메뉴 건너뛰기




Volumn 47, Issue 3, 2006, Pages 853-863

Expression of NADPH oxidase in rabbit corneal epithelial and stromal cells in culture

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; MESSENGER RNA; RAC PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; RNA; SUPEROXIDE DISMUTASE; PRIMER DNA; SUPEROXIDE;

EID: 33645401924     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.05-1063     Document Type: Article
Times cited : (20)

References (67)
  • 1
    • 0034638622 scopus 로고    scopus 로고
    • Superoxide as a messenger of endothelial function
    • Ulrich V, Bachschmid M. Superoxide as a messenger of endothelial function. Biochem Biophys Res Commun. 2000;278:1-8.
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 1-8
    • Ulrich, V.1    Bachschmid, M.2
  • 2
    • 0035066007 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS)-generating oxidases in the normal rabbit cornea and their involvement in the corneal damage evoked by UVB rays
    • Cejkova J, Stipek S, Crkovska J, Ardan T, Midelfart A. Reactive oxygen species (ROS)-generating oxidases in the normal rabbit cornea and their involvement in the corneal damage evoked by UVB rays. Histol Histopathol. 2001;16:523-533.
    • (2001) Histol Histopathol , vol.16 , pp. 523-533
    • Cejkova, J.1    Stipek, S.2    Crkovska, J.3    Ardan, T.4    Midelfart, A.5
  • 3
    • 0033817123 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase-derived superoxide contributes to hypereactivity in small mesenteric arteries from a rat model of chronic heart failure
    • Miller AA, Megson IL, Gray GA. Inducible nitric oxide synthase-derived superoxide contributes to hypereactivity in small mesenteric arteries from a rat model of chronic heart failure. Br J Pharmacol. 2000;131:29-36.
    • (2000) Br J Pharmacol , vol.131 , pp. 29-36
    • Miller, A.A.1    Megson, I.L.2    Gray, G.A.3
  • 4
    • 0034082278 scopus 로고    scopus 로고
    • Cellular oxygen sensing by mitochondria: Old questions, new insight
    • Chandel NS, Schumacker PT. Cellular oxygen sensing by mitochondria: old questions, new insight. J Appl Physiol. 2000;88:1880-1889.
    • (2000) J Appl Physiol , vol.88 , pp. 1880-1889
    • Chandel, N.S.1    Schumacker, P.T.2
  • 5
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • Vignais PV. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol Biol. 2002;59:1428-1459.
    • (2002) Cell Mol Biol , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 6
    • 0347711117 scopus 로고    scopus 로고
    • NADPH oxidases: Not just for leukocytes anymore!
    • Bokoch GM, Knaus UG. NADPH oxidases: not just for leukocytes anymore! Trends Biochem Sci. 2003;28:502-508.
    • (2003) Trends Biochem Sci , vol.28 , pp. 502-508
    • Bokoch, G.M.1    Knaus, U.G.2
  • 8
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H Oxidase: Role in cardiovascular biology and disease
    • Griendling KK, Sorescu D, Ushio-Fukai M. NAD(P)H Oxidase: role in cardiovascular biology and disease. Circ Res. 2000;86:494-501.
    • (2000) Circ Res , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 9
    • 0036257467 scopus 로고    scopus 로고
    • Corneal epithelial VEGF and cytochrome P450 4B1 expression in a rabbit model of closed eye contact lens wear
    • Mastyugin V, Mosaed S, Bonazzi A, Dunn MW, Schwartzman ML. Corneal epithelial VEGF and cytochrome P450 4B1 expression in a rabbit model of closed eye contact lens wear. Curr Eye Res. 2001;23:1-10.
