메뉴 건너뛰기




Volumn 162, Issue 11, 1999, Pages 6776-6783

Negative regulation by protein tyrosine phosphatase of IFN-γ-dependent expression of inducible nitric oxide synthase

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; PROTEIN TYROSINE PHOSPHATASE; TRANSCRIPTION FACTOR;

EID: 0033153484     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (28)

References (52)
  • 1
    • 0031456352 scopus 로고    scopus 로고
    • Elimination, blocking, and activation of macrophages: Three of a kind?
    • van Rooijen, N., and A. Sanders. 1997. Elimination, blocking, and activation of macrophages: three of a kind? J. Leukocyte Biol. 62:702.
    • (1997) J. Leukocyte Biol. , vol.62 , pp. 702
    • Van Rooijen, N.A.1    Sanders, A.2
  • 2
    • 0028347865 scopus 로고
    • Macrophage activation revisited
    • Celada, A., and C. Nathan. 1994. Macrophage activation revisited. Immunol. Today 15:100.
    • (1994) Immunol. Today , vol.15 , pp. 100
    • Celada, A.1    Nathan, C.2
  • 3
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan, C. 1992. Nitric oxide as a secretory product of mammalian cells. FASEB J. 6:3051.
    • (1992) FASEB J. , vol.6 , pp. 3051
    • Nathan, C.1
  • 4
    • 0027411525 scopus 로고
    • The molecular cell biology of IFN-γ and its receptor
    • Farrar, M. A., and R. D. Schreiber. 1993. The molecular cell biology of IFN-γ and its receptor. Annu. Rev. Immunol. 11:571.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 571
    • Farrar, M.A.1    Schreiber, R.D.2
  • 5
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett, B. S., and E. R. Stadtman. 1997. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272:20313.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313
    • Berlett, B.S.1    Stadtman, E.R.2
  • 6
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell, J. E., Jr., I. M. Kerr, and G. R. Stark. 1994. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264:1415.
    • (1994) Science , vol.264 , pp. 1415
    • Darnell J.E., Jr.1    Kerr, I.M.2    Stark, G.R.3
  • 7
    • 0029101772 scopus 로고
    • Transcriptional regulation of endothelial cell adhesion molecules, NF-κB and cytokine-inducible enhancers
    • Collins, T., M. A. Read, A. S. Neish, M. Z. Whitley, D. Thanos, and T. Maniatis. 1995. Transcriptional regulation of endothelial cell adhesion molecules, NF-κB and cytokine-inducible enhancers. FASEB J. 9:899.
    • (1995) FASEB J. , vol.9 , pp. 899
    • Collins, T.1    Read, M.A.2    Neish, A.S.3    Whitley, M.Z.4    Thanos, D.5    Maniatis, T.6
  • 8
    • 0030936627 scopus 로고    scopus 로고
    • GAS elements: A few nucleotides with a major impact on cytokine-induced gene expression
    • Decker, T., P. Kovarik, and A. Meinke. 1997. GAS elements: a few nucleotides with a major impact on cytokine-induced gene expression. J. Interferon Cylokine Res. 17:121.
    • (1997) J. Interferon Cylokine Res. , vol.17 , pp. 121
    • Decker, T.1    Kovarik, P.2    Meinke, A.3
  • 9
    • 0028791664 scopus 로고
    • Roles of protein-tyrosine phosphatases in Stat 1 α-mediated cell signaling
    • Haque, S. J., V. Flati, A. Deb, and B. R. Williams. 1995. Roles of protein-tyrosine phosphatases in Stat 1 α-mediated cell signaling. J. Biol. Chem. 270:25709.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25709
    • Haque, S.J.1    Flati, V.2    Deb, A.3    Williams, B.R.4
  • 10
    • 0031012543 scopus 로고    scopus 로고
    • Peroxovanadate induces tyrosine phosphorylation of multiple signaling proteins in mouse liver and kidney
    • Ruff, S. J., K. Chen, and S. Cohen. 1997. Peroxovanadate induces tyrosine phosphorylation of multiple signaling proteins in mouse liver and kidney. J. Biol. Chem. 272:1263.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1263
    • Ruff, S.J.1    Chen, K.2    Cohen, S.3
  • 12
    • 0028092958 scopus 로고
    • Nitric oxide synthases: Roles, tolls, and controls
    • Nathan, C., and Q.-w. Xie. 1994. Nitric oxide synthases: roles, tolls, and controls. Cell 78:915.
