메뉴 건너뛰기




Volumn 34, Issue 4, 2013, Pages 227-232

NADPH oxidase of neutrophils and diseases associated with its disfunction

Author keywords

Chronic granulomatous disease (CGD); NADPH oxidase; Neutrophils; Reactive oxygen species; Signalling

Indexed keywords

REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 84990842355     PISSN: 02064952     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (10)

References (60)
  • 1
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal A.W. How neutrophils kill microbes. Annu. Rev. Immunol. 2005; 23: 197-223.
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 4
    • 0037442128 scopus 로고    scopus 로고
    • The mitochondrial network of human neutrophils: Role in chemotaxis, phagocytosis, respiratory burst activation, and commitment to apoptosis
    • Fossati G., Moulding D.A., Spiller D.G. et al. The mitochondrial network of human neutrophils: role in chemotaxis, phagocytosis, respiratory burst activation, and commitment to apoptosis. J. Immunol. 2003; 170: 1964-72.
    • (2003) J. Immunol. , vol.170 , pp. 1964-1972
    • Fossati, G.1    Moulding, D.A.2    Spiller, D.G.3
  • 5
    • 33750924781 scopus 로고    scopus 로고
    • Regulation of the phagocyte NADPH oxidase by Rac GTPase
    • Bokoch G.M., Zhao T. Regulation of the phagocyte NADPH oxidase by Rac GTPase. Antioxid. Redox Signal. 2006; 8: 1533-48.
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 1533-1548
    • Bokoch, G.M.1    Zhao, T.2
  • 6
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase friend and foe
    • Klebanoff S.J. Myeloperoxidase friend and foe. J. Leukoc. Biol. 2005; 77: 598-625.
    • (2005) J. Leukoc. Biol , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 7
    • 0242713072 scopus 로고    scopus 로고
    • Neutrophil granules and secretory vesicles in inflammation
    • Faurschou M., Borregaard N. Neutrophil granules and secretory vesicles in inflammation. Microbes Infect. 2003; 5: 1317-27.
    • (2003) Microbes Infect. , vol.5 , pp. 1317-1327
    • Faurschou, M.1    Borregaard, N.2
  • 8
    • 0020540731 scopus 로고
    • Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase: Translocation during activation
    • Borregaard N., Heiple J.M., Simons E.R. et al. Subcellular localization of the b-cytochrome component of the human neutrophil microbicidal oxidase: translocation during activation. J. Cell Biol. 1983; 97: 52-61.
    • (1983) J. Cell Biol , vol.97 , pp. 52-61
    • Borregaard, N.1    Heiple, J.M.2    Simons, E.R.3
  • 9
    • 0031975515 scopus 로고    scopus 로고
    • Identification of intracellular sites of superoxide production in stimulated neutrophils
    • Kobayashi T., Robinson J.M., Seguchi H. Identification of intracellular sites of superoxide production in stimulated neutrophils. J. Cell Sci. 1998; 11: 81-91.
    • (1998) J. Cell Sci. , vol.11 , pp. 81-91
    • Kobayashi, T.1    Robinson, J.M.2    Seguchi, H.3
  • 10
    • 0036193431 scopus 로고    scopus 로고
    • Assembly and activation of the neutrophil NADPH oxidase in granule membranes
    • Karlsson A., Dahlgren C. Assembly and activation of the neutrophil NADPH oxidase in granule membranes. Antioxid. Redox Signal. 2002; 4: 49-60.
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 49-60
    • Karlsson, A.1    Dahlgren, C.2
  • 11
    • 0344299171 scopus 로고    scopus 로고
    • NADPH oxidase is functionally assembled in specific granules during activation of human neutrophils
    • Vaissiere C., Le Cabec V., Maridonneau-Parini I. NADPH oxidase is functionally assembled in specific granules during activation of human neutrophils. J. Leukoc. Biol. 1999; 65: 629-34.