    • (2001) Curr Eye Res , vol.23 , pp. 1-10
    • Mastyugin, V.1    Mosaed, S.2    Bonazzi, A.3    Dunn, M.W.4    Schwartzman, M.L.5
  • 11
    • 0034607821 scopus 로고    scopus 로고
    • Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly
    • DeLeo FR, Burritt JB, Yu L, Jesaitis AJ, Dinauer MC, Nauseef WM. Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly. J Biol Chem. 2000;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
  • 12
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping Y, Lapouge K, Smerdon SJ, Rittinger K. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell. 2003;113:343-355.
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 13
    • 0037155889 scopus 로고    scopus 로고
    • Architecture of the p40-p47-p67phox complex in the resting state of the NADPH oxidase: A central role for p67phox
    • Lapouge K, Smith SJ, Groemping Y, Rittinger K. Architecture of the p40-p47-p67phox complex in the resting state of the NADPH oxidase: a central role for p67phox. J Biol Chem. 2002;277:10121-10128.
    • (2002) J Biol Chem , vol.277 , pp. 10121-10128
    • Lapouge, K.1    Smith, S.J.2    Groemping, Y.3    Rittinger, K.4
  • 14
    • 0037108109 scopus 로고    scopus 로고
    • Current molecular models for NADPH oxidase regulation by Rac GTPase
    • Bokoch GM, Diebold BA. Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood. 2002;100:2692-2896.
    • (2002) Blood , vol.100 , pp. 2692-2896
    • Bokoch, G.M.1    Diebold, B.A.2
  • 15
    • 0142103458 scopus 로고    scopus 로고
    • Human monocytes use Rac1, not Rac2, in the NADPH oxidase complex
    • Zhao X, Carnevale KA, Cathcart MK. Human monocytes use Rac1, not Rac2, in the NADPH oxidase complex. J Biol Chem. 2003;278:40788-40792.
    • (2003) J Biol Chem , vol.278 , pp. 40788-40792
    • Zhao, X.1    Carnevale, K.A.2    Cathcart, M.K.3
  • 16
    • 0037097733 scopus 로고    scopus 로고
    • Multiple PU. 1 sites cooperate in the regulation of p40(phox) transcription during granulocytic differentiation of myeloid cells
    • Li SL, Valente AJ, Qiang M, Schlegel W, Gamez M, Clark RA. Multiple PU. 1 sites cooperate in the regulation of p40(phox) transcription during granulocytic differentiation of myeloid cells. Blood. 2002;99:4578-4587.
    • (2002) Blood , vol.99 , pp. 4578-4587
    • Li, S.L.1    Valente, A.J.2    Qiang, M.3    Schlegel, W.4    Gamez, M.5    Clark, R.A.6
  • 17
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • Cheng G, Cao Z, Xu X, van Meir EG, Lambeth JD. Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene. 2001;269:131-140.
    • (2001) Gene , vol.269 , pp. 131-140
    • Cheng, G.1    Cao, Z.2    Xu, X.3    van Meir, E.G.4    Lambeth, J.D.5
  • 18
    • 0038036799 scopus 로고    scopus 로고
    • Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells
    • Geiszt M, Lekstrom K, Witta J, Leto TL. Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J Biol Chem. 2003;278:20006-20012.
    • (2003) J Biol Chem , vol.278 , pp. 20006-20012
    • Geiszt, M.1    Lekstrom, K.2    Witta, J.3    Leto, T.L.4
  • 20
    • 0025765398 scopus 로고
    • Combined anti-herpes virus activity of nucleoside analogs and interferon
    • Taylor JL, Punda-Polic V, O'Brien WJ. Combined anti-herpes virus activity of nucleoside analogs and interferon. Curr Eye Res. 1991;10(suppl):205- 211.
    • (1991) Curr Eye Res , vol.10 , Issue.SUPPL. , pp. 205-211
    • Taylor, J.L.1    Punda-Polic, V.2    O'Brien, W.J.3
  • 21
    • 0035847051 scopus 로고    scopus 로고
    • A novel superoxide-producing NAD(P)H oxidase in kidney
    • Shiose A, Kuroda J, Tsuruya K, et al. A novel superoxide-producing NAD(P)H oxidase in kidney. J Biol Chem. 2001;276:1417-1423.
