메뉴 건너뛰기




Volumn 4, Issue 10-11, 2004, Pages 1287-1300

Triacyl-lipopentapeptide adjuvants: TLR2-dependent activation of macrophages and modulation of receptor-mediated cell activation by altering acyl-moieties

Author keywords

Biochemistry; BMDMs; Bone marrow derived macrophages; Bovine serum albumin; BSA; Cellular activation; ELISA; Enzyme linked immunosorbent assay; ERK; Extracellular signal regulated protein kinase; FCS; Immunochemistry; Monocytes macrophages; Protein kinases

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IMMUNOLOGICAL ADJUVANT; INTERLEUKIN 1; INTERLEUKIN 6; LIPOPEPTIDE; PYRROLIDINE DITHIOCARBAMATE; REACTIVE OXYGEN METABOLITE; TOLL LIKE RECEPTOR 2; TUMOR NECROSIS FACTOR ALPHA;

EID: 4143087182     PISSN: 15675769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.intimp.2004.04.012     Document Type: Article
Times cited : (17)

References (60)
  • 1
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a non-clonal system of recognition
    • Medzhitow R., Janeway C.A. Innate immunity: the virtues of a non-clonal system of recognition. Cell. 91:1997;295-298
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitow, R.1    Janeway, C.A.2
  • 2
    • 0033517989 scopus 로고    scopus 로고
    • Lipoproteins take their toll on the host
    • Janeway C.A., Medzhitow R. Lipoproteins take their toll on the host. Curr. Biol. 9:1999;R879-R882
    • (1999) Curr. Biol. , vol.9 , pp. 879-R882
    • Janeway, C.A.1    Medzhitow, R.2
  • 4
  • 5
    • 0024299087 scopus 로고
    • The toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein
    • Hashimoto C., Hudson K.L., Anderson K.V. The toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein. Cell. 52:1988;269-279
    • (1988) Cell , vol.52 , pp. 269-279
    • Hashimoto, C.1    Hudson, K.L.2    Anderson, K.V.3
  • 6
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila TOLL protein signals activation of adaptive immunity
    • Medzhitow R., Preston-Hurlburt P., Janeway C.A. A human homologue of the Drosophila TOLL protein signals activation of adaptive immunity. Nature. 388:1997;394-397
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitow, R.1    Preston-Hurlburt, P.2    Janeway, C.A.3
  • 8
    • 0032100444 scopus 로고    scopus 로고
    • Cloning and characterization of two Toll/interleukin-1 receptor-like genes TIL3 and TIL4: Evidence for a multi-gene receptor family in humans
    • Chaudhary P.M., Ferguson C., Nguyen V., Nguyen O., Massa H.F., Eby M., et al. Cloning and characterization of two Toll/interleukin-1 receptor-like genes TIL3 and TIL4: evidence for a multi-gene receptor family in humans. Blood. 91:1998;4020-4027
    • (1998) Blood , vol.91 , pp. 4020-4027
    • Chaudhary, P.M.1    Ferguson, C.2    Nguyen, V.3    Nguyen, O.4    Massa, H.F.5    Eby, M.6
  • 10
    • 0034457684 scopus 로고    scopus 로고
    • Cloning and characterization of a sub-family of human toll-like receptors: HTLR7, hTLR8 and hTLR9
    • Chuang T.H., Ulevitch R.J. Cloning and characterization of a sub-family of human toll-like receptors: hTLR7, hTLR8 and hTLR9. Eur. Cytokine Netw. 11:2000;372-380
    • (2000) Eur. Cytokine Netw. , vol.11 , pp. 372-380
    • Chuang, T.H.1    Ulevitch, R.J.2
  • 12
    • 0035104961 scopus 로고    scopus 로고
    • Toll-like receptors; Their physiological role and signal transduction system
    • Takeuchi O., Akira S. Toll-like receptors; their physiological role and signal transduction system. Int. Immunopharmacol. 1:2001;625-635
    • (2001) Int. Immunopharmacol. , vol.1 , pp. 625-635
    • Takeuchi, O.1    Akira, S.2
  • 13
