메뉴 건너뛰기




Volumn 181, Issue 9, 2008, Pages 6491-6502

Zinc signals are essential for lipopolysaccharide-induced signal transduction in monocytes

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CHELATING AGENT; CYTOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INSULIN; LIPOPOLYSACCHARIDE; METAL ION; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; SIGNAL PEPTIDE; TUMOR NECROSIS FACTOR ALPHA; ZINC ION; AUTACOID; CALCIUM; DIVALENT CATION; ZINC;

EID: 58749098604     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.181.9.6491     Document Type: Article
Times cited : (239)

References (58)
  • 1
    • 33845617033 scopus 로고    scopus 로고
    • Zinc homeostasis and immunity
    • Rink, L., and H. Haase. 2007. Zinc homeostasis and immunity. Trends Immunol. 28: 1-4.
    • (2007) Trends Immunol. , vol.28 , pp. 1-4
    • Rink, L.1    Haase, H.2
  • 3
    • 2942564045 scopus 로고    scopus 로고
    • Labile zinc and zinc transporter ZnT4 in mast cell granules: Role in regulation of caspase activation and NF-κB translocation
    • Ho, L. H., R. E. Ruffin, C. Murgia, L. Li, S. A. Krilis, and P. D. Zalewski. 2004. Labile zinc and zinc transporter ZnT4 in mast cell granules: role in regulation of caspase activation and NF-κB translocation. J. Immunol. 172: 7750-7760.
    • (2004) J. Immunol. , vol.172 , pp. 7750-7760
    • Ho, L.H.1    Ruffin, R.E.2    Murgia, C.3    Li, L.4    Krilis, S.A.5    Zalewski, P.D.6
  • 7
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L., and K. H. Falchuk. 1993. The biochemical basis of zinc physiology. Physiol. Rev. 73: 79-118.
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 8
    • 0035696301 scopus 로고    scopus 로고
    • Functions of zinc in signaling, proliferation and differentiation of mammalian cells
    • DOI 10.1023/A:1012905406548
    • Beyersmann, D., and H. Haase. 2001. Functions of zinc in signaling, proliferation and differentiation of mammalian cells. Biometals 14: 331-341. (Pubitemid 34066636)
    • (2001) BioMetals , vol.14 , Issue.3-4 , pp. 331-341
    • Beyersmann, D.1    Haase, H.2
  • 9
    • 34248646765 scopus 로고    scopus 로고
    • Signal transduction in monocytes: The role of zinc ions
    • DOI 10.1007/s10534-006-9029-8, Biometals: function and transport in bacteria, fungi, and humans
    • Haase, H., and L. Rink. 2007. Signal transduction in monocytes: the role of zinc ions. Biometals 20: 579-585. (Pubitemid 46776557)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 579-585
    • Haase, H.1    Rink, L.2
  • 10
    • 0037064536 scopus 로고    scopus 로고
    • Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family
    • Martin, M. U., and H. Wesche. 2002. Summary and comparison of the signaling mechanisms of the Toll/interleukin-1 receptor family. Biochim. Biophys. Acta 1592: 265-280.
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 265-280
    • Martin, M.U.1    Wesche, H.2
  • 11
    • 0028364801 scopus 로고
    • Lipopolysaccharide-induced cytokine production in human monocytes: Role of tyrosine phosphorylation in transmembrane signal transduction
    • Beaty, C. D., T. L. Franklin, Y. Uehara, and C. B. Wilson. 1994. Lipopolysaccharide-induced cytokine production in human monocytes: role of tyrosine phosphorylation in transmembrane signal transduction. Eur. J. Immunol. 24: 1278-1284.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1278-1284
    • Beaty, C.D.1    Franklin, T.L.2    Uehara, Y.3    Wilson, C.B.4
  • 12
    • 0030070975 scopus 로고    scopus 로고
    • lyn and phosphatidylinositol 3-kinase in human monocytes
    • lyn and phosphatidylinositol 3-kinase in human monocytes. J. Immunol. 156: 1157-1165.
