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Volumn 16, Issue 1, 2004, Pages 42-47

NADPH oxidase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; ANTIFUNGAL AGENT; COTRIMOXAZOLE; PROTEIN; PROTEIN P22; PROTEIN P40; PROTEIN P47; PROTEIN P67; PROTEIN P91; PROTEIN SH3; RECOMBINANT GAMMA INTERFERON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; UNCLASSIFIED DRUG;

EID: 1042278903     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coi.2003.12.001     Document Type: Review
Times cited : (690)

References (65)
  • 1
    • 0033585122 scopus 로고    scopus 로고
    • Mechanism for phosphorylation-induced activation of the phagocyte NADPH oxidase protein p47(phox). Triple replacement of serines 303, 304, and 328 with aspartates disrupts the sh3 domain-mediated intramolecular interaction in p47(phox), thereby activating the oxidase
    • Ago T., Nunoi H., Ito T., Sumimoto H. Mechanism for phosphorylation- induced activation of the phagocyte NADPH oxidase protein p47(phox). Triple replacement of serines 303, 304, and 328 with aspartates disrupts the sh3 domain-mediated intramolecular interaction in p47(phox), thereby activating the oxidase. J. Biol. Chem. 274:1999;33644-33653.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33644-33653
    • Ago, T.1    Nunoi, H.2    Ito, T.3    Sumimoto, H.4
  • 3
    • 0019880799 scopus 로고
    • Cytochrome b-245 of neutrophils is also present in human monocytes, macrophages and eosinophils
    • Segal A.W., Garcia R., Goldstone A.H., Cross A.R., Jones O.T.G. Cytochrome b-245 of neutrophils is also present in human monocytes, macrophages and eosinophils. Biochem. J. 196:1981;363-367.
    • (1981) Biochem. J. , vol.196 , pp. 363-367
    • Segal, A.W.1    Garcia, R.2    Goldstone, A.H.3    Cross, A.R.4    Jones, O.T.G.5
  • 4
    • 0037154250 scopus 로고    scopus 로고
    • Reactive oxygen generated by Nox1 triggers the angiogenic switch
    • The reactive oxygen-generating enzyme Nox1 was shown to be a potent trigger of the angiogenic switch, increasing the vascularity of tumors and inducing molecular markers of angiogenesis.
    • Arbiser J.L., Petros J., Klafter R., Govindajaran B., McLaughlin E.R., Brown L.F., Cohen C., Moses M., Kilroy S., Arnold R.S., Lambeth J.D. Reactive oxygen generated by Nox1 triggers the angiogenic switch. Proc. Natl. Acad. Sci. USA. 99:2002;715-720 The reactive oxygen-generating enzyme Nox1 was shown to be a potent trigger of the angiogenic switch, increasing the vascularity of tumors and inducing molecular markers of angiogenesis.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 715-720
    • Arbiser, J.L.1    Petros, J.2    Klafter, R.3    Govindajaran, B.4    Mclaughlin, E.R.5    Brown, L.F.6    Cohen, C.7    Moses, M.8    Kilroy, S.9    Arnold, R.S.10    Lambeth, J.D.11
  • 5
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox 3, Nox4, and Nox5
    • Cheng G., Cao Z., Xu X., van Meir E.G., Lambeth J.D. Homologs of gp91phox: cloning and tissue expression of Nox 3, Nox4, and Nox5. Gene. 269:2001;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
  • 6
    • 0024410891 scopus 로고
    • Antibody to interleukin-5 inhibits helminth-induced eosinophilia in mice
    • Coffman R.L., Seymour B.W.P., Hudak S., Jackson J., Rennick D. Antibody to interleukin-5 inhibits helminth-induced eosinophilia in mice. Science. 245:1989;308-310.
    • (1989) Science , vol.245 , pp. 308-310
    • Coffman, R.L.1    Seymour, B.W.P.2    Hudak, S.3    Jackson, J.4    Rennick, D.5
  • 7
    • 0016414528 scopus 로고
    • Superoxide dismutases
    • Fridovich I. Superoxide dismutases. Annu. Rev. Biochem. 44:1975;147-159.