    • 0037070113 scopus 로고    scopus 로고
    • Toll-like receptors as adjuvant receptors
    • Kaisho T., Akira S. Toll-like receptors as adjuvant receptors. Biochim. Biophys. Acta. 1589:2002;1-13
    • (2002) Biochim. Biophys. Acta , vol.1589 , pp. 1-13
    • Kaisho, T.1    Akira, S.2
  • 16
    • 0343118085 scopus 로고    scopus 로고
    • Drug specific antibodies: T-cell epitope-lipopeptide conjugates are potent adjuvants for small antigens in vivo and in vitro
    • Mittenbühler K., Loleit M., Baier W., Fischer B., Sedelmeier E., Jung G., et al. Drug specific antibodies: T-cell epitope-lipopeptide conjugates are potent adjuvants for small antigens in vivo and in vitro. Int. J. Immunopharmacol. 19:1997;277-287
    • (1997) Int. J. Immunopharmacol. , vol.19 , pp. 277-287
    • Mittenbühler, K.1    Loleit, M.2    Baier, W.3    Fischer, B.4    Sedelmeier, E.5    Jung, G.6
  • 17
    • 2542571188 scopus 로고    scopus 로고
    • The lipopeptide Pam3Cys-Ser-(Lys)4. An alternative adjuvant to Freund's adjuvant for the immunization of chicken to produce egg yolk antibodies
    • Erhard M.H., Schmidt P., Hofmann A., Bergmann J., Mittermeier P., Kaufmann P., et al. The lipopeptide Pam3Cys-Ser-(Lys)4. An alternative adjuvant to Freund's adjuvant for the immunization of chicken to produce egg yolk antibodies. ATLA. 25:1997;173-181
    • (1997) ATLA , vol.25 , pp. 173-181
    • Erhard, M.H.1    Schmidt, P.2    Hofmann, A.3    Bergmann, J.4    Mittermeier, P.5    Kaufmann, P.6
  • 18
    • 0033950921 scopus 로고    scopus 로고
    • Lipopeptides as immunoadjuvants and immunostimulants in mucosal immunization
    • Baier W., Masihi N., Huber M., Hoffmann P., Bessler W.G. Lipopeptides as immunoadjuvants and immunostimulants in mucosal immunization. Immunobiology. 201:1999;391-405
    • (1999) Immunobiology , vol.201 , pp. 391-405
    • Baier, W.1    Masihi, N.2    Huber, M.3    Hoffmann, P.4    Bessler, W.G.5
  • 19
    • 17644443773 scopus 로고    scopus 로고
    • Generation of antibodies directed against the low-immunogenic peptide-toxins microcystin-LR/RR and nodularin
    • Baier W., Loleit M., Fischer B., Jung G., Neumann U., Weiss M., et al. Generation of antibodies directed against the low-immunogenic peptide-toxins microcystin-LR/RR and nodularin. Int. J. Immunopharmacol. 22:2000;339-353
    • (2000) Int. J. Immunopharmacol. , vol.22 , pp. 339-353
    • Baier, W.1    Loleit, M.2    Fischer, B.3    Jung, G.4    Neumann, U.5    Weiss, M.6
  • 21
    • 0024786740 scopus 로고
    • Fully automatic simultaneous multiple peptide synthesis in micromolar scale-rapid synthesis of series of peptides for screening in biological assays
    • Schnorrenberg G., Gerhardt H. Fully automatic simultaneous multiple peptide synthesis in micromolar scale-rapid synthesis of series of peptides for screening in biological assays. Tetrahedron. 45:1989;7759-7764
    • (1989) Tetrahedron , vol.45 , pp. 7759-7764
    • Schnorrenberg, G.1    Gerhardt, H.2
  • 22
    • 0025783777 scopus 로고
    • Lipopeptides containing 2-palmitoylamino-6,7-bis(palmitoyloxy)-heptanoic acid: Synthesis, stereospecific stimulation of B-lymphocytes and adjuvanticity
    • Metzger J., Jung G., Bessler W.G., Hoffmann P., Strecker M., Lieberknecht A., et al. Lipopeptides containing 2-palmitoylamino-6,7-bis(palmitoyloxy)- heptanoic acid: synthesis, stereospecific stimulation of B-lymphocytes and adjuvanticity. J. Med. Chem. 34:1991;1969-1974
    • (1991) J. Med. Chem. , vol.34 , pp. 1969-1974
    • Metzger, J.1    Jung, G.2    Bessler, W.G.3    Hoffmann, P.4    Strecker, M.5    Lieberknecht, A.6
