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Volumn 42, Issue 10, 2010, Pages 1736-1743

Subcellular localisation of the p40phox component of NADPH oxidase involves direct interactions between the Phox homology domain and F-actin

Author keywords

Cell biology; Cytoskeleton; Neutrophils; Phosphoinositide; Protein interaction

Indexed keywords

CYTOCHALASIN D; F ACTIN; PROTEIN P40; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; ACTIN; CELL EXTRACT; NEUTROPHIL CYTOSOL FACTOR 40K; PHOSPHOPROTEIN;

EID: 77956186429     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2010.07.009     Document Type: Article
Times cited : (16)

References (46)
  • 1
    • 0033562347 scopus 로고    scopus 로고
    • Transient association of the nicotinamide adenine dinucleotide phosphate oxidase subunits p47phox and p67phox with phagosomes in neutrophils from patients with X-linked chronic granulomatous disease
    • Allen L.A., DeLeo F.R., Gallois A., Toyoshima S., Suzuki K., Nauseef W.M. Transient association of the nicotinamide adenine dinucleotide phosphate oxidase subunits p47phox and p67phox with phagosomes in neutrophils from patients with X-linked chronic granulomatous disease. Blood 1999, 93:3521-3530.
    • (1999) Blood , vol.93 , pp. 3521-3530
    • Allen, L.A.1    DeLeo, F.R.2    Gallois, A.3    Toyoshima, S.4    Suzuki, K.5    Nauseef, W.M.6
  • 2
    • 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., Brown G.E., Ellson C.D., Yaffe M.B. Phosphatidylinositol 3-phosphate-dependent and -independent functions of p40phox in activation of the neutrophil NADPH oxidase. J Biol Chem 2008, 283:2108-2119.
    • (2008) J Biol Chem , vol.283 , pp. 2108-2119
    • Bissonnette, S.A.1    Glazier, C.M.2    Stewart, M.Q.3    Brown, G.E.4    Ellson, C.D.5    Yaffe, M.B.6
  • 3
    • 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., Pacold M.E., Ellson C.D., Anderson K.E., et al. The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol Cell 2001, 8:829-839.
    • (2001) Mol Cell , vol.8 , pp. 829-839
    • Bravo, J.1    Karathanassis, D.2    Pacold, C.M.3    Pacold, M.E.4    Ellson, C.D.5    Anderson, K.E.6
  • 4
    • 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., Ha V.L., Yaffe M.B. 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    Ha, V.L.4    Yaffe, M.B.5
  • 5
    • 35648957271 scopus 로고    scopus 로고
    • Characterization of a mutation in the phox homology domain of the NADPH oxidase component p40phox identifies a mechanism for negative regulation of superoxide production
    • Chen J., He R., Minshall R.D., Dinauer M.C., Ye R.D. Characterization of a mutation in the phox homology domain of the NADPH oxidase component p40phox identifies a mechanism for negative regulation of superoxide production. J Biol Chem 2007, 282:30273-30284.
    • (2007) J Biol Chem , vol.282 , pp. 30273-30284
    • Chen, J.1    He, R.2    Minshall, R.D.3    Dinauer, M.C.4    Ye, R.D.5
  • 6
    • 3242752788 scopus 로고    scopus 로고
    • Neutrophil protein kinase C delta as a mediator of stroke-reperfusion injury
    • Chou W.H., Choi D.S., Zhang H., Mu D., McMahon T., Kharazia V.N., et al. Neutrophil protein kinase C delta as a mediator of stroke-reperfusion injury. J Clin Invest 2004, 114:49-56.
    • (2004) J Clin Invest , vol.114 , pp. 49-56
    • Chou, W.H.1    Choi, D.S.2    Zhang, H.3    Mu, D.4    McMahon, T.5    Kharazia, V.N.6
  • 7
    • 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., Ellson C.D., Crabbe T., Okkenhaug K., 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, 106:1432-1440.
