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Volumn 49, Issue 9, 2010, Pages 1342-1353

Nox enzymes from fungus to fly to fish and what they tell us about Nox function in mammals

Author keywords

Duox enzymes; Free radicals; Nox enzymes; Reactive oxygen; Stress response; Tyrosine cross linking

Indexed keywords

CYTOCHROME; DUOX1 PROTEIN; DUOX2 PROTEIN; NOX PROTEIN; NOX3 PROTEIN; NOX5 PROTEIN; NOXB PROTEIN; NOXC PROTEIN; PROTEIN NOXA; PROTEIN P67; RAC1 PROTEIN; RAC2 PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; UNCLASSIFIED DRUG;

EID: 77957240694     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.07.027     Document Type: Review
Times cited : (131)

References (90)
  • 1
    • 34547697113 scopus 로고    scopus 로고
    • Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes
    • Kawahara B.T., Quinn M.T., Lambeth J.D. Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes. BMC Evol. Biol. 2007, 7:109.
    • (2007) BMC Evol. Biol. , vol.7 , pp. 109
    • Kawahara, B.T.1    Quinn, M.T.2    Lambeth, J.D.3
  • 8
    • 57349116981 scopus 로고    scopus 로고
    • Phosphatidylinositol (4, 5)-bisphosphate modulates Nox5 localization via an N-terminal polybasic region
    • Kawahara T., Lambeth J.D. Phosphatidylinositol (4, 5)-bisphosphate modulates Nox5 localization via an N-terminal polybasic region. Mol. Biol. Cell 2008, 19:4020-4031.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4020-4031
    • Kawahara, T.1    Lambeth, J.D.2
  • 9
    • 66849111512 scopus 로고    scopus 로고
    • Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells
    • Luxen S., Noack D., Frausto M., Davanture S., Torbett B.E., Knaus U.G. Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells. J. Cell Sci. 2009, 122:1238-1247.
    • (2009) J. Cell Sci. , vol.122 , pp. 1238-1247
    • Luxen, S.1    Noack, D.2    Frausto, M.3    Davanture, S.4    Torbett, B.E.5    Knaus, U.G.6
  • 10
    • 34147130314 scopus 로고    scopus 로고
    • Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3
    • Nakano Y., Banfi B., Jesaitis A.J., Dinauer M.C., Allen L.A., Nauseef W.M. Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3. Biochem. J. 2007, 403:97-108.
    • (2007) Biochem. J. , vol.403 , pp. 97-108
    • Nakano, Y.1    Banfi, B.2    Jesaitis, A.J.3    Dinauer, M.C.4    Allen, L.A.5    Nauseef, W.M.6
  • 11
    • 0013397105 scopus 로고
    • Generation of superoxide by potato tuber protoplasts during the hypersensitive response to hyphal cell wall components of Phytophthora infestans and specific inhibition of the reaction by suppressors of hypersensitivity
    • Doke N. Generation of superoxide by potato tuber protoplasts during the hypersensitive response to hyphal cell wall components of Phytophthora infestans and specific inhibition of the reaction by suppressors of hypersensitivity. Physiol. Plant Pathol. 1983, 23:359-367.
    • (1983) Physiol. Plant Pathol. , vol.23 , pp. 359-367
    • Doke, N.1
  • 12
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 1994, 79:583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 13
    • 0037039157 scopus 로고    scopus 로고
    • Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for accumulation of reactive oxygen intermediates in the plant defense response
    • Torres M.A., Dangl J.L., Jones J.D. Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for accumulation of reactive oxygen intermediates in the plant defense response. Proc. Natl. Acad. Sci. USA 2002, 99:517-522.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 517-522
    • Torres, M.A.1    Dangl, J.L.2    Jones, J.D.3
  • 21
    • 40049098844 scopus 로고    scopus 로고
    • Local positive feedback regulation determines cell shape in root hair cells
    • Takeda S., Gapper C., Kaya H., Bell E., Kuchitsu K., Dolan L. Local positive feedback regulation determines cell shape in root hair cells. Science 2008, 319:1241-1244.