  • 23
    • 33751143402 scopus 로고
    • Multiple peptide synthesis methods and their applications
    • Jung G., Beck-Sickinger A.G. Multiple peptide synthesis methods and their applications. Angew. Chem., Int. Ed. Engl. 31:1992;367-383
    • (1992) Angew. Chem., Int. Ed. Engl. , vol.31 , pp. 367-383
    • Jung, G.1    Beck-Sickinger, A.G.2
  • 25
    • 0025010210 scopus 로고
    • Preparation of human and murine monoclonal antibodies: Antigens combined with or conjugated to lipopeptides constitute potent immunogens for in vitro and in vivo immunizations
    • Hoffmann P., Jiménez-Dias M., Loleit M., Troger W., Wiesmüller K.-H., Metzger J., et al. Preparation of human and murine monoclonal antibodies: antigens combined with or conjugated to lipopeptides constitute potent immunogens for in vitro and in vivo immunizations. Hum. Antib. Hybrid. 1:1990;137-144
    • (1990) Hum. Antib. Hybrid. , vol.1 , pp. 137-144
    • Hoffmann, P.1    Jiménez-Dias, M.2    Loleit, M.3    Troger, W.4    Wiesmüller, K.-H.5    Metzger, J.6
  • 26
    • 0030843007 scopus 로고    scopus 로고
    • Bacterial lipopeptides as activators of human monocytes and monocyte-derived macrophages for tumor cytostasis
    • Hoffmann P., Semmler K., Müller B., Wiesmüller K.-H., Jung G., Bessler W.G. Bacterial lipopeptides as activators of human monocytes and monocyte-derived macrophages for tumor cytostasis. Immunobiology. 197:1997;344
    • (1997) Immunobiology , vol.197 , pp. 344
    • Hoffmann, P.1    Semmler, K.2    Müller, B.3    Wiesmüller, K.-H.4    Jung, G.5    Bessler, W.G.6
  • 27
    • 0030693258 scopus 로고    scopus 로고
    • A comparative analysis of cytokine production and tolerance induction by bacterial lipopeptides, lipopolysaccharides, and Staphyloccocus aureus in human monocytes
    • Kreutz M., Ackermann U., Hauschildt S., Krause S.W., Riedel D., Bessler W.G., et al. A comparative analysis of cytokine production and tolerance induction by bacterial lipopeptides, lipopolysaccharides, and Staphyloccocus aureus in human monocytes. Immunology. 92:1997;396-401
    • (1997) Immunology , vol.92 , pp. 396-401
    • Kreutz, M.1    Ackermann, U.2    Hauschildt, S.3    Krause, S.W.4    Riedel, D.5    Bessler, W.G.6
  • 28
    • 0035074481 scopus 로고    scopus 로고
    • Induction of soluble antitumoral mediators by synthetic analogues of bacterial lipoprotein in bone marrow-derived macrophages from LPS-responder and -nonresponder mice
    • Pfannes S.D.C., Müller B., Körner S., Bessler W.G., Hoffmann P. Induction of soluble antitumoral mediators by synthetic analogues of bacterial lipoprotein in bone marrow-derived macrophages from LPS-responder and -nonresponder mice. J. Leukoc. Biol. 69:2001;590-597
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 590-597
    • Pfannes, S.D.C.1    Müller, B.2    Körner, S.3    Bessler, W.G.4    Hoffmann, P.5
  • 29
    • 0033198204 scopus 로고    scopus 로고
    • Inflammatory signaling by Borrelia burgdorferi lipoproteins is mediated by toll-like receptor 2
    • Hirschfeld M., Kirschning C.J., Schwandner R., Wesche H., Weis J.H., Wooten R.M., et al. Inflammatory signaling by Borrelia burgdorferi lipoproteins is mediated by toll-like receptor 2. J. Immunol. 163:1999;2382-2386
    • (1999) J. Immunol. , vol.163 , pp. 2382-2386
    • Hirschfeld, M.1    Kirschning, C.J.2    Schwandner, R.3    Wesche, H.4    Weis, J.H.5    Wooten, R.M.6
  • 30
    • 0032921174 scopus 로고    scopus 로고
    • Induction of pro- and anti-inflammatory cytokines by Borrelia burgdorferi lipoproteins in monocytes is mediated by CD14
