메뉴 건너뛰기




Volumn 8, Issue 5, 2012, Pages

Extracellular superoxide dismutase protects Histoplasma yeast cells from host-derived oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; CYTOKINE; EXTRACELLULAR SUPEROXIDE DISMUTASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; SMALL INTERFERING RNA; SUPEROXIDE DISMUTASE;

EID: 84863692804     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002713     Document Type: Article
Times cited : (123)

References (78)
  • 1
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay JA, (2003) Pathways of oxidative damage. Annu Rev Microbiol 57: 395-418.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 2
    • 0022393848 scopus 로고
    • Molecular basis for the enhanced respiratory burst of activated macrophages
    • Johnston RB Jr, Kitagawa S, (1985) Molecular basis for the enhanced respiratory burst of activated macrophages. Fed Proc 44: 2927-2932.
    • (1985) Fed Proc , vol.44 , pp. 2927-2932
    • Johnston Jr., R.B.1    Kitagawa, S.2
  • 3
    • 0021928078 scopus 로고
    • Activation of mouse peritoneal macrophages in vitro and in vivo by interferon-gamma
    • Murray HW, Spitalny GL, Nathan CF, (1985) Activation of mouse peritoneal macrophages in vitro and in vivo by interferon-gamma. J Immunol 134: 1619-1622.
    • (1985) J Immunol , vol.134 , pp. 1619-1622
    • Murray, H.W.1    Spitalny, G.L.2    Nathan, C.F.3
  • 4
    • 0015059322 scopus 로고
    • The medical mycological iceberg
    • Ajello L, (1971) The medical mycological iceberg. HSMHA Health Rep 86: 437-448.
    • (1971) HSMHA Health Rep , vol.86 , pp. 437-448
    • Ajello, L.1
  • 5
    • 0025105115 scopus 로고
    • The intracellular fate of Histoplasma capsulatum in human macrophages is unaffected by recombinant human interferon-gamma
    • Fleischmann J, Wu-Hsieh B, Howard DH, (1990) The intracellular fate of Histoplasma capsulatum in human macrophages is unaffected by recombinant human interferon-gamma. J Infect Dis 161: 143-145.
    • (1990) J Infect Dis , vol.161 , pp. 143-145
    • Fleischmann, J.1    Wu-Hsieh, B.2    Howard, D.H.3
  • 6
    • 0028862107 scopus 로고
    • Antifungal mechanisms of activated murine bronchoalveolar or peritoneal macrophages for Histoplasma capsulatum
    • Brummer E, Stevens DA, (1995) Antifungal mechanisms of activated murine bronchoalveolar or peritoneal macrophages for Histoplasma capsulatum. Clin Exp Immunol 102: 65-70.
    • (1995) Clin Exp Immunol , vol.102 , pp. 65-70
    • Brummer, E.1    Stevens, D.A.2
  • 7
    • 0025099677 scopus 로고
    • Phagocytosis of Histoplasma capsulatum yeasts and microconidia by human cultured macrophages and alveolar macrophages. Cellular cytoskeleton requirement for attachment and ingestion
    • Newman SL, Bucher C, Rhodes J, Bullock WE, (1990) Phagocytosis of Histoplasma capsulatum yeasts and microconidia by human cultured macrophages and alveolar macrophages. Cellular cytoskeleton requirement for attachment and ingestion. J Clin Invest 85: 223-230.
    • (1990) J Clin Invest , vol.85 , pp. 223-230
    • Newman, S.L.1    Bucher, C.2    Rhodes, J.3    Bullock, W.E.4
  • 9
    • 0009038048 scopus 로고    scopus 로고
    • Pulmonary histoplasmosis
    • Kauffman CA, (2001) Pulmonary histoplasmosis. Curr Infect Dis Rep 3: 279-285.
    • (2001) Curr Infect Dis Rep , vol.3 , pp. 279-285
    • Kauffman, C.A.1
  • 10
    • 0023078585 scopus 로고
    • Histoplasma capsulatum fails to trigger release of superoxide from macrophages
    • Eissenberg LG, Goldman WE, (1987) Histoplasma capsulatum fails to trigger release of superoxide from macrophages. Infect Immun 55: 29-34.
    • (1987) Infect Immun , vol.55 , pp. 29-34
    • Eissenberg, L.G.1    Goldman, W.E.2
  • 11
    • 0023093781 scopus 로고
    • Modulation of the macrophage oxidative burst by Histoplasma capsulatum
    • Wolf JE, Kerchberger V, Kobayashi GS, Little JR, (1987) Modulation of the macrophage oxidative burst by Histoplasma capsulatum. J Immunol 138: 582-586.
    • (1987) J Immunol , vol.138 , pp. 582-586
    • Wolf, J.E.1    Kerchberger, V.2    Kobayashi, G.S.3    Little, J.R.4
  • 12
    • 0025355997 scopus 로고
    • In vivo activation of macrophage oxidative burst activity by cytokines and amphotericin B
    • Wolf JE, Massof SE, (1990) In vivo activation of macrophage oxidative burst activity by cytokines and amphotericin B. Infect Immun 58: 1296-1300.