    • (1999) J. Leukoc. Biol , vol.65 , pp. 629-634
    • Vaissiere, C.1    Le Cabec, V.2    Maridonneau-Parini, I.3
  • 12
    • 70449140148 scopus 로고
    • A fatal granulomatosus of childhood: The clinical study of a new syndrome
    • Berendes H., Bridges R.A., Good R.A. A fatal granulomatosus of childhood: the clinical study of a new syndrome. Minn. Med. 1957; 8: 309-12.
    • (1957) Minn. Med , vol.8 , pp. 309-312
    • Berendes, H.1    Bridges, R.A.2    Good, R.A.3
  • 13
    • 0014124339 scopus 로고
    • Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function
    • Holmes B., Page A.R., Good R.A. Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function. J. Clin. Invest. 1967; 46: 1422-32.
    • (1967) J. Clin. Invest , vol.46 , pp. 1422-1432
    • Holmes, B.1    Page, A.R.2    Good, R.A.3
  • 14
    • 0014078091 scopus 로고
    • In vitro bactericidal capacity of human polymorphonuclear leukocytes: Diminished activity in chronic granulomatous disease of childhood
    • Quie P.G., White J.G., Holmes B. et al. In vitro bactericidal capacity of human polymorphonuclear leukocytes: diminished activity in chronic granulomatous disease of childhood. J. Clin. Invest. 1967; 46: 668-79.
    • (1967) J. Clin. Invest , vol.46 , pp. 668-679
    • Quie, P.G.1    White, J.G.2    Holmes, B.3
  • 15
    • 12944284786 scopus 로고    scopus 로고
    • Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation
    • Ambruso D.R., Knall C., Abell A.N. et al. Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. Proc. Natl Acad. Sci. USA. 2000; 97: 4654-9.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4654-4659
    • Ambruso, D.R.1    Knall, C.2    Abell, A.N.3
  • 16
    • 0034973568 scopus 로고    scopus 로고
    • Clinical features of a human Rac2 mutation: A complex neutrophil dysfunction disease
    • Kurkchubasche A.G., Panepinto J.A., Tracy Jr T.F. et al. Clinical features of a human Rac2 mutation: a complex neutrophil dysfunction disease. J. Pediatr. 2001; 139: 141-7.
    • (2001) J. Pediatr , vol.139 , pp. 141-147
    • Kurkchubasche, A.G.1    Panepinto, J.A.2    Tracy, J.T.F.3
  • 17
    • 0034040532 scopus 로고    scopus 로고
    • Chronic granulomatous disease: Report on a national registry of 368 patients
    • Baltimore
    • Winkelstein J.A., Marino M.C., Johnston Jr. R.B. et al. Chronic granulomatous disease: report on a national registry of 368 patients. Medicine (Baltimore). 2000; 79: 155-69.
    • (2000) Medicine , vol.79 , pp. 155-169
    • Winkelstein, J.A.1    Marino, M.C.2    Johnston, Jr.R.B.3
  • 18
    • 0028074206 scopus 로고
    • The superoxide-generating system of human neutrophils possesses a novel diaphorase activity: Evidence for distinct regulation of electron flow within NADPH oxidase by p67-phox and p47-phox
    • Cross A.R., Yarchover J.L., Curnutte J.T. The superoxide-generating system of human neutrophils possesses a novel diaphorase activity: evidence for distinct regulation of electron flow within NADPH oxidase by p67-phox and p47-phox. J. Biol. Chem. 1994; 269: 21448-54.
    • (1994) J. Biol. Chem , vol.269 , pp. 21448-21454
    • Cross, A.R.1    Yarchover, J.L.2    Curnutte, J.T.3
  • 19
    • 0034128751 scopus 로고    scopus 로고
    • Genetic, biochemical, and clinical features of chronic granulomatous disease
    • Baltimore
    • Segal B.H., Leto T.L., Gallin J.I. et al. Genetic, biochemical, and clinical features of chronic granulomatous disease. Medicine (Baltimore). 2000; 79: 170-200.