    • (1996) J. Immunol. , vol.156 , pp. 1157-1165
    • Herrera-Velit, P.1    Reiner, N.E.2
  • 13
    • 0028129888 scopus 로고
    • CD14-dependent activation of protein kinase C and mitogen-activated protein kinases (p42 and p44) in human monocytes treated with bacterial lipopolysaccharide
    • Liu, M. K., P. Herrera-Velit, R. W. Brownsey, and N. E. Reiner. 1994. CD14-dependent activation of protein kinase C and mitogen-activated protein kinases (p42 and p44) in human monocytes treated with bacterial lipopolysaccharide. J. Immunol. 153: 2642-2652.
    • (1994) J. Immunol. , vol.153 , pp. 2642-2652
    • Liu, M.K.1    Herrera-Velit, P.2    Brownsey, R.W.3    Reiner, N.E.4
  • 14
    • 0028068084 scopus 로고
    • Involvement of protein kinase C and protein tyrosine kinase in lipopolysaccharide-induced TNF-α and IL-1β production by human monocytes
    • Shapira, L., S. Takashiba, C. Champagne, S. Amar, and T. E. Van Dyke. 1994. Involvement of protein kinase C and protein tyrosine kinase in lipopolysaccharide-induced TNF-α and IL-1β production by human monocytes. J. Immunol. 153: 1818-1824. (Pubitemid 24251127)
    • (1994) Journal of Immunology , vol.153 , Issue.4 , pp. 1818-1824
    • Shapira, L.1    Takashiba, S.2    Champagne, C.3    Amar, S.4    Van Dyke, T.E.5
  • 16
    • 1942501608 scopus 로고    scopus 로고
    • Abrogation of Nuclear Factor-κB Activation Is Involved in Zinc Inhibition of Lipopolysaccharide-Induced Tumor Necrosis Factor-α Production and Liver Injury
    • Zhou, Z., L. Wang, Z. Song, J. T. Saari, C. J. McClain, and Y. J. Kang. 2004. Abrogation of nuclear factor-κB activation is involved in zinc inhibition of lipopolysaccharide-induced tumor necrosis factor-α production and liver injury. Am. J. Pathol. 164: 1547-1556. (Pubitemid 38529757)
    • (2004) American Journal of Pathology , vol.164 , Issue.5 , pp. 1547-1556
    • Zhou, Z.1    Wang, L.2    Song, Z.3    Saari, J.T.4    McClain, C.J.5    Kang, Y.J.6
  • 17
    • 25444477239 scopus 로고    scopus 로고
    • Zinc-mediated inhibition of cyclic nucleotide phosphodiesterase activity and expression suppresses TNF-α and IL-1β production in monocytes by elevation of guanosine 3′,5′-cyclic monophosphate
    • von Bulow, V., L. Rink, and H. Haase. 2005. Zinc-mediated inhibition of cyclic nucleotide phosphodiesterase activity and expression suppresses TNF-α and IL-1β production in monocytes by elevation of guanosine 3′,5′-cyclic monophosphate. J. Immunol. 175: 4697-4705.
    • (2005) J. Immunol. , vol.175 , pp. 4697-4705
    • Von Bulow, V.1    Rink, L.2    Haase, H.3
  • 18
    • 35748954915 scopus 로고    scopus 로고
    • Zinc-dependent suppression of TNF-α production is mediated by protein kinase A-induced inhibition of Raf-1, IκB kinase α, and NF-κB
    • von Bulow, V., S. Dubben, G. Engelhardt, S. Hebel, B. Plumakers, H. Heine, L. Rink, and H. Haase. 2007. Zinc-dependent suppression of TNF-α production is mediated by protein kinase A-induced inhibition of Raf-1, IκB kinase α, and NF-κB. J. Immunol. 179: 4180-4186.
