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Volumn 9, Issue 4, 2007, Pages 861-874

Degradation of p22phox and inhibition of superoxide generation by Ehrlichia chaffeensis in human monocytes

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CELL SURFACE PROTEIN; HEMIN; HYDROGEN PEROXIDE; LIPOPOLYSACCHARIDE; OXYGEN; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN P22 PHOX; PROTEINASE INHIBITOR; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SUPEROXIDE; TRYPSIN; UNCLASSIFIED DRUG; CYBA PROTEIN, HUMAN; CYBB PROTEIN, HUMAN; MEMBRANE PROTEIN;

EID: 33947101530     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2006.00835.x     Document Type: Article
Times cited : (39)

References (52)
  • 1
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • Babior, B.M. (1999) NADPH oxidase: An update. Blood 93: 1464-1476.
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 2
    • 0034655260 scopus 로고    scopus 로고
    • Cutting edge: Infection by the agent of human granulocytic ehrlichiosis prevents the respiratory burst by down-regulating gp91 phox
    • Banerjee, R., Anguita, J., Roos, D., and Fikrig, E. (2000) Cutting edge: infection by the agent of human granulocytic ehrlichiosis prevents the respiratory burst by down-regulating gp91 phox. J Immunol 164: 3946-3949.
    • (2000) J Immunol , vol.164 , pp. 3946-3949
    • Banerjee, R.1    Anguita, J.2    Roos, D.3    Fikrig, E.4
  • 3
    • 0027938009 scopus 로고
    • Abrogation of gamma interferon-induced inhibition of Ehrlichia chaffeensis infection in human monocytes with iron-transferrin
    • Barnewall, R.E., and Rikihisa, Y. (1994) Abrogation of gamma interferon-induced inhibition of Ehrlichia chaffeensis infection in human monocytes with iron-transferrin. Infect Immun 62: 4804-4810.
    • (1994) Infect Immun , vol.62 , pp. 4804-4810
    • Barnewall, R.E.1    Rikihisa, Y.2
  • 4
    • 0030959591 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis inclusions are early endosomes which selectively accumulate transferrin receptor
    • Barnewall, R.E., Rikihisa, Y., and Lee, E.H. (1997) Ehrlichia chaffeensis inclusions are early endosomes which selectively accumulate transferrin receptor. Infect Immun 65: 1455-1461.
    • (1997) Infect Immun , vol.65 , pp. 1455-1461
    • Barnewall, R.E.1    Rikihisa, Y.2    Lee, E.H.3
  • 6
    • 18744367006 scopus 로고    scopus 로고
    • Insights into pathogen immune evasion mechanisms: Anaplasma phagocytophilum fails to induce an apoptosis differentiation program in human neutrophils
    • Borjesson, D.L., Kobayashi, S.D., Whitney, A.R., Voyich, J.M., Argue, C.M., and Deleo, F.R. (2005) Insights into pathogen immune evasion mechanisms: Anaplasma phagocytophilum fails to induce an apoptosis differentiation program in human neutrophils. J Immunol 174: 6364-6372.
    • (2005) J Immunol , vol.174 , pp. 6364-6372
    • Borjesson, D.L.1    Kobayashi, S.D.2    Whitney, A.R.3    Voyich, J.M.4    Argue, C.M.5    Deleo, F.R.6
  • 7
    • 0035910466 scopus 로고    scopus 로고
    • Phage display epitope mapping of human neutrophil flavocytochrome b558. Identification of two juxtaposed extracellular domains
    • Burritt, J.B., DeLeo, F.R., McDonald, C.L., Prigge, J.R., Dinauer, M.C., Nakamura, M., et al. (2001) Phage display epitope mapping of human neutrophil flavocytochrome b558. Identification of two juxtaposed extracellular domains. J Biol Chem 276: 2053-2061.
    • (2001) J Biol Chem , vol.276 , pp. 2053-2061
    • Burritt, J.B.1    DeLeo, F.R.2    McDonald, C.L.3    Prigge, J.R.4    Dinauer, M.C.5    Nakamura, M.6
  • 8
    • 33644836708 scopus 로고    scopus 로고
    • Mechanisms of evasion of neutrophil killing by Anaplasma phagocytophilum
    • Carlyon, J.A., and Fikrig, E. (2006) Mechanisms of evasion of neutrophil killing by Anaplasma phagocytophilum. Curr Opin Hematol 13: 28-33.