    • Giambartolomei G.H., Dennis V.A., Lasater B.L., Philipp M.T. Induction of pro- and anti-inflammatory cytokines by Borrelia burgdorferi lipoproteins in monocytes is mediated by CD14. Infect. Immun. 67:1999;140-147
    • (1999) Infect. Immun. , vol.67 , pp. 140-147
    • Giambartolomei, G.H.1    Dennis, V.A.2    Lasater, B.L.3    Philipp, M.T.4
  • 31
    • 0035018485 scopus 로고    scopus 로고
    • Immunostimulation by the synthetic lipopeptide P3CSK4: TLR4-independent activation of the ERK1/2 signal transduction pathway in macrophages
    • Müller M.R., Pfannes S.D.C., Ayoub M., Hoffmann P., Bessler W.G., Mittenbühler K. Immunostimulation by the synthetic lipopeptide P3CSK4: TLR4-independent activation of the ERK1/2 signal transduction pathway in macrophages. Immunology. 103:2001;49-60
    • (2001) Immunology , vol.103 , pp. 49-60
    • Müller, M.R.1    Pfannes, S.D.C.2    Ayoub, M.3    Hoffmann, P.4    Bessler, W.G.5    Mittenbühler, K.6
  • 34
    • 0029793659 scopus 로고    scopus 로고
    • Murine bone marrow-derived macrophages constitute feeder cells for human B cell hybridomas
    • Hoffmann P., Jiménez-Dias M., Weckesser J., Bessler W.G. Murine bone marrow-derived macrophages constitute feeder cells for human B cell hybridomas. J. Immunol. Methods. 196:1996;85-91
    • (1996) J. Immunol. Methods , vol.196 , pp. 85-91
    • Hoffmann, P.1    Jiménez-Dias, M.2    Weckesser, J.3    Bessler, W.G.4
  • 35
    • 0029840830 scopus 로고    scopus 로고
    • Measurement of nitrate and nitrite in biological samples using nitrate reductase and Griess reaction
    • Granger D.L., Taintor R.R., Boockvar K.S., Hibbs J.B. Jr. Measurement of nitrate and nitrite in biological samples using nitrate reductase and Griess reaction. Methods Enzymol. 268:1996;142-151
    • (1996) Methods Enzymol. , vol.268 , pp. 142-151
    • Granger, D.L.1    Taintor, R.R.2    Boockvar, K.S.3    Hibbs Jr., J.B.4
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
  • 38
    • 0023706894 scopus 로고
    • Release of reactive nitrogen intermediates and reactive oxygen intermediates from mouse peritoneal macrophages. Comparison of activating cytokines and evidence for independent production
    • Ding A.H., Nathan C.F., Stuehr D.J. Release of reactive nitrogen intermediates and reactive oxygen intermediates from mouse peritoneal macrophages. Comparison of activating cytokines and evidence for independent production. J. Immunol. 141:1988;2407-2412
    • (1988) J. Immunol. , vol.141 , pp. 2407-2412
    • Ding, A.H.1    Nathan, C.F.2    Stuehr, D.J.3
  • 39
    • 0031893258 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase pathways by Mycoplasma fermentans membrane lipoproteins in murine macrophages: Involvement in cytokine synthesis
    • Rawadi G., Ramez V., Lemercier B., Roman-Roman S. Activation of mitogen-activated protein kinase pathways by Mycoplasma fermentans membrane lipoproteins in murine macrophages: involvement in cytokine synthesis. J. Immunol. 160:1998;1330-1339
    • (1998) J. Immunol. , vol.160 , pp. 1330-1339
    • Rawadi, G.1    Ramez, V.2    Lemercier, B.3    Roman-Roman, S.4
  • 40
    • 0032032651 scopus 로고    scopus 로고
    • Lipopolysaccharide and pneumococcal cell wall components activate the mitogen activated protein kinases (MAPK) erk-1, erk-2, and p38 in astrocytes
    • Schumann R.R., Pfeil D., Freyer D., Buerger W., Lamping N., Kirschning C.J., et al. Lipopolysaccharide and pneumococcal cell wall components activate the mitogen activated protein kinases (MAPK) erk-1, erk-2, and p38 in astrocytes. Glia. 22:1998;295-305