    • (2007) J. Immunol. , vol.179 , pp. 4180-4186
    • Von Bulow, V.1    Dubben, S.2    Engelhardt, G.3    Hebel, S.4    Plumakers, B.5    Heine, H.6    Rink, L.7    Haase, H.8
  • 19
    • 0028325882 scopus 로고
    • Induction of cytokines by zinc ions in human peripheral blood mononuclear cells and separated monocytes
    • Driessen, C., K. Hirv, L. Rink, and H. Kirchner. 1994. Induction of cytokines by zinc ions in human peripheral blood mononuclear cells and separated monocytes. Lymphokine Cytokine Res. 13: 15-20. (Pubitemid 24080650)
    • (1994) Lymphokine and Cytokine Research , vol.13 , Issue.1 , pp. 15-20
    • Driessen, C.1    Hirv, K.2    Rink, L.3    Kirchner, H.4
  • 20
    • 0030268035 scopus 로고    scopus 로고
    • Stimulation of human peripheral blood mononuclear cells by zinc and related cations
    • DOI 10.1006/cyto.1996.0102
    • Wellinghausen, N., C. Driessen, and L. Rink. 1996. Stimulation of human peripheral blood mononuclear cells by zinc and related cations. Cytokine 8: 767-771. (Pubitemid 27023295)
    • (1996) Cytokine , vol.8 , Issue.10 , pp. 767-771
    • Wellinghausen, N.1    Driessen, C.2    Rink, L.3
  • 21
    • 33646126495 scopus 로고    scopus 로고
    • Flow cytometric measurement of labile zinc in peripheral blood mononuclear cells
    • Haase, H., S. Hebel, G. Engelhardt, and L. Rink. 2006. Flow cytometric measurement of labile zinc in peripheral blood mononuclear cells. Anal. Biochem. 352: 222-230.
    • (2006) Anal. Biochem. , vol.352 , pp. 222-230
    • Haase, H.1    Hebel, S.2    Engelhardt, G.3    Rink, L.4
  • 22
    • 0344010194 scopus 로고    scopus 로고
    • Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling
    • DOI 10.1016/S0014-4827(03)00406-3
    • Haase, H., and W. Maret. 2003. Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling. Exp. Cell Res. 291: 289-298. (Pubitemid 37485719)
    • (2003) Experimental Cell Research , vol.291 , Issue.2 , pp. 289-298
    • Haase, H.1    Maret, W.2
  • 23
    • 0027276945 scopus 로고
    • A standardized approach to PCR-based semiquantitation of multiple cytokine gene transcripts from small cell samples
    • Lagoo-Deenadayalan, S., A. S. Lagoo, W. H. Barber, and K. J. Hardy. 1993. A standardized approach to PCR-based semiquantitation of multiple cytokine gene transcripts from small cell samples. Lymphokine Cytokine Res. 12: 59-67. (Pubitemid 23141776)
    • (1993) Lymphokine and Cytokine Research , vol.12 , Issue.2 , pp. 59-67
    • Lagoo-Deenadayalan, S.1    Lagoo, A.S.2    Barber, W.H.3    Hardy, K.J.4
  • 24
    • 0021681058 scopus 로고
    • Human tumour necrosis factor: Precursor structure, expression and homology to lymphotoxin
    • DOI 10.1038/312724a0
    • Pennica, D., G. E. Nedwin, J. S. Hayflick, P. H. Seeburg, R. Derynck, M. A. Palladino, W. J. Kohr, B. B. Aggarwal, and D. V. Goeddel. 1984. Human tumour necrosis factor: precursor structure, expression and homology to lymphotoxin. Nature 312: 724-729. (Pubitemid 15195918)
    • (1984) Nature , vol.312 , Issue.5996 , pp. 724-729
    • Pennica, D.1    Nedwin, G.E.2    Hayflick, J.S.3
  • 25
    • 0037028562 scopus 로고    scopus 로고
    • Detection and imaging of zinc secretion from pancreatic beta-cells using a new fluorescent zinc indicator
    • Gee, K. R., Z. L. Zhou, W. J. Qian, and R. Kennedy. 2002. Detection and imaging of zinc secretion from pancreatic beta-cells using a new fluorescent zinc indicator. J. Am. Chem. Soc. 124: 776-778.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 776-778