    • (1975) Annu. Rev. Biochem. , vol.44 , pp. 147-159
    • Fridovich, I.1
  • 8
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • Babior B.M. NADPH oxidase: an update. Blood. 93:1999;1464-1476.
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 10
    • 0035808392 scopus 로고    scopus 로고
    • Eosinophil peroxidase oxidation of thiocyanate. Characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system
    • Arlandson M., Decker T., Roongta V.A., Bonilla L., Mayo K.H., MacPherson J.C., Hazen S.L., Slungaard A. Eosinophil peroxidase oxidation of thiocyanate. Characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system. J. Biol. Chem. 276:2001;215-224.
    • (2001) J. Biol. Chem. , vol.276 , pp. 215-224
    • Arlandson, M.1    Decker, T.2    Roongta, V.A.3    Bonilla, L.4    Mayo, K.H.5    Macpherson, J.C.6    Hazen, S.L.7    Slungaard, A.8
  • 11
    • 0026762871 scopus 로고
    • Intracellular singlet oxygen generation by phagocytosing neutrophils in response to particles coated with a chemical trap
    • Steinbeck M.J., Khan A.U., Karnovsky M.J. Intracellular singlet oxygen generation by phagocytosing neutrophils in response to particles coated with a chemical trap. J. Biol. Chem. 267:1992;13425-13433.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13425-13433
    • Steinbeck, M.J.1    Khan, A.U.2    Karnovsky, M.J.3
  • 12
    • 0027185676 scopus 로고
    • Extracellular production of singlet oxygen by stimulated macrophages quantified using 9,10-diphenylanthracene and perylene in a polystyrene film
    • Steinbeck M.J., Khan A.U., Karnovsky M.J. Extracellular production of singlet oxygen by stimulated macrophages quantified using 9,10- diphenylanthracene and perylene in a polystyrene film. J. Biol. Chem. 268:1993;15649-15654.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15649-15654
    • Steinbeck, M.J.1    Khan, A.U.2    Karnovsky, M.J.3
  • 14
    • 0037453053 scopus 로고    scopus 로고
    • Ozone in biology
    • An informative commentary discussing the formation and role of ozone in biological systems.
    • Lerner R.A., Eschenmoser A. Ozone in biology. Proc. Natl. Acad. Sci. USA. 100:2003;3013-3015 An informative commentary discussing the formation and role of ozone in biological systems.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3013-3015
    • Lerner, R.A.1    Eschenmoser, A.2
  • 15
    • 0037073888 scopus 로고    scopus 로고
    • Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation
    • This study suggests that the antibody-catalyzed water-oxidation pathway produces both hydrogen peroxide and a molecular species with a chemical signature similar to that of ozone, which mediate the killing of bacteria.
    • Wentworth P. Jr., McDunn J.E., Wentworth A.D., Takeuchi C., Nieva J., Jones T., Bautista C., Ruedi J.M., Gutierrez A., Janda K.D.et al. Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation. Science. 298:2002;2195-2199 This study suggests that the antibody-catalyzed water-oxidation pathway produces both hydrogen peroxide and a molecular species with a chemical signature similar to that of ozone, which mediate the killing of bacteria.
    • (2002) Science , vol.298 , pp. 2195-2199
    • Wentworth, P.Jr.1    Mcdunn, J.E.2    Wentworth, A.D.3    Takeuchi, C.4    Nieva, J.5    Jones, T.6    Bautista, C.7    Ruedi, J.M.8    Gutierrez, A.9    Janda, K.D.10
  • 16
    • 0028198779 scopus 로고
    • The Fenton oxidation mechanism: Reactivities of biologically relevant substrates with two oxidizing intermediates differ from those predicted for the hydroxyl radical
    • Wink D.A., Nims R.W., Saavedra J.E., Utermahlen W.E. Jr., Ford P.C. The Fenton oxidation mechanism: reactivities of biologically relevant substrates with two oxidizing intermediates differ from those predicted for the hydroxyl radical. Proc. Natl. Acad. Sci. USA. 91:1994;6604-6608.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6604-6608
    • Wink, D.A.1    Nims, R.W.2    Saavedra, J.E.3    Utermahlen, W.E.Jr.4    Ford, P.C.5
  • 17
    • 0026011632 scopus 로고
    • Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase
    • Gardner P.R., Fridovich I. Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase. J. Biol. Chem. 266:1991;1478-1483.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1478-1483
    • Gardner, P.R.1    Fridovich, I.2
  • 18
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner P.R., Fridovich I. Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266:1991;19328-19333.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 19
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • Hausladen A., Fridovich I. Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J. Biol. Chem. 269:1994;29405-29408.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 21
    • 0642278047 scopus 로고    scopus 로고
    • PHOX
    • PHOX. J Vet Sci 2000, 1:19-26.
