메뉴 건너뛰기




Volumn 116, Issue 7, 2006, Pages 2033-2043

A specific p47phox-serine phosphorylated by convergent MAPKs mediates neutrophil NADPH oxidase priming at inflammatory sites

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; GENISTEIN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE P38; MITOGEN ACTIVATED PROTEIN KINASE P38 INHIBITOR; MUTANT PROTEIN; OXIDOREDUCTASE; P47 PHAGOCYTE OXIDASE; PROTEIN TYROSINE KINASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SERINE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; UO 126; ENZYME INHIBITOR; NEUTROPHIL CYTOSOLIC FACTOR 1; PEPTIDE;

EID: 33745843632     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI27544     Document Type: Article
Times cited : (267)

References (61)
  • 1
    • 0034725724 scopus 로고    scopus 로고
    • Phagocytes and oxidative stress
    • Babior, B.M. 2000. Phagocytes and oxidative stress. Am. J. Med. 109:33-44.
    • (2000) Am. J. Med. , vol.109 , pp. 33-44
    • Babior, B.M.1
  • 2
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff, S.J. 2005. Myeloperoxidase: friend and foe. J. Leukoc. Biol. 77:598-625.
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 3
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal, A.W. 2005. How neutrophils kill microbes. Annu. Rev. Immunol. 23:197-223.
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 4
    • 0021739838 scopus 로고
    • Oxidants from phagocytes: Agents of defense and destruction
    • Babior, B.M. 1984. Oxidants from phagocytes: agents of defense and destruction. Blood. 64:959-966.
    • (1984) Blood , vol.64 , pp. 959-966
    • Babior, B.M.1
  • 6
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases
    • Quinn, M.T., and Gauss, K.A. 2004. Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J. Leukoc. Biol. 76:760-781.
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 7
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH oxidase: A structural perspective
    • Groemping, Y., and Rittinger, K. 2005. Activation and assembly of the NADPH oxidase: a structural perspective. Biochem. J. 386:401-416.
    • (2005) Biochem. J. , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 8
    • 0025259712 scopus 로고
    • Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation
    • Clark, R.A., Volpp, B.D., Leidal, K.G., and Nauseef, W.M. 1990. Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation. J. Clin. Invest. 85:714-721.
    • (1990) J. Clin. Invest. , vol.85 , pp. 714-721
    • Clark, R.A.1    Volpp, B.D.2    Leidal, K.G.3    Nauseef, W.M.4
  • 9
    • 0027520431 scopus 로고
    • Translocation of Rac correlates with NADPH oxidase activation. Evidence for equimolar translocation of oxidase components
    • Quinn, M.T., Evans, T., Loetterle, L.R., Jesaitis, A.J., and Bokoch, G.M. 1993. Translocation of Rac correlates with NADPH oxidase activation. Evidence for equimolar translocation of oxidase components. J. Biol. Chem. 268:20983-20987.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20983-20987
    • Quinn, M.T.1    Evans, T.2    Loetterle, L.R.3    Jesaitis, A.J.4    Bokoch, G.M.5
  • 10
    • 0028299331 scopus 로고
    • Activation of NADPH oxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane
    • Abo, A., Webb, M.R., Grogan, A., and Segal, A.W. 1994. Activation of NADPH oxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane. Biochem. J. 298:585-591.