    • (2008) Science , vol.319 , pp. 1241-1244
    • Takeda, S.1    Gapper, C.2    Kaya, H.3    Bell, E.4    Kuchitsu, K.5    Dolan, L.6
  • 22
    • 38049098108 scopus 로고    scopus 로고
    • Oscillations in extracellular pH and reactive oxygen species modulate tip growth of Arabidopsis root hairs
    • Monshausen G.B., Bibikova T.N., Messerli M.A., Shi C., Gilroy S. Oscillations in extracellular pH and reactive oxygen species modulate tip growth of Arabidopsis root hairs. Proc. Natl. Acad. Sci. USA 2007, 104:20996-21001.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20996-21001
    • Monshausen, G.B.1    Bibikova, T.N.2    Messerli, M.A.3    Shi, C.4    Gilroy, S.5
  • 23
    • 0031704475 scopus 로고    scopus 로고
    • Localized changes in apoplastic and cytoplasmic pH are associated with root hair development in Arabidopsis thaliana
    • Bibikova T.N., Jacob T., Dahse I., Gilroy S. Localized changes in apoplastic and cytoplasmic pH are associated with root hair development in Arabidopsis thaliana. Development 1998, 125:2925-2934.
    • (1998) Development , vol.125 , pp. 2925-2934
    • Bibikova, T.N.1    Jacob, T.2    Dahse, I.3    Gilroy, S.4
  • 24
    • 0033512346 scopus 로고    scopus 로고
    • Enzymes and other agents that enhance cell wall extensibility
    • Cosgrove D.J. Enzymes and other agents that enhance cell wall extensibility. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1999, 50:391-417.
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 391-417
    • Cosgrove, D.J.1
  • 25
    • 0020483177 scopus 로고
    • Isodityrosine, a new cross-linking amino acid from plant cell-wall glycoprotein
    • Fry S.C. Isodityrosine, a new cross-linking amino acid from plant cell-wall glycoprotein. Biochem. J. 1982, 204:449-455.
    • (1982) Biochem. J. , vol.204 , pp. 449-455
    • Fry, S.C.1
  • 26
    • 11244311665 scopus 로고    scopus 로고
    • Di-isodityrosine is the intermolecular cross-link of isodityrosine-rich extensin analogs cross-linked in vitro
    • Held M.A., Tan L., Kamyab A., Hare M., Shpak E., Kieliszewski M.J. Di-isodityrosine is the intermolecular cross-link of isodityrosine-rich extensin analogs cross-linked in vitro. J. Biol. Chem. 2004, 279:55474-55482.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55474-55482
    • Held, M.A.1    Tan, L.2    Kamyab, A.3    Hare, M.4    Shpak, E.5    Kieliszewski, M.J.6
  • 27
    • 0029963544 scopus 로고    scopus 로고
    • Di-isodityrosine, a novel tetrametric derivative of tyrosine in plant cell wall proteins: a new potential cross-link
    • Brady J.D., Sadler I.H., Fry S.C. Di-isodityrosine, a novel tetrametric derivative of tyrosine in plant cell wall proteins: a new potential cross-link. Biochem. J. 1996, 315(Pt 1):323-327.
    • (1996) Biochem. J. , vol.315 , Issue.PART 1 , pp. 323-327
    • Brady, J.D.1    Sadler, I.H.2    Fry, S.C.3
  • 28
    • 0032007587 scopus 로고    scopus 로고
    • Pulcherosine, an oxidatively coupled trimer of tyrosine in plant cell walls: its role in cross-link formation
    • Brady J.D., Sadler I.H., Fry S.C. Pulcherosine, an oxidatively coupled trimer of tyrosine in plant cell walls: its role in cross-link formation. Phytochemistry 1998, 47:349-353.