    • (2000) Medicine , vol.79 , pp. 170-200
    • Segal, B.H.1    Leto, T.L.2    Gallin, J.I.3
  • 20
    • 58149402411 scopus 로고    scopus 로고
    • CD18-dependent activation of the neutrophil NADPH oxidase during phagocytosis of Escherichia coli or staphylococcus aureus is regulated by class III but not class I or II PI3Ks
    • Anderson K.E., Boyle K.B., Davidson K. et al. CD18-dependent activation of the neutrophil NADPH oxidase during phagocytosis of Escherichia coli or Staphylococcus aureus is regulated by class III but not class I or II PI3Ks. Blood. 2008; 112: 5202-11.
    • (2008) Blood , vol.112 , pp. 5202-5211
    • Anderson, K.E.1    Boyle, K.B.2    Davidson, K.3
  • 21
    • 38349132540 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate-dependent and -independent functions of p40phox in activation of the neutrophil NADPH oxidase
    • Bissonnette S.A., Glazier C.M., Stewart M.Q. et al. Phosphatidylinositol 3-phosphate-dependent and -independent functions of p40phox in activation of the neutrophil NADPH oxidase. J. Biol. Chem. 2008; 283: 2108-19.
    • (2008) J. Biol. Chem , vol.283 , pp. 2108-2119
    • Bissonnette, S.A.1    Glazier, C.M.2    Stewart, M.Q.3
  • 22
    • 0035899869 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate is generated in phagosomal membranes
    • Ellson C.D., Anderson K.E., Morgan G. et al. Phosphatidylinositol 3-phosphate is generated in phagosomal membranes. Curr. Biol. 2001; 1: 1631-5.
    • (2001) Curr. Biol , vol.1 , pp. 1631-1635
    • Ellson, C.D.1    Anderson, K.E.2    Morgan, G.3
  • 23
    • 0034743311 scopus 로고    scopus 로고
    • PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40(phox)
    • Ellson C.D., Gobert-Gosse S., Anderson K.E. et al. PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40(phox). Nature Cell Biol. 2001; 3(7): 679-82.
    • (2001) Nature Cell Biol , vol.3 , Issue.7 , pp. 679-682
    • Ellson, C.D.1    Gobert-Gosse, S.2    Anderson, K.E.3
  • 24
    • 33749317192 scopus 로고    scopus 로고
    • PtdIns3P binding to the PX domain of p40phox is a physiological signal in NADPH oxidase activation
    • Ellson C.D., Davidson K., Anderson K. et al. PtdIns3P binding to the PX domain of p40phox is a physiological signal in NADPH oxidase activation. EMBO J. 2006; 25: 4468-78.
    • (2006) EMBO J. , vol.25 , pp. 4468-4478
    • Ellson, C.D.1    Davidson, K.2    Anderson, K.3
  • 25
    • 33746885455 scopus 로고    scopus 로고
    • Neutrophils from p40phox-/- mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing
    • Ellson C.D., Davidson K., Ferguson G.J. et al. Neutrophils from p40phox-/- mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing. J. Exp. Med. 2006; 203(8): 1927-37.
    • (2006) J. Exp. Med , vol.203 , Issue.8 , pp. 1927-1937
    • Ellson, C.D.1    Davidson, K.2    Ferguson, G.J.3
  • 26
    • 0034946472 scopus 로고    scopus 로고
    • The PXdomains of p47phox and p40phox bind to lipid products of PI(3)K
    • Kanai F., Liu H., Field S.J. et al. The PXdomains of p47phox and p40phox bind to lipid products of PI(3)K. Nature Cell Biol. 2001; 3: 675-8.
    • (2001) Nature Cell Biol. , vol.3 , pp. 675-678
    • Kanai, F.1    Liu, H.2    Field, S.J.3
  • 27
    • 35948968392 scopus 로고    scopus 로고
    • A case-control study of rheumatoid arthritis identifies an associated single nucleotide polymorphism in the NCF4 gene, supporting a role for the NADPH-oxidase complex in autoimmunity
    • Olsson L.M., Lindqvist A.K., Kallberg H. et al. A case-control study of rheumatoid arthritis identifies an associated single nucleotide polymorphism in the NCF4 gene, supporting a role for the NADPH-oxidase complex in autoimmunity. Arthrit. Res. Ther. 2007; 9(5): 1-11.