    • Gee, K.R.1    Zhou, Z.L.2    Qian, W.J.3    Kennedy, R.4
  • 26
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S., and K. Takeda. 2004. Toll-like receptor signalling. Nat. Rev. Immunol. 4: 499-511.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 27
    • 0037113925 scopus 로고    scopus 로고
    • Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen
    • DOI 10.1074/jbc.M205634200
    • Korichneva, I., B. Hoyos, R. Chua, E. Levi, and U. Hammerling. 2002. Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen. J. Biol. Chem. 277: 44327-44331. (Pubitemid 36157867)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 44327-44331
    • Korichneva, I.1    Hoyos, B.2    Chua, R.3    Levi, E.4    Hammerling, U.5
  • 28
    • 0031714877 scopus 로고    scopus 로고
    • SB202190, a selective inhibitor of p38 mitogen-activated protein kinase, is a powerful regulator of LPS-induced mRNAs in monocytes
    • Manthey, C. L., S. W. Wang, S. D. Kinney, and Z. Yao. 1998. SB202190, a selective inhibitor of p38 mitogen-activated protein kinase, is a powerful regulator of LPS-induced mRNAs in monocytes. J. Leukocyte Biol. 64: 409-417.
    • (1998) J. Leukocyte Biol. , vol.64 , pp. 409-417
    • Manthey, C.L.1    Wang, S.W.2    Kinney, S.D.3    Yao, Z.4
  • 30
    • 0017283573 scopus 로고
    • Inhibition of lethality in endotoxin-challenged mice treated with zinc chloride
    • Snyder, S. L., and R. I. Walker. 1976. Inhibition of lethality in endotoxin-challenged mice treated with zinc chloride. Infect. Immun. 13: 998-1000.
    • (1976) Infect. Immun. , vol.13 , pp. 998-1000
    • Snyder, S.L.1    Walker, R.I.2
  • 31
    • 0030266626 scopus 로고    scopus 로고
    • Zinc Enhances Lipopolysaccharide-Induced Monokine Secretion by Alteration of Fluidity State of Lipopolysaccharide
    • Wellinghausen, N., A. B. Schromm, U. Seydel, K. Brandenburg, J. Luhm, H. Kirchner, and L. Rink. 1996. Zinc enhances lipopolysaccharide-induced monokine secretion by alteration of fluidity state of lipopolysaccharide. J. Immunol. 157: 3139-3145. (Pubitemid 126450075)
    • (1996) Journal of Immunology , vol.157 , Issue.7 , pp. 3139-3145
    • Wellinghausen, N.1    Schromm, A.B.2    Seydel, U.3    Brandenburg, K.4    Luhm, J.5    Kirchner, H.6    Rink, L.7
  • 32
    • 33746929895 scopus 로고    scopus 로고
    • Zinc transporters and the cellular trafficking of zinc
    • Eide, D. J. 2006. Zinc transporters and the cellular trafficking of zinc. Biochim. Biophys. Acta 1763: 711-722.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 711-722
    • Eide, D.J.1
  • 33
    • 33747723380 scopus 로고    scopus 로고
    • Mammalian zinc transport, trafficking, and signals
    • Cousins, R. J., J. P. Liuzzi, and L. A. Lichten. 2006. Mammalian zinc transport, trafficking, and signals. J. Biol. Chem. 281: 24085-24089.
    • (2006) J. Biol. Chem. , vol.281 , pp. 24085-24089
    • Cousins, R.J.1    Liuzzi, J.P.2    Lichten, L.A.3
  • 35
    • 0028198581 scopus 로고
    • Activation of human monocytes with lipopolysaccharide induces metallothionein expression and is diminished by zinc
    • Leibbrandt, M. E., and J. Koropatnick. 1994. Activation of human monocytes with lipopolysaccharide induces metallothionein expression and is diminished by zinc. Toxicol. Appl. Pharmacol. 124: 72-81.