    • (1998) Phytochemistry , vol.47 , pp. 349-353
    • Brady, J.D.1    Sadler, I.H.2    Fry, S.C.3
  • 29
    • 33644537394 scopus 로고    scopus 로고
    • NADPH oxidases in Eukaryotes: red algae provide new hints!
    • Herve C., Tonon T., Collen J., Corre E., Boyen C. NADPH oxidases in Eukaryotes: red algae provide new hints!. Curr. Genet. 2006, 49:190-204.
    • (2006) Curr. Genet. , vol.49 , pp. 190-204
    • Herve, C.1    Tonon, T.2    Collen, J.3    Corre, E.4    Boyen, C.5
  • 31
    • 0032696649 scopus 로고    scopus 로고
    • Sulfated oligosaccharides mediate the interaction between a marine red alga and its green algal pathogenic endophyte
    • Bouarab K., Potin P., Correa J., Kloareg B. Sulfated oligosaccharides mediate the interaction between a marine red alga and its green algal pathogenic endophyte. Plant Cell 1999, 11:1635-1650.
    • (1999) Plant Cell , vol.11 , pp. 1635-1650
    • Bouarab, K.1    Potin, P.2    Correa, J.3    Kloareg, B.4
  • 32
    • 0042887137 scopus 로고    scopus 로고
    • Superoxide signalling required for multicellular development of Dictyostelium
    • Bloomfield G., Pears C. Superoxide signalling required for multicellular development of Dictyostelium. J. Cell Sci. 2003, 116:3387-3397.
    • (2003) J. Cell Sci. , vol.116 , pp. 3387-3397
    • Bloomfield, G.1    Pears, C.2
  • 33
    • 0345689448 scopus 로고    scopus 로고
    • Reactive oxygen species generated by microbial NADPH oxidase NoxA regulate sexual development in Aspergillus nidulans
    • Lara-Ortiz T., Riveros-Rosas H., Aguirre J. Reactive oxygen species generated by microbial NADPH oxidase NoxA regulate sexual development in Aspergillus nidulans. Mol. Microbiol. 2003, 50:1241-1255.
    • (2003) Mol. Microbiol. , vol.50 , pp. 1241-1255
    • Lara-Ortiz, T.1    Riveros-Rosas, H.2    Aguirre, J.3
  • 34
    • 20444381691 scopus 로고    scopus 로고
    • NADPH oxidase homologs are required for normal cell differentiation and morphogenesis in Dictyostelium discoideum
    • Lardy B., Bof M., Aubry L., Paclet M.H., Morel F., Satre M., Klein G. NADPH oxidase homologs are required for normal cell differentiation and morphogenesis in Dictyostelium discoideum. Biochim. Biophys. Acta 2005, 1744:199-212.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 199-212
    • Lardy, B.1    Bof, M.2    Aubry, L.3    Paclet, M.H.4    Morel, F.5    Satre, M.6    Klein, G.7
  • 36
    • 70349900168 scopus 로고    scopus 로고
    • Functions and regulation of the Nox family in the filamentous fungus Podospora anserina: a new role in cellulose degradation
    • Brun S., Malagnac F., Bidard F., Lalucque H., Silar P. Functions and regulation of the Nox family in the filamentous fungus Podospora anserina: a new role in cellulose degradation. Mol. Microbiol. 2009, 74:480-496.
    • (2009) Mol. Microbiol. , vol.74 , pp. 480-496
    • Brun, S.1    Malagnac, F.2    Bidard, F.3    Lalucque, H.4    Silar, P.5
  • 37
    • 33751001612 scopus 로고    scopus 로고
    • A p67Phox-like regulator is recruited to control hyphal branching in a fungal-grass mutualistic symbiosis
    • Takemoto D., Tanaka A., Scott B. A p67Phox-like regulator is recruited to control hyphal branching in a fungal-grass mutualistic symbiosis. Plant Cell 2006, 18:2807-2821.