    • (2001) J Biol Chem , vol.276 , pp. 1417-1423
    • Shiose, A.1    Kuroda, J.2    Tsuruya, K.3
  • 22
    • 0028138966 scopus 로고
    • The functional expression of p47-phox and p67-phox may contribute to the generation of superoxide by an NADPH oxidase-like system in human fibroblasts
    • Jones SA, Wood JD, Coffey MJ, Jones OT. The functional expression of p47-phox and p67-phox may contribute to the generation of superoxide by an NADPH oxidase-like system in human fibroblasts. FEBS Lett. 1994;355:178-182.
    • (1994) FEBS Lett , vol.355 , pp. 178-182
    • Jones, S.A.1    Wood, J.D.2    Coffey, M.J.3    Jones, O.T.4
  • 23
    • 0031848577 scopus 로고    scopus 로고
    • Angiotensin II induces p67phox mRNA expression and NADPH oxidase superoxide generation in rabbit aortic adventitial fibroblasts
    • Pagano PJ, Chanock SJ, Siwik DA, Colucci WS, Clark JK. Angiotensin II induces p67phox mRNA expression and NADPH oxidase superoxide generation in rabbit aortic adventitial fibroblasts. Hypertension. 1998;32:331-337.
    • (1998) Hypertension , vol.32 , pp. 331-337
    • Pagano, P.J.1    Chanock, S.J.2    Siwik, D.A.3    Colucci, W.S.4    Clark, J.K.5
  • 24
    • 0026865323 scopus 로고
    • Analysis of gene expression: Use of oligonucleotide primers for glyceraldehyde-3-phosphate dehydrogenase
    • Dveksler GS, Basile AA, Dieffenbach CW. Analysis of gene expression: use of oligonucleotide primers for glyceraldehyde-3-phosphate dehydrogenase. PCR Methods Appl. 1992;1:283-285.
    • (1992) PCR Methods Appl , vol.1 , pp. 283-285
    • Dveksler, G.S.1    Basile, A.A.2    Dieffenbach, C.W.3
  • 25
    • 0037205457 scopus 로고    scopus 로고
    • Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells
    • Li JM, Shah AM. Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells. J Biol Chem. 2002;277:19952-19960.
    • (2002) J Biol Chem , vol.277 , pp. 19952-19960
    • Li, J.M.1    Shah, A.M.2
  • 26
    • 0035451497 scopus 로고    scopus 로고
    • Synthesis and biochemical applications of a solid cyclic nitrone spin trap: A relatively superior trap for detecting superoxide anions and glutathiyl radicals
    • Zhao H, Joseph J, Zhang H, Karoui H, Kalyanaraman B. Synthesis and biochemical applications of a solid cyclic nitrone spin trap: a relatively superior trap for detecting superoxide anions and glutathiyl radicals. Free Radic Biol Med. 2001;31:599-606.
    • (2001) Free Radic Biol Med , vol.31 , pp. 599-606
    • Zhao, H.1    Joseph, J.2    Zhang, H.3    Karoui, H.4    Kalyanaraman, B.5
  • 27
    • 0028455102 scopus 로고
    • Simulation of multiple isotropic spin-trap EPR spectra
    • Duling D. Simulation of multiple isotropic spin-trap EPR spectra. J Magn Reson B. 1994;104:105-110.