    • (2000) J Vet Sci , vol.1 , pp. 19-26
  • 22
    • 0028982947 scopus 로고
    • Cytochrome b245 of the neutrophil superoxide-generating system contains two nonidentical hemes. Potentiometric studies of a mutant form of gp91phox
    • Cross A.R., Rae J., Curnutte J.T. Cytochrome b245 of the neutrophil superoxide-generating system contains two nonidentical hemes. Potentiometric studies of a mutant form of gp91phox. J. Biol. Chem. 270:1995;17075-17077.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17075-17077
    • Cross, A.R.1    Rae, J.2    Curnutte, J.T.3
  • 24
    • 0032706039 scopus 로고    scopus 로고
    • The active form of the ferric heme in neutrophil Cytochrome b(558) is low-spin in the reconstituted cell-free system in the presence of amphophil
    • Fujii H., Finnegan M.G., Johnson M.K. The active form of the ferric heme in neutrophil Cytochrome b(558) is low-spin in the reconstituted cell-free system in the presence of amphophil. J. Biochem. (Tokyo). 126:1999;708-714.
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 708-714
    • Fujii, H.1    Finnegan, M.G.2    Johnson, M.K.3
  • 25
    • 0024340666 scopus 로고
    • Use of an affinity label to probe the function of the NADPH binding component of the respiratory burst oxidase of human neutrophils
    • Smith R.M., Curnutte J.T., Mayo L.A., Babior B.M. Use of an affinity label to probe the function of the NADPH binding component of the respiratory burst oxidase of human neutrophils. J. Biol. Chem. 264:1989;12243-12248.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12243-12248
    • Smith, R.M.1    Curnutte, J.T.2    Mayo, L.A.3    Babior, B.M.4
  • 26
    • 0024586594 scopus 로고
    • Affinity labeling of the cytosolic and membrane components of respiratory burst oxidase by the 2′,3′-dialdehyde derivative of NADPH. Evidence for a cytosolic location of the nucleotide-binding site in the resting cell
    • Smith R.M., Curnutte J.T., Babior B.M. Affinity labeling of the cytosolic and membrane components of respiratory burst oxidase by the 2′,3′-dialdehyde derivative of NADPH. Evidence for a cytosolic location of the nucleotide-binding site in the resting cell. J. Biol. Chem. 264:1989;1958-1962.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1958-1962
    • Smith, R.M.1    Curnutte, J.T.2    Babior, B.M.3
  • 27
    • 0029665045 scopus 로고    scopus 로고
    • The cytosolic subunit p67phox contains an NADPH-binding site that participates in catalysis by the leukocyte NADPH oxidase
    • Smith R.M., Connor J.A., Chen L.M., Babior B.M. The cytosolic subunit p67phox contains an NADPH-binding site that participates in catalysis by the leukocyte NADPH oxidase. J. Clin. Invest. 98:1996;977-983.
    • (1996) J. Clin. Invest. , vol.98 , pp. 977-983
    • Smith, R.M.1    Connor, J.A.2    Chen, L.M.3    Babior, B.M.4
  • 28
    • 0033522453 scopus 로고    scopus 로고
    • PHOX, a cystosolic subunit of the leukocyte NADPH oxidase
    • PHOX, a cystosolic subunit of the leukocyte NADPH oxidase. Biochemistry. 38:1999;5746-5753.