    • (2006) Curr Opin Hematol , vol.13 , pp. 28-33
    • Carlyon, J.A.1    Fikrig, E.2
  • 9
    • 0037114184 scopus 로고    scopus 로고
    • Repression of rac2 mRNA expression by Anaplasma phagocytophila is essential to the inhibition of superoxide production and bacterial proliferation
    • Carlyon, J.A., Chan, W.T., Galan, J., Roos, D., and Fikrig, E. (2002) Repression of rac2 mRNA expression by Anaplasma phagocytophila is essential to the inhibition of superoxide production and bacterial proliferation. J Immunol 169: 7009-7018.
    • (2002) J Immunol , vol.169 , pp. 7009-7018
    • Carlyon, J.A.1    Chan, W.T.2    Galan, J.3    Roos, D.4    Fikrig, E.5
  • 10
    • 3342959166 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum utilizes multiple host evasion mechanisms to thwart NADPH oxidase-mediated killing during neutrophil infection
    • Carlyon, J.A., Abdel-Latif, D., Pypaert, M., Lacy, P., and Fikrig, E. (2004) Anaplasma phagocytophilum utilizes multiple host evasion mechanisms to thwart NADPH oxidase-mediated killing during neutrophil infection. Infect Immun 72: 4772-4783.
    • (2004) Infect Immun , vol.72 , pp. 4772-4783
    • Carlyon, J.A.1    Abdel-Latif, D.2    Pypaert, M.3    Lacy, P.4    Fikrig, E.5
  • 11
    • 0025245629 scopus 로고
    • Molecular basis of interferon-gamma and lipopolysaccharide enhancement of phagocyte respiratory burst capability. Studies on the gene expression of several NADPH oxidase components
    • Cassatella, M.A., Bazzoni, F., Flynn, R.M., Dusi, S., Trinchieri, G., and Rossi, F. (1990) Molecular basis of interferon-gamma and lipopolysaccharide enhancement of phagocyte respiratory burst capability. Studies on the gene expression of several NADPH oxidase components. J Biol Chem 265: 20241-20246.
    • (1990) J Biol Chem , vol.265 , pp. 20241-20246
    • Cassatella, M.A.1    Bazzoni, F.2    Flynn, R.M.3    Dusi, S.4    Trinchieri, G.5    Rossi, F.6
  • 12
    • 0022355371 scopus 로고
    • Activation of the human neutrophil nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase by protein kinase C
    • Cox, J.A., Jeng, A.Y., Sharkey, N.A., Blumberg, P.M., and Tauber, A.I. (1985) Activation of the human neutrophil nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase by protein kinase C. J Clin Invest 76: 1932-1938.
    • (1985) J Clin Invest , vol.76 , pp. 1932-1938
    • Cox, J.A.1    Jeng, A.Y.2    Sharkey, N.A.3    Blumberg, P.M.4    Tauber, A.I.5
  • 13
    • 0343098557 scopus 로고
    • Measurement of luminol-dependent leukocyte chemiluminescence originated from intracellular and extracellular events
    • In Kricka, L.J., Stanley, P.E., Thorpe, G.H.G., and Whitehead, T.P. (eds). New York: Academic Press
    • Dahlgren, C., Briheim, G., and Stendahl, O. (1984) Measurement of luminol-dependent leukocyte chemiluminescence originated from intracellular and extracellular events. In Annals of Applied Bioluminescence Chemiluminescence: Proceedings. Kricka, L.J., Stanley, P.E., Thorpe, G.H.G., and Whitehead, T.P. (eds). New York: Academic Press, pp. 335-338.
    • (1984) Annals of Applied Bioluminescence Chemiluminescence: Proceedings , pp. 335-338
    • Dahlgren, C.1    Briheim, G.2    Stendahl, O.3
  • 15
    • 0032741371 scopus 로고    scopus 로고
    • NADPH oxidase activation and assembly during phagocytosis
    • DeLeo, F.R., Allen, L.A., Apicella, M., and Nauseef, W.M. (1999) NADPH oxidase activation and assembly during phagocytosis. J Immunol 163: 6732-6740.
    • (1999) J Immunol , vol.163 , pp. 6732-6740
    • DeLeo, F.R.1    Allen, L.A.2    Apicella, M.3    Nauseef, W.M.4
  • 16
    • 0034607821 scopus 로고    scopus 로고
    • Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly
    • DeLeo, F.R., Burritt, J.B., Yu, L., Jesaitis, A.J., Dinauer, M.C., and Nauseef, W.M. (2000) Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly. J Biol Chem 275: 13986-13993.
