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Volumn 10, Issue 9, 2011, Pages 4018-4032

Mapping of interactions between human macrophages and Staphylococcus aureus reveals an involvement of MAP kinase signaling in the host defense

Author keywords

host pathogen interaction; kinase profiling; signal transduction

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; TOLL LIKE RECEPTOR 2;

EID: 80052508991     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200224x     Document Type: Article
Times cited : (24)

References (97)
  • 2
    • 0033046220 scopus 로고    scopus 로고
    • Mechanisms of phagocytosis in macrophages
    • DOI 10.1146/annurev.immunol.17.1.593
    • Aderem, A.; Underhill, D. M. Mechanisms of phagocytosis in macrophages Annu. Rev. Immunol. 1999, 17, 593-623 (Pubitemid 29241135)
    • (1999) Annual Review of Immunology , vol.17 , pp. 593-623
    • Aderem, A.1    Underhill, D.M.2
  • 4
    • 0036078539 scopus 로고    scopus 로고
    • Role of Yops and adhesins in resistance of Yersinia enterocolitica to phagocytosis
    • DOI 10.1128/IAI.70.8.4165-4176.2002
    • Grosdent, N.; Maridonneau-Parini, I.; Sory, M. P.; Cornelis, G. R. Role of Yops and adhesins in resistance of Yersinia enterocolitica to phagocytosis Infect. Immun. 2002, 70 (8) 4165-76 (Pubitemid 34790925)
    • (2002) Infection and Immunity , vol.70 , Issue.8 , pp. 4165-4176
    • Grosdent, N.1    Maridonneau-Parini, I.2    Sory, M.-P.3    Cornelis, G.R.4
  • 5
    • 46449133631 scopus 로고    scopus 로고
    • Incorporation of Mycobacterium tuberculosis lipoarabinomannan into macrophage membrane rafts is a prerequisite for the phagosomal maturation block
    • Welin, A.; Winberg, M. E.; Abdalla, H.; Sarndahl, E.; Rasmusson, B.; Stendahl, O.; Lerm, M. Incorporation of Mycobacterium tuberculosis lipoarabinomannan into macrophage membrane rafts is a prerequisite for the phagosomal maturation block Infect. Immun. 2008, 76 (7) 2882-7
    • (2008) Infect. Immun. , vol.76 , Issue.7 , pp. 2882-7
    • Welin, A.1    Winberg, M.E.2    Abdalla, H.3    Sarndahl, E.4    Rasmusson, B.5    Stendahl, O.6    Lerm, M.7
  • 6
    • 25444457508 scopus 로고    scopus 로고
    • Characterization of Listeria monocytogenes expressing anthrolysin O and phosphatidylinositol-specific phospholipase C from Bacillus anthracis
    • DOI 10.1128/IAI.73.10.6639-6646.2005
    • Wei, Z.; Schnupf, P.; Poussin, M. A.; Zenewicz, L. A.; Shen, H.; Goldfine, H. Characterization of Listeria monocytogenes expressing anthrolysin O and phosphatidylinositol-specific phospholipase C from Bacillus anthracis Infect. Immun. 2005, 73 (10) 6639-46 (Pubitemid 41368829)
    • (2005) Infection and Immunity , vol.73 , Issue.10 , pp. 6639-6646
    • Wei, Z.1    Schnupf, P.2    Poussin, M.A.3    Zenewicz, L.A.4    Shen, H.5    Goldfine, H.6
  • 7
    • 0028117139 scopus 로고
    • The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton
    • Pistor, S.; Chakraborty, T.; Niebuhr, K.; Domann, E.; Wehland, J. The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton EMBO J. 1994, 13 (4) 758-63 (Pubitemid 24057506)
    • (1994) EMBO Journal , vol.13 , Issue.4 , pp. 758-763
    • Pistor, S.1    Chakraborty, T.2    Niebuhr, K.3    Domann, E.4    Wehland, J.5
  • 8
    • 0035691622 scopus 로고    scopus 로고
    • How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: Implications for conversion of plasma membrane to the ER membrane
    • Tilney, L. G.; Harb, O. S.; Connelly, P. S.; Robinson, C. G.; Roy, C. R. How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane J. Cell Sci. 2001, 114 (Pt 24) 4637-50 (Pubitemid 34082882)
    • (2001) Journal of Cell Science , vol.114 , Issue.24 , pp. 4637-4650
    • Tilney, L.G.1    Harb, O.S.2    Connelly, P.S.3    Robinson, C.G.4    Roy, C.R.5
  • 9
    • 0028356055 scopus 로고
    • Surface-associated proteins of Staphylococcus aureus: Their possible roles in virulence
    • DOI 10.1016/0378-1097(94)90504-5
    • Foster, T. J.; McDevitt, D. Surface-associated proteins of Staphylococcus aureus: their possible roles in virulence FEMS Microbiol. Let.t 1994, 118 (3) 199-205 (Pubitemid 124012144)
    • (1994) FEMS Microbiology Letters , vol.118 , Issue.3 , pp. 199-205
    • Foster, T.J.1    McDevitt, D.2
  • 10
    • 0032551901 scopus 로고    scopus 로고
    • Staphylococcus aureus infections
    • Lowy, F. D. Staphylococcus aureus infections N. Engl. J. Med. 1998, 339 (8) 520-32
    • (1998) N. Engl. J. Med. , vol.339 , Issue.8 , pp. 520-32
    • Lowy, F.D.1
  • 14
    • 0042233644 scopus 로고    scopus 로고
    • Intracellular survival of Staphylococcus aureus within cultured enterocytes
    • DOI 10.1016/S0022-4804(03)00314-7
    • Hess, D. J.; Henry-Stanley, M. J.; Erickson, E. A.; Wells, C. L. Intracellular survival of Staphylococcus aureus within cultured enterocytes J. Surg. Res. 2003, 114 (1) 42-9 (Pubitemid 37108674)