    • (2006) Plant Cell , vol.18 , pp. 2807-2821
    • Takemoto, D.1    Tanaka, A.2    Scott, B.3
  • 38
    • 33745443572 scopus 로고    scopus 로고
    • Reactive oxygen species play a role in regulating a fungus-perennial ryegrass mutualistic interaction
    • Tanaka A., Christensen M.J., Takemoto D., Park P., Scott B. Reactive oxygen species play a role in regulating a fungus-perennial ryegrass mutualistic interaction. Plant Cell 2006, 18:1052-1066.
    • (2006) Plant Cell , vol.18 , pp. 1052-1066
    • Tanaka, A.1    Christensen, M.J.2    Takemoto, D.3    Park, P.4    Scott, B.5
  • 39
    • 48949086212 scopus 로고    scopus 로고
    • NADPH oxidases NOX-1 and NOX-2 require the regulatory subunit NOR-1 to control cell differentiation and growth in Neurospora crassa
    • Cano-Dominguez N., Alvarez-Delfin K., Hansberg W., Aguirre J. NADPH oxidases NOX-1 and NOX-2 require the regulatory subunit NOR-1 to control cell differentiation and growth in Neurospora crassa. Eukaryotic Cell 2008, 7:1352-1361.
    • (2008) Eukaryotic Cell , vol.7 , pp. 1352-1361
    • Cano-Dominguez, N.1    Alvarez-Delfin, K.2    Hansberg, W.3    Aguirre, J.4
  • 40
    • 55749098656 scopus 로고    scopus 로고
    • Regulation of apical dominance in Aspergillus nidulans hyphae by reactive oxygen species
    • Semighini C.P., Harris S.D. Regulation of apical dominance in Aspergillus nidulans hyphae by reactive oxygen species. Genetics 2008, 179:1919-1932.
    • (2008) Genetics , vol.179 , pp. 1919-1932
    • Semighini, C.P.1    Harris, S.D.2
  • 42
    • 36849064316 scopus 로고    scopus 로고
    • Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes
    • Kawahara T., Lambeth J.D. Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes. BMC Evol. Biol. 2007, 7:178.
    • (2007) BMC Evol. Biol. , vol.7 , pp. 178
    • Kawahara, T.1    Lambeth, J.D.2
  • 43
    • 42549130034 scopus 로고    scopus 로고
    • Characterisation of Aspergillus nidulans polarisome component BemA
    • Leeder A.C., Turner G. Characterisation of Aspergillus nidulans polarisome component BemA. Fungal Genet. Biol. 2008, 45:897-911.
    • (2008) Fungal Genet. Biol. , vol.45 , pp. 897-911
    • Leeder, A.C.1    Turner, G.2
  • 44
    • 0029812877 scopus 로고    scopus 로고
    • NADPH oxidase activity is independent of p47phox in vitro
    • Freeman J.L., Lambeth J.D. NADPH oxidase activity is independent of p47phox in vitro. J. Biol. Chem. 1996, 271:22578-22582.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22578-22582
    • Freeman, J.L.1    Lambeth, J.D.2
  • 45
    • 0029828538 scopus 로고    scopus 로고
    • phox is not a sine qua non participant in the activation of NADPH oxidase but is required for optimal superoxide production
    • phox is not a sine qua non participant in the activation of NADPH oxidase but is required for optimal superoxide production. J. Biol. Chem. 1996, 271:30326-30329.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30326-30329
    • Koshkin, V.1    Lotan, O.2    Pick, E.3
  • 46
    • 33750735355 scopus 로고    scopus 로고
    • Impact of ROS on ageing of two fungal model systems: Saccharomyces cerevisiae and Podospora anserina
    • Osiewacz H.D., Scheckhuber C.Q. Impact of ROS on ageing of two fungal model systems: Saccharomyces cerevisiae and Podospora anserina. Free Radic. Res. 2006, 40:1350-1358.