    • (1994) Biochem. J. , vol.298 , pp. 585-591
    • Abo, A.1    Webb, M.R.2    Grogan, A.3    Segal, A.W.4
  • 11
    • 0028227249 scopus 로고
    • Cytosolic guanine nucleotide-binding protein Rac 2 operates in vivo as a component of the neutrophil respiratory burst oxidase. Transfer of Rac 2 and the cytosolic oxidase components p47phox and p67phox to the submembranous actin cytoskeleton during oxidase activation
    • El Benna, J., Ruedi, J.M., and Babior, B.M.1994. Cytosolic guanine nucleotide-binding protein Rac 2 operates in vivo as a component of the neutrophil respiratory burst oxidase. Transfer of Rac 2 and the cytosolic oxidase components p47phox and p67phox to the submembranous actin cytoskeleton during oxidase activation. J. Biol. Chem. 269:6729-6734.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6729-6734
    • El Benna, J.1    Ruedi, J.M.2    Babior, B.M.3
  • 12
    • 0023937220 scopus 로고
    • Relationship of protein phosphorylation to the activation of the respiratory burst in human neutrophils. Defects in the phosphorylation of a group of closely related 47-kDa proteins in two forms of chronic granulomatous disease
    • Okamura, N., Curnutte, J.T., Roberts, R.L., and Babior, B.M. 1988. Relationship of protein phosphorylation to the activation of the respiratory burst in human neutrophils. Defects in the phosphorylation of a group of closely related 47-kDa proteins in two forms of chronic granulomatous disease. J. Biol. Chem. 263:6777-6782.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6777-6782
    • Okamura, N.1    Curnutte, J.T.2    Roberts, R.L.3    Babior, B.M.4
  • 13
    • 0027364858 scopus 로고
    • Activation of NADPH oxidase of human neutrophils involves the phosphorylation and the translocation of cytosolic p67phox
    • Dusi, S., and Rossi, F. 1993. Activation of NADPH oxidase of human neutrophils involves the phosphorylation and the translocation of cytosolic p67phox. Biochem. J. 296:367-371.
    • (1993) Biochem. J. , vol.296 , pp. 367-371
    • Dusi, S.1    Rossi, F.2
  • 14
    • 0030764621 scopus 로고    scopus 로고
    • Phosphorylation of the respiratory burst oxidase subunit p67phox during human neutrophil activation. Regulation by protein kinase C-dependent and independent pathways
    • El-Benna, J., et al. 1997. Phosphorylation of the respiratory burst oxidase subunit p67phox during human neutrophil activation. Regulation by protein kinase C-dependent and independent pathways. J. Biol. Chem. 272:17204-17208.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17204-17208
    • El-Benna, J.1
  • 15
    • 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, A.P., Grandvaux, N., Vignais, P.V., and Fuchs, A. 1998. 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. 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
  • 16
    • 0034664253 scopus 로고    scopus 로고
    • Phosphorylation of p22phox is mediated by phospholipase D-dependent and independent mechanisms. Correlation of NADPH oxidase activity and p22phox phosphorylation
    • Regier, D.S., Greene, D.G., Sergeant, S., Jesaitis, A.J., and McPhail, L.C. 2000. Phosphorylation of p22phox is mediated by phospholipase D-dependent and independent mechanisms. Correlation of NADPH oxidase activity and p22phox phosphorylation. J. Biol. Chem. 275:28406-28412.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28406-28412
    • Regier, D.S.1    Greene, D.G.2    Sergeant, S.3    Jesaitis, A.J.4    McPhail, L.C.5
  • 17
    • 0028142461 scopus 로고
    • The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases
    • El Benna, J., Faust, L.P., and Babior, B.M. 1994. The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases. J. Biol. Chem. 269:23431-23436.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23431-23436
    • El Benna, J.1    Faust, L.P.2    Babior, B.M.3
  • 18
    • 0029983262 scopus 로고    scopus 로고
    • Phosphorylation of the respiratory burst oxidase subunit p47phox as determined by two-dimensional phosphopeptide mapping. Phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase
    • El Benna, J., Faust, L.P., Johnson, J.L., and Babior, B.M. 1996. Phosphorylation of the respiratory burst oxidase subunit p47phox as determined by two-dimensional phosphopeptide mapping. Phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase. J. Biol. Chem. 271:6374-6378.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6374-6378
    • El Benna, J.1    Faust, L.P.2    Johnson, J.L.3    Babior, B.M.4
  • 19
    • 0028978633 scopus 로고
    • The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase. Functions of the individual target serines as evaluated by site-directed mutagenesis
    • Faust, L.P., El Benna, J., Babior, B.M., and Chanock, S.J. 1995. The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase. Functions of the individual target serines as evaluated by site-directed mutagenesis. J. Clin. Invest. 96:1499-1505.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1499-1505
    • Faust, L.P.1    El Benna, J.2    Babior, B.M.3    Chanock, S.J.4
  • 21
    • 0029008602 scopus 로고
    • Neutrophil priming: The cellular signals that say 'amber' but not 'green'
    • Hallett, M.B., and Lloyds, D.L. 1995. Neutrophil priming: the cellular signals that say 'amber' but not 'green.' Immunol. Today. 16:264-268.
