monocyte-derived dendritic cell differentiation and interleukin-12 production by complement iC3b via a mitogen-activated protein kinase signalling pathway
    • Luo X, Liu L, Tang N, Lu KQ, McCormick TS, et al. (2005) Inhibition of monocyte-derived dendritic cell differentiation and interleukin-12 production by complement iC3b via a mitogen-activated protein kinase signalling pathway. Exp Dermatol 14: 303-310.
    • (2005) Exp Dermatol , vol.14 , pp. 303-310
    • Luo, X.1    Liu, L.2    Tang, N.3    Lu, K.Q.4    McCormick, T.S.5
  • 88
    • 0025216480 scopus 로고
    • Phagocytosis of Mycobacterium tuberculosis is mediated by human monocyte complement receptors and complement component C3
    • Schlesinger LS, Bellinger-Kawahara CG, Payne NR, Horwitz MA, (1990) Phagocytosis of Mycobacterium tuberculosis is mediated by human monocyte complement receptors and complement component C3. J Immunol 144: 2771-2780.
    • (1990) J Immunol , vol.144 , pp. 2771-2780
    • Schlesinger, L.S.1    Bellinger-Kawahara, C.G.2    Payne, N.R.3    Horwitz, M.A.4
  • 89
    • 0023853958 scopus 로고
    • Roles of CR3 and mannose receptors in the attachment and ingestion of Leishmania donovani by human mononuclear phagocytes
    • Wilson ME, Pearson RD, (1988) Roles of CR3 and mannose receptors in the attachment and ingestion of Leishmania donovani by human mononuclear phagocytes. Infect Immun 56: 363-369.
    • (1988) Infect Immun , vol.56 , pp. 363-369
    • Wilson, M.E.1    Pearson, R.D.2
  • 90
    • 0023133779 scopus 로고
    • Leishmania promastigotes are recognized by the macrophage receptor for advanced glycosylation endproducts
    • Mosser DM, Vlassara H, Edelson PJ, Cerami A, (1987) Leishmania promastigotes are recognized by the macrophage receptor for advanced glycosylation endproducts. J Exp Med 165: 140-145.
    • (1987) J Exp Med , vol.165 , pp. 140-145
    • Mosser, D.M.1    Vlassara, H.2    Edelson, P.J.3    Cerami, A.4
  • 91
    • 0023609704 scopus 로고
    • Phagocytosis of Legionella pneumophila is mediated by human monocyte complement receptors
    • Payne NR, Horwitz MA, (1987) Phagocytosis of Legionella pneumophila is mediated by human monocyte complement receptors. J Exp Med 166: 1377-1389.
    • (1987) J Exp Med , vol.166 , pp. 1377-1389
    • Payne, N.R.1    Horwitz, M.A.2
  • 92
    • 19444365690 scopus 로고    scopus 로고
    • Induction of murine macrophage TNF-alpha synthesis by Mycobacterium avium is modulated through complement-dependent interaction via complement receptors 3 and 4 in relation to M. avium glycopeptidolipid
    • Irani VR, Maslow JN, (2005) Induction of murine macrophage TNF-alpha synthesis by Mycobacterium avium is modulated through complement-dependent interaction via complement receptors 3 and 4 in relation to M. avium glycopeptidolipid. FEMS Microbiol Lett 246: 221-228.
    • (2005) FEMS Microbiol Lett , vol.246 , pp. 221-228
    • Irani, V.R.1    Maslow, J.N.2
  • 93
    • 0033830087 scopus 로고    scopus 로고
    • In experimental leishmaniasis deficiency of CD18 results in parasite dissemination associated with altered macrophage functions and incomplete Th1 cell response
    • Schonlau F, Scharffetter-Kochanek K, Grabbe S, Pietz B, Sorg C, et al. (2000) In experimental leishmaniasis deficiency of CD18 results in parasite dissemination associated with altered macrophage functions and incomplete Th1 cell response. Eur J Immunol 30: 2729-2740.
    • (2000) Eur J Immunol , vol.30 , pp. 2729-2740
    • Schonlau, F.1    Scharffetter-Kochanek, K.2    Grabbe, S.3    Pietz, B.4    Sorg, C.5
  • 94
    • 79951496236 scopus 로고    scopus 로고
    • NOD2 controls the nature of the inflammatory response and subsequent fate of Mycobacterium tuberculosis and M. bovis BCG in human macrophages
    • Brooks MN, Rajaram MV, Azad AK, Amer AO, Valdivia-Arenas MA, et al. (2011) NOD2 controls the nature of the inflammatory response and subsequent fate of Mycobacterium tuberculosis and M. bovis BCG in human macrophages. Cell Microbiol 13: 402-418.
    • (2011) Cell Microbiol , vol.13 , pp. 402-418
    • Brooks, M.N.1    Rajaram, M.V.2    Azad, A.K.3    Amer, A.O.4    Valdivia-Arenas, M.A.5
  • 95
    • 73449101489 scopus 로고    scopus 로고
    • Mannose receptor-dependent delay in phagosome maturation by Mycobacterium avium glycopeptidolipids
    • Sweet L, Singh PP, Azad AK, Rajaram MV, Schlesinger LS, et al. (2010) Mannose receptor-dependent delay in phagosome maturation by Mycobacterium avium glycopeptidolipids. Infect Immun 78: 518-526.
    • (2010) Infect Immun , vol.78 , pp. 518-526
    • Sweet, L.1    Singh, P.P.2    Azad, A.K.3    Rajaram, M.V.4    Schlesinger, L.S.5


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