    • (1999) Biochemistry , vol.38 , pp. 5746-5753
    • Dang, P.M.C.1    Babior, B.M.2    Smith, R.M.3
  • 29
    • 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. 271:1996;22578-22582.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22578-22582
    • Freeman, J.L.1    Lambeth, J.D.2
  • 30
    • 0032540225 scopus 로고    scopus 로고
    • Activation of the leukocyte NADPH oxidase by phorbol ester requires the phosphorylation of p47phox on serine S303 or S304
    • Inanami O., Johnson J.L., McAdara J.K., El Benna J., Faust L.P., Newburger P.E., Babior B.M. Activation of the leukocyte NADPH oxidase by phorbol ester requires the phosphorylation of p47phox on serine S303 or S304. J. Biol. Chem. 273:1998;9539-9543.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9539-9543
    • Inanami, O.1    Johnson, J.L.2    Mcadara, J.K.3    El Benna, J.4    Faust, L.P.5    Newburger, P.E.6    Babior, B.M.7
  • 31
    • 0032567417 scopus 로고    scopus 로고
    • Activation of p47(PHOX), a cytosolic subunit of the leukocyte NADPH oxidase. Phosphorylation of ser-359 or ser-370 precedes phosphorylation at other sites and is required for activity
    • Johnson J.L., Park J.W., El Benna J., Faust L.P., Inanami O., Babior B.M. Activation of p47(PHOX), a cytosolic subunit of the leukocyte NADPH oxidase. Phosphorylation of ser-359 or ser-370 precedes phosphorylation at other sites and is required for activity. J. Biol. Chem. 273:1998;35147-35152.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35147-35152
    • Johnson, J.L.1    Park, J.W.2    El Benna, J.3    Faust, L.P.4    Inanami, O.5    Babior, B.M.6
  • 32
    • 0038303192 scopus 로고    scopus 로고
    • Modulation of p47PHOX activity by site-specific phosphorylation: Akt-dependent activation of the NADPH oxidase
    • Activation of the oxidase by a kinase other than protein kinase C. This work brings the oxidase into the domain of phosphoinositide 3-kinase.
    • Hoyal C.R., Gutierrez A., Young B.M., Catz S.D., Lin J.H., Tsichlis P.N., Babior B.M. Modulation of p47PHOX activity by site-specific phosphorylation: Akt-dependent activation of the NADPH oxidase. Proc. Natl. Acad. Sci. USA. 100:2003;5130-5135 Activation of the oxidase by a kinase other than protein kinase C. This work brings the oxidase into the domain of phosphoinositide 3-kinase.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5130-5135
    • Hoyal, C.R.1    Gutierrez, A.2    Young, B.M.3    Catz, S.D.4    Lin, J.H.5    Tsichlis, P.N.6    Babior, B.M.7
  • 33
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • A highly original crystallographic study that reveals a great deal about how the oxidase is activated.
    • Groemping Y., Lapouge K., Smerdon M.J., Rittinger K. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell. 113:2003;343-355 A highly original crystallographic study that reveals a great deal about how the oxidase is activated.
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, M.J.3    Rittinger, K.4
  • 34
    • 0025114585 scopus 로고
    • Human neutrophil Cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease
    • Dinauer M.C., Pierce E.A., Bruns G.A.P., Curnutte J.T., Orkin S.H. Human neutrophil Cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease. J. Clin. Invest. 86:1990;1729-1737.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1729-1737
    • Dinauer, M.C.1    Pierce, E.A.2    Bruns, G.A.P.3    Curnutte, J.T.4    Orkin, S.H.5
  • 35
    • 0037155889 scopus 로고    scopus 로고
    • Architecture of the P40-p47-p67 phox complex in the resting state of the NADPH oxidase. A central role for p67phox
    • Lapouge K., Smith S.J., Groemping Y., Rittinger K. Architecture of the P40-p47-p67 phox complex in the resting state of the NADPH oxidase. A central role for p67phox. J. Biol. Chem. 277:2002;10121-10128.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10121-10128
    • Lapouge, K.1    Smith, S.J.2    Groemping, Y.3    Rittinger, K.4
  • 37
    • 0030975474 scopus 로고    scopus 로고
    • P40phox down-regulates NADPH oxidase activity through interactions with its SH3 domain
    • Sathyamoorthy M., de Mendez I., Adams A.G., Leto T.L. p40phox down-regulates NADPH oxidase activity through interactions with its SH3 domain. J. Biol. Chem. 272:1997;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
  • 39
    • 0036141820 scopus 로고    scopus 로고
    • Upregulation of Nox-based NAD(P)H oxidases in restenosis after carotid injury
    • An important study concerning the relationship between the NADPH oxidases (in this case a nox) and vascular injury.