    • (2003) Journal of Surgical Research , vol.114 , Issue.1 , pp. 42-49
    • Hess, D.J.1    Henry-Stanley, M.J.2    Erickson, E.A.3    Wells, C.L.4
  • 16
    • 25844449637 scopus 로고    scopus 로고
    • Hematogenous vertebral osteomyelitis due to Staphylococcus aureus in the adult: Clinical features and therapeutic outcomes
    • DOI 10.1097/01.smj.0000168666.98129.33
    • Priest, D. H.; Peacock, J. E., Jr. Hematogenous vertebral osteomyelitis due to Staphylococcus aureus in the adult: clinical features and therapeutic outcomes South Med J 2005, 98 (9) 854-62 (Pubitemid 41396080)
    • (2005) Southern Medical Journal , vol.98 , Issue.9 , pp. 854-862
    • Priest, D.H.1    Peacock Jr., J.E.2
  • 17
    • 10344223002 scopus 로고    scopus 로고
    • Kinome profiling for studying lipopolysaccharide signal transduction in human peripheral blood mononuclear cells
    • DOI 10.1074/jbc.M405028200
    • Diks, S. H.; Kok, K.; O'Toole, T.; Hommes, D. W.; van Dijken, P.; Joore, J.; Peppelenbosch, M. P. Kinome profiling for studying lipopolysaccharide signal transduction in human peripheral blood mononuclear cells J. Biol. Chem. 2004, 279 (47) 49206-13 (Pubitemid 39625804)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 49206-49213
    • Diks, S.H.1    Kok, K.2    O'Toole, T.3    Hommes, D.W.4    Van Dijkenii, P.5    Joore, J.6    Peppelenbosch, M.P.7
  • 19
    • 77955373398 scopus 로고    scopus 로고
    • Protein phosphorylation and kinome profiling reveal altered regulation of multiple signaling pathways in B lymphocytes from patients with systemic lupus erythematosus
    • Taher, T. E.; Parikh, K.; Flores-Borja, F.; Mletzko, S.; Isenberg, D. A.; Peppelenbosch, M. P.; Mageed, R. A. Protein phosphorylation and kinome profiling reveal altered regulation of multiple signaling pathways in B lymphocytes from patients with systemic lupus erythematosus Arthritis Rheum. 2010, 62 (8) 2412-23
    • (2010) Arthritis Rheum. , vol.62 , Issue.8 , pp. 2412-23
    • Taher, T.E.1    Parikh, K.2    Flores-Borja, F.3    Mletzko, S.4    Isenberg, D.A.5    Peppelenbosch, M.P.6    Mageed, R.A.7
  • 20
    • 70949099677 scopus 로고    scopus 로고
    • Kinome profiling of sugar signaling in plants using multiple platforms
    • Ritsema, T.; Peppelenbosch, M. P. Kinome profiling of sugar signaling in plants using multiple platforms Plant Signaling Behav. 2009, 4, 12
    • (2009) Plant Signaling Behav. , vol.4 , pp. 12
    • Ritsema, T.1    Peppelenbosch, M.P.2
  • 22
    • 51149102710 scopus 로고    scopus 로고
    • Trypan blue exclusion test of cell viability
    • Appendix 3, Appendix 3B.
    • Strober, W., Trypan blue exclusion test of cell viability. Curr. Protoc. Immunol. 2001, Appendix 3, Appendix 3B.
    • (2001) Curr. Protoc. Immunol.
    • Strober, W.1
  • 23
    • 0020026263 scopus 로고
    • Induction of maturation in cultured human monocytic leukemia cells by a phorbol diester
    • Tsuchiya, S.; Kobayashi, Y.; Goto, Y.; Okumura, H.; Nakae, S.; Konno, T.; Tada, K. Induction of maturation in cultured human monocytic leukemia cells by a phorbol diester Cancer Res. 1982, 42 (4) 1530-6 (Pubitemid 12148801)
    • (1982) Cancer Research , vol.42 , Issue.4 , pp. 1530-1536
    • Tsuchiya, S.1    Kobayashi, Y.2    Goto, Y.3
  • 24
    • 0032922002 scopus 로고    scopus 로고
    • PhosphoBase, a database of phosphorylation sites: Release 2.0
    • DOI 10.1093/nar/27.1.237
    • Kreegipuu, A.; Blom, N.; Brunak, S. PhosphoBase, a database of phosphorylation sites: release 2.0 Nucleic Acids Res. 1999, 27 (1) 237-9 (Pubitemid 29209448)
    • (1999) Nucleic Acids Research , vol.27 , Issue.1 , pp. 237-239
    • Kreegipuu, A.1    Blom, N.2    Brunak, S.3
  • 26
    • 0025159501 scopus 로고
    • 2+ transients
    • Della Bianca, V.; Grzeskowiak, M.; Rossi, F. Studies on molecular regulation of phagocytosis and activation of the NADPH oxidase in neutrophils. IgG- and C3b-mediated ingestion and associated respiratory burst independent of phospholipid turnover and Ca2+ transients J. Immunol. 1990, 144 (4) 1411-7 (Pubitemid 20072914)
    • (1990) Journal of Immunology , vol.144 , Issue.4 , pp. 1411-1417
    • Delle Bianca, V.1    Grzeskowiak, M.2    Rossi, F.3
  • 27
    • 0036826762 scopus 로고    scopus 로고
    • Calcium spikes in activated macrophages during Fcγ receptor-mediated phagocytosis
    • Myers, J. T.; Swanson, J. A. Calcium spikes in activated macrophages during Fcgamma receptor-mediated phagocytosis J. Leukocyte Biol. 2002, 72 (4) 677-84 (Pubitemid 36277838)
    • (2002) Journal of Leukocyte Biology , vol.72 , Issue.4 , pp. 677-684
    • Myers, J.T.1    Swanson, J.A.2
  • 28
    • 0000698690 scopus 로고