    • (1994) Toxicol. Appl. Pharmacol. , vol.124 , pp. 72-81
    • Leibbrandt, M.E.1    Koropatnick, J.2
  • 37
    • 33751223540 scopus 로고    scopus 로고
    • Zinc-buffering capacity of a eukaryotic cell at physiological pZn
    • DOI 10.1007/s00775-006-0150-5
    • Krezel, A., and W. Maret. 2006. Zinc-buffering capacity of a eukaryotic cell at physiological pZn. J. Biol. Inorg. Chem. 11: 1049-1062. (Pubitemid 44786393)
    • (2006) Journal of Biological Inorganic Chemistry , vol.11 , Issue.8 , pp. 1049-1062
    • Krezel, A.1    Maret, W.2
  • 38
    • 0027501386 scopus 로고
    • Correlation of apoptosis with change in intracellular labile Zn(II) using zinquin ((2-methyl-8-p-toluenesulphonamido-6-quinolyloxy)acetic acid), a new specific fluorescent probe for Zn(II)
    • Zalewski, P. D., I. J. Forbes, and W. H. Betts. 1993. Correlation of apoptosis with change in intracellular labile Zn(II) using zinquin ((2-methyl-8-p-toluenesulphonamido-6-quinolyloxy)acetic acid), a new specific fluorescent probe for Zn(II). Biochem. J. 296: 403-408.
    • (1993) Biochem. J. , vol.296 , pp. 403-408
    • Zalewski, P.D.1    Forbes, I.J.2    Betts, W.H.3
  • 39
    • 0036622949 scopus 로고    scopus 로고
    • Post-transcriptional regulation of TNF-α during in vitro differentiation of human monocytes/macrophages in primary culture
    • MacKenzie, S., N. Fernandez-Troy, and E. Espel. 2002. Post-transcriptional regulation of TNF-α during in vitro differentiation of human monocytes/macrophages in primary culture. J. Leukocyte Biol. 71: 1026-1032.
    • (2002) J. Leukocyte Biol. , vol.71 , pp. 1026-1032
    • MacKenzie, S.1    Fernandez-Troy, N.2    Espel, E.3
  • 40
    • 0032806197 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced tumor necrosis factor alpha production by human monocytes involves the Raf-1/MEK1-MEK2/ERK1-ERK2 pathway
    • van der Bruggen, T., S. Nijenhuis, E. van Raaij, J. Verhoef, and B. S. van Asbeck. 1999. Lipopolysaccharide-induced tumor necrosis factor α production by human monocytes involves the raf-1/MEK1-MEK2/ERK1-ERK2 pathway. Infect. Immun. 67: 3824-3829. (Pubitemid 29356998)
    • (1999) Infection and Immunity , vol.67 , Issue.8 , pp. 3824-3829
    • Van Der Bruggen, T.1    Nijenhuis, S.2    Van Raaij, E.3    Verhoef, J.4    Van Asbeck, B.S.5
  • 41
    • 0034644837 scopus 로고    scopus 로고
    • Regulation of tumour necrosis factor α mRNA stability by the mitogen-activated protein kinase p38 signalling cascade
    • DOI 10.1016/S0014-5793(00)02084-6, PII S0014579300020846
    • Brook, M., G. Sully, A. R. Clark, and J. Saklatvala. 2000. Regulation of tumour necrosis factor α mRNA stability by the mitogen-activated protein kinase p38 signalling cascade. FEBS Lett. 483: 57-61. (Pubitemid 30738608)
    • (2000) FEBS Letters , vol.483 , Issue.1 , pp. 57-61
    • Brook, M.1    Sully, G.2    Clark, A.R.3    Saklatvala, J.4
  • 45
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen, F. E., D. B. Huang, Y. Q. Chen, and G. Ghosh. 1998. Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature 391: 410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 47
    • 0033193247 scopus 로고    scopus 로고
    • Tyrosine phosphatases as targets in metal-induced signaling in human airway epithelial cells
    • Samet, J. M., R. Silbajoris, W. Wu, and L. M. Graves. 1999. Tyrosine phosphatases as targets in metal-induced signaling in human airway epithelial cells. Am. J. Respir. Cell Mol. Biol. 21: 357-364.