    • (1995) Immunol. Today , vol.16 , pp. 264-268
    • Hallett, M.B.1    Lloyds, D.L.2
  • 22
    • 0028290562 scopus 로고
    • Differential priming effects of proinflammatory cytokines on human neutrophil oxidative burst in response to bacterial N-formyl peptides
    • Elbim, C., Bailly, S., Chollet-Martin, S., Hakim, J., and Gougerot-Pocidalo, M.A. 1994. Differential priming effects of proinflammatory cytokines on human neutrophil oxidative burst in response to bacterial N-formyl peptides. Infect. Immun. 62:2195-2201.
    • (1994) Infect. Immun. , vol.62 , pp. 2195-2201
    • Elbim, C.1    Bailly, S.2    Chollet-Martin, S.3    Hakim, J.4    Gougerot-Pocidalo, M.A.5
  • 23
    • 0027179125 scopus 로고
    • Priming of polymorphonuclear neutrophils by tumor necrosis factor alpha in whole blood: Identification of two polymorphonuclear neutrophil subpopulations in response to formyl-peptides
    • Elbim, C., Chollet-Martin, S., Bailly, S., Hakim, J., and Gougerot-Pocidalo, M.A. 1993. Priming of polymorphonuclear neutrophils by tumor necrosis factor alpha in whole blood: identification of two polymorphonuclear neutrophil subpopulations in response to formyl-peptides. Blood. 82:633-640.
    • (1993) Blood , vol.82 , pp. 633-640
    • Elbim, C.1    Chollet-Martin, S.2    Bailly, S.3    Hakim, J.4    Gougerot-Pocidalo, M.A.5
  • 24
    • 0025134964 scopus 로고
    • Priming of the human neutrophil respiratory burst by granulocyte- macrophage colony-stimulating factor and tumor necrosis factor-alpha involves regulation at a post-cell surface receptor level. Enhancement of the effect of agents which directly activate G proteins
    • McColl, S.R., Beauseigle, D., Gilbert, C., and Naccache, P.H. 1990. Priming of the human neutrophil respiratory burst by granulocyte-macrophage colony-stimulating factor and tumor necrosis factor-alpha involves regulation at a post-cell surface receptor level. Enhancement of the effect of agents which directly activate G proteins. J. Immunol. 145:3047-3053.
    • (1990) J. Immunol. , vol.145 , pp. 3047-3053
    • McColl, S.R.1    Beauseigle, D.2    Gilbert, C.3    Naccache, P.H.4
  • 25
    • 0037458967 scopus 로고    scopus 로고
    • Priming-induced localization of G(ialpha2) in high density membrane microdomains
    • Keil, M.L., et al. 2003. Priming-induced localization of G(ialpha2) in high density membrane microdomains. Biochem. Biophys. Res. Commun. 301:862-872.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 862-872
    • Keil, M.L.1
  • 26
    • 0032518557 scopus 로고    scopus 로고
    • Neutrophils exposed to bacterial lipopolysaccharide upregulate NADPH oxidase assembly
    • DeLeo, F.R., et al. 1998. Neutrophils exposed to bacterial lipopolysaccharide upregulate NADPH oxidase assembly. J. Clin. Invest. 101:455-463.