    • Szocs K., Lassegue B., Sorescu D., Hilenski L.L., Valppu L., Couse T.L., Wilcox J.N., Quinn M.T., Lambeth J.D., Griendling K.K. Upregulation of Nox-based NAD(P)H oxidases in restenosis after carotid injury. Arterioscler. Thromb. Vasc. Biol. 22:2002;4-5 An important study concerning the relationship between the NADPH oxidases (in this case a nox) and vascular injury.
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 4-5
    • Szocs, K.1    Lassegue, B.2    Sorescu, D.3    Hilenski, L.L.4    Valppu, L.5    Couse, T.L.6    Wilcox, J.N.7    Quinn, M.T.8    Lambeth, J.D.9    Griendling, K.K.10
  • 40
    • 0037177164 scopus 로고    scopus 로고
    • Superoxide production and expression of nox family proteins in human atherosclerosis
    • A study tying superoxide production by NADPH oxidases to atherosclerosis.
    • Sorescu D., Weiss D., Lassegue B., Clempus R.E., Szocs K., Sorescu G.P., Valppu L., Quinn M.T., Lambeth J.D., Vega J.D.et al. Superoxide production and expression of nox family proteins in human atherosclerosis. Circulation. 105:2002;1429-1435 A study tying superoxide production by NADPH oxidases to atherosclerosis.
    • (2002) Circulation , vol.105 , pp. 1429-1435
    • Sorescu, D.1    Weiss, D.2    Lassegue, B.3    Clempus, R.E.4    Szocs, K.5    Sorescu, G.P.6    Valppu, L.7    Quinn, M.T.8    Lambeth, J.D.9    Vega, J.D.10
  • 41
    • 0035877848 scopus 로고    scopus 로고
    • PHOX. Structure at 1.8 Å resolution and biochemical characterization of the A182V mutant implicated in chronic granulomatous disease
    • PHOX. Structure at 1.8. Å resolution and biochemical characterization of the A182V mutant implicated in chronic granulomatous disease J. Biol. Chem. 276:2001;21627-21631.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21627-21631
    • Grizot, S.1    Fieschi, F.2    Dagher, M.-C.3    Pebay-Peyroula, E.4
  • 44
    • 0024453201 scopus 로고
    • Genetic variants of chronic granulomatous disease: Prevalence of deficiencies of two discrete cytosolic components of the NADPH oxidase system
    • Clark R.A., Malech H.L., Gallin J.I., Nunoi H., Volpp B., Pearson D.W., Nauseef W.M., Curnutte J.T. Genetic variants of chronic granulomatous disease: prevalence of deficiencies of two discrete cytosolic components of the NADPH oxidase system. N. Engl. J. Med. 321:1989;647-652.
    • (1989) N. Engl. J. Med. , vol.321 , pp. 647-652
    • Clark, R.A.1    Malech, H.L.2    Gallin, J.I.3    Nunoi, H.4    Volpp, B.5    Pearson, D.W.6    Nauseef, W.M.7    Curnutte, J.T.8
  • 45
    • 3042580001 scopus 로고
    • Cytosolic components of the respiratory burst oxidase: Resolution of four components, two of which are missing in complementing types of chronic granulomatous disease
    • Curnutte J.T., Scott P.J., Mayo L.A. Cytosolic components of the respiratory burst oxidase: resolution of four components, two of which are missing in complementing types of chronic granulomatous disease. Proc. Natl. Acad. Sci. USA. 86:1989;825-829.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 825-829
    • Curnutte, J.T.1    Scott, P.J.2    Mayo, L.A.3
  • 46
    • 0016391727 scopus 로고
    • Defective superoxide production by granulocytes from patients with chronic granulomatous disease
    • Curnutte J.T., Whitten D.M., Babior B.M. Defective superoxide production by granulocytes from patients with chronic granulomatous disease. N Engl. J. Med. 290:1974;593-597.