    • (1994) J Magn Reson B , vol.104 , pp. 105-110
    • Duling, D.1
  • 28
    • 0031443873 scopus 로고    scopus 로고
    • Localization of a constitutively active, phagocyte-like NADPH oxidase in rabbit aortic adventitia: Enhancement by angiotensin II
    • Pagano PJ, Clark JK, Cifuentes-Pagano ME, Clark SM, Callis GM, Quinn MT. Localization of a constitutively active, phagocyte-like NADPH oxidase in rabbit aortic adventitia: enhancement by angiotensin II. Proc Natl Acad Sci USA. 1997;94:14483-14488.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14483-14488
    • Pagano, P.J.1    Clark, J.K.2    Cifuentes-Pagano, M.E.3    Clark, S.M.4    Callis, G.M.5    Quinn, M.T.6
  • 29
    • 0031002421 scopus 로고    scopus 로고
    • Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages
    • Xia Y, Zweier JL. Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages. Proc Natl Acad Sci USA. 1997;94:6954-6958.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6954-6958
    • Xia, Y.1    Zweier, J.L.2
  • 30
    • 4544274760 scopus 로고    scopus 로고
    • Nox3 regulation by NOXO1, p47phox, and p67phox
    • Cheng G, Ritsick D, Lambeth JD. Nox3 regulation by NOXO1, p47phox, and p67phox. J Biol Chem. 2004;279:34250-34255.
    • (2004) J Biol Chem , vol.279 , pp. 34250-34255
    • Cheng, G.1    Ritsick, D.2    Lambeth, J.D.3
  • 31
    • 0038205912 scopus 로고    scopus 로고
    • NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes
    • Geiszt M, Lekstrom K, Brenner S, et al. NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes. J Immunol. 2003;171:299-306.
    • (2003) J Immunol , vol.171 , pp. 299-306
    • Geiszt, M.1    Lekstrom, K.2    Brenner, S.3
  • 32
    • 0036486772 scopus 로고    scopus 로고
    • Cloning and sequencing of rabbit leukocyte NADPH oxidase genes reveals a unique p67(phox) homolog
    • Gauss KA, Mascolo PL, Siemsen DW, et al. Cloning and sequencing of rabbit leukocyte NADPH oxidase genes reveals a unique p67(phox) homolog. J Leukoc Biol. 2002;71:319-328.
    • (2002) J Leukoc Biol , vol.71 , pp. 319-328
    • Gauss, K.A.1    Mascolo, P.L.2    Siemsen, D.W.3
  • 33
    • 11144356447 scopus 로고    scopus 로고
    • Upregulation of NAD(P)H oxidase 1 in hypoxia activates hypoxia-inducible factor 1 via increase in reactive oxygen species
    • Goyal P, Weissmann N, Grimminger F, et al. Upregulation of NAD(P)H oxidase 1 in hypoxia activates hypoxia-inducible factor 1 via increase in reactive oxygen species. Free Radic Biol Med. 2004;36:1279-1288.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1279-1288
    • Goyal, P.1    Weissmann, N.2    Grimminger, F.3
  • 34
    • 0036882103 scopus 로고    scopus 로고
    • Cytochrome b558-dependent NAD(P)H oxidase-phox units in smooth muscle and macrophages of atherosclerotic lesions
    • Kalinina N, Agrotis A, Tararak E, et al. Cytochrome b558-dependent NAD(P)H oxidase-phox units in smooth muscle and macrophages of atherosclerotic lesions. Arterioscler Thromb Vasc Biol. 2002;22:2037-2043.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 2037-2043
    • Kalinina, N.1    Agrotis, A.2    Tararak, E.3
  • 35
    • 0035072492 scopus 로고    scopus 로고
    • Evaluation of the expression of NADPH oxidase components during maturation of HL-60 clone 15 cells to eosinophilic lineage
    • Hua J, Hasebe T, Someya A, Nakamura S, Sugimoto K, Nagaoka I. Evaluation of the expression of NADPH oxidase components during maturation of HL-60 clone 15 cells to eosinophilic lineage. Inflamm Res. 2001;50:156-167.
    • (2001) Inflamm Res , vol.50 , pp. 156-167
    • Hua, J.1    Hasebe, T.2    Someya, A.3    Nakamura, S.4    Sugimoto, K.5    Nagaoka, I.6
  • 36
    • 0035914317 scopus 로고    scopus 로고
    • Identification of a spectrally stable proteolytic fragment of human neutrophil flavocytochrome b composed of the NH2-terminal regions of gp91phox and p22phox
    • Foubert TR, Bleazard JB, Burritt JB, et al. Identification of a spectrally stable proteolytic fragment of human neutrophil flavocytochrome b composed of the NH2-terminal regions of gp91phox and p22phox. J Biol Chem. 2001;276:38852-38861.