    • (1990) Infect Immun , vol.58 , pp. 1296-1300
    • Wolf, J.E.1    Massof, S.E.2
  • 13
    • 0024529069 scopus 로고
    • Effects of Histoplasma capsulatum on murine macrophage functions: inhibition of macrophage priming, oxidative burst, and antifungal activities
    • Wolf JE, Abegg AL, Travis SJ, Kobayashi GS, Little JR, (1989) Effects of Histoplasma capsulatum on murine macrophage functions: inhibition of macrophage priming, oxidative burst, and antifungal activities. Infect Immun 57: 513-519.
    • (1989) Infect Immun , vol.57 , pp. 513-519
    • Wolf, J.E.1    Abegg, A.L.2    Travis, S.J.3    Kobayashi, G.S.4    Little, J.R.5
  • 14
    • 0022445380 scopus 로고
    • The pathogenesis of experimental pulmonary histoplasmosis. Correlative studies of histopathology, bronchoalveolar lavage, and respiratory function
    • Baughman RP, Kim CK, Vinegar A, Hendricks DE, Schmidt DJ, et al. (1986) The pathogenesis of experimental pulmonary histoplasmosis. Correlative studies of histopathology, bronchoalveolar lavage, and respiratory function. Am Rev Respir Dis 134: 771-776.
    • (1986) Am Rev Respir Dis , vol.134 , pp. 771-776
    • Baughman, R.P.1    Kim, C.K.2    Vinegar, A.3    Hendricks, D.E.4    Schmidt, D.J.5
  • 15
    • 50849090978 scopus 로고    scopus 로고
    • Histoplasma capsulatum manifests preferential invasion of phagocytic subpopulations in murine lungs
    • Deepe GS Jr, Gibbons RS, Smulian AG, (2008) Histoplasma capsulatum manifests preferential invasion of phagocytic subpopulations in murine lungs. J Leukocyte Biol 84: 669-678.
    • (2008) J Leukocyte Biol , vol.84 , pp. 669-678
    • Deepe Jr., G.S.1    Gibbons, R.S.2    Smulian, A.G.3
  • 16
    • 0025363271 scopus 로고
    • The respiratory burst response to Histoplasma capsulatum by human neutrophils. Evidence for intracellular trapping of superoxide anion
    • Schnur RA, Newman SL, (1990) The respiratory burst response to Histoplasma capsulatum by human neutrophils. Evidence for intracellular trapping of superoxide anion. J Immunol 144: 4765-4772.
    • (1990) J Immunol , vol.144 , pp. 4765-4772
    • Schnur, R.A.1    Newman, S.L.2
  • 17
    • 0025883361 scopus 로고
    • Antifungal activity of murine polymorphonuclear neutrophils against Histoplasma capsulatum
    • Kurita N, Brummer E, Yoshida S, Nishimura K, Miyaji M, (1991) Antifungal activity of murine polymorphonuclear neutrophils against Histoplasma capsulatum. J Med Vet Mycol 29: 133-143.
    • (1991) J Med Vet Mycol , vol.29 , pp. 133-143
    • Kurita, N.1    Brummer, E.2    Yoshida, S.3    Nishimura, K.4    Miyaji, M.5
  • 18
    • 0026218419 scopus 로고
    • Resistance of Histoplasma capsulatum to killing by human neutrophils. Evasion of oxidative burst and lysosomal-fusion products
    • Kurita N, Terao K, Brummer E, Ito E, Nishimura K, et al. (1991) Resistance of Histoplasma capsulatum to killing by human neutrophils. Evasion of oxidative burst and lysosomal-fusion products. Mycopathologia 115: 207-213.
    • (1991) Mycopathologia , vol.115 , pp. 207-213
    • Kurita, N.1    Terao, K.2    Brummer, E.3    Ito, E.4    Nishimura, K.5
  • 19
    • 0022447847 scopus 로고
    • In vitro susceptibility of fungi to killing by neutrophil granulocytes discriminates between primary pathogenicity and opportunism
    • Schaffner A, Davis CE, Schaffner T, Markert M, Douglas H, et al. (1986) In vitro susceptibility of fungi to killing by neutrophil granulocytes discriminates between primary pathogenicity and opportunism. J Clin Invest 78: 511-524.
    • (1986) J Clin Invest , vol.78 , pp. 511-524
    • Schaffner, A.1    Davis, C.E.2    Schaffner, T.3    Markert, M.4    Douglas, H.5
  • 20
    • 0025998936 scopus 로고
    • Fungistatic activity of human neutrophils against Histoplasma capsulatum: correlation with phagocytosis
    • Brummer E, Kurita N, Yosihida S, Nishimura K, Miyaji M, (1991) Fungistatic activity of human neutrophils against Histoplasma capsulatum: correlation with phagocytosis. J Infect Dis 164: 158-162.