    • Association of phosphatidylinositol kinase, phosphatidylinositol monophosphate kinase, and diacylglycerol kinase with the cytoskeleton and F-actin fractions of carrot (Daucus carota L.) cells grown in suspension culture: Response to cell wall-degrading enzymes
    • Tan, Z.; Boss, W. F. Association of phosphatidylinositol kinase, phosphatidylinositol monophosphate kinase, and diacylglycerol kinase with the cytoskeleton and F-actin fractions of carrot (Daucus carota L.) cells grown in suspension culture: response to cell wall-degrading enzymes Plant Physiol. 1992, 100 (4) 2116-20
    • (1992) Plant Physiol. , vol.100 , Issue.4 , pp. 2116-20
    • Tan, Z.1    Boss, W.F.2
  • 29
    • 0020446216 scopus 로고
    • Mechanism of interaction of Dictyostelium severin with actin filaments
    • DOI 10.1083/jcb.95.3.711
    • Yamamoto, K.; Pardee, J. D.; Reidler, J.; Stryer, L.; Spudich, J. A. Mechanism of interaction of Dictyostelium severin with actin filaments J. Cell Biol. 1982, 95 (3) 711-9 (Pubitemid 13186091)
    • (1982) Journal of Cell Biology , vol.95 , Issue.3 , pp. 711-719
    • Yamamoto, K.1    Pardee, J.D.2    Reidler, J.3
  • 30
    • 0027284927 scopus 로고
    • Calmodulin and the contractile vacuole complex in mitotic cells of Dictyostelium discoideum
    • Zhu, Q.; Liu, T.; Clarke, M. Calmodulin and the contractile vacuole complex in mitotic cells of Dictyostelium discoideum J. Cell Sci. 1993, 104 (Pt 4) 1119-27 (Pubitemid 23154319)
    • (1993) Journal of Cell Science , vol.104 , Issue.4 , pp. 1119-1127
    • Zhu, Q.1    Liu, T.2    Clarke, M.3
  • 31
    • 0029018209 scopus 로고
    • The in vivo role of annexin VII (synexin): Characterization of an annexin VII-deficient Dictyostelium mutant indicates an involvement in Ca(2+)-regulated processes
    • Doring, V.; Veretout, F.; Albrecht, R.; Muhlbauer, B.; Schlatterer, C.; Schleicher, M.; Noegel, A. A. The in vivo role of annexin VII (synexin): characterization of an annexin VII-deficient Dictyostelium mutant indicates an involvement in Ca(2+)-regulated processes J. Cell Sci. 1995, 108 (Pt 5) 2065-76
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 5 , pp. 2065-76
    • Doring, V.1    Veretout, F.2    Albrecht, R.3    Muhlbauer, B.4    Schlatterer, C.5    Schleicher, M.6    Noegel, A.A.7
  • 32
    • 0028506122 scopus 로고
    • The Merck Frosst Award Lecture 1994. Calmodulin: A versatile calcium mediator protein
    • Vogel, H. J. The Merck Frosst Award Lecture 1994. Calmodulin: a versatile calcium mediator protein Biochem. Cell Biol. 1994, 72 (9-10) 357-76
    • (1994) Biochem. Cell Biol. , vol.72 , Issue.9-10 , pp. 357-76
    • Vogel, H.J.1
  • 33
    • 0032506349 scopus 로고    scopus 로고
    • 2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
    • DOI 10.1038/25133
    • Peters, C.; Mayer, A. Ca2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion Nature 1998, 396 (6711) 575-80 (Pubitemid 28563718)
    • (1998) Nature , vol.396 , Issue.6711 , pp. 575-580
    • Peters, C.1    Mayer, A.2
  • 34
    • 0030610085 scopus 로고    scopus 로고
    • 2+/calmodulin causes Rab3a to dissociate from synaptic membranes
    • DOI 10.1074/jbc.272.33.20857
    • Park, J. B.; Farnsworth, C. C.; Glomset, J. A. Ca2+/calmodulin causes Rab3A to dissociate from synaptic membranes J. Biol. Chem. 1997, 272 (33) 20857-65 (Pubitemid 27355656)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20857-20865
    • Park, J.B.1    Farnsworth, C.C.2    Glomset, J.A.3
  • 35
    • 0242515802 scopus 로고    scopus 로고
    • Phagocytosis and phagosome maturation are regulated by calcium in J774 macrophages interacting with unopsonized prey
    • DOI 10.1023/A:1022025903688
    • Tejle, K.; Magnusson, K. E.; Rasmusson, B. Phagocytosis and phagosome maturation are regulated by calcium in J774 macrophages interacting with unopsonized prey Biosci. Rep. 2002, 22 (5-6) 529-40 (Pubitemid 36250192)
    • (2002) Bioscience Reports , vol.22 , Issue.5-6 , pp. 529-540
    • Tejle, K.1    Magnusson, K.-E.2    Rasmusson, B.3
  • 36
  • 37
    • 0028917370 scopus 로고
    • The multifunctional calcium/calmodulin-dependent protein kinase: From form to function
    • Braun, A. P.; Schulman, H. The multifunctional calcium/calmodulin- dependent protein kinase: from form to function Annu. Rev. Physiol. 1995, 57, 417-45
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 417-45
    • Braun, A.P.1    Schulman, H.2
  • 38
    • 0033543561 scopus 로고    scopus 로고
    • Structural examination of autoregulation of multifunctional calcium/calmodulin-dependent protein kinase II
    • Yang, E.; Schulman, H. Structural examination of autoregulation of multifunctional calcium/calmodulin-dependent protein kinase II J. Biol. Chem. 1999, 274 (37) 26199-208
    • (1999) J. Biol. Chem. , vol.274 , Issue.37 , pp. 26199-208
    • Yang, E.1    Schulman, H.2