    • (2007) Arthrit. Res. Ther , vol.9 , Issue.5 , pp. 1-11
    • Olsson, L.M.1    Lindqvist, A.K.2    Kallberg, H.3
  • 28
    • 34247554965 scopus 로고    scopus 로고
    • Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis
    • Rioux J.D., Xavier R.J., Taylor K.D. et al. Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis. Nature Genet. 2007; 39: 596-604.
    • (2007) Nature Genet , vol.39 , pp. 596-604
    • Rioux, J.D.1    Xavier, R.J.2    Taylor, K.D.3
  • 29
    • 51249103405 scopus 로고    scopus 로고
    • Confirmation of association of IRGM and NCF4 with ileal Crohn's disease in a population-based cohort
    • Roberts R.L., Hollis-Moffatt J.E., Gearry R.B. et al. Confirmation of association of IRGM and NCF4 with ileal Crohn's disease in a population-based cohort. Genes Immun. 2008; 9: 561-5.
    • (2008) Genes Immun , vol.9 , pp. 561-565
    • Roberts, R.L.1    Hollis-Moffatt, J.E.2    Gearry, R.B.3
  • 30
    • 55749109709 scopus 로고    scopus 로고
    • FcγR-stimulated activation of the NADPH oxidase: Phosphoinositide-binding protein p40phox regulates NADPH oxidase activity after enzyme assembly on the phagosome
    • Tian W., Li X.J., Stull N.D. et al. FcγR-stimulated activation of the NADPH oxidase: phosphoinositide-binding protein p40phox regulates NADPH oxidase activity after enzyme assembly on the phagosome. Blood. 2008; 112(9): 3867-77.
    • (2008) Blood , vol.112 , Issue.9 , pp. 3867-3877
    • Tian, W.1    Li, X.J.2    Stull, N.D.3
  • 31
    • 0035494493 scopus 로고    scopus 로고
    • Distinct roles of class I and class III phosphatidylinositol 3-kinases in phagosome formation and maturation
    • Vieira O.V., Botelho R.J., Rameh L. et al. Distinct roles of class I and class III phosphatidylinositol 3-kinases in phagosome formation and maturation. J. Cell Biol. 2001; 155(1): 19-25.
    • (2001) J. Cell Biol. , vol.155 , Issue.1 , pp. 19-25
    • Vieira, O.V.1    Botelho, R.J.2    Rameh, L.3
  • 32
    • 33746896166 scopus 로고    scopus 로고
    • The phosphoinositide-binding protein p40phox activates the NADPH oxidase during FcγIIA receptor-induced phagocytosis
    • Suh C.I., Stull N.D., Li X.J. et al. The phosphoinositide-binding protein p40phox activates the NADPH oxidase during FcγIIA receptor-induced phagocytosis. J. Exp. Med. 2006; 203: 1915-25.
    • (2006) J. Exp. Med , vol.203 , pp. 1915-1925
    • Suh, C.I.1    Stull, N.D.2    Li, X.J.3
  • 33
    • 70350451062 scopus 로고    scopus 로고
    • A new genetic subgroup of chronic granulomatous disease with autosomal recessive mutations in p40 phox and selective defects in neutrophil NADPH oxidase activity
    • Matute J.D., Arias A.A., Wright N.A. et al. A new genetic subgroup of chronic granulomatous disease with autosomal recessive mutations in p40 phox and selective defects in neutrophil NADPH oxidase activity. Blood. 2009; 114: 3309-15.
    • (2009) Blood. , vol.114 , pp. 3309-3315
    • Matute, J.D.1    Arias, A.A.2    Wright, N.A.3
  • 34
    • 34548588559 scopus 로고    scopus 로고
    • How human neutrophils kill and degrade microbes: An integrated view
    • Nauseef W.M. How human neutrophils kill and degrade microbes: an integrated view. Immunol. Rev. 2007; 219: 88-102.