    • (2001) J Biol Chem , vol.276 , pp. 38852-38861
    • Foubert, T.R.1    Bleazard, J.B.2    Burritt, J.B.3
  • 37
    • 0141889087 scopus 로고    scopus 로고
    • TNF-alpha induces phosphorylation of p47(phox) in human neutrophils: Partial phosphorylation of p47phox is a common event of priming of human neutrophils by TNF-alpha and granulocyte-macrophage colony-stimulating factor
    • Dewas C, Dang PM, Gougerot-Pocidalo MA, El-Benna J. TNF-alpha induces phosphorylation of p47(phox) in human neutrophils: partial phosphorylation of p47phox is a common event of priming of human neutrophils by TNF-alpha and granulocyte-macrophage colony-stimulating factor. J Immunol. 2003;171:4392-4398.
    • (2003) J Immunol , vol.171 , pp. 4392-4398
    • Dewas, C.1    Dang, P.M.2    Gougerot-Pocidalo, M.A.3    El-Benna, J.4
  • 38
    • 0037783377 scopus 로고    scopus 로고
    • c-Src induces phosphorylation and translocation of p47phox: Role in superoxide generation by angiotensin II in human vascular smooth muscle cells (see comment)
    • Touyz RM, Yao G, Schiffrin EL. c-Src induces phosphorylation and translocation of p47phox: role in superoxide generation by angiotensin II in human vascular smooth muscle cells (see comment). Arterioscler Thromb Vasc Biol. 2003;23:981-987.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 981-987
    • Touyz, R.M.1    Yao, G.2    Schiffrin, E.L.3
  • 39
    • 0033215179 scopus 로고    scopus 로고
    • Molecular characterization of autosomal recessive chronic granulomatous disease caused by a defect of the nicotinamide adenine dinucleotide phosphate (reduced form) oxidase component p67-phox
    • Patino PJ, Rae J, Noack D, et al. Molecular characterization of autosomal recessive chronic granulomatous disease caused by a defect of the nicotinamide adenine dinucleotide phosphate (reduced form) oxidase component p67-phox. Blood. 1999;94:2505-2514.
    • (1999) Blood , vol.94 , pp. 2505-2514
    • Patino, P.J.1    Rae, J.2    Noack, D.3
  • 40
    • 1442307630 scopus 로고    scopus 로고
    • Molecular mechanism for activation of superoxide-producing NADPH oxidases
    • Takeya R, Sumimoto H. Molecular mechanism for activation of superoxide-producing NADPH oxidases. Mol Cells. 2003;16:271-277.
    • (2003) Mol Cells , vol.16 , pp. 271-277
    • Takeya, R.1    Sumimoto, H.2
  • 41
    • 0042991381 scopus 로고    scopus 로고
    • Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases
    • Takeya R, Ueno N, Kami K, et al. Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem. 2003;278:25234-25246.
    • (2003) J Biol Chem , vol.278 , pp. 25234-25246
    • Takeya, R.1    Ueno, N.2    Kami, K.3
  • 42
    • 0025081316 scopus 로고
    • A 63-kilodalton cytosolic polypeptide involved in superoxide generation in porcine neutrophils: Purification and characterization
    • Tanaka T, Imajoh-Ohmi S, Kanegasaki S, Takagi Y, Makino R, Ishimura Y. A 63-kilodalton cytosolic polypeptide involved in superoxide generation in porcine neutrophils: purification and characterization. J Biol Chem. 1990;265:18717-18720.