  • 40
    • 0029829896 scopus 로고    scopus 로고
    • Molecular definition of distinct cytoskeletal structures involved in complement- and Fc receptor-mediated phagocytosis in macrophages
    • Allen, L. A.; Aderem, A. Molecular definition of distinct cytoskeletal structures involved in complement- and Fc receptor-mediated phagocytosis in macrophages J. Exp. Med. 1996, 184 (2) 627-37 (Pubitemid 26324116)
    • (1996) Journal of Experimental Medicine , vol.184 , Issue.2 , pp. 627-637
    • Allen, L.-A.H.1    Aderem, A.2
  • 41
    • 0025732577 scopus 로고
    • Staurosporine inhibits neutrophil phagocytosis but not iC3b binding mediated by CR3 (CD11b/CD18)
    • Roubey, R. A.; Ross, G. D.; Merrill, J. T.; Walton, F.; Reed, W.; Winchester, R. J.; Buyon, J. P. Staurosporine inhibits neutrophil phagocytosis but not iC3b binding mediated by CR3 (CD11b/CD18) J. Immunol. 1991, 146 (10) 3557-62
    • (1991) J. Immunol. , vol.146 , Issue.10 , pp. 3557-62
    • Roubey, R.A.1    Ross, G.D.2    Merrill, J.T.3    Walton, F.4    Reed, W.5    Winchester, R.J.6    Buyon, J.P.7
  • 42
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation, and membrane trafficking
    • DOI 10.1146/annurev.cellbio.14.1.231
    • Martin, T. F. Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation, and membrane trafficking Annu. Rev. Cell Dev. Biol. 1998, 14, 231-64 (Pubitemid 29001455)
    • (1998) Annual Review of Cell and Developmental Biology , vol.14 , pp. 231-264
    • Martin, T.F.J.1
  • 43
    • 0033555931 scopus 로고    scopus 로고
    • A requirement for phosphatidylinositol 3-kinase in pseudopod extension
    • Cox, D.; Tseng, C. C.; Bjekic, G.; Greenberg, S. A requirement for phosphatidylinositol 3-kinase in pseudopod extension J. Biol. Chem. 1999, 274 (3) 1240-7
    • (1999) J. Biol. Chem. , vol.274 , Issue.3 , pp. 1240-7
    • Cox, D.1    Tseng, C.C.2    Bjekic, G.3    Greenberg, S.4
  • 46
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PBK1 connection: More than just a road to PKB
    • DOI 10.1042/0264-6021:3460561
    • Vanhaesebroeck, B.; Alessi, D. R. The PI3K-PDK1 connection: more than just a road to PKB Biochem. J. 2000, 346 (Pt 3) 561-76 (Pubitemid 30171014)
    • (2000) Biochemical Journal , vol.346 , Issue.3 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 47
    • 0027939928 scopus 로고
    • Fc receptor stimulation of phosphatidylinositol 3-kinase in natural killer cells is associated with protein kinase C-independent granule release and cell-mediated cytotoxicity
    • Bonnema, J. D.; Karnitz, L. M.; Schoon, R. A.; Abraham, R. T.; Leibson, P. J. Fc receptor stimulation of phosphatidylinositol 3-kinase in natural killer cells is associated with protein kinase C-independent granule release and cell-mediated cytotoxicity J. Exp. Med. 1994, 180 (4) 1427-35 (Pubitemid 24289616)
    • (1994) Journal of Experimental Medicine , vol.180 , Issue.4 , pp. 1427-1435
    • Bonnema, J.D.1    Karnitz, L.M.2    Schoon, R.A.3    Abraham, R.T.4    Leibson, P.J.5
  • 48
    • 0030772657 scopus 로고    scopus 로고
    • Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells
    • DOI 10.1083/jcb.138.6.1265
    • Dharmawardhane, S.; Sanders, L. C.; Martin, S. S.; Daniels, R. H.; Bokoch, G. M. Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells J. Cell Biol. 1997, 138 (6) 1265-78 (Pubitemid 27415053)
    • (1997) Journal of Cell Biology , vol.138 , Issue.6 , pp. 1265-1278
    • Dharmawardhane, S.1    Sanders, L.C.2    Martin, S.S.3    Daniels, R.H.4    Bokoch, G.M.5
  • 49
    • 0031127255 scopus 로고    scopus 로고
    • Emerging from the Pak: The p21-activated protein kinase family
    • DOI 10.1016/S0962-8924(97)01003-9, PII S0962892497010039
    • Sells, M. A.; Chernoff, J. Emerging from the Pak: the p21-activated protein kinase family Trends Cell Biol. 1997, 7 (4) 162-7 (Pubitemid 27135576)
    • (1997) Trends in Cell Biology , vol.7 , Issue.4 , pp. 162-167
    • Sells, M.A.1    Chernoff, J.2
  • 50
    • 77953854520 scopus 로고    scopus 로고
    • A loss-of-function screen reveals Ras- and Raf-independent MEK-ERK signaling during Chlamydia trachomatis infection
    • Gurumurthy, R. K.; Maurer, A. P.; Machuy, N.; Hess, S.; Pleissner, K. P.; Schuchhardt, J.; Rudel, T.; Meyer, T. F. A loss-of-function screen reveals Ras- and Raf-independent MEK-ERK signaling during Chlamydia trachomatis infection Sci Signal 2010, 3 (113) ra21
    • (2010) Sci Signal , vol.3 , Issue.113 , pp. 21
    • Gurumurthy, R.K.1    Maurer, A.P.2    MacHuy, N.3    Hess, S.4    Pleissner, K.P.5    Schuchhardt, J.6    Rudel, T.7    Meyer, T.F.8
  • 51
    • 0036199426 scopus 로고    scopus 로고
    • Phosphorylation and reorganization of vimentin by p21-activated kinase (PAK)
    • DOI 10.1046/j.1356-9597.2001.00504.x