    • (2000) J Biol Chem , vol.275 , pp. 13986-13993
    • DeLeo, F.R.1    Burritt, J.B.2    Yu, L.3    Jesaitis, A.J.4    Dinauer, M.C.5    Nauseef, W.M.6
  • 18
    • 4844227764 scopus 로고    scopus 로고
    • Antimicrobial reactive oxygen and nitrogen species: Concepts and controversies
    • Fang, F.C. (2004) Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nat Rev Microbiol 2: 820-832.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 820-832
    • Fang, F.C.1
  • 19
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr, S.B., and Kogoma, T. (1991) Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol Rev 55: 561-585.
    • (1991) Microbiol Rev , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 20
    • 0030806863 scopus 로고    scopus 로고
    • Superoxide anion radical (O2-.), superoxide dismutases, and related matters
    • Fridovich, I. (1997) Superoxide anion radical (O2-.), superoxide dismutases, and related matters. J Biol Chem 272: 18515-18517.
    • (1997) J Biol Chem , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 21
    • 0021684935 scopus 로고
    • Priming of neutrophils for enhanced release of oxygen metabolites by bacterial lipopolysaccharide. Evidence for increased activity of the superoxide-producing enzyme
    • Guthrie, L.A., McPhail, L.C., Henson, P.M., and Johnston, R.B., Jr (1984) Priming of neutrophils for enhanced release of oxygen metabolites by bacterial lipopolysaccharide. Evidence for increased activity of the superoxide-producing enzyme. J Exp Med 160: 1656-1671.
    • (1984) J Exp Med , vol.160 , pp. 1656-1671
    • Guthrie, L.A.1    McPhail, L.C.2    Henson, P.M.3    Johnston Jr., R.B.4
  • 22
    • 0018604132 scopus 로고
    • Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical
    • Hassan, H.M., and Fridovich, I. (1979) Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. J Biol Chem 254: 10846-10852.
    • (1979) J Biol Chem , vol.254 , pp. 10846-10852
    • Hassan, H.M.1    Fridovich, I.2
  • 23
    • 0023281070 scopus 로고
    • Bacteria form intracellular free radicals in response to paraquat and streptonigrin. Demonstration of the potency of hydroxyl radical
    • Hassett, D.J., Britigan, B.E., Svendsen, T., Rosen, G.M., and Cohen, M.S. (1987) Bacteria form intracellular free radicals in response to paraquat and streptonigrin. Demonstration of the potency of hydroxyl radical. J Biol Chem 262: 13404-13408.
    • (1987) J Biol Chem , vol.262 , pp. 13404-13408
    • Hassett, D.J.1    Britigan, B.E.2    Svendsen, T.3    Rosen, G.M.4    Cohen, M.S.5
  • 24
    • 0026698104 scopus 로고
    • Coxiella burnetii superoxide dismutase gene: Cloning, sequencing, and expression in Escherichia coli
    • Heinzen, R.A., Frazier, M.E., and Mallavia, L.P. (1992) Coxiella burnetii superoxide dismutase gene: Cloning, sequencing, and expression in Escherichia coli. Infect Immun 60: 3814-3823.
    • (1992) Infect Immun , vol.60 , pp. 3814-3823
    • Heinzen, R.A.1    Frazier, M.E.2    Mallavia, L.P.3
  • 25
    • 33947111305 scopus 로고    scopus 로고
    • Evidence that the human granulocytic ehrlichiosis agent utilizes a novel oxygen radical detoxification system; cytochrome C re-oxidation
    • Abstract #50 Big Sky MN, USA In American Society for Rickettsiology -Bartonella as an Emerging Pathogen Group 2001 Joint Conference. Big Sky, MN, USA, Abstract #50
    • Herron, H.J., and Goodman, J.L. (2001) Evidence that the human granulocytic ehrlichiosis agent utilizes a novel oxygen radical detoxification system; cytochrome C re-oxidation. In American Society for Rickettsiology -Bartonella as an Emerging Pathogen Group 2001 Joint Conference. Big Sky, MN, USA, Abstract #50.
    • (2001)
    • Herron, H.J.1    Goodman, J.L.2
  • 26
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996) Ubiquitin-dependent protein degradation. Annu Rev Genet 30: 405-439.
    • (1996) Annu Rev Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 27
    • 4544382411 scopus 로고    scopus 로고
    • Neutrophil NADPH oxidase is reduced at the Anaplasma phagocytophilum phagosome
    • IJdo, J., and Mueller, A.C. (2004) Neutrophil NADPH oxidase is reduced at the Anaplasma phagocytophilum phagosome. Infect Immun 72: 5392-5401.