    • (1990) J Biol Chem , vol.265 , pp. 18717-18720
    • Tanaka, T.1    Imajoh-Ohmi, S.2    Kanegasaki, S.3    Takagi, Y.4    Makino, R.5    Ishimura, Y.6
  • 43
    • 0030592955 scopus 로고    scopus 로고
    • Translocation of guinea pig p40-phox during activation of NADPH oxidase
    • Someya A, Nagaoka I, Nunoi H, Yamashita T. Translocation of guinea pig p40-phox during activation of NADPH oxidase. Biochim Biophys Acta. 1996;1277:217-225.
    • (1996) Biochim Biophys Acta , vol.1277 , pp. 217-225
    • Someya, A.1    Nagaoka, I.2    Nunoi, H.3    Yamashita, T.4
  • 44
    • 0033864438 scopus 로고    scopus 로고
    • Evaluation of the expression of NADPH oxidase components during maturation of HL-60 cells to neutrophil lineage
    • Hua J, Hasebe T, Someya A, Nakamura S, Sugimoto K, Nagaoka I. Evaluation of the expression of NADPH oxidase components during maturation of HL-60 cells to neutrophil lineage. J Leukoc Biol. 2000;68:216-224.
    • (2000) J Leukoc Biol , vol.68 , pp. 216-224
    • Hua, J.1    Hasebe, T.2    Someya, A.3    Nakamura, S.4    Sugimoto, K.5    Nagaoka, I.6
  • 45
    • 0032733897 scopus 로고    scopus 로고
    • Phosphorylation of p40-phox during activation of neutrophil NADPH oxidase
    • Someya A, Nunoi H, Hasebe T, Nagaoka I. Phosphorylation of p40-phox during activation of neutrophil NADPH oxidase. J Leukoc Biol. 1999;66:851-857.
    • (1999) J Leukoc Biol , vol.66 , pp. 851-857
    • Someya, A.1    Nunoi, H.2    Hasebe, T.3    Nagaoka, I.4
  • 46
    • 4644253368 scopus 로고    scopus 로고
    • Corneal fibroblasts respond rapidly to changes in local mechanical stress
    • Petroll WM, Vishwanath M, Ma L. Corneal fibroblasts respond rapidly to changes in local mechanical stress. Invest Ophthalmol Vis Sci. 2004;45:3466-3474.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 3466-3474
    • Petroll, W.M.1    Vishwanath, M.2    Ma, L.3
  • 47
    • 0030453086 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Molecular interaction of oxidase proteins
    • DeLeo FR, Quinn MT. Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase proteins. J Leukoc Biol. 1996;60:677-691.
    • (1996) J Leukoc Biol , vol.60 , pp. 677-691
    • DeLeo, F.R.1    Quinn, M.T.2
  • 48
    • 0021225120 scopus 로고
    • Unsaturated fatty acids stimulate NADPH-dependent superoxide production by cell-free system derived from macrophages
    • Bromberg Y, Pick E. Unsaturated fatty acids stimulate NADPH-dependent superoxide production by cell-free system derived from macrophages. Cell Immunol. 1984;88:213-221.
    • (1984) Cell Immunol , vol.88 , pp. 213-221
    • Bromberg, Y.1    Pick, E.2
  • 49
    • 21144434217 scopus 로고    scopus 로고
    • Extension of murine life span by overexpression of catalase targeted to mitochondria
    • Schriner SE, Linford NJ, Martin GM, et al. Extension of murine life span by overexpression of catalase targeted to mitochondria. Science. 2005;308:1909-1911.
    • (2005) Science , vol.308 , pp. 1909-1911
    • Schriner, S.E.1    Linford, N.J.2    Martin, G.M.3
  • 51
    • 0035514402 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces manganese-superoxide dismutase expression in endothelial cells by a Rac1-regulated NADPH oxidase-dependent mechanism
    • Abid MR, Tsai JC, Spokes KC, Deshpande SS, Irani K, Aird WC. Vascular endothelial growth factor induces manganese-superoxide dismutase expression in endothelial cells by a Rac1-regulated NADPH oxidase-dependent mechanism. FASEB J. 2001;15:2548-2550.