    • (2007) Immunol. Rev , vol.219 , pp. 88-102
    • Nauseef, W.M.1
  • 35
    • 0025220564 scopus 로고
    • Ultrastructural localization of cytochrome b in the membranes of resting and phagocytosing human granulocytes
    • Jesaitis A.J., Buescher E.S., Harrison D. et al. Ultrastructural localization of cytochrome b in the membranes of resting and phagocytosing human granulocytes. J. Clin. Invest. 1990; 85: 821-35.
    • (1990) J. Clin. Invest , vol.85 , pp. 821-835
    • Jesaitis, A.J.1    Buescher, E.S.2    Harrison, D.3
  • 36
    • 0035017408 scopus 로고    scopus 로고
    • An intact cytoskeleton is required for prolonged respiratory burst activity during neutrophil phagocytosis
    • Granfeldt D., Dahlgren C. An intact cytoskeleton is required for prolonged respiratory burst activity during neutrophil phagocytosis. Inflammation. 2001; 25: 165-9.
    • (2001) Inflammation , vol.25 , pp. 165-169
    • Granfeldt, D.1    Dahlgren, C.2
  • 37
    • 0025171929 scopus 로고
    • Neutrophil killing of two type 1 fimbria-bearing Escherichia coli strains: Dependence on respiratory burst activation
    • Lock R., Dahlgren C., Linden M. et al. Neutrophil killing of two type 1 fimbria-bearing Escherichia coli strains: dependence on respiratory burst activation. Infect. and Immun. 1990; 58: 37-42.
    • (1990) Infect. and Immun , vol.58 , pp. 37-42
    • Lock, R.1    Dahlgren, C.2    Linden, M.3
  • 38
    • 48749128084 scopus 로고    scopus 로고
    • Reactive oxygen species in phagocytic leukocytes
    • Robinson J.M. Reactive oxygen species in phagocytic leukocytes, Histochem. Cell Biol. 2008; 130: 281-97.
    • (2008) Histochem. Cell Biol , vol.130 , pp. 281-297
    • Robinson, J.M.1
  • 39
    • 64649087275 scopus 로고    scopus 로고
    • Phagocytic leukocytes and reactive oxygen species
    • Robinson J.M. Phagocytic leukocytes and reactive oxygen species. Histochem. Cell Biol. 2009; 131: 465-9.
    • (2009) Histochem. Cell Biol , vol.131 , pp. 465-469
    • Robinson, J.M.1
  • 40
    • 0036241542 scopus 로고    scopus 로고
    • Study of NADPH oxidase-activated sites in human neutrophils
    • Tokyo
    • Seguchi H., Kobayashi T. Study of NADPH oxidase-activated sites in human neutrophils. J. Electron Microsc. (Tokyo). 2002; 51: 87-91.
    • (2002) J. Electron Microsc , vol.51 , pp. 87-91
    • Seguchi, H.1    Kobayashi, T.2
  • 41
    • 0023252104 scopus 로고
    • Difference in extracellular radical release after chemotactic factor and calcium ionophore activation of the oxygen radical-generating system in human neutrophils
    • Dahlgren C. Difference in extracellular radical release after chemotactic factor and calcium ionophore activation of the oxygen radical-generating system in human neutrophils. Biochim. Biophys. Acta. 1987; 930: 33-8.
    • (1987) Biochim. Biophys. Acta , vol.930 , pp. 33-38
    • Dahlgren, C.1
  • 42
    • 0030904423 scopus 로고    scopus 로고
    • Chemoattractant- induced respiratory burst: Increases in cytosolic Ca2+ concentrations are essential and synergize with a kinetically distinct second signal
    • Foyouzi Youssefi R., Petersson F., Lew D.P. et al. Chemoattractant- induced respiratory burst: increases in cytosolic Ca2+ concentrations are essential and synergize with a kinetically distinct second signal. Biochem. J. 1997; 322: 709-18.