    • (1998) J. Clin. Invest. , vol.101 , pp. 455-463
    • DeLeo, F.R.1
  • 27
    • 0034711296 scopus 로고    scopus 로고
    • Priming of the neutrophil respiratory burst involves p38 mitogen-activated protein kinase-dependent exocytosis of flavocytochrome b558-containing granules
    • Ward, R.A., Nakamura, M., and McLeish, K.R. 2000. Priming of the neutrophil respiratory burst involves p38 mitogen-activated protein kinase-dependent exocytosis of flavocytochrome b558-containing granules. J. Biol. Chem. 275:36713-36719.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36713-36719
    • Ward, R.A.1    Nakamura, M.2    McLeish, K.R.3
  • 28
    • 0035984132 scopus 로고    scopus 로고
    • Granulocyte colony-stimulating factor primes NADPH oxidase in neutrophils through translocation of cytochrome b(558) by gelatinase-granule release
    • Mansfield, P.J., Hinkovska-Galcheva, V., Shayman, J.A., and Boxer, L.A. 2002. Granulocyte colony-stimulating factor primes NADPH oxidase in neutrophils through translocation of cytochrome b(558) by gelatinase-granule release. J. Lab. Clin. Med. 140:9-16.
    • (2002) J. Lab. Clin. Med. , vol.140 , pp. 9-16
    • Mansfield, P.J.1    Hinkovska-Galcheva, V.2    Shayman, J.A.3    Boxer, L.A.4
  • 29
    • 0003337889 scopus 로고    scopus 로고
    • Priming of human neutrophil respiratory burst by granulocyte/macrophage colony-stimulating factor (GM-CSF) involves partial phosphorylation of p47phox
    • Dang, P.M., et al. 1999. Priming of human neutrophil respiratory burst by granulocyte/macrophage colony-stimulating factor (GM-CSF) involves partial phosphorylation of p47phox. J. Biol. Chem. 274:20704-20708.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20704-20708
    • Dang, P.M.1
  • 30
    • 0141889087 scopus 로고    scopus 로고
    • TNF induces phosphorylation of p47phox in human neutrophils: Partial phosphorylation of p47phox is a common event of priming of human neutrophils by TNF and granulocyte-macrophage colony-stimulating factor
    • Dewas, C., Dang, P.M., Gougerot-Pocidalo, M.-A., and El-Benna, J. 2003. TNF induces phosphorylation of p47phox in human neutrophils: partial phosphorylation of p47phox is a common event of priming of human neutrophils by TNF and granulocyte-macrophage colony-stimulating factor. J. Immunol. 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
  • 31
    • 3042695344 scopus 로고    scopus 로고
    • Distinct ligand-dependent roles for p38 MAPK in priming and activation of the neutrophil NADPH oxidase
    • Brown, G.E., et al. 2004. Distinct ligand-dependent roles for p38 MAPK in priming and activation of the neutrophil NADPH oxidase. J. Biol. Chem. 279:27059-27068.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27059-27068
    • Brown, G.E.1
  • 32
    • 0027489710 scopus 로고
    • Receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3, and interleukin-5
    • Miyajima, A., Mui, A.L., Ogorochi, T., and Sakamaki, K. 1993. Receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3, and interleukin-5. Blood. 82:1960-1974.
    • (1993) Blood , vol.82 , pp. 1960-1974
    • Miyajima, A.1    Mui, A.L.2    Ogorochi, T.3    Sakamaki, K.4
  • 33
    • 0031036882 scopus 로고    scopus 로고
    • The structural and functional basis of cytokine receptor activation: Lessons from the common beta subunit of the granulocyte-macrophage colony-stimulating factor, interleukin-3 (IL-3), and IL-5 receptors
    • Bagley, C.J., Woodcock, J.M., Stomski, F.C., and Lopez, A.F. 1997. The structural and functional basis of cytokine receptor activation: lessons from the common beta subunit of the granulocyte-macrophage colony-stimulating factor, interleukin-3 (IL-3), and IL-5 receptors. Blood. 89:1471-1482.
    • (1997) Blood , vol.89 , pp. 1471-1482
    • Bagley, C.J.1    Woodcock, J.M.2    Stomski, F.C.3    Lopez, A.F.4
  • 34
    • 0027201616 scopus 로고
    • Granulocyte macrophage-colony stimulating factor stimulates both association and activation of phosphoinositide 3OH-kinase and src-related tyrosine kinase(s) in human myeloid derived cells
    • Corey, S., et al. 1993. Granulocyte macrophage-colony stimulating factor stimulates both association and activation of phosphoinositide 3OH-kinase and src-related tyrosine kinase(s) in human myeloid derived cells. EMBO J. 12:2681-2690.