    • (2001) FASEB J , vol.15 , pp. 2548-2550
    • Abid, M.R.1    Tsai, J.C.2    Spokes, K.C.3    Deshpande, S.S.4    Irani, K.5    Aird, W.C.6
  • 52
    • 0141425760 scopus 로고    scopus 로고
    • Ribonucleotide reductases: Radical chemistry and inhibition at the active site
    • Robins MJ. Ribonucleotide reductases: radical chemistry and inhibition at the active site. Nucleosides Nucleotides Nucleic Acids. 2003;22:519-534.
    • (2003) Nucleosides Nucleotides Nucleic Acids , vol.22 , pp. 519-534
    • Robins, M.J.1
  • 53
  • 54
    • 0031966263 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) generated by xanthine oxidase in the corneal epithelium and their potential participation in the damage of the corneal epithelium after prolonged use of contact lenses in rabbits
    • Cejkova J, Labsky J, Vacik J. Reactive oxygen species (ROS) generated by xanthine oxidase in the corneal epithelium and their potential participation in the damage of the corneal epithelium after prolonged use of contact lenses in rabbits. Acta Histochem. 1998;100:171-184.
    • (1998) Acta Histochem , vol.100 , pp. 171-184
    • Cejkova, J.1    Labsky, J.2    Vacik, J.3
  • 56
    • 4644350365 scopus 로고    scopus 로고
    • Cutting edge: Direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B
    • Park HS, Jung HY, Park EY, Kim J, Lee WJ, Bae YS. Cutting edge: direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B. J Immunol. 2004;173:3589-3593.
    • (2004) J Immunol , vol.173 , pp. 3589-3593
    • Park, H.S.1    Jung, H.Y.2    Park, E.Y.3    Kim, J.4    Lee, W.J.5    Bae, Y.S.6
  • 57
    • 0242298634 scopus 로고    scopus 로고
    • Contrasting roles of NADPH oxidase isoforms in pressure-overload versus angiotensin II-induced cardiac hypertrophy
    • Byrne JA, Grieve DJ, Bendall JK, et al. Contrasting roles of NADPH oxidase isoforms in pressure-overload versus angiotensin II-induced cardiac hypertrophy. Circ Res. 2003;93:802-805.
    • (2003) Circ Res , vol.93 , pp. 802-805
    • Byrne, J.A.1    Grieve, D.J.2    Bendall, J.K.3
  • 58
    • 0038363940 scopus 로고    scopus 로고
    • Single-step immunoaffinity purification and characterization of dodecylmaltoside-solubilized human neutrophil flavocytochrome b
    • Taylor RM, Burritt JB, Foubert TR, et al. Single-step immunoaffinity purification and characterization of dodecylmaltoside-solubilized human neutrophil flavocytochrome b. Biochim Biophys Acta. 2003;1612:65-75.
    • (2003) Biochim Biophys Acta , vol.1612 , pp. 65-75
    • Taylor, R.M.1    Burritt, J.B.2    Foubert, T.R.3
  • 59
    • 0033585122 scopus 로고    scopus 로고
    • Mechanism for phosphorylation-induced activation of the phagocyte NADPH oxidase protein p47phox. Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47phox, thereby activating the oxidase
    • Ago T, Nunoi H, Ito T, Sumimoto H. Mechanism for phosphorylation-induced activation of the phagocyte NADPH oxidase protein p47phox. Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47phox, thereby activating the oxidase. J Biol Chem. 1999;274:33644-33653.
