메뉴 건너뛰기




Volumn 64, Issue 4, 1998, Pages 555-562

Role of the mitogen-activated protein kinases and tyrosine kinases during leukotriene B4-induced eosinophil activation

Author keywords

Homotypic aggregation; NADPH oxidase; Phospholipase A2

Indexed keywords

HERBIMYCIN; LAVENDUSTIN A; LEUKOTRIENE B4; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE A2; PROTEIN TYROSINE KINASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 0031687981     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.64.4.555     Document Type: Article
Times cited : (36)

References (58)
  • 1
    • 0001847205 scopus 로고
    • Eosinophils and parasitic diseases
    • H. Smith and R. M. Cook, eds., London: Academic Press
    • Butterworth, A. E., Thorne, K. J. (1993) Eosinophils and parasitic diseases. In Immunopharmacology of the Eosinophil (H. Smith and R. M. Cook, eds.), London: Academic Press, 119-150.
    • (1993) Immunopharmacology of the Eosinophil , pp. 119-150
    • Butterworth, A.E.1    Thorne, K.J.2
  • 2
    • 0002011047 scopus 로고
    • Eosinophil accumulation, secretion and activation
    • H. Smith and R. M. Cook, eds., London: Academic Press
    • Walsh, G. M., Wardlaw, A. J., Kay A. B. (1993) Eosinophil accumulation, secretion and activation. In Immunopharmacology of the Eosinophil (H. Smith and R. M. Cook, eds.), London: Academic Press, 73-90.
    • (1993) Immunopharmacology of the Eosinophil , pp. 73-90
    • Walsh, G.M.1    Wardlaw, A.J.2    Kay, A.B.3
  • 3
    • 0021857482 scopus 로고
    • Response of superoxide anion production by guinea pig eosinophils to various soluble stimuli: Comparison to neutrophils
    • Yamashita, T., Someya, A., Hara, E. (1985) Response of superoxide anion production by guinea pig eosinophils to various soluble stimuli: comparison to neutrophils. Arch. Biochem. Biophys. 241, 447-452.
    • (1985) Arch. Biochem. Biophys. , vol.241 , pp. 447-452
    • Yamashita, T.1    Someya, A.2    Hara, E.3
  • 5
    • 0023900572 scopus 로고
    • Stimulus-dependent differences in superoxide anion generation by normal human eosinophils and neutrophils
    • Sedgwick, J. B., Vrtis, R. F., Gourley, M. F., Busse, W. W. (1988) Stimulus-dependent differences in superoxide anion generation by normal human eosinophils and neutrophils. J. Allergy Clin. Immunol. 81, 876-883.
    • (1988) J. Allergy Clin. Immunol. , vol.81 , pp. 876-883
    • Sedgwick, J.B.1    Vrtis, R.F.2    Gourley, M.F.3    Busse, W.W.4
  • 6
    • 0002500975 scopus 로고
    • Lipid, peptide and cytokine mediators elaborated by eosinophils
    • H. Smith and R. M. Cook, eds., London: Academic Press
    • Weller, P. F. (1993) Lipid, peptide and cytokine mediators elaborated by eosinophils. In Immunopharmacology of the Eosinophil (H. Smith and R. M. Cook, eds.), London: Academic Press, 25-42.
    • (1993) Immunopharmacology of the Eosinophil , pp. 25-42
    • Weller, P.F.1
  • 7
    • 0015596284 scopus 로고
    • Biological defense mechanism: The production by leukocytes of superoxide, a potentail bactericidal agent
    • Babior, B. M., Kipnes, R. S., Curnette, J. T. (1973) Biological defense mechanism: the production by leukocytes of superoxide, a potentail bactericidal agent. J. Clin. Invest. 52, 741-744.
    • (1973) J. Clin. Invest. , vol.52 , pp. 741-744
    • Babior, B.M.1    Kipnes, R.S.2    Curnette, J.T.3
  • 8
    • 37049188738 scopus 로고
    • Brominating oxidants generated by human eosinophils
    • Weiss, S. J., Test, S. T., Eckmann, C. M., Roos, D., Regiani, S. (1986) Brominating oxidants generated by human eosinophils. Science 234, 200-203.
    • (1986) Science , vol.234 , pp. 200-203
    • Weiss, S.J.1    Test, S.T.2    Eckmann, C.M.3    Roos, D.4    Regiani, S.5
  • 9
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel, T. (1998) Oxygen radicals and signaling. Curr. Op. Cell Biol. 10, 248-253.