    • (1991) J Infect Dis , vol.164 , pp. 158-162
    • Brummer, E.1    Kurita, N.2    Yosihida, S.3    Nishimura, K.4    Miyaji, M.5
  • 21
    • 79953675108 scopus 로고    scopus 로고
    • Definition of the extracellular proteome of pathogenic-phase Histoplasma capsulatum
    • Holbrook ED, Edwards JA, Youseff BH, Rappleye CA, (2011) Definition of the extracellular proteome of pathogenic-phase Histoplasma capsulatum. J Proteome Res 10: 1929-1943.
    • (2011) J Proteome Res , vol.10 , pp. 1929-1943
    • Holbrook, E.D.1    Edwards, J.A.2    Youseff, B.H.3    Rappleye, C.A.4
  • 22
    • 0034680884 scopus 로고    scopus 로고
    • Intracellular parasitism by Histoplasma capsulatum: fungal virulence and calcium dependence
    • Sebghati TS, Engle JT, Goldman WE, (2000) Intracellular parasitism by Histoplasma capsulatum: fungal virulence and calcium dependence. Science 290: 1368-1372.
    • (2000) Science , vol.290 , pp. 1368-1372
    • Sebghati, T.S.1    Engle, J.T.2    Goldman, W.E.3
  • 23
    • 0033950664 scopus 로고    scopus 로고
    • A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1)
    • Peskin AV, Winterbourn CC, (2000) A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1). Clin Chim Acta 293: 157-166.
    • (2000) Clin Chim Acta , vol.293 , pp. 157-166
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 24
    • 20544439767 scopus 로고    scopus 로고
    • Features and functions of covalently linked proteins in fungal cell walls
    • De Groot PW, Ram AF, Klis FM, (2005) Features and functions of covalently linked proteins in fungal cell walls. Fungal Genet Biol 42: 657-675.
    • (2005) Fungal Genet Biol , vol.42 , pp. 657-675
    • De Groot, P.W.1    Ram, A.F.2    Klis, F.M.3
  • 25
    • 33947232747 scopus 로고    scopus 로고
    • Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae
    • Pittet M, Conzelmann A, (2007) Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1771: 405-420.
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 405-420
    • Pittet, M.1    Conzelmann, A.2
  • 26
    • 78651483688 scopus 로고    scopus 로고
    • The yeast-phase virulence requirement for alpha-glucan synthase differs among Histoplasma capsulatum chemotypes
    • Edwards JA, Alore EA, Rappleye CA, (2011) The yeast-phase virulence requirement for alpha-glucan synthase differs among Histoplasma capsulatum chemotypes. Eukaryot Cell 10: 87-97.
    • (2011) Eukaryot Cell , vol.10 , pp. 87-97
    • Edwards, J.A.1    Alore, E.A.2    Rappleye, C.A.3
  • 27
    • 0021288059 scopus 로고
    • Paraquat: model for oxidant-initiated toxicity
    • Bus JS, Gibson JE, (1984) Paraquat: model for oxidant-initiated toxicity. Environ Health Perspect 55: 37-46.
    • (1984) Environ Health Perspect , vol.55 , pp. 37-46
    • Bus, J.S.1    Gibson, J.E.2
  • 28
    • 38349105900 scopus 로고    scopus 로고
    • Complex I is the major site of mitochondrial superoxide production by paraquat
    • Cocheme HM, Murphy MP, (2008) Complex I is the major site of mitochondrial superoxide production by paraquat. J Biol Chem 283: 1786-1798.
    • (2008) J Biol Chem , vol.283 , pp. 1786-1798
    • Cocheme, H.M.1    Murphy, M.P.2
  • 29
    • 0025187370 scopus 로고
    • The use of diphenylene iodonium, an inhibitor of NADPH oxidase, to investigate the antimicrobial action of human monocyte derived macrophages
    • Robertson AK, Cross AR, Jones OT, Andrew PW, (1990) The use of diphenylene iodonium, an inhibitor of NADPH oxidase, to investigate the antimicrobial action of human monocyte derived macrophages. J Immunol Methods 133: 175-179.
    • (1990) J Immunol Methods , vol.133 , pp. 175-179
    • Robertson, A.K.1    Cross, A.R.2    Jones, O.T.3    Andrew, P.W.4
  • 30
    • 0023894234 scopus 로고
    • The effect of the NADPH oxidase inhibitor diphenyleneiodonium on aerobic and anaerobic microbicidal activities of human neutrophils
    • Ellis JA, Mayer SJ, Jones OT, (1988) The effect of the NADPH oxidase inhibitor diphenyleneiodonium on aerobic and anaerobic microbicidal activities of human neutrophils. Biochem J 251: 887-891.
    • (1988) Biochem J , vol.251 , pp. 887-891
    • Ellis, J.A.1    Mayer, S.J.2    Jones, O.T.3
  • 31
    • 0028984840 scopus 로고
    • The p47phox mouse knock-out model of chronic granulomatous disease
    • Jackson SH, Gallin JI, Holland SM, (1995) The p47phox mouse knock-out model of chronic granulomatous disease. J Exp Med 182: 751-758.