    • (1999) J Biol Chem , vol.274 , pp. 33644-33653
    • Ago, T.1    Nunoi, H.2    Ito, T.3    Sumimoto, H.4
  • 60
    • 0037446850 scopus 로고    scopus 로고
    • Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation
    • Ago T, Kuribayashi F, Hiroaki H, et al. Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation. Proc Natl Acad Sci USA. 2003;100:4474-4479.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4474-4479
    • Ago, T.1    Kuribayashi, F.2    Hiroaki, H.3
  • 61
    • 0038303192 scopus 로고    scopus 로고
    • Modulation of p47PHOX activity by site-specific phosphorylation: Akt-dependent activation of the NADPH oxidase
    • Hoyal CR, Gutierrez A, Young BM, et al. Modulation of p47PHOX activity by site-specific phosphorylation: Akt-dependent activation of the NADPH oxidase. Proc Natl Acad Sci USA. 2003;100:5130-5135.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5130-5135
    • Hoyal, C.R.1    Gutierrez, A.2    Young, B.M.3
  • 62
    • 0027325899 scopus 로고
    • Purification of the 260 kDa cytosolic complex involved in the superoxide production of guinea pig neutrophils
    • Someya A, Nagaoka I, Yamashita T. Purification of the 260 kDa cytosolic complex involved in the superoxide production of guinea pig neutrophils. FEBS Lett. 1993;330:215-218.
    • (1993) FEBS Lett , vol.330 , pp. 215-218
    • Someya, A.1    Nagaoka, I.2    Yamashita, T.3
  • 63
    • 0030975474 scopus 로고    scopus 로고
    • p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain
    • Sathyamoorthy M, de Mendez I, Adams AG, Leto TL. p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain. J Biol Chem. 1997;272:9141-9146.
    • (1997) J Biol Chem , vol.272 , pp. 9141-9146
    • Sathyamoorthy, M.1    de Mendez, I.2    Adams, A.G.3    Leto, T.L.4
  • 64
    • 0032514915 scopus 로고    scopus 로고
    • p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase: Implication of a protein kinase c-type kinase in the phosphorylation process
    • Bouin AP, Grandvaux N, Vignais PV, Fuchs A. p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase: implication of a protein kinase c-type kinase in the phosphorylation process. J Biol Chem. 1998;273:30097-30103.
    • (1998) J Biol Chem , vol.273 , pp. 30097-30103
    • Bouin, A.P.1    Grandvaux, N.2    Vignais, P.V.3    Fuchs, A.4
  • 65
    • 1642408280 scopus 로고    scopus 로고
    • Phosphorylated p40PHOX as a negative regulator of NADPH oxidase
    • Lopes LR, Dagher MC, Gutierrez A, et al. Phosphorylated p40PHOX as a negative regulator of NADPH oxidase. Biochemistry. 2004;43:3723-3730.
    • (2004) Biochemistry , vol.43 , pp. 3723-3730
    • Lopes, L.R.1    Dagher, M.C.2    Gutierrez, A.3
  • 66
    • 0029076724 scopus 로고
    • Interactions between the cytosolic components p47phox and p67phox of the human neutrophil NADPH oxidase that are not required for activation in the cell-free system
    • Leusen JH, Fluiter K, Hilarius PM, Roos D, Verhoeven AJ, Bolscher BG. Interactions between the cytosolic components p47phox and p67phox of the human neutrophil NADPH oxidase that are not required for activation in the cell-free system. J Biol Chem. 1995;270:11216-11221.
    • (1995) J Biol Chem , vol.270 , pp. 11216-11221
    • Leusen, J.H.1    Fluiter, K.2    Hilarius, P.M.3    Roos, D.4    Verhoeven, A.J.5    Bolscher, B.G.6
  • 67
    • 0037007097 scopus 로고    scopus 로고
    • Assembly of the neutrophil respiratory burst oxidase: A direct interaction between p67PHOX and cytochrome b558 II
    • Dang PM, Cross AR, Quinn MT, Babior BM. Assembly of the neutrophil respiratory burst oxidase: a direct interaction between p67PHOX and cytochrome b558 II. Proc Natl Acad Sci USA. 2002;99:4262-4265.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4262-4265
    • Dang, P.M.1    Cross, A.R.2    Quinn, M.T.3    Babior, B.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.