    • (1994) Cell , vol.78 , pp. 915
    • Nathan, C.1    Xie, Q.-W.2
  • 13
    • 0028270719 scopus 로고
    • Regulation of biosynthesis of nitric oxide
    • Nathan, C., and Q.-w. Xie. 1994. Regulation of biosynthesis of nitric oxide. J. Biol. Chem. 269:13725.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13725
    • Nathan, C.1    Xie, Q.-W.2
  • 15
    • 0031022516 scopus 로고    scopus 로고
    • An IFN-γ-activated site (GAS) is necessary for full expression of the mouse iNOS gene in response to IFN-γ and lipopolysaccharide
    • Gao, J., D. C. Morrison, T. J. Parmely, S. W. Russell, and W. J. Murphy. 1997. An IFN-γ-activated site (GAS) is necessary for full expression of the mouse iNOS gene in response to IFN-γ and lipopolysaccharide. J. Biol. Chem. 272:1226.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1226
    • Gao, J.1    Morrison, D.C.2    Parmely, T.J.3    Russell, S.W.4    Murphy, W.J.5
  • 16
    • 0028106830 scopus 로고
    • Role of interferon regulatory factor 1 in induction of nitric oxide synthase
    • Martin, E., C. Nathan, and Q.-w. Xie. 1994. Role of interferon regulatory factor 1 in induction of nitric oxide synthase. J. Exp. Med. 180:977.
    • (1994) J. Exp. Med. , vol.180 , pp. 977
    • Martin, E.1    Nathan, C.2    Xie, Q.-W.3
  • 18
    • 0027255749 scopus 로고
    • Promoter of the mouse gene encoding calcium-independent nitric oxide synthase confers inducibility by interferon-γ and bacterial lipopolysaccharide
    • Xie, Q.-w., R. Whisnant, and C. Nathan. 1993. Promoter of the mouse gene encoding calcium-independent nitric oxide synthase confers inducibility by interferon-γ and bacterial lipopolysaccharide. J. Exp. Med. 177:1779.
    • (1993) J. Exp. Med. , vol.177 , pp. 1779
    • Xie, Q.-W.1    Whisnant, R.2    Nathan, C.3
  • 19
    • 0029997562 scopus 로고    scopus 로고
    • In vivo foot-printing of the mouse inducible nitric oxide synthase gene: Inducible protein occupation of numerous sites including Oct and NF-IL6
    • Goldring, C. E., S. Reveneau, M. Algarte, and J. F. Jeannin. 1996. In vivo foot-printing of the mouse inducible nitric oxide synthase gene: inducible protein occupation of numerous sites including Oct and NF-IL6. Nucleic Acids Res. 24:1682.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1682
    • Goldring, C.E.1    Reveneau, S.2    Algarte, M.3    Jeannin, J.F.4
  • 20
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle, P. A., and T. Henkel. 1994. Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12:141.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141
    • Baeuerle, P.A.1    Henkel, T.2
  • 21
    • 0028986193 scopus 로고
    • NF-κB: A lesson in family values
    • Thanos, D., and T. Maniatis. 1995. NF-κB: a lesson in family values. Cell 80:529.