    • Goto, H.; Tanabe, K.; Manser, E.; Lim, L.; Yasui, Y.; Inagaki, M. Phosphorylation and reorganization of vimentin by p21-activated kinase (PAK) Genes Cells 2002, 7 (2) 91-7 (Pubitemid 34213355)
    • (2002) Genes to Cells , vol.7 , Issue.2 , pp. 91-97
    • Goto, H.1    Tanabe, K.2    Manser, E.3    Lim, L.4    Yasui, Y.5    Inagaki, M.6
  • 52
    • 21544435993 scopus 로고    scopus 로고
    • Insights into regulation of human Schwann cell proliferation by Erk1/2 via a MEK-independent and p56Lck-dependent pathway from leprosy bacilli
    • DOI 10.1073/pnas.0501196102
    • Tapinos, N.; Rambukkana, A. Insights into regulation of human Schwann cell proliferation by Erk1/2 via a MEK-independent and p56Lck-dependent pathway from leprosy bacilli Proc. Natl. Acad. Sci. U.S.A. 2005, 102 (26) 9188-93 (Pubitemid 40923539)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.26 , pp. 9188-9193
    • Tapinos, N.1    Rambukkana, A.2
  • 53
    • 65349084974 scopus 로고    scopus 로고
    • Phagocytosis of Staphylococcus aureus by macrophages exerts cytoprotective effects manifested by the upregulation of antiapoptotic factors
    • Koziel, J.; Maciag-Gudowska, A.; Mikolajczyk, T.; Bzowska, M.; Sturdevant, D. E.; Whitney, A. R.; Shaw, L. N.; DeLeo, F. R.; Potempa, J. Phagocytosis of Staphylococcus aureus by macrophages exerts cytoprotective effects manifested by the upregulation of antiapoptotic factors PLoS One 2009, 4 (4) e5210
    • (2009) PLoS One , vol.4 , Issue.4 , pp. 5210
    • Koziel, J.1    MacIag-Gudowska, A.2    Mikolajczyk, T.3    Bzowska, M.4    Sturdevant, D.E.5    Whitney, A.R.6    Shaw, L.N.7    Deleo, F.R.8    Potempa, J.9
  • 54
    • 0035209941 scopus 로고    scopus 로고
    • Role of Src kinases and Syk in Fcγ receptor-mediated phagocytosis and phagosome-lysosome fusion
    • Majeed, M.; Caveggion, E.; Lowell, C. A.; Berton, G. Role of Src kinases and Syk in Fcgamma receptor-mediated phagocytosis and phagosome-lysosome fusion J. Leukocyte Biol. 2001, 70 (5) 801-11 (Pubitemid 33127015)
    • (2001) Journal of Leukocyte Biology , vol.70 , Issue.5 , pp. 801-811
    • Majeed, M.1    Caveggion, E.2    Lowell, C.A.3    Berton, G.4
  • 56
    • 0018859761 scopus 로고
    • Demonstration of a chemotactic factor receptor on macrophages
    • Snyderman, R.; Fudman, E. J. Demonstration of a chemotactic factor receptor on macrophages J. Immunol. 1980, 124 (6) 2754-7 (Pubitemid 10116049)
    • (1980) Journal of Immunology , vol.124 , Issue.6 , pp. 2754-2757
    • Snyderman, R.1    Fudman, E.J.2
  • 57
    • 0033558054 scopus 로고    scopus 로고
    • Bacterial superantigens induce down-modulation of CC chemokine responsiveness in human monocytes via an alternative chemokine ligand- independent mechanism
    • Rahimpour, R.; Mitchell, G.; Khandaker, M. H.; Kong, C.; Singh, B.; Xu, L.; Ochi, A.; Feldman, R. D.; Pickering, J. G.; Gill, B. M.; Kelvin, D. J. Bacterial superantigens induce down-modulation of CC chemokine responsiveness in human monocytes via an alternative chemokine ligand-independent mechanism J. Immunol. 1999, 162 (4) 2299-307 (Pubitemid 29288854)
    • (1999) Journal of Immunology , vol.162 , Issue.4 , pp. 2299-2307
    • Rahimpour, R.1    Mitchell, G.2    Khandaker, M.H.3    Kong, C.4    Singh, B.5    Xu, L.6    Ochi, A.7    Feldman, R.D.8    Pickering, J.G.9    Gill, B.M.10    Kelvin, D.J.11
  • 59
    • 46249134182 scopus 로고    scopus 로고
    • Analysis of fyn function in hemostasis and αllbβ3-integrin signaling
    • DOI 10.1242/jcs.014076
    • Reddy, K. B.; Smith, D. M.; Plow, E. F. Analysis of Fyn function in hemostasis and αIIbbeta3-integrin signaling J. Cell Sci. 2008, 121 (Pt 10) 1641-8 (Pubitemid 351911821)
    • (2008) Journal of Cell Science , vol.121 , Issue.10 , pp. 1641-1648
    • Reddy, K.B.1    Smith, D.M.2    Plow, E.F.3
  • 60
    • 0032436996 scopus 로고    scopus 로고
    • Surface protein adhesins of Staphylococcus aureus
    • DOI 10.1016/S0966-842X(98)01400-0, PII S0966842X98014000
    • Foster, T. J.; Hook, M. Surface protein adhesins of Staphylococcus aureus Trends Microbiol. 1998, 6 (12) 484-8 (Pubitemid 29002881)
    • (1998) Trends in Microbiology , vol.6 , Issue.12 , pp. 484-488
    • Foster, T.J.1    Hook, M.2
  • 61
    • 0033754023 scopus 로고    scopus 로고
    • Cellular invasion by Staphylococcus aureus involves a fibronectin bridge between the bacterial fibronectin-binding MSCRAMMs and host cell beta1 integrins
    • Fowler, T.; Wann, E. R.; Joh, D.; Johansson, S.; Foster, T. J.; Hook, M. Cellular invasion by Staphylococcus aureus involves a fibronectin bridge between the bacterial fibronectin-binding MSCRAMMs and host cell beta1 integrins Eur. J. Cell Biol. 2000, 79 (10) 672-9
    • (2000) Eur. J. Cell Biol. , vol.79 , Issue.10 , pp. 672-9