    • (1974) N Engl. J. Med. , vol.290 , pp. 593-597
    • Curnutte, J.T.1    Whitten, D.M.2    Babior, B.M.3
  • 47
    • 85142969804 scopus 로고    scopus 로고
    • Forrest CB, Forehand JR, Axtell RA, Roberts RL, Johnston RB Jr: Clinical features and current management of chronic granulomatous disease. In Hematology/Oncology Clinics of North America. Phagocytic Defects II, Vol. 2. Edited by Curnutte JT. Philadelphia: W.B. Saunders; 1988:253-266.
    • Forrest CB, Forehand JR, Axtell RA, Roberts RL, Johnston RB Jr: Clinical features and current management of chronic granulomatous disease. In Hematology/Oncology Clinics of North America. Phagocytic Defects II, Vol. 2. Edited by Curnutte JT. Philadelphia: W.B. Saunders; 1988:253-266.
  • 49
    • 0025336870 scopus 로고
    • Chronic granulomatous disease
    • Babior B.M., Woodman R.C. Chronic granulomatous disease. Semin Hematol. 27:1990;247-259.
    • (1990) Semin Hematol. , vol.27 , pp. 247-259
    • Babior, B.M.1    Woodman, R.C.2
  • 50
    • 0026628807 scopus 로고
    • Chronic granulomatous disease
    • Dinauer M.C., Orkin S.H. Chronic granulomatous disease. Annu. Rev. Med. 43:1992;117-124.
    • (1992) Annu. Rev. Med. , vol.43 , pp. 117-124
    • Dinauer, M.C.1    Orkin, S.H.2
  • 51
    • 0028000143 scopus 로고
    • Infection with Pseudomonas cepacia in chronic granulomatous disease: Role of nonoxidative killing by neutrophils in host defense
    • Speert D.P., Bond M., Woodman R.C., Curnutte J.T. Infection with Pseudomonas cepacia in chronic granulomatous disease: role of nonoxidative killing by neutrophils in host defense. J. Infect. Dis. 170:1994;1524-1531.
    • (1994) J. Infect. Dis. , vol.170 , pp. 1524-1531
    • Speert, D.P.1    Bond, M.2    Woodman, R.C.3    Curnutte, J.T.4
  • 53
    • 0032080869 scopus 로고    scopus 로고
    • Virulence of catalase-deficient aspergillus nidulans in p47(phox)-/- mice. Implications for fungal pathogenicity and host defense in chronic granulomatous disease
    • Chang Y.C., Segal B.H., Holland S.M., Miller G.F., Kwon-Chung K.J. Virulence of catalase-deficient aspergillus nidulans in p47(phox)-/- mice. Implications for fungal pathogenicity and host defense in chronic granulomatous disease. J. Clin. Invest. 101:1998;1843-1850.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1843-1850
    • Chang, Y.C.1    Segal, B.H.2    Holland, S.M.3    Miller, G.F.4    Kwon-Chung, K.J.5
  • 55
    • 0030941931 scopus 로고    scopus 로고
    • Dose-dependent enhancements by interferon-gamma on functional responses of neutrophils from chronic granulomatous disease patients
    • Ahlin A., Elinder G., Palmblad J. Dose-dependent enhancements by interferon-gamma on functional responses of neutrophils from chronic granulomatous disease patients. Blood. 89:1997;3396-3401.