    • (1998) Curr. Op. Cell Biol. , vol.10 , pp. 248-253
    • Finkel, T.1
  • 11
    • 0032056356 scopus 로고    scopus 로고
    • 4 activates the NADPH oxidase in eosinophils via a pertussis toxin-sensitive mechanism that is largely independent of arachidonic acid mobilization
    • 4 activates the NADPH oxidase in eosinophils via a pertussis toxin-sensitive mechanism that is largely independent of arachidonic acid mobilization. J. Immunol. 160, 4526-4534.
    • (1998) J. Immunol. , vol.160 , pp. 4526-4534
    • Lindsay, M.A.1    Perkins, R.S.2    Barnes, P.J.3    Giembycz, M.A.4
  • 13
    • 0029099616 scopus 로고
    • Chemoattractant signaling and leukocyte activation
    • Bokoch, G. M. (1995) Chemoattractant signaling and leukocyte activation. Blood 86, 1649-1660.
    • (1995) Blood , vol.86 , pp. 1649-1660
    • Bokoch, G.M.1
  • 14
    • 0026611730 scopus 로고
    • 4 induced steady state calcium rise and superoxide anion generation in guinea pig eosinophils are not related events
    • 4 induced steady state calcium rise and superoxide anion generation in guinea pig eosinophils are not related events. Biochem. Biophys. Res. Commun. 187, 670-676.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 670-676
    • Subramanian, N.1
  • 16
    • 0029162733 scopus 로고
    • Eosinophil adhesion to vascular cell adhesion molecule-1 activates superoxide anion generation
    • Nagata, M., Sedgwick, J. B., Bates, M. E., Kita, H., Busse, W. W. (1995) Eosinophil adhesion to vascular cell adhesion molecule-1 activates superoxide anion generation. J. Immunol. 155, 2194-2202.
    • (1995) J. Immunol. , vol.155 , pp. 2194-2202
    • Nagata, M.1    Sedgwick, J.B.2    Bates, M.E.3    Kita, H.4    Busse, W.W.5
  • 17
    • 0029788914 scopus 로고    scopus 로고
    • Human eotaxin represents a potent activator of the respiratory burst of human eosinophils
    • Elsner, J., Hochstetter, R., Kimmig, D., Kapp, A. (1996) Human eotaxin represents a potent activator of the respiratory burst of human eosinophils. Eur. J. Immunol. 26, 1919-1925.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1919-1925
    • Elsner, J.1    Hochstetter, R.2    Kimmig, D.3    Kapp, A.4
  • 18
    • 0029025036 scopus 로고
    • The regulation of tyrosine kinase signalling pathways by growth factor and G-protein-coupled receptors
    • Malarkey, K., Belham, C. M., Paul, A., Graham, A., McLees, A., Scott, P. H. (1995) The regulation of tyrosine kinase signalling pathways by growth factor and G-protein-coupled receptors. Biochem. J. 309, 361-375.
    • (1995) Biochem. J. , vol.309 , pp. 361-375
    • Malarkey, K.1    Belham, C.M.2    Paul, A.3    Graham, A.4    McLees, A.5    Scott, P.H.6
  • 19
    • 3543111599 scopus 로고
    • Cytokine signaling through nonreceptor protein tyrosine kinases
    • Taniguchi, T. (1995) Cytokine signaling through nonreceptor protein tyrosine kinases. Nature 270, 1523-1528.
    • (1995) Nature , vol.270 , pp. 1523-1528
    • Taniguchi, T.1
  • 20
    • 0029815128 scopus 로고    scopus 로고
    • Interplay between ras-related and heterotrimeric GTP binding proteins - Lifestyles of the big and little
    • Bokoch, G. M. (1996) Interplay between ras-related and heterotrimeric GTP binding proteins - lifestyles of the big and little. FASEB J. 10, 1290-1295.
    • (1996) FASEB J. , vol.10 , pp. 1290-1295
    • Bokoch, G.M.1
  • 21
    • 0029900434 scopus 로고    scopus 로고
    • G protein-coupled receptors and signaling pathways regulating growth responses
    • Post, G. R., Brown, J. H. (1996) G protein-coupled receptors and signaling pathways regulating growth responses. FASEB J. 10, 741-749.
    • (1996) FASEB J. , vol.10 , pp. 741-749
    • Post, G.R.1    Brown, J.H.2
  • 22
    • 0030175485 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase cascades and regulation of gene expression
    • Su, B., Karin, M. (1996) Mitogen-activated protein kinase cascades and regulation of gene expression. Curr. Op. Immunol. 8, 402-411.