    • (1995) J Exp Med , vol.182 , pp. 751-758
    • Jackson, S.H.1    Gallin, J.I.2    Holland, S.M.3
  • 32
    • 0033802422 scopus 로고    scopus 로고
    • Identification of constituents of human neutrophil azurophil granules that mediate fungistasis against Histoplasma capsulatum
    • Newman SL, Gootee L, Gabay JE, Selsted ME, (2000) Identification of constituents of human neutrophil azurophil granules that mediate fungistasis against Histoplasma capsulatum. Infect Immun 68: 5668-5672.
    • (2000) Infect Immun , vol.68 , pp. 5668-5672
    • Newman, S.L.1    Gootee, L.2    Gabay, J.E.3    Selsted, M.E.4
  • 33
    • 0028362109 scopus 로고
    • Inhibition of intracellular Histoplasma capsulatum replication by murine macrophages that produce human defensin
    • Couto MA, Liu L, Lehrer RI, Ganz T, (1994) Inhibition of intracellular Histoplasma capsulatum replication by murine macrophages that produce human defensin. Infect Immun 62: 2375-2378.
    • (1994) Infect Immun , vol.62 , pp. 2375-2378
    • Couto, M.A.1    Liu, L.2    Lehrer, R.I.3    Ganz, T.4
  • 34
    • 0028267445 scopus 로고
    • Antihistoplasma effect of activated mouse splenic macrophages involves production of reactive nitrogen intermediates
    • Lane TE, Wu-Hsieh BA, Howard DH, (1994) Antihistoplasma effect of activated mouse splenic macrophages involves production of reactive nitrogen intermediates. Infect Immun 62: 1940-1945.
    • (1994) Infect Immun , vol.62 , pp. 1940-1945
    • Lane, T.E.1    Wu-Hsieh, B.A.2    Howard, D.H.3
  • 35
    • 0034697387 scopus 로고    scopus 로고
    • Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-1 to produce a soluble formazan: a simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents
    • Tan AS, Berridge MV, (2000) Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-1 to produce a soluble formazan: a simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents. J Immunol Methods 238: 59-68.
    • (2000) J Immunol Methods , vol.238 , pp. 59-68
    • Tan, A.S.1    Berridge, M.V.2
  • 36
    • 84907134394 scopus 로고
    • Evidence that the M antigen of Histoplasma capsulatum var. capsulatum is a catalase which exhibits cross-reactivity with other dimorphic fungi
    • Hamilton AJ, Bartholomew MA, Figueroa J, Fenelon LE, Hay RJ, (1990) Evidence that the M antigen of Histoplasma capsulatum var. capsulatum is a catalase which exhibits cross-reactivity with other dimorphic fungi. J Med Vet Mycol 28: 479-485.
    • (1990) J Med Vet Mycol , vol.28 , pp. 479-485
    • Hamilton, A.J.1    Bartholomew, M.A.2    Figueroa, J.3    Fenelon, L.E.4    Hay, R.J.5
  • 38
    • 0036231821 scopus 로고    scopus 로고
    • Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases
    • Johnson CH, Klotz MG, York JL, Kruft V, McEwen JE, (2002) Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases. Microbiology 148: 1129-1142.
    • (2002) Microbiology , vol.148 , pp. 1129-1142
    • Johnson, C.H.1    Klotz, M.G.2    York, J.L.3    Kruft, V.4    McEwen, J.E.5
  • 39
    • 0034917354 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst
    • Piddington DL, Fang FC, Laessig T, Cooper AM, Orme IM, et al. (2001) Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst. Infect Immun 69: 4980-4987.
    • (2001) Infect Immun , vol.69 , pp. 4980-4987
    • Piddington, D.L.1    Fang, F.C.2    Laessig, T.3    Cooper, A.M.4    Orme, I.M.5
  • 40
    • 0009543864 scopus 로고    scopus 로고
    • Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase
    • De Groote MA, Ochsner UA, Shiloh MU, Nathan C, McCord JM, et al. (1997) Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase. Proc Natl Acad Sci U S A 94: 13997-14001.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13997-14001
    • De Groote, M.A.1    Ochsner, U.A.2    Shiloh, M.U.3    Nathan, C.4    McCord, J.M.5
  • 42
    • 70350449301 scopus 로고    scopus 로고
    • Identification of Francisella tularensis live vaccine strain CuZn superoxide dismutase as critical for resistance to extracellularly generated reactive oxygen species
    • Melillo AA, Mahawar M, Sellati TJ, Malik M, Metzger DW, et al. (2009) Identification of Francisella tularensis live vaccine strain CuZn superoxide dismutase as critical for resistance to extracellularly generated reactive oxygen species. J Bacteriol 191: 6447-6456.