    • (2006) Free Radic. Res. , vol.40 , pp. 1350-1358
    • Osiewacz, H.D.1    Scheckhuber, C.Q.2
  • 47
    • 0027450048 scopus 로고
    • Reactive oxygen species associated with cell differentiation in Neurospora crassa
    • Hansberg W., de Groot H., Sies H. Reactive oxygen species associated with cell differentiation in Neurospora crassa. Free Radic. Biol. Med. 1993, 14:287-293.
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 287-293
    • Hansberg, W.1    de Groot, H.2    Sies, H.3
  • 48
    • 0025056817 scopus 로고
    • Hyperoxidant states cause microbial cell differentiation by cell isolation from dioxygen
    • Hansberg W., Aguirre J. Hyperoxidant states cause microbial cell differentiation by cell isolation from dioxygen. J. Theor. Biol. 1990, 142:201-221.
    • (1990) J. Theor. Biol. , vol.142 , pp. 201-221
    • Hansberg, W.1    Aguirre, J.2
  • 49
    • 4744362719 scopus 로고    scopus 로고
    • Two NADPH oxidase isoforms are required for sexual reproduction and ascospore germination in the filamentous fungus Podospora anserina
    • Malagnac F., Lalucque H., Lepere G., Silar P. Two NADPH oxidase isoforms are required for sexual reproduction and ascospore germination in the filamentous fungus Podospora anserina. Fungal Genet. Biol. 2004, 41:982-997.
    • (2004) Fungal Genet. Biol. , vol.41 , pp. 982-997
    • Malagnac, F.1    Lalucque, H.2    Lepere, G.3    Silar, P.4
  • 50
    • 34547456941 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by fungal NADPH oxidases is required for rice blast disease
    • Egan M.J., Wang Z.Y., Jones M.A., Smirnoff N., Talbot N.J. Generation of reactive oxygen species by fungal NADPH oxidases is required for rice blast disease. Proc. Natl. Acad. Sci. USA 2007, 104:11772-11777.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11772-11777
    • Egan, M.J.1    Wang, Z.Y.2    Jones, M.A.3    Smirnoff, N.4    Talbot, N.J.5
  • 51
    • 41049113238 scopus 로고    scopus 로고
    • The NADPH oxidase Cpnox1 is required for full pathogenicity of the ergot fungus Claviceps purpurea
    • Giesbert S., Schürg T., Scheele S., Tudzynski P. The NADPH oxidase Cpnox1 is required for full pathogenicity of the ergot fungus Claviceps purpurea. Mol. Plant Pathol. 2008, 9:317-327.
    • (2008) Mol. Plant Pathol. , vol.9 , pp. 317-327
    • Giesbert, S.1    Schürg, T.2    Scheele, S.3    Tudzynski, P.4
  • 52
    • 0035921417 scopus 로고    scopus 로고
    • Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox
    • Edens W.A., Sharling L., Cheng G., Shapira R., Kinkade J.M., Edens H.A., Tang X., Flaherty D.B., Benian G., Lambeth J.D. Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. J. Cell Biol. 2001, 154:879-891.
    • (2001) J. Cell Biol. , vol.154 , pp. 879-891
    • Edens, W.A.1    Sharling, L.2    Cheng, G.3    Shapira, R.4    Kinkade, J.M.5    Edens, H.A.6    Tang, X.7    Flaherty, D.B.8    Benian, G.9    Lambeth, J.D.10
  • 54
    • 70350439116 scopus 로고    scopus 로고
    • Ce-Duox1/BLI-3 generates reactive oxygen species as a protective innate immune mechanism in Caenorhabditis elegans
    • Chavez V., Mohri-Shiomi A., Garsin D.A. Ce-Duox1/BLI-3 generates reactive oxygen species as a protective innate immune mechanism in Caenorhabditis elegans. Infect. Immun. 2009, 77:4983-4989.