    • (2005) Blood , vol.106 , pp. 1432-1440
    • Condliffe, A.M.1    Davidson, K.2    Anderson, K.E.3    Ellson, C.D.4    Crabbe, T.5    Okkenhaug, K.6
  • 8
    • 0036534465 scopus 로고    scopus 로고
    • Involvement of protein kinase D in Fc gamma-receptor activation of the NADPH oxidase in neutrophils
    • Davidson-Moncada J.K., Lopez-Lluch G., Segal A.W., Dekker L.V. Involvement of protein kinase D in Fc gamma-receptor activation of the NADPH oxidase in neutrophils. Biochem J 2002, 363:95-103.
    • (2002) Biochem J , vol.363 , pp. 95-103
    • Davidson-Moncada, J.K.1    Lopez-Lluch, G.2    Segal, A.W.3    Dekker, L.V.4
  • 9
    • 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, 17:2177-2185.
    • (1997) Mol Cell Biol , vol.17 , pp. 2177-2185
    • de Mendez, I.1    Homayounpour, N.2    Leto, T.L.3
  • 10
    • 0034177184 scopus 로고    scopus 로고
    • Protein kinase C-beta contributes to NADPH oxidase activation in neutrophils
    • Dekker L.V., Leitges M., Altschuler G., Mistry N., McDermott A., Roes J., et al. Protein kinase C-beta contributes to NADPH oxidase activation in neutrophils. Biochem J 2000, 347:285-289.
    • (2000) Biochem J , vol.347 , pp. 285-289
    • Dekker, L.V.1    Leitges, M.2    Altschuler, G.3    Mistry, N.4    McDermott, A.5    Roes, J.6
  • 11
    • 0028169005 scopus 로고
    • Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity
    • Diekmann D., Abo A., Johnston C., Segal A.W., Hall A. Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity. Science 1994, 265:531-533.
    • (1994) Science , vol.265 , pp. 531-533
    • Diekmann, D.1    Abo, A.2    Johnston, C.3    Segal, A.W.4    Hall, A.5
  • 12
    • 0030588684 scopus 로고    scopus 로고
    • Mechanisms of stimulation of the respiratory burst by TNF in nonadherent neutrophils: its independence of lipidic transmembrane signaling and dependence on protein tyrosine phosphorylation and cytoskeleton
    • Dusi S., Della Bianca V., Donini M., Nadalini K.A., Rossi F. Mechanisms of stimulation of the respiratory burst by TNF in nonadherent neutrophils: its independence of lipidic transmembrane signaling and dependence on protein tyrosine phosphorylation and cytoskeleton. J Immunol 1996, 157:4615-4623.
    • (1996) J Immunol , vol.157 , pp. 4615-4623
    • Dusi, S.1    Della Bianca, V.2    Donini, M.3    Nadalini, K.A.4    Rossi, F.5
  • 13
    • 0033233262 scopus 로고    scopus 로고
    • P40phox associates with the neutrophil Triton X-100-insoluble cytoskeletal fraction and PMA-activated membrane skeleton: a comparative study with P67phox and P47phox
    • El Benna J., Dang P.M., Andrieu V., Vergnaud S., Dewas C., Cachia O., et al. P40phox associates with the neutrophil Triton X-100-insoluble cytoskeletal fraction and PMA-activated membrane skeleton: a comparative study with P67phox and P47phox. J Leukoc Biol 1999, 66:1014-1020.
    • (1999) J Leukoc Biol , vol.66 , pp. 1014-1020
    • El Benna, J.1    Dang, P.M.2    Andrieu, V.3    Vergnaud, S.4    Dewas, C.5    Cachia, O.6
  • 16
    • 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., Stephens L.R., Hawkins P.T. PtdIns3P binding to the PX domain of p40phox is a physiological signal in NADPH oxidase activation. EMBO J 2006, 25:4468-4478.
    • (2006) EMBO J , vol.25 , pp. 4468-4478
    • Ellson, C.D.1    Davidson, K.2    Anderson, K.3    Stephens, L.R.4    Hawkins, P.T.5
  • 17
    • 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., O'Connor R., Stephens L.R., Hawkins P.T. Neutrophils from p40phox-/- mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing. J Exp Med 2006, 203:1927-1937.