    • (1995) Cell , vol.80 , pp. 529
    • Thanos, D.1    Maniatis, T.2
  • 22
    • 0030823758 scopus 로고    scopus 로고
    • Rapid up-regulation of IκBβ and abrogation of NF-κB activity in peritoneal macrophages stimulated with lipopolysaccharide
    • Velasco, M., M. J. M. Diaz-Guerra, P. Maitin-Sanz, A. Alvarez, and L. Boscá. 1997. Rapid up-regulation of IκBβ and abrogation of NF-κB activity in peritoneal macrophages stimulated with lipopolysaccharide. J. Biol. Chem. 272:23025.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23025
    • Velasco, M.1    Diaz-Guerra, M.J.M.2    Maitin-Sanz, P.3    Alvarez, A.4    Boscá, L.5
  • 23
    • 0030611595 scopus 로고    scopus 로고
    • IκB kinase-K: NF-κB activation and complex formation with IκB kinase-α and NIK
    • Woronicz, J. D., X. Gao, Z. Cao, M. Rothe, and D. V. Goeddel. 1997. IκB kinase-K: NF-κB activation and complex formation with IκB kinase-α and NIK. Science 278:866.
    • (1997) Science , vol.278 , pp. 866
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 26
    • 0028032360 scopus 로고
    • Hypoxic activation of nuclear factor-κB is mediated by a Ras and Raf signaling pathway and does not involve MAP kinase (ERK1 or ERK2)
    • Koong, A. C., E. Y. Chen, N. F. Mivechi, N. C. Denko, P. Stambrook, and A. J. Giaccia. 1994. Hypoxic activation of nuclear factor-κB is mediated by a Ras and Raf signaling pathway and does not involve MAP kinase (ERK1 or ERK2). Cancer Res. 54:5273.
    • (1994) Cancer Res. , vol.54 , pp. 5273
    • Koong, A.C.1    Chen, E.Y.2    Mivechi, N.F.3    Denko, N.C.4    Stambrook, P.5    Giaccia, A.J.6
  • 27
    • 0029860947 scopus 로고    scopus 로고
    • Evidence for common mechanisms in the transcriptional control of type II nitric oxide synthase in isolated hepatocytes: Requirement of NF-κB activation after stimulation with bacterial cell wall products and phorbol esters
    • Diaz-Guerra, M. J. M., M. Velasco, P. Maitin-Sanz, and L. Bosca. 1996. Evidence for common mechanisms in the transcriptional control of type II nitric oxide synthase in isolated hepatocytes: requirement of NF-κB activation after stimulation with bacterial cell wall products and phorbol esters J. Biol. Chem. 271:30114.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30114
    • Diaz-Guerra, M.J.M.1    Velasco, M.2    Maitin-Sanz, P.3    Bosca, L.4
  • 28
    • 0028850008 scopus 로고
    • The cytokine responsive vascular smooth muscle cell enhancer of inducible nitric oxide synthase: Activation by nuclear factor-κB
    • Spink, J., J. Cohen, and T. J. Evans. 1995. The cytokine responsive vascular smooth muscle cell enhancer of inducible nitric oxide synthase: activation by nuclear factor-κB. J. Biol. Chem. 270:29541.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29541
    • Spink, J.1    Cohen, J.2    Evans, T.J.3
  • 29
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with "mini-extracts" prepared from a small number of cells
    • Schreiber, E., P. Matthias, M. M. Muller, and W. Schaffner. 1989. Rapid detection of octamer binding proteins with "mini-extracts" prepared from a small number of cells. Nucleic Acids Res. 17:6419.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 30
    • 0027496114 scopus 로고
    • A common nuclear signal transduction pathway activated by growth factor and cytokine receptors
    • Sadowski, H. B., K. Shuai, J. E. Damell, Jr., and M. Z. Gilman. 1993. A common nuclear signal transduction pathway activated by growth factor and cytokine receptors. Science 261:1739.
    • (1993) Science , vol.261 , pp. 1739
    • Sadowski, H.B.1    Shuai, K.2    Damell J.E., Jr.3    Gilman, M.Z.4
  • 32
    • 0017762129 scopus 로고
    • Antibody-dependent killing of erythrocyte and tumor targets by macrophage-related cell lines: Enrichment by PPD and LPS
    • Ralph, P., and I. Nakoinz. 1977. Antibody-dependent killing of erythrocyte and tumor targets by macrophage-related cell lines: enrichment by PPD and LPS. J. Immunol. 119:950.