    • (2009) Infect. Immun. , vol.77 , pp. 4983-4989
    • Chavez, V.1    Mohri-Shiomi, A.2    Garsin, D.A.3
  • 55
    • 67650564929 scopus 로고    scopus 로고
    • Caenorhabditis elegans and human dual oxidase 1 (DUOX1) "peroxidase" domains: insights into heme binding and catalytic activity
    • Meitzler J.L., Ortiz de Montellano P.R. Caenorhabditis elegans and human dual oxidase 1 (DUOX1) "peroxidase" domains: insights into heme binding and catalytic activity. J. Biol. Chem. 2009, 284:18634-18643.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18634-18643
    • Meitzler, J.L.1    Ortiz de Montellano, P.R.2
  • 56
    • 67650510676 scopus 로고    scopus 로고
    • Combined extracellular matrix cross-linking activity of the peroxidase MLT-7 and the dual oxidase BLI-3 is critical for post-embryonic viability in Caenorhabditis elegans
    • Thein M.C., Winter A.D., Stepek G., McCormack G., Stapleton G., Johnstone I.L., Page A.P. Combined extracellular matrix cross-linking activity of the peroxidase MLT-7 and the dual oxidase BLI-3 is critical for post-embryonic viability in Caenorhabditis elegans. J. Biol. Chem. 2009, 284:17549-17563.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17549-17563
    • Thein, M.C.1    Winter, A.D.2    Stepek, G.3    McCormack, G.4    Stapleton, G.5    Johnstone, I.L.6    Page, A.P.7
  • 57
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing
    • Hampton M.B., Kettle A.J., Winterbourn C.C. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 1998, 92:3007-3017.
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 58
    • 0042203535 scopus 로고    scopus 로고
    • Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense
    • Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L. Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. FASEB J. 2003, 17:1502-1504.
    • (2003) FASEB J. , vol.17 , pp. 1502-1504
    • Geiszt, M.1    Witta, J.2    Baffi, J.3    Lekstrom, K.4    Leto, T.L.5
  • 60
    • 0033601327 scopus 로고    scopus 로고
    • Purification of a novel flavoprotein involved in the thyroid NADPH oxidase
    • Dupuy C., Ohayon R., Valent A., Noe-Hudson M., Dee D., Virion A. Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. J. Biol. Chem. 1999, 274:37265-37269.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37265-37269
    • Dupuy, C.1    Ohayon, R.2    Valent, A.3    Noe-Hudson, M.4    Dee, D.5    Virion, A.6
  • 62
    • 27644498442 scopus 로고    scopus 로고
    • A direct role for dual oxidase in Drosophila gut immunity
    • Ha E.M., Oh C.T., Bae Y.S., Lee W.J. A direct role for dual oxidase in Drosophila gut immunity. Science 2005, 310:847-850.
    • (2005) Science , vol.310 , pp. 847-850
    • Ha, E.M.1    Oh, C.T.2    Bae, Y.S.3    Lee, W.J.4
  • 63
    • 77950234253 scopus 로고    scopus 로고
    • A peroxidase/dual oxidase system modulates midgut epithelial immunity in Anopheles gambiae
    • Kumar S., Molina-Cruz A., Gupta L., Rodrigues J., Barillas-Mury C. A peroxidase/dual oxidase system modulates midgut epithelial immunity in Anopheles gambiae. Science 2010, 327:1644-1648.
    • (2010) Science , vol.327 , pp. 1644-1648
    • Kumar, S.1    Molina-Cruz, A.2    Gupta, L.3    Rodrigues, J.4    Barillas-Mury, C.5
  • 65
    • 33750926794 scopus 로고    scopus 로고
    • Role of Nox family NADPH oxidases in host defense
    • Leto T.L., Geiszt M. Role of Nox family NADPH oxidases in host defense. Antioxid. Redox Signaling 2006, 8:1549-1561.