    • (2006) J Exp Med , vol.203 , pp. 1927-1937
    • Ellson, C.D.1    Davidson, K.2    Ferguson, G.J.3    O'Connor, R.4    Stephens, L.R.5    Hawkins, P.T.6
  • 18
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping Y., Lapouge K., Smerdon S.J., 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
  • 19
    • 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, 386:401-416.
    • (2005) Biochem J , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 20
    • 0031455048 scopus 로고    scopus 로고
    • Cytosolic phox proteins interact with and regulate the assembly of coronin in neutrophils
    • Grogan A., Reeves E., Keep N., Wientjes F., Totty N.F., Burlingame A.L., et al. Cytosolic phox proteins interact with and regulate the assembly of coronin in neutrophils. J Cell Sci 1997, 110:3071-3081.
    • (1997) J Cell Sci , vol.110 , pp. 3071-3081
    • Grogan, A.1    Reeves, E.2    Keep, N.3    Wientjes, F.4    Totty, N.F.5    Burlingame, A.L.6
  • 21
    • 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., Takeya R., Suzuki N.N., Kamakura S., et al. Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding. EMBO J 2007, 26:1176-1186.
    • (2007) EMBO J , vol.26 , pp. 1176-1186
    • Honbou, K.1    Minakami, R.2    Yuzawa, S.3    Takeya, R.4    Suzuki, N.N.5    Kamakura, S.6
  • 22
    • 33746586545 scopus 로고    scopus 로고
    • Localized PtdIns 3,5-P2 synthesis to regulate early endosome dynamics and fusion
    • Ikonomov O.C., Sbrissa D., Shisheva A. Localized PtdIns 3,5-P2 synthesis to regulate early endosome dynamics and fusion. Am J Physiol Cell Physiol 2006, 291:C393-C404.
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Ikonomov, O.C.1    Sbrissa, D.2    Shisheva, A.3
  • 23
    • 0028984840 scopus 로고
    • The p47phox mouse knock-out model of chronic granulomatous disease
    • Jackson S.H., Gallin J.I., Holland S.M. The p47phox mouse knock-out model of chronic granulomatous disease. J Exp Med 1995, 182:751-758.
    • (1995) J Exp Med , vol.182 , pp. 751-758
    • Jackson, S.H.1    Gallin, J.I.2    Holland, S.M.3
  • 24
    • 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., Kohda D. Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p. EMBO J 2002, 21:4268-4276.
    • (2002) EMBO J , vol.21 , pp. 4268-4276
    • Kami, K.1    Takeya, R.2    Sumimoto, H.3    Kohda, D.4
  • 25
    • 0034946472 scopus 로고    scopus 로고
    • The PX domains of p47phox and p40phox bind to lipid products of PI(3)K
    • Kanai F., Liu H., Field S.J., Akbary H., Matsuo T., Brown G.E., et al. The PX domains of p47phox and p40phox bind to lipid products of PI(3)K. Nat Cell Biol 2001, 3:675-678.
    • (2001) Nat Cell Biol , vol.3 , pp. 675-678
    • Kanai, F.1    Liu, H.2    Field, S.J.3    Akbary, H.4    Matsuo, T.5    Brown, G.E.6
  • 26
    • 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., Perisic O., Pacold C.M., Cho W., 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, 21:5057-5068.
    • (2002) EMBO J , vol.21 , pp. 5057-5068
    • Karathanassis, D.1    Stahelin, R.V.2    Bravo, J.3    Perisic, O.4    Pacold, C.M.5    Cho, W.6
  • 27
    • 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., Tsunawaki S., Sato K., Ito T., et al. The adaptor protein p40(phox) as a positive regulator of the superoxide-producing phagocyte oxidase. EMBO J 2002, 21:6312-6320.
    • (2002) EMBO J , vol.21 , pp. 6312-6320
    • Kuribayashi, F.1    Nunoi, H.2    Wakamatsu, K.3    Tsunawaki, S.4    Sato, K.5    Ito, T.6
  • 29
    • 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 S.J., 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
  • 30
    • 0035396862 scopus 로고    scopus 로고
    • Protein kinase C-delta C2-like domain is a binding site for actin and enables actin redistribution in neutrophils
    • Lopez-Lluch G., Bird M.M., Canas B., Godovac-Zimmerman J., Ridley A., Segal A.W., et al. Protein kinase C-delta C2-like domain is a binding site for actin and enables actin redistribution in neutrophils. Biochem J 2001, 357:39-47.