    • (1997) Biochem. J. , vol.322 , pp. 709-718
    • Foyouzi, Y.R.1    Petersson, F.2    Lew, D.P.3
  • 43
    • 0033551703 scopus 로고    scopus 로고
    • The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558)
    • Nisimoto Y., Motalebi S., Han C.H. et al. The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558). J. Biol. Chem. 1999; 274: 22999-3005.
    • (1999) J. Biol. Chem , vol.274 , pp. 22999-23005
    • Nisimoto, Y.1    Motalebi, S.2    Han, C.H.3
  • 44
    • 0028169005 scopus 로고
    • Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity
    • Diekmann D., Abo A., Johnston C. et al. Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity. Science. 1994; 265: 531-3.
    • (1994) Science , vol.265 , pp. 531-533
    • Diekmann, D.1    Abo, A.2    Johnston, C.3
  • 45
    • 0033635228 scopus 로고    scopus 로고
    • Structure of the TPR domain of p67phox in complex with Rac.
    • Lapouge K., Smith S.J., Walker P.A. et al. Structure of the TPR domain of p67phox in complex with Rac.GTP. Mol. Cell. 2000; 6: 899-907.
    • (2000) GTP. Mol. Cell , vol.6 , pp. 899-907
    • Lapouge, K.1    Smith, S.J.2    Walker, P.A.3
  • 46
    • 0037248553 scopus 로고    scopus 로고
    • A Novel assay system implicates PtdIns(3, 4)P(2), PtdIns(3)P, and PKC delta in intracellular production of reactive oxygen species by the NADPH oxidase
    • Brown G.E., Stewart M.Q., Liu H. et al. A novel assay system implicates PtdIns(3, 4)P(2), PtdIns(3)P, and PKC delta in intracellular production of reactive oxygen species by the NADPH oxidase. Mol. Cell. 2003; 11: 35-47.
    • (2003) Mol. Cell. , vol.11 , pp. 35-47
    • Brown, G.E.1    Stewart, M.Q.2    Liu, H.3
  • 47
    • 0027787417 scopus 로고
    • P40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains
    • Wientjes F.B., Hsuan J.J., Totty N.F. et al. p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. Biochem. J. 1993; 296 (Pt3): 557-61.
    • (1993) Biochem. J. , vol.296 , pp. 557-561
    • Wientjes, F.B.1    Hsuan, J.J.2    Totty, N.F.3
  • 48
    • 0029835305 scopus 로고    scopus 로고
    • Interactions between cytosolic components of the NADPH oxidase: P40phox interacts with both p67phox and 47phox
    • Wientjes F.B., Panayotou G., Reeves E. et al. Interactions between cytosolic components of the NADPH oxidase: p40phox interacts with both p67phox and 47phox. Biochem. J. 1996; 317 (Pt3): 919-24.
    • (1996) Biochem. J. , vol.317 , pp. 919-924
    • Wientjes, F.B.1    Panayotou, G.2    Reeves, E.3
  • 49
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH oxidase: A structural perspective
    • Groemping Y., Rittinger K. Activation and assembly of the NADPH oxidase: a structural perspective. Biochem. J. 2005; 386: 401-16.
    • (2005) Biochem. J. , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 50
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping Y., Lapouge K., Smerdon S.J. et al. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell. 2003; 113: 343-55.
    • (2003) Cell. , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3
  • 51
    • 0030615088 scopus 로고    scopus 로고
    • Specificity of p47phox SH3 domain interactions in NADPH oxidase assembly and activation
    • de Mendez I., Homayounpour N., Leto T.L. Specificity of p47phox SH3 domain interactions in NADPH oxidase assembly and activation. Mol. Cell. Biol. 1997; 17: 2177-85.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 2177-2185
    • De Mendez, I.1    Homayounpour, N.2    Leto, T.L.3
  • 52
    • 0037102138 scopus 로고    scopus 로고
    • Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p
    • Kami K., Takeya R., Sumimoto H. et al. Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p. EMBO J. 2002; 21: 4268-76.