    • (2009) J Bacteriol , vol.191 , pp. 6447-6456
    • Melillo, A.A.1    Mahawar, M.2    Sellati, T.J.3    Malik, M.4    Metzger, D.W.5
  • 43
    • 13744258600 scopus 로고    scopus 로고
    • Cryptococcus neoformans mitochondrial superoxide dismutase: an essential link between antioxidant function and high-temperature growth
    • Giles SS, Batinic-Haberle I, Perfect JR, Cox GM, (2005) Cryptococcus neoformans mitochondrial superoxide dismutase: an essential link between antioxidant function and high-temperature growth. Eukaryot Cell 4: 46-54.
    • (2005) Eukaryot Cell , vol.4 , pp. 46-54
    • Giles, S.S.1    Batinic-Haberle, I.2    Perfect, J.R.3    Cox, G.M.4
  • 44
    • 0345268706 scopus 로고    scopus 로고
    • Characterization of Cu,Zn superoxide dismutase (SOD1) gene knock-out mutant of Cryptococcus neoformans var. gattii: role in biology and virulence
    • Narasipura SD, Ault JG, Behr MJ, Chaturvedi V, Chaturvedi S, (2003) Characterization of Cu,Zn superoxide dismutase (SOD1) gene knock-out mutant of Cryptococcus neoformans var. gattii: role in biology and virulence. Mol Microbiol 47: 1681-1694.
    • (2003) Mol Microbiol , vol.47 , pp. 1681-1694
    • Narasipura, S.D.1    Ault, J.G.2    Behr, M.J.3    Chaturvedi, V.4    Chaturvedi, S.5
  • 45
    • 15944368964 scopus 로고    scopus 로고
    • Characterization of Cryptococcus neoformans variety gattii SOD2 reveals distinct roles of the two superoxide dismutases in fungal biology and virulence
    • Narasipura SD, Chaturvedi V, Chaturvedi S, (2005) Characterization of Cryptococcus neoformans variety gattii SOD2 reveals distinct roles of the two superoxide dismutases in fungal biology and virulence. Mol Microbiol 55: 1782-1800.
    • (2005) Mol Microbiol , vol.55 , pp. 1782-1800
    • Narasipura, S.D.1    Chaturvedi, V.2    Chaturvedi, S.3
  • 46
    • 0036854503 scopus 로고    scopus 로고
    • Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of Candida albicans against oxidative stresses and the expression of its full virulence
    • Hwang CS, Rhie GE, Oh JH, Huh WK, Yim HS, et al. (2002) Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of Candida albicans against oxidative stresses and the expression of its full virulence. Microbiology 148: 3705-3713.
    • (2002) Microbiology , vol.148 , pp. 3705-3713
    • Hwang, C.S.1    Rhie, G.E.2    Oh, J.H.3    Huh, W.K.4    Yim, H.S.5
  • 47
    • 0037218164 scopus 로고    scopus 로고
    • Superoxide dismutase influences the virulence of Cryptococcus neoformans by affecting growth within macrophages
    • Cox GM, Harrison TS, McDade HC, Taborda CP, Heinrich G, et al. (2003) Superoxide dismutase influences the virulence of Cryptococcus neoformans by affecting growth within macrophages. Infect Immun 71: 173-180.
    • (2003) Infect Immun , vol.71 , pp. 173-180
    • Cox, G.M.1    Harrison, T.S.2    McDade, H.C.3    Taborda, C.P.4    Heinrich, G.5
  • 48
    • 77953232523 scopus 로고    scopus 로고
    • Characterization of a CuZn superoxide dismutase gene in the arbuscular mycorrhizal fungus Glomus intraradices
    • Gonzalez-Guerrero M, Oger E, Benabdellah K, Azcon-Aguilar C, Lanfranco L, et al. (2010) Characterization of a CuZn superoxide dismutase gene in the arbuscular mycorrhizal fungus Glomus intraradices. Curr Genet 56: 265-274.
    • (2010) Curr Genet , vol.56 , pp. 265-274
    • Gonzalez-Guerrero, M.1    Oger, E.2    Benabdellah, K.3    Azcon-Aguilar, C.4    Lanfranco, L.5
  • 49
    • 20444431976 scopus 로고    scopus 로고
    • The mycorrhizal fungus Gigaspora margarita possesses a CuZn superoxide dismutase that is up-regulated during symbiosis with legume hosts
    • Lanfranco L, Novero M, Bonfante P, (2005) The mycorrhizal fungus Gigaspora margarita possesses a CuZn superoxide dismutase that is up-regulated during symbiosis with legume hosts. Plant Physiol 137: 1319-1330.
    • (2005) Plant Physiol , vol.137 , pp. 1319-1330
    • Lanfranco, L.1    Novero, M.2    Bonfante, P.3
  • 50
    • 67650494287 scopus 로고    scopus 로고
    • The YAP1 homolog-mediated oxidative stress tolerance is crucial for pathogenicity of the necrotrophic fungus Alternaria alternata in citrus
    • Lin CH, Yang SL, Chung KR, (2009) The YAP1 homolog-mediated oxidative stress tolerance is crucial for pathogenicity of the necrotrophic fungus Alternaria alternata in citrus. Mol Plant Microbe Interact 22: 942-952.