    • (2004) Infect Immun , vol.72 , pp. 5392-5401
    • IJdo, J.1    Mueller, A.C.2
  • 28
    • 0033945345 scopus 로고    scopus 로고
    • Regulation of Brucella abortus catalase
    • Kim, J.A., Sha, Z., and Mayfield, J.E. (2000) Regulation of Brucella abortus catalase. Infect Immun 68: 3861-3866.
    • (2000) Infect Immun , vol.68 , pp. 3861-3866
    • Kim, J.A.1    Sha, Z.2    Mayfield, J.E.3
  • 29
    • 0042825338 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival
    • Lin, M., and Rikihisa, Y. (2003) Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival. Infect Immun 71: 5324-5331.
    • (2003) Infect Immun , vol.71 , pp. 5324-5331
    • Lin, M.1    Rikihisa, Y.2
  • 30
    • 1642473014 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis downregulates surface Toll-like receptors 2/4, CD14 and transcription factors PU.1 and inhibits lipopolysaccharide activation of NF-κB, ERK 1/2 and p38 MAPK in host monocytes
    • Lin, M., and Rikihisa, Y. (2004) Ehrlichia chaffeensis downregulates surface Toll-like receptors 2/4, CD14 and transcription factors PU.1 and inhibits lipopolysaccharide activation of NF-κB, ERK 1/2 and p38 MAPK in host monocytes. Cell Microbiol 6: 175-186.
    • (2004) Cell Microbiol , vol.6 , pp. 175-186
    • Lin, M.1    Rikihisa, Y.2
  • 31
    • 0036150092 scopus 로고    scopus 로고
    • Rapid activation of protein tyrosine kinase and phospholipase C-γ2 and increase in cytosolic free calcium are required by Ehrlichia chaffeensis for internalization and growth in THP-1 cells
    • Lin, M., Zhu, M.X., and Rikihisa, Y. (2002) Rapid activation of protein tyrosine kinase and phospholipase C-γ2 and increase in cytosolic free calcium are required by Ehrlichia chaffeensis for internalization and growth in THP-1 cells. Infect Immun 70: 889-898.
    • (2002) Infect Immun , vol.70 , pp. 889-898
    • Lin, M.1    Zhu, M.X.2    Rikihisa, Y.3
  • 32
    • 0035448083 scopus 로고    scopus 로고
    • Inhibition of the neutrophil NADPH oxidase and associated H+ channel by diethyl pyrocarbonate (DEPC), a histidine-modifying agent: Evidence for at least two target sites
    • Mankelow, T.J., and Henderson, L.M. (2001) Inhibition of the neutrophil NADPH oxidase and associated H+ channel by diethyl pyrocarbonate (DEPC), a histidine-modifying agent: Evidence for at least two target sites. Biochem J 358: 315-324.
    • (2001) Biochem J , vol.358 , pp. 315-324
    • Mankelow, T.J.1    Henderson, L.M.2
  • 33
    • 0022930671 scopus 로고
    • A demonstration that O2- is a crucial intermediate in the high quantum yield luminescence of luminol
    • Miller, E.K., and Fridovich, I. (1986) A demonstration that O2- is a crucial intermediate in the high quantum yield luminescence of luminol. J Free Radic Biol Med 2: 107-110.
    • (1986) J Free Radic Biol Med , vol.2 , pp. 107-110
    • Miller, E.K.1    Fridovich, I.2
  • 34
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxidants in microbial pathophysiology
    • Miller, R.A., and Britigan, B.E. (1997) Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10: 1-18.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 35
    • 0034442469 scopus 로고    scopus 로고
    • Human granulocytic ehrlichiosis agent inhibits superoxide anion generation by human neutrophils
    • Mott, J., and Rikihisa, Y. (2000) Human granulocytic ehrlichiosis agent inhibits superoxide anion generation by human neutrophils. Infect Immun 68: 6697-6703.
    • (2000) Infect Immun , vol.68 , pp. 6697-6703
    • Mott, J.1    Rikihisa, Y.2
  • 36
    • 0033009747 scopus 로고    scopus 로고
    • Human granulocytic ehrlichiosis agent and Ehrlichia chaffeensis reside in different cytoplasmic compartments in HL-60 cells
    • Mott, J., Barnewall, R.E., and Rikihisa, Y. (1999) Human granulocytic ehrlichiosis agent and Ehrlichia chaffeensis reside in different cytoplasmic compartments in HL-60 cells. Infect Immun 67: 1368-1378.