    • (2006) Antioxid. Redox Signaling , vol.8 , pp. 1549-1561
    • Leto, T.L.1    Geiszt, M.2
  • 66
    • 27844528008 scopus 로고    scopus 로고
    • Expression of Nox genes in rat organs, mouse oocytes, and sea urchin eggs
    • Maru Y., Nishino T., Kakinuma K. Expression of Nox genes in rat organs, mouse oocytes, and sea urchin eggs. DNA Seq. 2005, 16:83-88.
    • (2005) DNA Seq. , vol.16 , pp. 83-88
    • Maru, Y.1    Nishino, T.2    Kakinuma, K.3
  • 67
    • 0018764368 scopus 로고
    • Membrane events of fertilization in the sea urchin
    • Eddy E.M., Shapiro B.M. Membrane events of fertilization in the sea urchin. Scan. Electron Microsc. 1979, 3:287-297.
    • (1979) Scan. Electron Microsc. , vol.3 , pp. 287-297
    • Eddy, E.M.1    Shapiro, B.M.2
  • 68
    • 0344978352 scopus 로고
    • Release of ovoperoxidase from sea urchin eggs hardens the fertilization membrane with tyrosine crosslinks
    • Foerder C.A., Shapiro B.M. Release of ovoperoxidase from sea urchin eggs hardens the fertilization membrane with tyrosine crosslinks. Proc. Natl. Acad. Sci. USA 1977, 74:4214-4218.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4214-4218
    • Foerder, C.A.1    Shapiro, B.M.2
  • 70
    • 0025303650 scopus 로고
    • A specific requirement for protein kinase C in activation of the respiratory burst oxidase of fertilization
    • Heinecke J.W., Meier K.E., Lorenzen J.A., Shapiro B.M. A specific requirement for protein kinase C in activation of the respiratory burst oxidase of fertilization. J. Biol. Chem. 1990, 265:7717-7720.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7717-7720
    • Heinecke, J.W.1    Meier, K.E.2    Lorenzen, J.A.3    Shapiro, B.M.4
  • 71
    • 10644230060 scopus 로고    scopus 로고
    • The oxidative burst at fertilization is dependent upon activation of the dual oxidase Udx1
    • Wong J.L., Creton R., Wessel G.M. The oxidative burst at fertilization is dependent upon activation of the dual oxidase Udx1. Dev. Cell 2004, 7:801-814.
    • (2004) Dev. Cell , vol.7 , pp. 801-814
    • Wong, J.L.1    Creton, R.2    Wessel, G.M.3
  • 72
    • 29044436293 scopus 로고    scopus 로고
    • Reactive oxygen species and Udx1 during early sea urchin development
    • Wong J.L., Wessel G.M. Reactive oxygen species and Udx1 during early sea urchin development. Dev. Biol. 2005, 288:317-333.
    • (2005) Dev. Biol. , vol.288 , pp. 317-333
    • Wong, J.L.1    Wessel, G.M.2
  • 73
    • 25844516430 scopus 로고    scopus 로고
    • Characteristics of NADPH oxidase genes (Nox2, p22, p47, and p67) and Nox4 gene expressed in blood cells of juvenile Ciona intestinalis
    • Inoue Y., Ogasawara M., Moroi T., Satake M., Azumi K., Moritomo T., Nakanishi T. Characteristics of NADPH oxidase genes (Nox2, p22, p47, and p67) and Nox4 gene expressed in blood cells of juvenile Ciona intestinalis. Immunogenetics 2005, 57:520-534.
    • (2005) Immunogenetics , vol.57 , pp. 520-534
    • Inoue, Y.1    Ogasawara, M.2    Moroi, T.3    Satake, M.4    Azumi, K.5    Moritomo, T.6    Nakanishi, T.7
  • 74
    • 33751232341 scopus 로고    scopus 로고
    • Restricted expression of NADPH oxidase/peroxidase gene (Duox) in zone VII of the ascidian endostyle
    • Hiruta J., Mazet F., Ogasawara M. Restricted expression of NADPH oxidase/peroxidase gene (Duox) in zone VII of the ascidian endostyle. Cell Tissue Res. 2006, 326:835-841.