    • Fowler, T.1    Wann, E.R.2    Joh, D.3    Johansson, S.4    Foster, T.J.5    Hook, M.6
  • 62
    • 0037220347 scopus 로고    scopus 로고
    • Fibronectin bound to the surface of Staphylococcus aureus induces association of very late antigen 5 and intracellular signaling factors with macrophage cytoskeleton
    • DOI 10.1128/IAI.71.1.140-146.2003
    • Shinji, H.; Seki, K.; Tajima, A.; Uchida, A.; Masuda, S. Fibronectin bound to the surface of Staphylococcus aureus induces association of very late antigen 5 and intracellular signaling factors with macrophage cytoskeleton Infect. Immun. 2003, 71 (1) 140-6 (Pubitemid 36026014)
    • (2003) Infection and Immunity , vol.71 , Issue.1 , pp. 140-146
    • Shinji, H.1    Seki, K.2    Tajima, A.3    Uchida, A.4    Masuda, S.5
  • 64
    • 23744514918 scopus 로고    scopus 로고
    • Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain
    • DOI 10.1083/jcb.200501113
    • Stuart, L. M.; Deng, J.; Silver, J. M.; Takahashi, K.; Tseng, A. A.; Hennessy, E. J.; Ezekowitz, R. A.; Moore, K. J. Response to Staphylococcus aureus requires CD36-mediated phagocytosis triggered by the COOH-terminal cytoplasmic domain J. Cell Biol. 2005, 170 (3) 477-85 (Pubitemid 41126946)
    • (2005) Journal of Cell Biology , vol.170 , Issue.3 , pp. 477-485
    • Stuart, L.M.1    Deng, J.2    Silver, J.M.3    Takahashi, K.4    Tseng, A.A.5    Hennessy, E.J.6    Ezekowitz, R.A.B.7    Moore, K.J.8
  • 65
    • 0037273063 scopus 로고    scopus 로고
    • Oxidative stress in ataxia telangiectasia
    • DOI 10.1179/135100003125001206
    • Watters, D. J. Oxidative stress in ataxia telangiectasia Redox Rep. 2003, 8 (1) 23-9 (Pubitemid 36204249)
    • (2003) Redox Report , vol.8 , Issue.1 , pp. 23-29
    • Watters, D.J.1
  • 66
    • 0038146962 scopus 로고    scopus 로고
    • ATR/ATM targets are phosphorylated by ATR in response to hypoxia and ATM in response to reoxygenation
    • DOI 10.1074/jbc.M212360200
    • Hammond, E. M.; Dorie, M. J.; Giaccia, A. J. ATR/ATM targets are phosphorylated by ATR in response to hypoxia and ATM in response to reoxygenation J. Biol. Chem. 2003, 278 (14) 12207-13 (Pubitemid 36800201)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12207-12213
    • Hammond, E.M.1    Dorie, M.J.2    Giaccia, A.J.3
  • 67
    • 0038188668 scopus 로고    scopus 로고
    • Nitric oxide promotes p53 nuclear retention and sensitizes neuroblastoma cells to apoptosis by ionizing radiation
    • DOI 10.1038/sj.cdd.4401181
    • Wang, X.; Zalcenstein, A.; Oren, M. Nitric oxide promotes p53 nuclear retention and sensitizes neuroblastoma cells to apoptosis by ionizing radiation Cell Death Differ. 2003, 10 (4) 468-76 (Pubitemid 36626359)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.4 , pp. 468-476
    • Wang, X.1    Zalcenstein, A.2    Oren, M.3
  • 69
    • 34247095700 scopus 로고    scopus 로고
    • TLR2-mediated survival of Staphylococcus aureus in macrophages: A novel bacterial strategy against host innate immunity
    • Watanabe, I.; Ichiki, M.; Shiratsuchi, A.; Nakanishi, Y. TLR2-mediated survival of Staphylococcus aureus in macrophages: a novel bacterial strategy against host innate immunity J. Immunol. 2007, 178 (8) 4917-25 (Pubitemid 46595274)
    • (2007) Journal of Immunology , vol.178 , Issue.8 , pp. 4917-4925
    • Watanabe, I.1    Ichiki, M.2    Shiratsuchi, A.3    Nakanishi, Y.4
  • 70
    • 0034695441 scopus 로고    scopus 로고
    • Reactive oxygen species activate p90 ribosomal S6 kinase via Fyn and Ras
    • DOI 10.1074/jbc.275.3.1739
    • Abe, J.; Okuda, M.; Huang, Q.; Yoshizumi, M.; Berk, B. C. Reactive oxygen species activate p90 ribosomal S6 kinase via Fyn and Ras J. Biol. Chem. 2000, 275 (3) 1739-48 (Pubitemid 30060794)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1739-1748
    • Jun-Ichi, A.1    Okuda, M.2    Huang, Q.3    Yoshizumi, M.4    Berk, B.C.5
  • 71
    • 0034964353 scopus 로고    scopus 로고
    • Role of extracellular signal-regulated protein kinase cascade in macrophage killing of Candida albicans
    • Ibata-Ombetta, S.; Jouault, T.; Trinel, P. A.; Poulain, D. Role of extracellular signal-regulated protein kinase cascade in macrophage killing of Candida albicans J. Leukocyte Biol. 2001, 70 (1) 149-54 (Pubitemid 32613675)
    • (2001) Journal of Leukocyte Biology , vol.70 , Issue.1 , pp. 149-154
    • Ibata-Ombetta, S.1    Jouault, T.2    Trinel, P.-A.3    Poulain, D.4
  • 72
    • 0028237509 scopus 로고
    • Cloning and characterisation of cDNAs encoding a novel non-receptor tyrosine kinase, brk, expressed in human breast tumours
    • Mitchell, P. J.; Barker, K. T.; Martindale, J. E.; Kamalati, T.; Lowe, P. N.; Page, M. J.; Gusterson, B. A.; Crompton, M. R. Cloning and characterisation of cDNAs encoding a novel non-receptor tyrosine kinase, brk, expressed in human breast tumours Oncogene 1994, 9 (8) 2383-90 (Pubitemid 24228691)