    • (1999) Am. J. Respir. Cell Mol. Biol. , vol.21 , pp. 357-364
    • Samet, J.M.1    Silbajoris, R.2    Wu, W.3    Graves, L.M.4
  • 48
    • 24344488003 scopus 로고    scopus 로고
    • Fluctuations of cellular, available zinc modulate insulin signaling via inhibition of protein tyrosine phosphatases
    • DOI 10.1016/j.jtemb.2005.02.004, PII S0946672X05000131
    • Haase, H., and W. Maret. 2005. Fluctuations of cellular, available zinc modulate insulin signaling via inhibition of protein tyrosine phosphatases. J. Trace Elem. Med. Biol. 19: 37-42. (Pubitemid 41253915)
    • (2005) Journal of Trace Elements in Medicine and Biology , vol.19 , Issue.1 SPEC. ISSUE , pp. 37-42
    • Haase, H.1    Maret, W.2
  • 50
    • 0027144465 scopus 로고
    • Protein tyrosine kinase activation is required for lipopolysaccharide induction of cytokines in human blood monocytes
    • Geng, Y., B. Zhang, and M. Lotz. 1993. Protein tyrosine kinase activation is required for lipopolysaccharide induction of cytokines in human blood monocytes. J. Immunol. 151: 6692-6700. (Pubitemid 24001043)
    • (1993) Journal of Immunology , vol.151 , Issue.12 , pp. 6692-6700
    • Geng, Y.1    Zhang, B.2    Lotz, M.3
  • 51
    • 0037378954 scopus 로고    scopus 로고
    • Involvement of protein tyrosine kinase in Toll-like receptor 4-mediated NF-κB activation in human peripheral blood monocytes
    • Chen, L. Y., B. L. Zuraw, M. Zhao, F. T. Liu, S. Huang, and Z. K. Pan. 2003. Involvement of protein tyrosine kinase in Toll-like receptor 4-mediated NF-κB activation in human peripheral blood monocytes. Am. J. Physiol. 284: L607-L613.
    • (2003) Am. J. Physiol. , vol.284
    • Chen, L.Y.1    Zuraw, B.L.2    Zhao, M.3    Liu, F.T.4    Huang, S.5    Pan, Z.K.6
  • 52
    • 0037352702 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4-mediated cytokine expression in mouse macrophages
    • DOI 10.1002/eji.200323376
    • Ojaniemi, M., V. Glumoff, K. Harju, M. Liljeroos, K. Vuori, and M. Hallman. 2003. Phosphatidylinositol 3-kinase is involved in Toll-like receptor 4-mediated cytokine expression in mouse macrophages. Eur. J. Immunol. 33: 597-605. (Pubitemid 36367663)
    • (2003) European Journal of Immunology , vol.33 , Issue.3 , pp. 597-605
    • Ojaniemi, M.1    Glumoff, V.2    Harju, K.3    Liljeroos, M.4    Vuori, K.5    Hallman, M.6
  • 57
    • 31144452241 scopus 로고    scopus 로고
    • Essential role of MAPK phosphatase-1 in the negative control of innate immune responses
    • Salojin, K. V., I. B. Owusu, K. A. Millerchip, M. Potter, K. A. Platt, and T. Oravecz. 2006. Essential role of MAPK phosphatase-1 in the negative control of innate immune responses. J. Immunol. 176: 1899-1907. (Pubitemid 43134335)
    • (2006) Journal of Immunology , vol.176 , Issue.3 , pp. 1899-1907
    • Salojin, K.V.1    Owusu, I.B.2    Millerchip, K.A.3    Potter, M.4    Platt, K.A.5    Oravecz, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.