    • (2006) Cell Tissue Res. , vol.326 , pp. 835-841
    • Hiruta, J.1    Mazet, F.2    Ogasawara, M.3
  • 75
    • 67649255876 scopus 로고    scopus 로고
    • A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
    • Niethammer P., Grabher C., Look A.T., Mitchison T.J. A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish. Nature 2009, 459:996-999.
    • (2009) Nature , vol.459 , pp. 996-999
    • Niethammer, P.1    Grabher, C.2    Look, A.T.3    Mitchison, T.J.4
  • 76
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K., Krause K.H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 2007, 87:245-313.
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 78
  • 80
    • 33748333105 scopus 로고    scopus 로고
    • The NADPH oxidase NOX4 drives cardiac differentiation: role in regulating cardiac transcription factors and MAP kinase activation
    • Li J., Stouffs M., Serrander L., Banfi B., Bettiol E., Charnay Y., Steger K., Krause K.H., Jaconi M.E. The NADPH oxidase NOX4 drives cardiac differentiation: role in regulating cardiac transcription factors and MAP kinase activation. Mol. Biol. Cell 2006, 17:3978-3988.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3978-3988
    • Li, J.1    Stouffs, M.2    Serrander, L.3    Banfi, B.4    Bettiol, E.5    Charnay, Y.6    Steger, K.7    Krause, K.H.8    Jaconi, M.E.9
  • 81
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn C.C., Hampton M.B. Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med. 2008, 45:549-561.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 82
    • 0036139524 scopus 로고    scopus 로고
    • Reactive oxygen species and signal transduction
    • Finkel T. Reactive oxygen species and signal transduction. IUBMB Life 2001, 52:3-6.
    • (2001) IUBMB Life , vol.52 , pp. 3-6
    • Finkel, T.1
  • 83
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.-R., Kwon K.-S., Kim S.-R., Rhee S.G. Reversible inactivation of protein tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 1998, 273:15366-15372.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.-R.1    Kwon, K.-S.2    Kim, S.-R.3    Rhee, S.G.4
  • 84
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: revisiting PTPs and the control of cell signaling
    • Tonks N.K. Redox redux: revisiting PTPs and the control of cell signaling. Cell 2005, 121:667-670.
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 87
    • 50849097044 scopus 로고    scopus 로고
    • H5N1 and 1918 pandemic influenza virus infection results in early and excessive infiltration of macrophages and neutrophils in the lungs of mice
    • Perrone L.A., Plowden J.K., Garcia-Sastre A., Katz J.M., Tumpey T.M. H5N1 and 1918 pandemic influenza virus infection results in early and excessive infiltration of macrophages and neutrophils in the lungs of mice. PLoS Pathog. 2008, 4:e1000115.
    • (2008) PLoS Pathog. , vol.4
    • Perrone, L.A.1    Plowden, J.K.2    Garcia-Sastre, A.3    Katz, J.M.4    Tumpey, T.M.5
  • 89
    • 0027417395 scopus 로고
    • Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages
    • Heinecke J., Li W., Daehnke H., Goldstein J. Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages. J. Biol. Chem. 1993, 268:4069-4077.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4069-4077
    • Heinecke, J.1    Li, W.2    Daehnke, H.3    Goldstein, J.4
  • 90
    • 67749086712 scopus 로고    scopus 로고
    • SLC30A3 (ZnT3) oligomerization by dityrosine bonds regulates its subcellular localization and metal transport capacity
    • Salazar G., Falcon-Perez J.M., Harrison R., Faundez V. SLC30A3 (ZnT3) oligomerization by dityrosine bonds regulates its subcellular localization and metal transport capacity. PLoS One 2009, 4:e5896.
    • (2009) PLoS One , vol.4
    • Salazar, G.1    Falcon-Perez, J.M.2    Harrison, R.3    Faundez, V.4


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