    • (1999) Infect Immun , vol.67 , pp. 1368-1378
    • Mott, J.1    Barnewall, R.E.2    Rikihisa, Y.3
  • 37
    • 0036181922 scopus 로고    scopus 로고
    • Effects of Anaplasma phagocytophila on NADPH oxidase components in human neutrophils and HL-60 cells
    • Mott, J., Rikihisa, Y., and Tsunawaki, S. (2002) Effects of Anaplasma phagocytophila on NADPH oxidase components in human neutrophils and HL-60 cells. Infect Immun 70: 1359-1366.
    • (2002) Infect Immun , vol.70 , pp. 1359-1366
    • Mott, J.1    Rikihisa, Y.2    Tsunawaki, S.3
  • 38
    • 0023198590 scopus 로고
    • Monoclonal antibody 7D5 raised to cytochrome b558 of human neutrophils: Immunocytochemical detection of the antigen in peripheral phagocytes of normal subjects, patients with chronic granulomatous disease, and their carrier mothers
    • Nakamura, M., Murakami, M., Koga, T., Tanaka, Y., and Minakami, S. (1987) Monoclonal antibody 7D5 raised to cytochrome b558 of human neutrophils: Immunocytochemical detection of the antigen in peripheral phagocytes of normal subjects, patients with chronic granulomatous disease, and their carrier mothers. Blood 69: 1404-1408.
    • (1987) Blood , vol.69 , pp. 1404-1408
    • Nakamura, M.1    Murakami, M.2    Koga, T.3    Tanaka, Y.4    Minakami, S.5
  • 39
    • 0028999362 scopus 로고
    • Reconstitution of flavin-depleted neutrophil flavocytochrome b558 with 8-mercapto-FAD and characterization of the flavin-reconstituted enzyme
    • Nisimoto, Y., Otsuka-Murakami, H., and Lambeth, D.J. (1995) Reconstitution of flavin-depleted neutrophil flavocytochrome b558 with 8-mercapto-FAD and characterization of the flavin-reconstituted enzyme. J Biol Chem 270: 16428-16434.
    • (1995) J Biol Chem , vol.270 , pp. 16428-16434
    • Nisimoto, Y.1    Otsuka-Murakami, H.2    Lambeth, D.J.3
  • 40
    • 0036126936 scopus 로고    scopus 로고
    • Characterization and transcriptional analysis of gene clusters for a type IV secretion machinery in human granulocytic and monocytic ehrlichiosis agents
    • Ohashi, N., Zhi, N., Lin, Q., and Rikihisa, Y. (2002) Characterization and transcriptional analysis of gene clusters for a type IV secretion machinery in human granulocytic and monocytic ehrlichiosis agents. Infect Immun 70: 2128-2138.
    • (2002) Infect Immun , vol.70 , pp. 2128-2138
    • Ohashi, N.1    Zhi, N.2    Lin, Q.3    Rikihisa, Y.4
  • 41
    • 0018899419 scopus 로고
    • Increased production of superoxide anion by macrophages exposed in vitro to muramyl dipeptide or lipopolysaccharide
    • Pabst, M.J., and Johnston, R.B., Jr (1980) Increased production of superoxide anion by macrophages exposed in vitro to muramyl dipeptide or lipopolysaccharide. J Exp Med 151: 101-114.
    • (1980) J Exp Med , vol.151 , pp. 101-114
    • Pabst, M.J.1    Johnston Jr., R.B.2
  • 42
    • 0037240533 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis: A prototypical emerging pathogen
    • Paddock, C.D., and Childs, J.E. (2003) Ehrlichia chaffeensis: A prototypical emerging pathogen. Clin Microbiol Rev 16: 37-64.
    • (2003) Clin Microbiol Rev , vol.16 , pp. 37-64
    • Paddock, C.D.1    Childs, J.E.2
  • 43
    • 28444478749 scopus 로고    scopus 로고
    • Leishmania pifanoi amastigotes avoid macrophage production of superoxide by inducing heme degradation
    • Pham, N.-K., Mouriz, J., and Kima, P.E. (2005) Leishmania pifanoi amastigotes avoid macrophage production of superoxide by inducing heme degradation. Infect Immun 73: 8322-8333.