    • (1977) J. Immunol. , vol.119 , pp. 950
    • Ralph, P.1    Nakoinz, I.2
  • 33
    • 0018180802 scopus 로고
    • Functional macrophage cell lines transformed by Abelson leukemia virus
    • Raschke, W. C., S. Baird, P. Ralph, and I. Nakoinz. 1978. Functional macrophage cell lines transformed by Abelson leukemia virus. Cell 15:261.
    • (1978) Cell , vol.15 , pp. 261
    • Raschke, W.C.1    Baird, S.2    Ralph, P.3    Nakoinz, I.4
  • 34
    • 0027459588 scopus 로고
    • Expression of the nitric oxide synthase gene in mouse mac-rophages activated for tumor cell killing: Molecular basis for the synergy between interferon-γ and lipopolysaccharide
    • Lorsbach, R. B., W. J. Murphy, C. J. Lowenstein, S. H. Snyder, and S. W. Russell. 1993. Expression of the nitric oxide synthase gene in mouse mac-rophages activated for tumor cell killing: molecular basis for the synergy between interferon-γ and lipopolysaccharide. J. Biol. Chem. 268:1908.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1908
    • Lorsbach, R.B.1    Murphy, W.J.2    Lowenstein, C.J.3    Snyder, S.H.4    Russell, S.W.5
  • 35
    • 0031886864 scopus 로고    scopus 로고
    • The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation
    • Ricote, M., A. C. Li, T. M. Willson, C. J. Kelly, and C. K. Glass. 1998. The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation. Nature 391:79.
    • (1998) Nature , vol.391 , pp. 79
    • Ricote, M.1    Li, A.C.2    Willson, T.M.3    Kelly, C.J.4    Glass, C.K.5
  • 36
    • 0242613613 scopus 로고    scopus 로고
    • Triggering of peritoneal macrophages with IFN-α/β attenuates the expression of inducible nitric oxide synthase through a decrease in NF-κB activation
    • Lopez-Collazo, E., S. Hortelano, A. Rojas, and L. Bosca. 1998. Triggering of peritoneal macrophages with IFN-α/β attenuates the expression of inducible nitric oxide synthase through a decrease in NF-κB activation. J. Immunol. 160:2889.
    • (1998) J. Immunol. , vol.160 , pp. 2889
    • Lopez-Collazo, E.1    Hortelano, S.2    Rojas, A.3    Bosca, L.4
  • 37
    • 0029912242 scopus 로고    scopus 로고
    • Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-κB
    • Griscavage, J. M., S. Wilk, and L. J. Ignarro. 1996. Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-κB. Proc. Natl. Acad. Sci. USA 93:3308.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3308
    • Griscavage, J.M.1    Wilk, S.2    Ignarro, L.J.3
  • 38
    • 0029956644 scopus 로고    scopus 로고
    • Site-specific tyrosine phosphorylation of IκBα negatively regulates its inducible phosphorylation and degradation
    • Singh, S., B. G. Damay, and B. B. Aggarwal. 1996. Site-specific tyrosine phosphorylation of IκBα negatively regulates its inducible phosphorylation and degradation. J. Biol. Chem. 271:31049.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31049
    • Singh, S.1    Damay, B.G.2    Aggarwal, B.B.3
  • 39
    • 0032493859 scopus 로고    scopus 로고
    • Switching signals on or off by receptor dimerization
    • Weiss, A., and J. Schlessinger. 1998. Switching signals on or off by receptor dimerization. Cell 94:277.