    • (1997) Blood , vol.89 , pp. 3396-3401
    • Ahlin, A.1    Elinder, G.2    Palmblad, J.3
  • 57
    • 0020838428 scopus 로고
    • Application of bone marrow transplantation in genetic diseases
    • Rappeport J.M., Smith B.R., Parkman R., Rosen F.S. Application of bone marrow transplantation in genetic diseases. Clin. Haematol. 12:1983;755-773.
    • (1983) Clin. Haematol. , vol.12 , pp. 755-773
    • Rappeport, J.M.1    Smith, B.R.2    Parkman, R.3    Rosen, F.S.4
  • 58
    • 0037114622 scopus 로고    scopus 로고
    • Treatment of chronic granulomatous disease with myeloablative conditioning and an unmodified hemopoietic allograft: A survey of the European experience, 1985-2000
    • Seger R.A., Gungor T., Belohradsky B.H., Blanche S., Bordigoni P., Di Bartolomeo P., Flood T., Landais P., Müller S., Ozsahin H.et al. Treatment of chronic granulomatous disease with myeloablative conditioning and an unmodified hemopoietic allograft: a survey of the European experience, 1985-2000. Blood. 100:2002;4344-4350.
    • (2002) Blood , vol.100 , pp. 4344-4350
    • Seger, R.A.1    Gungor, T.2    Belohradsky, B.H.3    Blanche, S.4    Bordigoni, P.5    Di Bartolomeo, P.6    Flood, T.7    Landais, P.8    Müller, S.9    Ozsahin, H.10
  • 59
    • 0025781389 scopus 로고
    • Point mutations in the β-subunit of Cytochrome b558 leading to X-linked chronic granulomatous disease
    • Bolscher B.G.J.M., deBoer M., deKlein A., Weening R.S., Roos D. Point mutations in the β-subunit of Cytochrome b558 leading to X-linked chronic granulomatous disease. Blood. 77:1991;2482-2487.
    • (1991) Blood , vol.77 , pp. 2482-2487
    • Bolscher, B.G.J.M.1    Deboer, M.2    Deklein, A.3    Weening, R.S.4    Roos, D.5
  • 60
    • 0028803342 scopus 로고
    • Molecular analysis in three cases of X91- variant chronic granulomatous disease
    • Bu-Ghanim H.N., Segal A.W., Keep N.H., Casimir C.M. Molecular analysis in three cases of X91- variant chronic granulomatous disease. Blood. 86:1995;3575-3582.
    • (1995) Blood , vol.86 , pp. 3575-3582
    • Bu-Ghanim, H.N.1    Segal, A.W.2    Keep, N.H.3    Casimir, C.M.4
  • 61
    • 0028086550 scopus 로고
    • Mutations in the promoter region of the gene for gp91-phox in X-linked chronic granulomatous disease with decreased expression of Cytochrome b558
    • Newburger P.E., Skalnik D.G., Hopkins P.J., Eklund E.A., Curnutte J.T. Mutations in the promoter region of the gene for gp91-phox in X-linked chronic granulomatous disease with decreased expression of Cytochrome b558. J. Clin. Invest. 94:1994;1205-1211.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1205-1211
    • Newburger, P.E.1    Skalnik, D.G.2    Hopkins, P.J.3    Eklund, E.A.4    Curnutte, J.T.5
  • 64
    • 0344272734 scopus 로고
    • Recombination events between the normal p47-phox gene and a highly homologous pseudogene are the main cause of autosomal recessive chronic granulomatous disease
    • Roesler J., Gorlach A., Rae J., Hopkins P.J., Patino P., Lee P., Curnutte J.T., Chanock S.J. Recombination events between the normal p47-phox gene and a highly homologous pseudogene are the main cause of autosomal recessive chronic granulomatous disease. Blood. 86:1995;260a.
    • (1995) Blood , vol.86
    • Roesler, J.1    Gorlach, A.2    Rae, J.3    Hopkins, P.J.4    Patino, P.5    Lee, P.6    Curnutte, J.T.7    Chanock, S.J.8
  • 65
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping Y., Lapouge K., Smerdon M.J., Rittinger K. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell. 113:2002;343-355.
    • (2002) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, M.J.3    Rittinger, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.