    • (1996) Curr. Op. Immunol. , vol.8 , pp. 402-411
    • Su, B.1    Karin, M.2
  • 23
    • 0028142461 scopus 로고
    • phox during neutrophil activation. Phosphorylation of sites recognised by protein kinase C and by proline-directed kinases
    • phox during neutrophil activation. Phosphorylation of sites recognised 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
  • 24
    • 0029983262 scopus 로고    scopus 로고
    • phox as determined by two-dimensional phosphopeptide mapping - Phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase
    • phox 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
  • 26
    • 0029019812 scopus 로고
    • Distinct tyrosine kinase activation and Triton X-100 insolubility upon Fcγ RII or Fcγ RIIIB ligation in human polymorhonuclear leukocytes. Implications for immune complex activation of the respiratory burst
    • Zhou, M. J., Lublin, U. M., Link, D. C., Brown, E. J. (1995) Distinct tyrosine kinase activation and Triton X-100 insolubility upon Fcγ RII or Fcγ RIIIB ligation in human polymorhonuclear leukocytes. Implications for immune complex activation of the respiratory burst. J. Biol. Chem. 270, 13553-13560.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13553-13560
    • Zhou, M.J.1    Lublin, U.M.2    Link, D.C.3    Brown, E.J.4
  • 27
    • 0029823946 scopus 로고    scopus 로고
    • A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3,4,5-trisphosphate formation in the chemoattractant-stimulated human neutrophils
    • Ptasznik, A., Prossnitz, E. R., Yoshikawa, D., Smrcka, A., Traynor-Kaplan, A. E., Bokoch, G. M. (1996) A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3,4,5-trisphosphate formation in the chemoattractant-stimulated human neutrophils. J. Biol. Chem. 271, 25204-25207.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25204-25207
    • Ptasznik, A.1    Prossnitz, E.R.2    Yoshikawa, D.3    Smrcka, A.4    Traynor-Kaplan, A.E.5    Bokoch, G.M.6
  • 28
    • 0029907265 scopus 로고    scopus 로고
    • A role for pyk2 and src in linking G-protein-coupled receptors with MAP kinase activation
    • Dikic, L. Tokiwa, G., Lev, S., Courtneidge, S. A., Schlessinger, J. (1996) A role for pyk2 and src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383, 547-550.
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, L.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 30
    • 0029892373 scopus 로고    scopus 로고
    • Tyrosine kinases in activation of the MAP kinase cascade by G-protein-coupled receptors
    • Wan, Y., Kurosaki, T., Huang, X. Y. (1996) Tyrosine kinases in activation of the MAP kinase cascade by G-protein-coupled receptors. Nature 380, 541-544.
    • (1996) Nature , vol.380 , pp. 541-544
    • Wan, Y.1    Kurosaki, T.2    Huang, X.Y.3
  • 32
    • 0018859803 scopus 로고
    • Separation of human eosinophils in density gradients of polyvinylpyrrolidone-coated silica gel (Percoll)
    • Gartner, I. (1980) Separation of human eosinophils in density gradients of polyvinylpyrrolidone-coated silica gel (Percoll). Immunol. 40, 133-136.
    • (1980) Immunol. , vol.40 , pp. 133-136
    • Gartner, I.1
  • 33
    • 0016591134 scopus 로고
    • 2 release from human granulocytes during phagocytosis. I. Documentation, quantification, and some regulating factors
    • 2 release from human granulocytes during phagocytosis. I. Documentation, quantification, and some regulating factors. J. Clin. Invest. 55, 945-955.
    • (1975) J. Clin. Invest. , vol.55 , pp. 945-955
    • Root, R.K.1    Metcalf, J.2    Oshino, N.3    Chance, B.4
  • 34
    • 0024440968 scopus 로고
    • 2 activation and exocytosis in HL60 cells and human neutrophils
    • 2 activation and exocytosis in HL60 cells and human neutrophils. Biochem. J. 263, 715-723.
    • (1989) Biochem. J. , vol.263 , pp. 715-723
    • Cockcroft, S.1    Stutchfield, J.2
  • 35
    • 0024358172 scopus 로고
    • A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel
    • Kameshita, I., Fujisawa, H. (1989) A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. Anal. Biochem. 183, 139-143.