    • (2001) Biochem J , vol.357 , pp. 39-47
    • Lopez-Lluch, G.1    Bird, M.M.2    Canas, B.3    Godovac-Zimmerman, J.4    Ridley, A.5    Segal, A.W.6
  • 31
    • 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., Lambeth J.D. The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558). J Biol Chem 1999, 274:22999-23005.
    • (1999) J Biol Chem , vol.274 , pp. 22999-23005
    • Nisimoto, Y.1    Motalebi, S.2    Han, C.H.3    Lambeth, J.D.4
  • 32
    • 0942268724 scopus 로고    scopus 로고
    • N-Formyl peptide receptor subtypes in human neutrophils activate l-plastin phosphorylation through different signal transduction intermediates
    • Paclet M.H., Davis C., Kotsonis P., Godovac-Zimmermann J., Segal A.W., Dekker L.V. N-Formyl peptide receptor subtypes in human neutrophils activate l-plastin phosphorylation through different signal transduction intermediates. Biochem J 2004, 377:469-477.
    • (2004) Biochem J , vol.377 , pp. 469-477
    • Paclet, M.H.1    Davis, C.2    Kotsonis, P.3    Godovac-Zimmermann, J.4    Segal, A.W.5    Dekker, L.V.6
  • 33
    • 0037149510 scopus 로고    scopus 로고
    • Killing activity of neutrophils is mediated through activation of proteases by K+ flux
    • Reeves E.P., Lu H., Jacobs H.L., Messina C.G., Bolsover S., Gabella G., et al. Killing activity of neutrophils is mediated through activation of proteases by K+ flux. Nature 2002, 416:291-297.
    • (2002) Nature , vol.416 , pp. 291-297
    • Reeves, E.P.1    Lu, H.2    Jacobs, H.L.3    Messina, C.G.4    Bolsover, S.5    Gabella, G.6
  • 34
    • 0025203499 scopus 로고
    • Phosphorylation of neutrophil 47-kDa cytosolic oxidase factor. Translocation to membrane is associated with distinct phosphorylation events
    • Rotrosen D., Leto T.L. Phosphorylation of neutrophil 47-kDa cytosolic oxidase factor. Translocation to membrane is associated with distinct phosphorylation events. J Biol Chem 1990, 265:19910-19915.
    • (1990) J Biol Chem , vol.265 , pp. 19910-19915
    • Rotrosen, D.1    Leto, T.L.2
  • 35
    • 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
  • 36
    • 0037853270 scopus 로고    scopus 로고
    • Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox
    • Stahelin R.V., Burian A., Bruzik K.S., Murray D., Cho W. Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox. J Biol Chem 2003, 278:14469-14479.
    • (2003) J Biol Chem , vol.278 , pp. 14469-14479
    • Stahelin, R.V.1    Burian, A.2    Bruzik, K.S.3    Murray, D.4    Cho, W.5
  • 37
    • 33746896166 scopus 로고    scopus 로고
    • The phosphoinositide-binding protein p40phox activates the NADPH oxidase during Fc{gamma}IIA receptor-induced phagocytosis
    • Suh C.I., Stull N.D., Li X.J., Tian W., Price M.O., Grinstein S., et al. The phosphoinositide-binding protein p40phox activates the NADPH oxidase during Fc{gamma}IIA receptor-induced phagocytosis. J Exp Med 2006.
    • (2006) J Exp Med
    • Suh, C.I.1    Stull, N.D.2    Li, X.J.3    Tian, W.4    Price, M.O.5    Grinstein, S.6
  • 38
    • 0029806925 scopus 로고    scopus 로고
    • Assembly and activation of the phagocyte NADPH oxidase. Specific interaction of the N-terminal Src homology 3 domain of p47phox with p22phox is required for activation of the NADPH oxidase
    • Sumimoto H., Hata K., Mizuki K., Ito T., Kage Y., Sakaki Y., et al. Assembly and activation of the phagocyte NADPH oxidase. Specific interaction of the N-terminal Src homology 3 domain of p47phox with p22phox is required for activation of the NADPH oxidase. J Biol Chem 1996, 271:22152-22158.