    • (2002) EMBO J. , vol.21 , pp. 4268-4276
    • Kami, K.1    Takeya, R.2    Sumimoto, H.3
  • 53
    • 0036791737 scopus 로고    scopus 로고
    • Binding of the PX domain of p47(phox) to phosphatidylinositol 3, 4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction
    • Karathanassis D., Stahelin R.V., Bravo J. et al. Binding of the PX domain of p47(phox) to phosphatidylinositol 3, 4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. EMBO J. 2002; 21: 5057-68.
    • (2002) EMBO J. , vol.21 , pp. 5057-5068
    • Karathanassis, D.1    Stahelin, R.V.2    Bravo, J.3
  • 54
    • 0029806925 scopus 로고    scopus 로고
    • Assembly and activation of the phagocyte NADPH oxidase. Specific interaction of the Nterminal Src homology 3 domain of p47phox with p22phox is required for activation of the NADPH oxidase
    • Sumimoto H., Hata K., Mizuki K. et al. Assembly and activation of the phagocyte NADPH oxidase. Specific interaction of the Nterminal Src homology 3 domain of p47phox with p22phox is required for activation of the NADPH oxidase. J. Biol. Chem. 1996; 27: 22152-8.
    • (1996) J. Biol. Chem , vol.27 , pp. 22152-22158
    • Sumimoto, H.1    Hata, K.2    Mizuki, K.3
  • 55
    • 17944367436 scopus 로고    scopus 로고
    • The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate
    • Bravo J., Karathanassis D., Pacold C.M. et al. The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol. Cell. 2001; 8: 829-39.
    • (2001) Mol. Cell , vol.8 , pp. 829-839
    • Bravo, J.1    Karathanassis, D.2    Pacold, C.M.3
  • 56
    • 18744403007 scopus 로고    scopus 로고
    • The adaptor protein p40(phox) as a positive regulator of the superoxide-producing phagocyte oxidase
    • Kuribayashi F., Nunoi H., Wakamatsu K. et al. The adaptor protein p40(phox) as a positive regulator of the superoxide-producing phagocyte oxidase. EMBO J. 2002; 21: 6312-20.
    • (2002) EMBO J , vol.21 , pp. 6312-6320
    • Kuribayashi, F.1    Nunoi, H.2    Wakamatsu, K.3
  • 57
    • 33847200398 scopus 로고    scopus 로고
    • Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding
    • Honbou K., Minakami R., Yuzawa S. et al. Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding. EMBO J. 2007; 26: 1176-86.
    • (2007) EMBO J , vol.26 , pp. 1176-1186
    • Honbou, K.1    Minakami, R.2    Yuzawa, S.3
  • 58
    • 47949102446 scopus 로고    scopus 로고
    • Sequential binding of cytosolic phox complex to phagosomes through regulated adaptor proteins: Evaluation using the novel monomeric kusabira- green system and live imaging of phagocytosis
    • Ueyama T., Kusakabe T., Karasawa S. et al. Sequential binding of cytosolic phox complex to phagosomes through regulated adaptor proteins: evaluation using the novel monomeric Kusabira- Green system and live imaging of phagocytosis. J. Immunol. 2008; 181: 629-40.
    • (2008) J. Immunol , vol.181 , pp. 629-640
    • Ueyama, T.1    Kusakabe, T.2    Karasawa, S.3
  • 59
    • 23744492188 scopus 로고    scopus 로고
    • Sequential activation of class IB and class IA PI3K is important for the primed respiratory burst of human but not murine neutrophils
    • Condliffe A.M., Davidson K., Anderson K.E. et al. Sequential activation of class IB and class IA PI3K is important for the primed respiratory burst of human but not murine neutrophils. Blood. 2005; 106: 1432-40.
    • (2005) Blood. , vol.106 , pp. 1432-1440
    • Condliffe, A.M.1    Davidson, K.2    Anderson, K.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.