    • (1989) Anal. Biochem. , vol.183 , pp. 139-143
    • Kameshita, I.1    Fujisawa, H.2
  • 36
    • 0028884033 scopus 로고
    • PD 098059 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., Saltiel, A. R. (1995) PD 098059 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
  • 38
    • 0031575752 scopus 로고    scopus 로고
    • Differential effects of a mitogen-activated protein kinase kinase inhibitor on human neutrophil responses to chemotactic factors
    • Kuroki, M., O'Flaherty, J. T. (1997) Differential effects of a mitogen-activated protein kinase kinase inhibitor on human neutrophil responses to chemotactic factors. Biochem. Biophys. Res. Commun. 232, 474-477.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 474-477
    • Kuroki, M.1    O'Flaherty, J.T.2
  • 39
    • 0029016789 scopus 로고
    • Dissociation of mitogen-activated protein kinase activation from the oxidative burst in differentiated HL-60 cells and human neutrophils
    • Yu, H., Suchard, S. J., Nairn, R., Jove, R. (1995) Dissociation of mitogen-activated protein kinase activation from the oxidative burst in differentiated HL-60 cells and human neutrophils. J. Biol. Chem. 270, 15719-15724.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15719-15724
    • Yu, H.1    Suchard, S.J.2    Nairn, R.3    Jove, R.4
  • 40
    • 0030937347 scopus 로고    scopus 로고
    • Common and distinct intracellular signaling pathways in human neutrophils utilized by platelet activating factor and FMLP
    • Nick, J. A., Avdi, N. J., Young, S. K., Knall, C., Gerwins, P. Johnson, G. L., Worthen, G. S. (1997) Common and distinct intracellular signaling pathways in human neutrophils utilized by platelet activating factor and FMLP. J. Clin. Invest. 99, 975-986.
    • (1997) J. Clin. Invest. , vol.99 , pp. 975-986
    • Nick, J.A.1    Avdi, N.J.2    Young, S.K.3    Knall, C.4    Gerwins, P.5    Johnson, G.L.6    Worthen, G.S.7
  • 41
    • 0029890991 scopus 로고    scopus 로고
    • Activation of the MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide treatment
    • Yu, H., Annette, Y. A., Labiadia, M. E., Sha'afi, R. I., Huang, C. K. (1996) Activation of the MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide treatment. Blood 87, 5287-5296.
    • (1996) Blood , vol.87 , pp. 5287-5296
    • Yu, H.1    Annette, Y.A.2    Labiadia, M.E.3    Sha'afi, R.I.4    Huang, C.K.5
  • 43
    • 0030919654 scopus 로고    scopus 로고
    • 2 by 38-kDa mitogen-activated protein kinase in collagen-stimulated human platelets
    • 2 by 38-kDa mitogen-activated protein kinase in collagen-stimulated human platelets. Eur. J. Biochem. 245, 751-759.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 751-759
    • Borsch-Haubold, A.G.1    Kramer, R.M.2    Watson, S.P.3
  • 44
    • 0029830685 scopus 로고    scopus 로고
    • Inhibition of mitogen-activated protein kinase kinase does not impair primary activation of human platelets
    • Borsch-Haubold, A. G., Kramer, R. M., Watson, S. P. (1996) Inhibition of mitogen-activated protein kinase kinase does not impair primary activation of human platelets. Biochem. J. 318, 207-212.
    • (1996) Biochem. J. , vol.318 , pp. 207-212
    • Borsch-Haubold, A.G.1    Kramer, R.M.2    Watson, S.P.3
  • 46
    • 0028503450 scopus 로고
    • The effects of two anti-CD18 antibodies on antigen-induced airway hyperresponsiveness and leukocyte accumulation in the guinea-pig
    • Milne, A. A. Y., Piper, P. J. (1994) The effects of two anti-CD18 antibodies on antigen-induced airway hyperresponsiveness and leukocyte accumulation in the guinea-pig. Am. J. Respir. Crit. Care Med. 11, 337-343.
    • (1994) Am. J. Respir. Crit. Care Med. , vol.11 , pp. 337-343
    • Milne, A.A.Y.1    Piper, P.J.2
  • 47
    • 0028358370 scopus 로고
    • Role of CD18 in the accumulation of eosinophils and neutrophils and local oedema formation in inflammatory reactions in guinea-pig skin
    • Teixeira, M. M., Reynia, S., Robinson, M., Shock, A., Williams, T. J., Williams, F. M., Rossi, A. G., Hellewell, P. G. (1994) Role of CD18 in the accumulation of eosinophils and neutrophils and local oedema formation in inflammatory reactions in guinea-pig skin. Br. J. Pharmacol. 111, 811-818.