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 942-952
    • Lin, C.H.1    Yang, S.L.2    Chung, K.R.3
  • 51
    • 79960482379 scopus 로고    scopus 로고
    • High levels of a fungal superoxide dismutase and increased concentration of a PR-10 plant protein in associations between the endophytic fungus Neotyphodium lolii and ryegrass
    • Zhang N, Zhang S, Borchert S, Richardson K, Schmid J, (2011) High levels of a fungal superoxide dismutase and increased concentration of a PR-10 plant protein in associations between the endophytic fungus Neotyphodium lolii and ryegrass. Mol Plant Microbe Interact 24: 984-992.
    • (2011) Mol Plant Microbe Interact , vol.24 , pp. 984-992
    • Zhang, N.1    Zhang, S.2    Borchert, S.3    Richardson, K.4    Schmid, J.5
  • 52
    • 57449114198 scopus 로고    scopus 로고
    • RNA-mediated gene silencing of superoxide dismutase (bcsod1) in Botrytis cinerea
    • Patel RM, van Kan JA, Bailey AM, Foster GD, (2008) RNA-mediated gene silencing of superoxide dismutase (bcsod1) in Botrytis cinerea. Phytopathology 98: 1334-1339.
    • (2008) Phytopathology , vol.98 , pp. 1334-1339
    • Patel, R.M.1    van Kan, J.A.2    Bailey, A.M.3    Foster, G.D.4
  • 53
    • 0842302365 scopus 로고    scopus 로고
    • Functional analysis of H(2)O(2)-generating systems in Botrytis cinerea: the major Cu-Zn-superoxide dismutase (BCSOD1) contributes to virulence on French bean, whereas a glucose oxidase (BCGOD1) is dispensable
    • Rolke Y, Liu S, Quidde T, Williamson B, Schouten A, et al. (2004) Functional analysis of H(2)O(2)-generating systems in Botrytis cinerea: the major Cu-Zn-superoxide dismutase (BCSOD1) contributes to virulence on French bean, whereas a glucose oxidase (BCGOD1) is dispensable. Mol Plant Pathol 5: 17-27.
    • (2004) Mol Plant Pathol , vol.5 , pp. 17-27
    • Rolke, Y.1    Liu, S.2    Quidde, T.3    Williamson, B.4    Schouten, A.5
  • 54
    • 17144368786 scopus 로고    scopus 로고
    • Granulocytes govern the transcriptional response, morphology and proliferation of Candida albicans in human blood
    • Fradin C, De Groot P, MacCallum D, Schaller M, Klis F, et al. (2005) Granulocytes govern the transcriptional response, morphology and proliferation of Candida albicans in human blood. Mol Microbiol 56: 397-415.
    • (2005) Mol Microbiol , vol.56 , pp. 397-415
    • Fradin, C.1    De Groot, P.2    MacCallum, D.3    Schaller, M.4    Klis, F.5
  • 55
    • 0742288065 scopus 로고    scopus 로고
    • Superoxide dismutases in Candida albicans: transcriptional regulation and functional characterization of the hyphal-induced SOD5 gene
    • Martchenko M, Alarco AM, Harcus D, Whiteway M, (2004) Superoxide dismutases in Candida albicans: transcriptional regulation and functional characterization of the hyphal-induced SOD5 gene. Mol Biol Cell 15: 456-467.
    • (2004) Mol Biol Cell , vol.15 , pp. 456-467
    • Martchenko, M.1    Alarco, A.M.2    Harcus, D.3    Whiteway, M.4
  • 56
    • 58149136353 scopus 로고    scopus 로고
    • Candida albicans cell surface superoxide dismutases degrade host-derived reactive oxygen species to escape innate immune surveillance
    • Frohner IE, Bourgeois C, Yatsyk K, Majer O, Kuchler K, (2009) Candida albicans cell surface superoxide dismutases degrade host-derived reactive oxygen species to escape innate immune surveillance. Mol Microbiol 71: 240-252.
    • (2009) Mol Microbiol , vol.71 , pp. 240-252
    • Frohner, I.E.1    Bourgeois, C.2    Yatsyk, K.3    Majer, O.4    Kuchler, K.5
  • 57
    • 80051804445 scopus 로고    scopus 로고
    • Superoxide dismutases are involved in Candida albicans biofilm persistence against miconazole
    • Bink A, Vandenbosch D, Coenye T, Nelis H, Cammue BP, et al. (2011) Superoxide dismutases are involved in Candida albicans biofilm persistence against miconazole. Antimicrob Agents Chemother 55: 4033-4037.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 4033-4037
    • Bink, A.1    Vandenbosch, D.2    Coenye, T.3    Nelis, H.4    Cammue, B.P.5
  • 58
    • 33846573404 scopus 로고    scopus 로고
    • Histoplasma capsulatum alpha-(1,3)-glucan blocks innate immune recognition by the beta-glucan receptor
    • Rappleye CA, Eissenberg LG, Goldman WE, (2007) Histoplasma capsulatum alpha-(1,3)-glucan blocks innate immune recognition by the beta-glucan receptor. Proc Natl Acad Sci U S A 104: 1366-1370.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1366-1370
    • Rappleye, C.A.1    Eissenberg, L.G.2    Goldman, W.E.3
  • 59
    • 33745207594 scopus 로고    scopus 로고
    • Immune sensing of Candida albicans requires cooperative recognition of mannans and glucans by lectin and Toll-like receptors
    • Netea MG, Gow NA, Munro CA, Bates S, Collins C, et al. (2006) Immune sensing of Candida albicans requires cooperative recognition of mannans and glucans by lectin and Toll-like receptors. J Clin Invest 116: 1642-1650.