    • (1993) EMBO J. , vol.12 , pp. 2681-2690
    • Corey, S.1
  • 35
    • 0033605359 scopus 로고    scopus 로고
    • Granulocyte-macrophage colony-stimulating factor-activated signaling pathways in human neutrophils. Involvement of Jak2 in the stimulation of phosphatidylinositol 3-kinase
    • Al-Shami, A., and Naccache, P.H. 1999. Granulocyte-macrophage colony-stimulating factor-activated signaling pathways in human neutrophils. Involvement of Jak2 in the stimulation of phosphatidylinositol 3-kinase. J. Biol. Chem. 274:5333-5338.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5333-5338
    • Al-Shami, A.1    Naccache, P.H.2
  • 36
    • 0033555720 scopus 로고    scopus 로고
    • Enhancement of chemotactic peptide-induced activation of phosphoinositide 3-kinase by granulocyte-macrophage colony-stimulating factor and its relation to the cytokine-mediated priming of neutrophil superoxide-anion production
    • Kodama, T., Hazeki, K., Hazeki, O., Okada, T., and Ui, M. 1999. Enhancement of chemotactic peptide-induced activation of phosphoinositide 3-kinase by granulocyte-macrophage colony-stimulating factor and its relation to the cytokine-mediated priming of neutrophil superoxide-anion production. Biochem. J. 337:201-209.
    • (1999) Biochem. J. , vol.337 , pp. 201-209
    • Kodama, T.1    Hazeki, K.2    Hazeki, O.3    Okada, T.4    Ui, M.5
  • 37
    • 0026668608 scopus 로고
    • Granulocyte-macrophage colony-stimulating factor-induced protein tyrosine phosphorylation of microtubule-associated protein kinase in human neutrophils
    • Gomez-Cambronero, J., et al. 1992. Granulocyte-macrophage colony-stimulating factor-induced protein tyrosine phosphorylation of microtubule-associated protein kinase in human neutrophils. Proc. Natl. Acad. Sci. U. S. A. 89:7551-7555.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 7551-7555
    • Gomez-Cambronero, J.1
  • 38
    • 0028180511 scopus 로고
    • Cytoplasmic phospholipase A2 translocates to membrane fraction in human neutrophils activated by stimuli that phosphorylate mitogen-activated protein kinase
    • Durstin, M., Durstin, S., Molski, T.F.P., Becker, E.L., and Sha'Afi, R.I. 1994. Cytoplasmic phospholipase A2 translocates to membrane fraction in human neutrophils activated by stimuli that phosphorylate mitogen-activated protein kinase. Proc. Natl. Acad. Sci. U. S. A. 91:3142-3146.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3142-3146
    • Durstin, M.1    Durstin, S.2    Molski, T.F.P.3    Becker, E.L.4    Sha'Afi, R.I.5
  • 39
    • 0031662161 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase cascades during priming of human neutrophils by TNF and GM-CSF
    • McLeish, K.R., et al. 1998. Activation of mitogen-activated protein kinase cascades during priming of human neutrophils by TNF and GM-CSF. J. Leukoc. Biol. 64:537-545.
    • (1998) J. Leukoc. Biol. , vol.64 , pp. 537-545
    • McLeish, K.R.1
  • 40
    • 0032908810 scopus 로고    scopus 로고
    • Cytokine-specific activation of distinct mitogen-activated protein kinase subtype cascades in human neutrophils stimulated by granulocyte colony-stimulating factor, granulocyte-macrophage colony-stimulating factor, and tumor necrosis factor-alpha
    • Suzuki, K., Hino, M., Hato, F., Tatsumi, N., and Kitagawa, S. 1999. Cytokine-specific activation of distinct mitogen-activated protein kinase subtype cascades in human neutrophils stimulated by granulocyte colony-stimulating factor, granulocyte-macrophage colony-stimulating factor, and tumor necrosis factor-alpha. Blood. 93:341-349.