    • (1994) Oncogene , vol.9 , Issue.8 , pp. 2383-2390
    • Mitchell, P.J.1    Barker, K.T.2    Martindale, J.E.3    Kamalati, T.4    Lowe, P.N.5    Page, M.J.6    Gusterson, B.A.7    Crompton, M.R.8
  • 73
    • 0034676337 scopus 로고    scopus 로고
    • Expression of the BRK tyrosine kinase in mammary epithelial cells enhances the coupling of EGF signalling to PI 3-kinase and Akt, via erbB3 phosphorylation
    • DOI 10.1038/sj.onc.1203931
    • Kamalati, T.; Jolin, H. E.; Fry, M. J.; Crompton, M. R. Expression of the BRK tyrosine kinase in mammary epithelial cells enhances the coupling of EGF signalling to PI 3-kinase and Akt, via erbB3 phosphorylation Oncogene 2000, 19 (48) 5471-6 (Pubitemid 32000914)
    • (2000) Oncogene , vol.19 , Issue.48 , pp. 5471-5476
    • Kamalati, T.1    Jolin, H.E.2    Fry, M.J.3    Crompton, M.R.4
  • 75
    • 0037046580 scopus 로고    scopus 로고
    • Identification of a factor that links apoptotic cells to phagocytes
    • DOI 10.1038/417182a
    • Hanayama, R.; Tanaka, M.; Miwa, K.; Shinohara, A.; Iwamatsu, A.; Nagata, S. Identification of a factor that links apoptotic cells to phagocytes Nature 2002, 417 (6885) 182-7 (Pubitemid 34506799)
    • (2002) Nature , vol.417 , Issue.6885 , pp. 182-187
    • Hanayama, R.1    Tanaka, M.2    Miwa, K.3    Shinohara, A.4    Iwamatsu, A.5    Nagata, S.6
  • 76
    • 0036223585 scopus 로고    scopus 로고
    • Bacillus subtilis functional genomics: Global characterization of the stringent response by proteome and transcriptome analysis
    • DOI 10.1128/JB.184.9.2500-2520.2002
    • Eymann, C.; Homuth, G.; Scharf, C.; Hecker, M. Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis J. Bacteriol. 2002, 184 (9) 2500-20 (Pubitemid 34311144)
    • (2002) Journal of Bacteriology , vol.184 , Issue.9 , pp. 2500-2520
    • Eymann, C.1    Homuth, G.2    Scharf, C.3    Hecker, M.4
  • 78
    • 3943111519 scopus 로고    scopus 로고
    • Activity of Staphylococcus epidermidis phenol-soluble modulin peptides expressed in Staphylococcus carnosus
    • DOI 10.1086/422157
    • Otto, M.; O'Mahoney, D. S.; Guina, T.; Klebanoff, S. J. Activity of Staphylococcus epidermidis phenol-soluble modulin peptides expressed in Staphylococcus carnosus J. Infect. Dis. 2004, 190 (4) 748-55 (Pubitemid 39050005)
    • (2004) Journal of Infectious Diseases , vol.190 , Issue.4 , pp. 748-755
    • Otto, M.1    O'Mahoney, D.S.2    Guina, T.3    Klebanoff, S.J.4
  • 79
    • 0033559244 scopus 로고    scopus 로고
    • An inflammatory polypeptide complex from Staphylococcus epidermidis: Isolation and characterization
    • Mehlin, C.; Headley, C. M.; Klebanoff, S. J. An inflammatory polypeptide complex from Staphylococcus epidermidis: isolation and characterization J. Exp. Med. 1999, 189 (6) 907-18
    • (1999) J. Exp. Med. , vol.189 , Issue.6 , pp. 907-18
    • Mehlin, C.1    Headley, C.M.2    Klebanoff, S.J.3
  • 81
    • 67649401960 scopus 로고    scopus 로고
    • Transcriptome and functional analysis of the eukaryotic-type serine/threonine kinase PknB in Staphylococcus aureus
    • Donat, S.; Streker, K.; Schirmeister, T.; Rakette, S.; Stehle, T.; Liebeke, M.; Lalk, M.; Ohlsen, K. Transcriptome and functional analysis of the eukaryotic-type serine/threonine kinase PknB in Staphylococcus aureus J. Bacteriol. 2009, 191 (13) 4056-69
    • (2009) J. Bacteriol. , vol.191 , Issue.13 , pp. 4056-69
    • Donat, S.1    Streker, K.2    Schirmeister, T.3    Rakette, S.4    Stehle, T.5    Liebeke, M.6    Lalk, M.7    Ohlsen, K.8
  • 82
    • 78449267357 scopus 로고    scopus 로고
    • A novel staphylococcal internalization mechanism involves the major autolysin Atl and heat shock cognate protein Hsc70 as host cell receptor
    • Hirschhausen, N.; Schlesier, T.; Schmidt, M. A.; Gotz, F.; Peters, G.; Heilmann, C. A novel staphylococcal internalization mechanism involves the major autolysin Atl and heat shock cognate protein Hsc70 as host cell receptor Cell Microbio.l 2010, 12 (12) 1746-64
    • (2010) Cell Microbio.l , vol.12 , Issue.12 , pp. 1746-64
    • Hirschhausen, N.1    Schlesier, T.2    Schmidt, M.A.3    Gotz, F.4    Peters, G.5    Heilmann, C.6
  • 83
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa, F. Discovery of the heat shock response Cell Stress Chaperones 1996, 1 (2) 97-8
    • (1996) Cell Stress Chaperones , vol.1 , Issue.2 , pp. 97-8
    • Ritossa, F.1
  • 85
    • 0037087398 scopus 로고    scopus 로고
    • Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs
    • Panjwani, N. N.; Popova, L.; Srivastava, P. K. Heat shock proteins gp96 and hsp70 activate the release of nitric oxide by APCs J. Immunol. 2002, 168 (6) 2997-3003 (Pubitemid 34211681)
    • (2002) Journal of Immunology , vol.168 , Issue.6 , pp. 2997-3003