    • (1998) Cell , vol.94 , pp. 277
    • Weiss, A.1    Schlessinger, J.2
  • 40
    • 0031456722 scopus 로고    scopus 로고
    • Bacterial LPS and IFN-γ trigger the tyrosine phosphorylation of vav in macrophages: Evidence for involvement of the hck tyrosine kinase
    • English, B. K., S. L. Orlicek, Z. Mei, and E. A. Meals. 1997. Bacterial LPS and IFN-γ trigger the tyrosine phosphorylation of vav in macrophages: evidence for involvement of the hck tyrosine kinase. J. Leukocyte Biol. 62:859.
    • (1997) J. Leukocyte Biol. , vol.62 , pp. 859
    • English, B.K.1    Orlicek, S.L.2    Mei, Z.3    Meals, E.A.4
  • 41
    • 0029952227 scopus 로고    scopus 로고
    • Hyaluronan fragments activate an NF-κB/I-κBα autoregulatory loop in murine macrophages
    • Noble, P.W., C. M. McKee, M. Cowman, and H. S. Shin. 1996. Hyaluronan fragments activate an NF-κB/I-κBα autoregulatory loop in murine macrophages. J. Exf. Med. 183:2373.
    • (1996) J. Exf. Med. , vol.183 , pp. 2373
    • Noble, P.W.1    McKee, C.M.2    Cowman, M.3    Shin, H.S.4
  • 42
    • 0030918939 scopus 로고    scopus 로고
    • Stimulation of interleukin-8 production by okadaic acid and vanadate in a human promyelocyte cell line, an HL-60 subline: Possible role of mitogen-activated protein kinase on the okadaic acid-induced NF-κB activation
    • Sonoda, Y., T. Kasahara, Y. Yamaguchi, K. Kuno, K. Matsushima, and N. Mukaida. 1997. Stimulation of interleukin-8 production by okadaic acid and vanadate in a human promyelocyte cell line, an HL-60 subline: possible role of mitogen-activated protein kinase on the okadaic acid-induced NF-κB activation. J. Bid. Chem. 272:15366.
    • (1997) J. Bid. Chem. , vol.272 , pp. 15366
    • Sonoda, Y.1    Kasahara, T.2    Yamaguchi, Y.3    Kuno, K.4    Matsushima, K.5    Mukaida, N.6
  • 43
    • 0028986194 scopus 로고
    • IκB-β regulates the persistent response in a biphasic activation of NF-κB
    • Thompson, J. E., R. J Phillips, H. Erdjument-Bromage, P. Tempst, and S. Ghosh. 1995. IκB-β regulates the persistent response in a biphasic activation of NF-κB. Cell 80:573.
    • (1995) Cell , vol.80 , pp. 573
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 44
    • 0030582370 scopus 로고    scopus 로고
    • Murine peritoneal macrophages induce a novel 60-kDa protein with structural similarity to a tyrosine kinase p561ck-associated protein in response to oxidative stress
    • Ishii, T., T. Yanagawa, T. Kawane, K. Yuki, J. Seita, H. Yoshida, and S. Bannai. 1996. Murine peritoneal macrophages induce a novel 60-kDa protein with structural similarity to a tyrosine kinase p561ck-associated protein in response to oxidative stress. Biochem. Biophys. Res. Common. 226:456.
    • (1996) Biochem. Biophys. Res. Common. , vol.226 , pp. 456
    • Ishii, T.1    Yanagawa, T.2    Kawane, T.3    Yuki, K.4    Seita, J.5    Yoshida, H.6    Bannai, S.7
  • 45
    • 0030613758 scopus 로고    scopus 로고
    • NF-κB activation: The IκB kinase revealed?
    • Stancovski, I., and D. Baltimore. 1997. NF-κB activation: the IκB kinase revealed? Cell 91:299.
    • (1997) Cell , vol.91 , pp. 299
    • Stancovski, I.1    Baltimore, D.2
  • 46
    • 0030800625 scopus 로고    scopus 로고
    • Effects of tyrphostins and genistein on the circulatory failure and organ dysfunction caused by endotoxin in the rat: A possible role for protein tyrosine kinase
    • Ruetten, H., and C. Thiemermann. 1997. Effects of tyrphostins and genistein on the circulatory failure and organ dysfunction caused by endotoxin in the rat: a possible role for protein tyrosine kinase. Br. J. Pharmacol. 122:59.