    • (1999) Blood , vol.93 , pp. 341-349
    • Suzuki, K.1    Hino, M.2    Hato, F.3    Tatsumi, N.4    Kitagawa, S.5
  • 41
    • 0030056861 scopus 로고    scopus 로고
    • Granulocyte-macrophage colony-stimulating factor stimulates JAK2 signaling pathway and rapidly activates p93fes, STAT1 p91, and STAT3 p92 in polymorphonuclear leukocytes
    • Brizzi, M.F., et al. 1996. Granulocyte-macrophage colony-stimulating factor stimulates JAK2 signaling pathway and rapidly activates p93fes, STAT1 p91, and STAT3 p92 in polymorphonuclear leukocytes. J. Biol. Chem. 271:3562-3567.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3562-3567
    • Brizzi, M.F.1
  • 42
    • 0031985128 scopus 로고    scopus 로고
    • Granulocyte-macrophage colony-stimulating factor-activated signaling pathways in human neutrophils. Selective activation of Jak2, Stat3, and Stat5b
    • Al-Shami, A., Mahanna, W., and Naccache, P.H. 1998. Granulocyte- macrophage colony-stimulating factor-activated signaling pathways in human neutrophils. Selective activation of Jak2, Stat3, and Stat5b. J. Biol. Chem. 273:1058-1063.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1058-1063
    • Al-Shami, A.1    Mahanna, W.2    Naccache, P.H.3
  • 43
    • 0029928366 scopus 로고    scopus 로고
    • Tumor necrosis factors: Developments during the last decade
    • Aggarwal, B.B., and Natarajan, K. 1996. Tumor necrosis factors: developments during the last decade. Eur. Cytokine Netw. 7:93-124.
    • (1996) Eur. Cytokine Netw. , vol.7 , pp. 93-124
    • Aggarwal, B.B.1    Natarajan, K.2
  • 44
    • 0001881531 scopus 로고
    • Rheumatoid arthritis: A disease of disordered immunity
    • J.I. Gallin, I.M. Goldstein, and R. Snyderman, editors. Raven Press. New York, New York, USA
    • Firestein, G.S., and Zvaifler, N.J. 1992. Rheumatoid arthritis: a disease of disordered immunity. In Inflammation: basic principles and clinical correlates. 2nd edition. J.I. Gallin, I.M. Goldstein, and R. Snyderman, editors. Raven Press. New York, New York, USA. 959-977.
    • (1992) Inflammation: Basic Principles and Clinical Correlates. 2nd Edition , pp. 959-977
    • Firestein, G.S.1    Zvaifler, N.J.2
  • 45
    • 0028556421 scopus 로고
    • Neutrophils, host defense, and inflammation: A double-edged sword
    • Smith, J.A. 1994. Neutrophils, host defense, and inflammation: a double-edged sword. J. Leukoc. Biol. 56:672-686.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 672-686
    • Smith, J.A.1
  • 46
    • 2442508934 scopus 로고    scopus 로고
    • Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins
    • Elortza, F., et al. 2003. Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins. Mol. Cell. Proteom. 2:1261-1270.
    • (2003) Mol. Cell. Proteom. , vol.2 , pp. 1261-1270
    • Elortza, F.1
  • 47
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • Mann, M., et al. 2002. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trend. Biotechnol. 20:261-268.
    • (2002) Trend. Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1
  • 48
    • 0028884033 scopus 로고
    • PD098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo
    • Alessi, D.R., Cuenda, A., Cohen, P., Dudley, D.T., and Saltiel, A.R. 1995. PD098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270:27489-27494.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 49
    • 14444279192 scopus 로고    scopus 로고
    • Identification of a novel inhibitor of mitogen activated protein kinase kinase (MEK)
    • Favata, M.F., et al. 1998. Identification of a novel inhibitor of mitogen activated protein kinase kinase (MEK). J. Biol. Chem. 273:18623-18632.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18623-18632
    • Favata, M.F.1
  • 50
    • 0028988138 scopus 로고
    • SB203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda, A., et al. 1995. SB203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 364:229-233.
    • (1995) FEBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1
  • 51
    • 0031759170 scopus 로고    scopus 로고
    • Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration
    • Nagahara, H., et al. 1998. Transduction of full-length TAT fusion proteins into mammalian cells: TAT-p27Kip1 induces cell migration. Nat. Med. 4:1449-1452.