    • (1998) Glia , vol.22 , pp. 295-305
    • Schumann, R.R.1    Pfeil, D.2    Freyer, D.3    Buerger, W.4    Lamping, N.5    Kirschning, C.J.6
  • 41
    • 0032934728 scopus 로고    scopus 로고
    • Involvement of mitogen-activated protein kinase pathways in interleukin-8 production by human monocytes and polymorphonuclear cells stimulated with lipopolysaccharide or Mycoplasma fermentans membrane
    • Marie C., Roman-Roman S., Rawadi G. Involvement of mitogen-activated protein kinase pathways in interleukin-8 production by human monocytes and polymorphonuclear cells stimulated with lipopolysaccharide or Mycoplasma fermentans membrane. Infect. Immun. 67:1999;688-693
    • (1999) Infect. Immun. , vol.67 , pp. 688-693
    • Marie, C.1    Roman-Roman, S.2    Rawadi, G.3
  • 43
    • 0034819803 scopus 로고    scopus 로고
    • Roles of toll-like receptors in innate immune responses
    • Takeda K., Akira S. Roles of toll-like receptors in innate immune responses. Genes Cells. 6:2001;733-742
    • (2001) Genes Cells , vol.6 , pp. 733-742
    • Takeda, K.1    Akira, S.2
  • 44
    • 0036134963 scopus 로고    scopus 로고
    • Toll-like receptors: How they work and what they do
    • Beutler B. Toll-like receptors: how they work and what they do. Curr. Opin. Hematol. 9:2002;2-10
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 2-10
    • Beutler, B.1
  • 45
    • 0037427976 scopus 로고    scopus 로고
    • TOLL-like receptors linking innate and adaptive immune response
    • Werling D., Jungi T.W. TOLL-like receptors linking innate and adaptive immune response. Vet. Immunol. Immunopathol. 91:2003;1-12
    • (2003) Vet. Immunol. Immunopathol. , vol.91 , pp. 1-12
    • Werling, D.1    Jungi, T.W.2
  • 46
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis J.M., Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81:2001;807-869
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 47
    • 0032609465 scopus 로고    scopus 로고
    • Making the connection: Coupling of the stress-activated ERK/MAPK (extracellular-signal-regulated kinase/mitogen-activated protein kinase) core signalling modules to extracellular stimuli and biological responses
    • Kyriakis J.M. Making the connection: coupling of the stress-activated ERK/MAPK (extracellular-signal-regulated kinase/mitogen-activated protein kinase) core signalling modules to extracellular stimuli and biological responses. Biochem. Soc. Symp. 64:1999;29-48
    • (1999) Biochem. Soc. Symp. , vol.64 , pp. 29-48
    • Kyriakis, J.M.1
  • 49
    • 0029043582 scopus 로고
    • How MAP kinases are regulated
    • Cobb M.H., Goldsmith E.J. How MAP kinases are regulated. J. Biol. Chem. 270:1995;14843-14846
    • (1995) J. Biol. Chem. , vol.270 , pp. 14843-14846
    • Cobb, M.H.1    Goldsmith, E.J.2
  • 51
    • 0028884033 scopus 로고
    • PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo
    • Alessi D.R., Cuenda A., Cohen P., Dudley D.T., Saltiel A.R. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270:1995;27489-27494
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 52
    • 0034177888 scopus 로고    scopus 로고
    • Cutting edge: Cell surface expression and lipopolysaccharide signaling via the TOLL-like receptor 4-MD-2 complex on mouse peritoneal macrophages
    • Akashi S., Shimazu R., Ogata H., Nagai Y., Takeda K., Kimoto M., et al. Cutting edge: cell surface expression and lipopolysaccharide signaling via the TOLL-like receptor 4-MD-2 complex on mouse peritoneal macrophages. J. Immunol. 164:2000;3471-3475
    • (2000) J. Immunol. , vol.164 , pp. 3471-3475