    • (1997) Br. J. Pharmacol. , vol.122 , pp. 59
    • Ruetten, H.1    Thiemermann, C.2
  • 47
    • 0030912071 scopus 로고    scopus 로고
    • Lipopolysaccharide (LPS)-induced macrophage activation and signal transduction in the absence of Src-family kinases Hck, Fgr, and Lyn
    • Meng, F., and C. A. Lowell. 1997. Lipopolysaccharide (LPS)-induced macrophage activation and signal transduction in the absence of Src-family kinases Hck, Fgr, and Lyn. J. Exp. Med. 185:1661.
    • (1997) J. Exp. Med. , vol.185 , pp. 1661
    • Meng, F.1    Lowell, C.A.2
  • 48
    • 0030587161 scopus 로고    scopus 로고
    • Regulation of inducible nitric oxide synthase expression in IFN-γ-treated murine macrophages cultured under hypoxic conditions
    • Melillo, G., L. S. Taylor, A. Brooks, G. W. Cox, and L. Varesio. 1996. Regulation of inducible nitric oxide synthase expression in IFN-γ-treated murine macrophages cultured under hypoxic conditions. J. Immunol. 157:2638.
    • (1996) J. Immunol. , vol.157 , pp. 2638
    • Melillo, G.1    Taylor, L.S.2    Brooks, A.3    Cox, G.W.4    Varesio, L.5
  • 49
    • 0030911247 scopus 로고    scopus 로고
    • Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine
    • Melillo, G., L. S. Taylor, A. Brooks, T. Musso, G. W. Cox, and L. Varesio. 1997. Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine. J. Biol. Chem. 272:12236.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12236
    • Melillo, G.1    Taylor, L.S.2    Brooks, A.3    Musso, T.4    Cox, G.W.5    Varesio, L.6
  • 50
    • 0027983608 scopus 로고
    • rel Is rapidly tyrosine-phosphorylated following granulocyte-colony stimulating factor treatment of human neutrophils
    • Druker, B. J., M. Neumann, K. Okuda, B. R. Franza, Jr., and J. D. Griffin. 1994. rel Is rapidly tyrosine-phosphorylated following granulocyte-colony stimulating factor treatment of human neutrophils. J. Biol. Chem. 269:5387.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5387
    • Druker, B.J.1    Neumann, M.2    Okuda, K.3    Franza B.R., Jr.4    Griffin, J.D.5
  • 51
    • 0030899516 scopus 로고    scopus 로고
    • Phosphorylation events modulate the ability of interferon consensus sequence binding protein to interact with interferon regulatory factors and to bind DNA
    • Sharf, R., D. Meraro, A. Azriel, A.M. Thoraton, K. Ozato, E.F. Petricoin, A. C. Lamer, F. Schaper, H. Hauser, and B. Z. Levi. 1997. Phosphorylation events modulate the ability of interferon consensus sequence binding protein to interact with interferon regulatory factors and to bind DNA. J. Biol. Chem. 272:9785.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9785
    • Sharf, R.1    Meraro, D.2    Azriel, A.3    Thoraton, A.M.4    Ozato, K.5    Petricoin, E.F.6    Lamer, A.C.7    Schaper, F.8    Hauser, H.9    Levi, B.Z.10
  • 52
    • 0030764347 scopus 로고    scopus 로고
    • Synergistic activation of NF-κB by tumor necrosis factor a and y interferon via enhanced IκBα degradation and de novo IκBβ degradation
    • Cheschire, J. L., and A. S. Baldwin, Jr. 1997. Synergistic activation of NF-κB by tumor necrosis factor a and y interferon via enhanced IκBα degradation and de novo IκBβ degradation. Mol. Cell. Biol. 17:6746.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6746
    • Cheschire, J.L.1    Baldwin A.S., Jr.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.