    • Panjwani, N.N.1    Popova, L.2    Srivastava, P.K.3
  • 86
    • 0030775140 scopus 로고    scopus 로고
    • Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity
    • DOI 10.1084/jem.186.8.1315
    • Blachere, N. E.; Li, Z.; Chandawarkar, R. Y.; Suto, R.; Jaikaria, N. S.; Basu, S.; Udono, H.; Srivastava, P. K. Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity J. Exp. Med. 1997, 186 (8) 1315-22 (Pubitemid 27469027)
    • (1997) Journal of Experimental Medicine , vol.186 , Issue.8 , pp. 1315-1322
    • Blachere, N.E.1    Li, Z.2    Chandawarkar, R.Y.3    Suto, R.4    Jaikaria, N.S.5    Basu, S.6    Udono, H.7    Srivastava, P.K.8
  • 87
    • 0038500959 scopus 로고    scopus 로고
    • Toll-like receptor ligand links innate and adaptive immune responses by the production of heat-shock proteins
    • DOI 10.1189/jlb.0902470
    • Kumaraguru, U.; Pack, C. D.; Rouse, B. T. Toll-like receptor ligand links innate and adaptive immune responses by the production of heat-shock proteins J. Leukocyte Biol. 2003, 73 (5) 574-83 (Pubitemid 38040469)
    • (2003) Journal of Leukocyte Biology , vol.73 , Issue.5 , pp. 574-583
    • Kumaraguru, U.1    Pack, C.D.2    Rouse, B.T.3
  • 88
    • 0033791977 scopus 로고    scopus 로고
    • Staphylococcal fibronectin binding protein interacts with heat shock protein 60 and integrins: Role in internalization by epithelial cells
    • Dziewanowska, K.; Carson, A. R.; Patti, J. M.; Deobald, C. F.; Bayles, K. W.; Bohach, G. A. Staphylococcal fibronectin binding protein interacts with heat shock protein 60 and integrins: role in internalization by epithelial cells Infect. Immun. 2000, 68 (11) 6321-8
    • (2000) Infect. Immun. , vol.68 , Issue.11 , pp. 6321-8
    • Dziewanowska, K.1    Carson, A.R.2    Patti, J.M.3    Deobald, C.F.4    Bayles, K.W.5    Bohach, G.A.6
  • 90
    • 0031058967 scopus 로고    scopus 로고
    • Histone H1 expression varies during the Leishmania major life cycle
    • DOI 10.1016/S0166-6851(96)02801-0, PII S0166685196028010
    • Noll, T. M.; Desponds, C.; Belli, S. I.; Glaser, T. A.; Fasel, N. J. Histone H1 expression varies during the Leishmania major life cycle Mol. Biochem. Parasitol. 1997, 84 (2) 215-27 (Pubitemid 27092984)
    • (1997) Molecular and Biochemical Parasitology , vol.84 , Issue.2 , pp. 215-227
    • Noll, T.M.1    Desponds, C.2    Belli, S.I.3    Glaser, T.A.4    Fasel, N.J.5
  • 91
    • 0032704475 scopus 로고    scopus 로고
    • The protective capacities of histone H1 against experimental murine cutaneous leishmaniasis
    • Solioz, N.; Blum-Tirouvanziam, U.; Jacquet, R.; Rafati, S.; Corradin, G.; Mauel, J.; Fasel, N. The protective capacities of histone H1 against experimental murine cutaneous leishmaniasis Vaccine 1999, 18 (9-10) 850-9
    • (1999) Vaccine , vol.18 , Issue.9-10 , pp. 850-859
    • Solioz, N.1    Blum-Tirouvanziam, U.2    Jacquet, R.3    Rafati, S.4    Corradin, G.5    Mauel, J.6    Fasel, N.7
  • 94
    • 32944465559 scopus 로고    scopus 로고
    • DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps
    • DOI 10.1016/j.cub.2005.12.039, PII S0960982206010219
    • Buchanan, J. T.; Simpson, A. J.; Aziz, R. K.; Liu, G. Y.; Kristian, S. A.; Kotb, M.; Feramisco, J.; Nizet, V. DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps Curr. Biol. 2006, 16 (4) 396-400 (Pubitemid 43259350)
    • (2006) Current Biology , vol.16 , Issue.4 , pp. 396-400
    • Buchanan, J.T.1    Simpson, A.J.2    Aziz, R.K.3    Liu, G.Y.4    Kristian, S.A.5    Kotb, M.6    Feramisco, J.7    Nizet, V.8
  • 95
    • 32944482526 scopus 로고    scopus 로고
    • An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps
    • DOI 10.1016/j.cub.2006.01.056, PII S0960982206011079
    • Beiter, K.; Wartha, F.; Albiger, B.; Normark, S.; Zychlinsky, A.; Henriques-Normark, B. An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps Curr. Biol. 2006, 16 (4) 401-7 (Pubitemid 43259351)
    • (2006) Current Biology , vol.16 , Issue.4 , pp. 401-407
    • Beiter, K.1    Wartha, F.2    Albiger, B.3    Normark, S.4    Zychlinsky, A.5    Henriques-Normark, B.6
  • 97
    • 72449139059 scopus 로고    scopus 로고
    • Surface-exposed histone-like protein a modulates adherence of Streptococcus gallolyticus to colon adenocarcinoma cells
    • Boleij, A.; Schaeps, R. M.; de Kleijn, S.; Hermans, P. W.; Glaser, P.; Pancholi, V.; Swinkels, D. W.; Tjalsma, H. Surface-exposed histone-like protein a modulates adherence of Streptococcus gallolyticus to colon adenocarcinoma cells Infect. Immun. 2009, 77 (12) 5519-27
    • (2009) Infect. Immun. , vol.77 , Issue.12 , pp. 5519-27
    • Boleij, A.1    Schaeps, R.M.2    De Kleijn, S.3    Hermans, P.W.4    Glaser, P.5    Pancholi, V.6    Swinkels, D.W.7    Tjalsma, H.8


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