    • (1996) J Biol Chem , vol.271 , pp. 22152-22158
    • Sumimoto, H.1    Hata, K.2    Mizuki, K.3    Ito, T.4    Kage, Y.5    Sakaki, Y.6
  • 39
    • 33846781304 scopus 로고    scopus 로고
    • A regulated adaptor function of p40phox: distinct p67phox membrane targeting by p40phox and by p47phox
    • Ueyama T., Tatsuno T., Kawasaki T., Tsujibe S., Shirai Y., Sumimoto H., et al. A regulated adaptor function of p40phox: distinct p67phox membrane targeting by p40phox and by p47phox. Mol Biol Cell 2007, 18:441-454.
    • (2007) Mol Biol Cell , vol.18 , pp. 441-454
    • Ueyama, T.1    Tatsuno, T.2    Kawasaki, T.3    Tsujibe, S.4    Shirai, Y.5    Sumimoto, H.6
  • 40
    • 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., Kawasaki T., Shimizu A., Son J., 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, 181:629-640.
    • (2008) J Immunol , vol.181 , pp. 629-640
    • Ueyama, T.1    Kusakabe, T.2    Karasawa, S.3    Kawasaki, T.4    Shimizu, A.5    Son, J.6
  • 41
    • 10944230901 scopus 로고    scopus 로고
    • The phox homology (PX) domain protein interaction network in yeast
    • Vollert C.S., Uetz P. The phox homology (PX) domain protein interaction network in yeast. Mol Cell Proteomics 2004, 3:1053-1064.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1053-1064
    • Vollert, C.S.1    Uetz, P.2
  • 42
    • 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., Segal A.W. p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. Biochem J 1993, 296(Pt 3):557-561.
    • (1993) Biochem J , vol.296 , Issue.PART 3 , pp. 557-561
    • Wientjes, F.B.1    Hsuan, J.J.2    Totty, N.F.3    Segal, A.W.4
  • 43
    • 0029835305 scopus 로고    scopus 로고
    • Interactions between cytosolic components of the NADPH oxidase: p40phox interacts with both p67phox and p47phox
    • Wientjes F.B., Panayotou G., Reeves E., Segal A.W. Interactions between cytosolic components of the NADPH oxidase: p40phox interacts with both p67phox and p47phox. Biochem J 1996, 317(Pt 3):919-924.
    • (1996) Biochem J , vol.317 , Issue.PART 3 , pp. 919-924
    • Wientjes, F.B.1    Panayotou, G.2    Reeves, E.3    Segal, A.W.4
  • 45
    • 0037039667 scopus 로고    scopus 로고
    • The p40phox and p47phox PX domains of NADPH oxidase target cell membranes via direct and indirect recruitment by phosphoinositides
    • Zhan Y., Virbasius J.V., Song X., Pomerleau D.P., Zhou G.W. The p40phox and p47phox PX domains of NADPH oxidase target cell membranes via direct and indirect recruitment by phosphoinositides. J Biol Chem 2002, 277:4512-4518.
    • (2002) J Biol Chem , vol.277 , pp. 4512-4518
    • Zhan, Y.1    Virbasius, J.V.2    Song, X.3    Pomerleau, D.P.4    Zhou, G.W.5
  • 46
    • 15944396277 scopus 로고    scopus 로고
    • P47(phox) PX domain of NADPH oxidase targets cell membrane via moesin-mediated association with the actin cytoskeleton
    • Zhan Y., He D., Newburger P.E., Zhou G.W. p47(phox) PX domain of NADPH oxidase targets cell membrane via moesin-mediated association with the actin cytoskeleton. J Cell Biochem 2004, 92:795-809.
    • (2004) J Cell Biochem , vol.92 , pp. 795-809
    • Zhan, Y.1    He, D.2    Newburger, P.E.3    Zhou, G.W.4


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