    • (2006) J Clin Invest , vol.116 , pp. 1642-1650
    • Netea, M.G.1    Gow, N.A.2    Munro, C.A.3    Bates, S.4    Collins, C.5
  • 60
    • 67649236160 scopus 로고    scopus 로고
    • Dectin-1 is required for human dendritic cells to initiate immune response to Candida albicans through Syk activation
    • Skrzypek F, Cenci E, Pietrella D, Rachini A, Bistoni F, et al. (2009) Dectin-1 is required for human dendritic cells to initiate immune response to Candida albicans through Syk activation. Microbes Infect 11: 661-670.
    • (2009) Microbes Infect , vol.11 , pp. 661-670
    • Skrzypek, F.1    Cenci, E.2    Pietrella, D.3    Rachini, A.4    Bistoni, F.5
  • 61
    • 27144521657 scopus 로고    scopus 로고
    • Dectin-1 activates Syk tyrosine kinase in a dynamic subset of macrophages for reactive oxygen production
    • Underhill DM, Rossnagle E, Lowell CA, Simmons RM, (2005) Dectin-1 activates Syk tyrosine kinase in a dynamic subset of macrophages for reactive oxygen production. Blood 106: 2543-2550.
    • (2005) Blood , vol.106 , pp. 2543-2550
    • Underhill, D.M.1    Rossnagle, E.2    Lowell, C.A.3    Simmons, R.M.4
  • 62
    • 17144370549 scopus 로고    scopus 로고
    • Dectin-1 mediates macrophage recognition of Candida albicans yeast but not filaments
    • Gantner BN, Simmons RM, Underhill DM, (2005) Dectin-1 mediates macrophage recognition of Candida albicans yeast but not filaments. EMBO J 24: 1277-1286.
    • (2005) EMBO J , vol.24 , pp. 1277-1286
    • Gantner, B.N.1    Simmons, R.M.2    Underhill, D.M.3
  • 64
    • 0025760580 scopus 로고
    • Killing of Histoplasma capsulatum by gamma-interferon-activated human monocyte-derived macrophages: evidence for a superoxide anion-dependent mechanism
    • Brummer E, Kurita N, Yoshida S, Nishimura K, Miyaji M, (1991) Killing of Histoplasma capsulatum by gamma-interferon-activated human monocyte-derived macrophages: evidence for a superoxide anion-dependent mechanism. J Med Microbiol 35: 29-34.
    • (1991) J Med Microbiol , vol.35 , pp. 29-34
    • Brummer, E.1    Kurita, N.2    Yoshida, S.3    Nishimura, K.4    Miyaji, M.5
  • 65
    • 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 AH, Nathan CF, Stuehr DJ, (1988) 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: 2407-2412.
    • (1988) J Immunol , vol.141 , pp. 2407-2412
    • Ding, A.H.1    Nathan, C.F.2    Stuehr, D.J.3
  • 66
    • 0029083882 scopus 로고
    • Killing of Histoplasma capsulatum by macrophage colony stimulating factor-treated human monocyte-derived macrophages: role for reactive oxygen intermediates
    • Desai G, Nassar F, Brummer E, Stevens DA, (1995) Killing of Histoplasma capsulatum by macrophage colony stimulating factor-treated human monocyte-derived macrophages: role for reactive oxygen intermediates. J Med Microbiol 43: 224-229.
    • (1995) J Med Microbiol , vol.43 , pp. 224-229
    • Desai, G.1    Nassar, F.2    Brummer, E.3    Stevens, D.A.4
  • 67
    • 0021246294 scopus 로고
    • Inhibition of growth of Histoplasma capsulatum by lymphokine-stimulated macrophages
    • Wu-Hsieh B, Howard DH, (1984) Inhibition of growth of Histoplasma capsulatum by lymphokine-stimulated macrophages. J Immunol 132: 2593-2597.
    • (1984) J Immunol , vol.132 , pp. 2593-2597
    • Wu-Hsieh, B.1    Howard, D.H.2
  • 68
    • 0023099501 scopus 로고
    • Inhibition of the intracellular growth of Histoplasma capsulatum by recombinant murine gamma interferon
    • Wu-Hsieh BA, Howard DH, (1987) Inhibition of the intracellular growth of Histoplasma capsulatum by recombinant murine gamma interferon. Infect Immun 55: 1014-1016.