    • (1998) Nat. Med. , vol.4 , pp. 1449-1452
    • Nagahara, H.1
  • 52
    • 0037240676 scopus 로고    scopus 로고
    • Critical role of the carboxyl terminus of proline-rich tyrosine kinase (Pyk2) in the activation of human neutrophils by tumor necrosis factor: Separation of signals for the respiratory burst and degranulation
    • Han, H., Fuortes, M., and Nathan, C. 2003. Critical role of the carboxyl terminus of proline-rich tyrosine kinase (Pyk2) in the activation of human neutrophils by tumor necrosis factor: separation of signals for the respiratory burst and degranulation. J. Exp. Med. 197:63-75.
    • (2003) J. Exp. Med. , vol.197 , pp. 63-75
    • Han, H.1    Fuortes, M.2    Nathan, C.3
  • 53
    • 0030588188 scopus 로고    scopus 로고
    • Activation of p38 in stimulated human neutrophils: Phosphorylation of oxidase component p47phox by p38 and ERK but not by JNK
    • El Benna, J., et al. 1996. Activation of p38 in stimulated human neutrophils: phosphorylation of oxidase component p47phox by p38 and ERK but not by JNK. Arch. Biochem. Biophys. 334:395-400.
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 395-400
    • El Benna, J.1
  • 54
    • 11344286593 scopus 로고    scopus 로고
    • MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation
    • Manke, I.A., et al. 2005. MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation. Mol. Cell. 17:37-48.
    • (2005) Mol. Cell. , vol.17 , pp. 37-48
    • Manke, I.A.1
  • 55
    • 0032497427 scopus 로고    scopus 로고
    • Conformational changes of leukocyte NADPH oxidase subunit p47phox during activation studied through its intrinsic fluorescence
    • Park, H.-S., and Park, J.-W. 1998. Conformational changes of leukocyte NADPH oxidase subunit p47phox during activation studied through its intrinsic fluorescence. Biochim. Biophys. Acta. 1387:406-411.
    • (1998) Biochim. Biophys. Acta , vol.1387 , pp. 406-411
    • Park, H.-S.1    Park, J.-W.2
  • 56
    • 0030682421 scopus 로고    scopus 로고
    • Analysis of activation-induced conformational changes in p47phox using tryptophan fluorescence spectroscopy
    • Swain, S.D., Helgerson, S.L., Davis, A.R., Nelson, L.K., and Quinn, M.T. 1997. Analysis of activation-induced conformational changes in p47phox using tryptophan fluorescence spectroscopy. J. Biol. Chem. 272:29502-29509.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29502-29509
    • Swain, S.D.1    Helgerson, S.L.2    Davis, A.R.3    Nelson, L.K.4    Quinn, M.T.5
  • 57
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping, Y., Lapouge, K., Smerdon, S.J., and Rittinger, K. 2003. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell. 113:343-355.
    • (2003) Cell. , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 58
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 59
    • 0026614921 scopus 로고
    • O2- production by B lymphocytes lacking the respiratory burst oxidase subunit p47phox after transfection with an expression vector containing a p47phox cDNA
    • Chanock, S.J., et al. 1992. O2- production by B lymphocytes lacking the respiratory burst oxidase subunit p47phox after transfection with an expression vector containing a p47phox cDNA. Proc. Natl. Acad. Sci. U. S. A. 89:10174-10177.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10174-10177
    • Chanock, S.J.1
  • 60
    • 0023945481 scopus 로고
    • The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis
    • Arnett, F.C., et al. 1988. The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis. Arthritis Rheum. 31:315-324.
    • (1988) Arthritis Rheum. , vol.31 , pp. 315-324
    • Arnett, F.C.1
  • 61
    • 0026003027 scopus 로고
    • The European Spondylarthropathy Study Group preliminary criteria for the classification of spondylarthropathy
    • Dougados, M., et al. 1991. The European Spondylarthropathy Study Group preliminary criteria for the classification of spondylarthropathy. Arthritis Rheum. 34:1218-1227.
    • (1991) Arthritis Rheum. , vol.34 , pp. 1218-1227
    • Dougados, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.