    • Akashi, S.1    Shimazu, R.2    Ogata, H.3    Nagai, Y.4    Takeda, K.5    Kimoto, M.6
  • 53
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on TOLL-like receptor 4
    • Shimazu R., Akashi S., Ogata H., Nagai Y., Fukudome K., Miyake K., et al. MD-2, a molecule that confers lipopolysaccharide responsiveness on TOLL-like receptor 4. J. Exp. Med. 189:1999;1777-1782
    • (1999) J. Exp. Med. , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6
  • 54
    • 0036918723 scopus 로고    scopus 로고
    • Differential recognition of structural details of bacterial lipopeptides by toll-like receptors
    • Morr M., Takeuchi O., Akira S., Simon M.M., Mühlradt P.F. Differential recognition of structural details of bacterial lipopeptides by toll-like receptors. Eur. J. Immunol. 32:2002;3337-3347
    • (2002) Eur. J. Immunol. , vol.32 , pp. 3337-3347
    • Morr, M.1    Takeuchi, O.2    Akira, S.3    Simon, M.M.4    Mühlradt, P.F.5
  • 55
    • 0033952703 scopus 로고    scopus 로고
    • Tlr4: Central component of the sole mammalian LPS sensor
    • Beutler B. Tlr4: central component of the sole mammalian LPS sensor. Curr. Opin. Immunol. 12:2000;20-26
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 20-26
    • Beutler, B.1
  • 56
    • 0026077605 scopus 로고
    • Inhibitors of poly (ADP-ribose) polymerase suppress lipopolysaccharide- induced nitrite formation in macrophages
    • Hauschildt S., Scheipers P., Bessler W.G. Inhibitors of poly (ADP-ribose) polymerase suppress lipopolysaccharide-induced nitrite formation in macrophages. Biochem. Biophys. Res. Comm. 179:1991;865-871
    • (1991) Biochem. Biophys. Res. Comm. , vol.179 , pp. 865-871
    • Hauschildt, S.1    Scheipers, P.2    Bessler, W.G.3
  • 57
    • 0026744830 scopus 로고
    • Molecular cloning and functional expression of an inducible nitric oxide synthase from a murine macrophage cell line
    • Lyons C.R., Orloff G.J., Cunningham J.M. Molecular cloning and functional expression of an inducible nitric oxide synthase from a murine macrophage cell line. J. Biol. Chem. 267:1992;6370-6374
    • (1992) J. Biol. Chem. , vol.267 , pp. 6370-6374
    • Lyons, C.R.1    Orloff, G.J.2    Cunningham, J.M.3
  • 58
    • 0031906550 scopus 로고    scopus 로고
    • Signal transduction through NF-κB
    • May M.J., Ghosh S. Signal transduction through NF-κB. Immunol. Today. 19:1998;80-88
    • (1998) Immunol. Today , vol.19 , pp. 80-88
    • May, M.J.1    Ghosh, S.2
  • 59
    • 0032403566 scopus 로고    scopus 로고
    • Antisense oligonucleotides targeting protein kinase C-α, -βI, or δ but not -η Inhibit lipopolysaccharide-induced nitric oxide synthase expression in RAW 264.7 macrophages: Involvement of a nuclear factor κb-dependent mechanism
    • Chen C.-C., Wang J.-K., Lin S.-B. Antisense oligonucleotides targeting protein kinase C-α, -βI, or δ but not -η inhibit lipopolysaccharide-induced nitric oxide synthase expression in RAW 264.7 macrophages: involvement of a nuclear factor κB-dependent mechanism. J. Immunobiol. 161:1998;6206-6214
    • (1998) J. Immunobiol. , vol.161 , pp. 6206-6214
    • Chen, C.-C.1    Wang, J.-K.2    Lin, S.-B.3
  • 60
    • 0036644042 scopus 로고    scopus 로고
    • Cutting edge: Role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins
    • Takeuchi O., Sati S., Horiuchi T., Hoshino K., Takeda K., Dong Z., et al. Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J. Immunol. 169:2002;10-14
    • (2002) J. Immunol. , vol.169 , pp. 10-14
    • Takeuchi, O.1    Sati, S.2    Horiuchi, T.3    Hoshino, K.4    Takeda, K.5    Dong, Z.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.