    • (1994) Br. J. Pharmacol. , vol.111 , pp. 811-818
    • Teixeira, M.M.1    Reynia, S.2    Robinson, M.3    Shock, A.4    Williams, T.J.5    Williams, F.M.6    Rossi, A.G.7    Hellewell, P.G.8
  • 48
    • 0028953395 scopus 로고
    • Lung eosinophilia is dependent on IL-5, and the adhesion molecules CD18 and VLA-4 in a guinea-pig model
    • Das, A. M., Williams, T. J., Lobb, R. R., Noursshargh, S. (1995) Lung eosinophilia is dependent on IL-5, and the adhesion molecules CD18 and VLA-4 in a guinea-pig model. Immunol. 84, 41-46.
    • (1995) Immunol. , vol.84 , pp. 41-46
    • Das, A.M.1    Williams, T.J.2    Lobb, R.R.3    Noursshargh, S.4
  • 49
    • 0028820650 scopus 로고
    • Mechanisms and pharmacological manipulation of eosinophil accumulation in vivo
    • Teixeira, M. M., Williams, T. J., Hellewell, P. G. (1995) Mechanisms and pharmacological manipulation of eosinophil accumulation in vivo. Trends. Pharmacol. Sci. 16, 418-423.
    • (1995) Trends. Pharmacol. Sci. , vol.16 , pp. 418-423
    • Teixeira, M.M.1    Williams, T.J.2    Hellewell, P.G.3
  • 50
    • 0029888085 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase in neutrophils and enucleate neutrophil cytoplasts: Evidence for regulation of cell-cell adhesion
    • Pillinger, M. H., Feoktistov, A. S., Capodici, C., Solitar, B., Levy, J., Oei, T. T., Philips, M. R. (1996) Mitogen-activated protein kinase in neutrophils and enucleate neutrophil cytoplasts: evidence for regulation of cell-cell adhesion. J. Biol. Chem. 271, 12049-12056.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12049-12056
    • Pillinger, M.H.1    Feoktistov, A.S.2    Capodici, C.3    Solitar, B.4    Levy, J.5    Oei, T.T.6    Philips, M.R.7
  • 51
    • 0024467122 scopus 로고
    • Irreversible inhibition of v-src tyrosine kinase by herbimycin A and its abrogation by sulfhydryl compounds
    • Uehara, Y., Kukazawa, H., Murakami, Y., Mizuno, S. (1989) Irreversible inhibition of v-src tyrosine kinase by herbimycin A and its abrogation by sulfhydryl compounds. Biochem. Biophys. Res. Commun. 163, 803-809.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 803-809
    • Uehara, Y.1    Kukazawa, H.2    Murakami, Y.3    Mizuno, S.4
  • 52
    • 0026003225 scopus 로고
    • Specific inhibition of cytoplasmic protein tyrosine kinases by herbimycin A in vitro
    • Fukazara, H., Li, P. M., Yamamoto, C., Murakami, Y., Mizuno, S., Uehara, Y. (1991) Specific inhibition of cytoplasmic protein tyrosine kinases by herbimycin A in vitro. Biochem. Pharmacol. 42, 1661-1671.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 1661-1671
    • Fukazara, H.1    Li, P.M.2    Yamamoto, C.3    Murakami, Y.4    Mizuno, S.5    Uehara, Y.6
  • 53
    • 0025995324 scopus 로고
    • Long-term potentiation in the hippocampus is blocked by tyrosine kinase inhibitors
    • O'Dell, T. J., Kandel, E. R., Grant, S. G. N. (1991) Long-term potentiation in the hippocampus is blocked by tyrosine kinase inhibitors. Nature 353, 558-560.
    • (1991) Nature , vol.353 , pp. 558-560
    • O'Dell, T.J.1    Kandel, E.R.2    Grant, S.G.N.3
  • 55
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phophatidylinositol 3,4,5-trisphosphate in neutrophil responses
    • Arcano, A., Wymann, M. P. (1993) Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phophatidylinositol 3,4,5-trisphosphate in neutrophil responses. Biochem. J. 296, 297-301.
    • (1993) Biochem. J. , vol.296 , pp. 297-301
    • Arcano, A.1    Wymann, M.P.2
  • 57
  • 58
    • 0029670488 scopus 로고    scopus 로고
    • 2 is required for the formation of interferon-stimulated gene factor three
    • 2 is required for the formation of interferon-stimulated gene factor three. EMBO J. 15, 1566-1571.
    • (1996) EMBO J. , vol.15 , pp. 1566-1571
    • Flati, V.1    Haque, S.J.2    Williams, B.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.