    • (2005) Infect Immun , vol.73 , pp. 8322-8333
    • Pham, N.-K.1    Mouriz, J.2    Kima, P.E.3
  • 44
    • 0037972836 scopus 로고    scopus 로고
    • Mechanisms to create a safe haven by members of the family Anaplasmataceae
    • Rikihisa, Y. (2003) Mechanisms to create a safe haven by members of the family Anaplasmataceae. Annals NY Acad Sci 990: 548-555.
    • (2003) Annals NY Acad Sci , vol.990 , pp. 548-555
    • Rikihisa, Y.1
  • 45
    • 31844445394 scopus 로고    scopus 로고
    • Ehrlichia subversion of host innate responses
    • Rikihisa, Y. (2006) Ehrlichia subversion of host innate responses. Curr Opin Microbiol 9: 95-101.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 95-101
    • Rikihisa, Y.1
  • 46
    • 0031015273 scopus 로고    scopus 로고
    • Ultrastructural and antigenic characterization of a granulocytic ehrlichiosis agent directly isolated and stably cultivated from a patient in New York state
    • Rikihisa, Y., Zhi, N., Wormser, G.P., Wen, B., Horowitz, H.W., and Hechemy, K.E. (1997) Ultrastructural and antigenic characterization of a granulocytic ehrlichiosis agent directly isolated and stably cultivated from a patient in New York state. J Infect Dis 175: 210-213.
    • (1997) J Infect Dis , vol.175 , pp. 210-213
    • Rikihisa, Y.1    Zhi, N.2    Wormser, G.P.3    Wen, B.4    Horowitz, H.W.5    Hechemy, K.E.6
  • 47
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver, L.C., and Imlay, J.A. (2001) Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J Bacteriol 183: 7173-7181.
    • (2001) J Bacteriol , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 48
    • 3142581994 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 inhibits NAD(P)H oxidase activity by down-regulating cytochrome b558 expression via the reduction of heme availability
    • Taille, C., El-Benna, J., Lanone, S., Dang, M.C., Ogier-Denis, E., Aubier, M., and Boczkowski, J. (2004) Induction of heme oxygenase-1 inhibits NAD(P)H oxidase activity by down-regulating cytochrome b558 expression via the reduction of heme availability. J Biol Chem 279: 28681-28688.
    • (2004) J Biol Chem , vol.279 , pp. 28681-28688
    • Taille, C.1    El-Benna, J.2    Lanone, S.3    Dang, M.C.4    Ogier-Denis, E.5    Aubier, M.6    Boczkowski, J.7
  • 49
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • Underhill, D.M., and Ozinsky, A. (2002) Phagocytosis of microbes: complexity in action. Annu Rev Immunol 20: 825-852.
    • (2002) Annu Rev Immunol , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 50
    • 0037099157 scopus 로고    scopus 로고
    • Superoxide anion production during Anaplasma phagocytophila infection
    • Wang, T., Malawista, S.E., Pal, U., Grey, M., Meek, J., Akkoyunlu, M., etal. (2002) Superoxide anion production during Anaplasma phagocytophila infection. J Infect Dis 186: 274-280.
    • (2002) J Infect Dis , vol.186 , pp. 274-280
    • Wang, T.1    Malawista, S.E.2    Pal, U.3    Grey, M.4    Meek, J.5    Akkoyunlu, M.6
  • 51
    • 0028510456 scopus 로고
    • Respiratory burst activity associated with phagocytosis of Ehrlichia risticii by mouse peritoneal macrophages
    • Williams, N.M., Cross, R.J., and Timoney, P.J. (1994) Respiratory burst activity associated with phagocytosis of Ehrlichia risticii by mouse peritoneal macrophages. Res Vet Sci 57: 194-199.
    • (1994) Res Vet Sci , vol.57 , pp. 194-199
    • Williams, N.M.1    Cross, R.J.2    Timoney, P.J.3
  • 52
    • 0030827909 scopus 로고    scopus 로고
    • Biosynthesis of the phagocyte NADPH oxidase cytochrome b558. Role of heme incorporation and heterodimer formation in maturation and stability of gp91phox and p22phox subunits
    • Yu, L., Zhen, L., and Dinauer, M.C. (1997) Biosynthesis of the phagocyte NADPH oxidase cytochrome b558. Role of heme incorporation and heterodimer formation in maturation and stability of gp91phox and p22phox subunits. J Biol Chem 272: 27288-27294.
    • (1997) J Biol Chem , vol.272 , pp. 27288-27294
    • Yu, L.1    Zhen, L.2    Dinauer, M.C.3


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