    • (1987) Infect Immun , vol.55 , pp. 1014-1016
    • Wu-Hsieh, B.A.1    Howard, D.H.2
  • 69
    • 0032039009 scopus 로고    scopus 로고
    • Evolution of the primary immune response to Histoplasma capsulatum in murine lung
    • Cain JA, Deepe GS Jr, (1998) Evolution of the primary immune response to Histoplasma capsulatum in murine lung. Infect Immun 66: 1473-1481.
    • (1998) Infect Immun , vol.66 , pp. 1473-1481
    • Cain, J.A.1    Deepe Jr., G.S.2
  • 70
    • 84907123709 scopus 로고
    • Quantitative plating of Histoplasma capsulatum without addition of conditioned medium or siderophores
    • Worsham PL, Goldman WE, (1988) Quantitative plating of Histoplasma capsulatum without addition of conditioned medium or siderophores. J Med Vet Mycol 26: 137-143.
    • (1988) J Med Vet Mycol , vol.26 , pp. 137-143
    • Worsham, P.L.1    Goldman, W.E.2
  • 71
    • 0032038703 scopus 로고    scopus 로고
    • Electrotransformation and expression of bacterial genes encoding hygromycin phosphotransferase and beta-galactosidase in the pathogenic fungus Histoplasma capsulatum
    • Woods JP, Heinecke EL, Goldman WE, (1998) Electrotransformation and expression of bacterial genes encoding hygromycin phosphotransferase and beta-galactosidase in the pathogenic fungus Histoplasma capsulatum. Infect Immun 66: 1697-1707.
    • (1998) Infect Immun , vol.66 , pp. 1697-1707
    • Woods, J.P.1    Heinecke, E.L.2    Goldman, W.E.3
  • 72
    • 0035033538 scopus 로고    scopus 로고
    • CAP1, an adenylate cyclase-associated protein gene, regulates bud-hypha transitions, filamentous growth, and cyclic AMP levels and is required for virulence of Candida albicans
    • Bahn YS, Sundstrom P, (2001) CAP1, an adenylate cyclase-associated protein gene, regulates bud-hypha transitions, filamentous growth, and cyclic AMP levels and is required for virulence of Candida albicans. J Bacteriol 183: 3211-3223.
    • (2001) J Bacteriol , vol.183 , pp. 3211-3223
    • Bahn, Y.S.1    Sundstrom, P.2
  • 73
    • 78651483269 scopus 로고    scopus 로고
    • RNAi-based gene silencing using a GFP sentinel system in Histoplasma capsulatum
    • In: Brand A, MacCallum D, editors, New York, Humana Press
    • Youseff BH, Rappleye CA, (2012) RNAi-based gene silencing using a GFP sentinel system in Histoplasma capsulatum. In: Brand A, MacCallum D, editors. Host-Fungal Interactions: Manipulation of Fungal Gene Expression New York Humana Press.
    • (2012) Host-Fungal Interactions: Manipulation of Fungal Gene Expression
    • Youseff, B.H.1    Rappleye, C.A.2
  • 74
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers RF Jr, Sizer IW, (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195: 133-140.
    • (1952) J Biol Chem , vol.195 , pp. 133-140
    • Beers Jr., R.F.1    Sizer, I.W.2
  • 75
    • 0033667989 scopus 로고    scopus 로고
    • A simple method for isolating human and rabbit polymorphonuclear neutrophils (PMNs)
    • Kouoh F, Gressier B, Luyckx M, Brunet C, Dine T, et al. (2000) A simple method for isolating human and rabbit polymorphonuclear neutrophils (PMNs). Biol Pharm Bull 23: 1382-1383.
    • (2000) Biol Pharm Bull , vol.23 , pp. 1382-1383
    • Kouoh, F.1    Gressier, B.2    Luyckx, M.3    Brunet, C.4    Dine, T.5
  • 76
    • 45549089809 scopus 로고    scopus 로고
    • Isolation of human neutrophils from venous blood
    • Nauseef WM, (2007) Isolation of human neutrophils from venous blood. Methods Mol Biol 412: 15-20.
    • (2007) Methods Mol Biol , vol.412 , pp. 15-20
    • Nauseef, W.M.1
  • 78
    • 33750480548 scopus 로고    scopus 로고
    • An alpha-(1,4)-amylase is essential for alpha-(1,3)-glucan production and virulence in Histoplasma capsulatum
    • Marion CL, Rappleye CA, Engle JT, Goldman WE, (2006) An alpha-(1,4)-amylase is essential for alpha-(1,3)-glucan production and virulence in Histoplasma capsulatum. Mol Microbiol 62: 970-983.
    • (2006) Mol Microbiol , vol.62 , pp. 970-983
    • Marion, C.L.1    Rappleye, C.A.2    Engle, J.T.3    Goldman, W.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.