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Volumn 161, Issue 3, 1998, Pages 1183-1193

TNF receptor-associated factor-3 signaling mediates activation of p38 and Jun N-terminal kinase, cytokine secretion, and Ig production following ligation of CD40 on human B cells

Author keywords

[No Author keywords available]

Indexed keywords

CD40 ANTIGEN; CYTOKINE; FAS ANTIGEN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; IMMUNOGLOBULIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERCELLULAR ADHESION MOLECULE 1; INTERLEUKIN 10; LYMPHOTOXIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PROTEIN TYROSINE KINASE; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0032146063     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (78)

References (97)
  • 1
    • 0030056358 scopus 로고    scopus 로고
    • CD40-CD40 ligand: A multifunctional receptor-ligand pair
    • van Kooten, C., and J. Banchereau. 1996. CD40-CD40 ligand: a multifunctional receptor-ligand pair. Adv. Immunol. 61:1.
    • (1996) Adv. Immunol. , vol.61 , pp. 1
    • Van Kooten, C.1    Banchereau, J.2
  • 3
    • 0028174234 scopus 로고
    • Hypercross-linking surface IgM or IgD receptors on mature B cells induces apoptosis that is reversed by costimulation with IL-4 and anti-CD40
    • Parry, S. L., M. J. Holman, J. Hasbold, and G. G. Klaus. 1994. Hypercross-linking surface IgM or IgD receptors on mature B cells induces apoptosis that is reversed by costimulation with IL-4 and anti-CD40. Eur. J. Immunol. 24:974.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 974
    • Parry, S.L.1    Holman, M.J.2    Hasbold, J.3    Klaus, G.G.4
  • 4
    • 0029931056 scopus 로고    scopus 로고
    • Ligation of CD40 influences the function of human Ig secreting B cell hybridomas both positively and negatively
    • Bergman, M. C., J. F. Attrep, A. C. Grammer, and P. E. Lipsky. 1996. Ligation of CD40 influences the function of human Ig secreting B cell hybridomas both positively and negatively. J. Immunol. 156:3118.
    • (1996) J. Immunol. , vol.156 , pp. 3118
    • Bergman, M.C.1    Attrep, J.F.2    Grammer, A.C.3    Lipsky, P.E.4
  • 6
    • 0024995864 scopus 로고
    • Identification of the intracytoplasmic region essential for signal transduction through a B cell activation molecule, CD40
    • Inui, S., T. Kaisho, H. Kikutani, I. Stamenkovic, B. Seed, E. A. Clark, and T. Kishimoto. 1990. Identification of the intracytoplasmic region essential for signal transduction through a B cell activation molecule, CD40. Eur. J. Immunol. 20:1747.
    • (1990) Eur. J. Immunol. , vol.20 , pp. 1747
    • Inui, S.1    Kaisho, T.2    Kikutani, H.3    Stamenkovic, I.4    Seed, B.5    Clark, E.A.6    Kishimoto, T.7
  • 7
    • 0027092054 scopus 로고
    • Responsiveness of chronic lymphocytic leukemia B cells activated via surface Igs or CD40 to B cell-trophic factors
    • Fluckiger, A. C., J. F. Rossi, A. Bussel, P. Bryon, J. Banchereau, and T. DeFrance. 1992. Responsiveness of chronic lymphocytic leukemia B cells activated via surface Igs or CD40 to B cell-trophic factors. Blood 80:3173.
    • (1992) Blood , vol.80 , pp. 3173
    • Fluckiger, A.C.1    Rossi, J.F.2    Bussel, A.3    Bryon, P.4    Banchereau, J.5    DeFrance, T.6
  • 8
  • 9
    • 0030266706 scopus 로고    scopus 로고
    • Identification of distinct domains in CD40 involved in B7-1 induction or growth inhibition
    • Goldstein, M. D., and T. H. Watts. 1996. Identification of distinct domains in CD40 involved in B7-1 induction or growth inhibition. J. Immunol. 157:2837.
    • (1996) J. Immunol. , vol.157 , pp. 2837
    • Goldstein, M.D.1    Watts, T.H.2
  • 10
    • 0030067795 scopus 로고    scopus 로고
    • A novel function of CD40: Induction of cell death in transformed cells
    • Hess, S., and H. Engelmann. 1996. A novel function of CD40: induction of cell death in transformed cells. J. Exp. Med. 183:159.
    • (1996) J. Exp. Med. , vol.183 , pp. 159
    • Hess, S.1    Engelmann, H.2
  • 12
    • 0026599838 scopus 로고
    • Generation of nondividing high rate Ig-secreting plasma cells in cultures of human B cells stimulated with anti-CD3-activated T cells
    • Vernino, L., L. M. McNally, J. Ramberg, and P. E. Lipsky. 1992. Generation of nondividing high rate Ig-secreting plasma cells in cultures of human B cells stimulated with anti-CD3-activated T cells. J Immunol. 148:404.
    • (1992) J Immunol. , vol.148 , pp. 404
    • Vernino, L.1    McNally, L.M.2    Ramberg, J.3    Lipsky, P.E.4
  • 13
    • 0029882545 scopus 로고    scopus 로고
    • Phosphalidylinositol 3-kinase activation in normal human lymphocytes: Differential sensitivity of growth and differentiation to wortmannin
    • Aagaard-Tillery, K., and D. F. Jelinek. 1996. Phosphalidylinositol 3-kinase activation in normal human lymphocytes: differential sensitivity of growth and differentiation to wortmannin, J. Immunol. 156:4543.
    • (1996) J. Immunol. , vol.156 , pp. 4543
    • Aagaard-Tillery, K.1    Jelinek, D.F.2
  • 14
    • 0031148886 scopus 로고    scopus 로고
    • CD40-triggered protein tyrosine phosphorylation on Vav and on phosphatidylinositol 3-kinase correlates with survival of the Ramos-Burkitt lymphoma B cell line
    • Padmore, L., S. An, R. H. Gunby, K. Kelly, G. K. Radda, and K. A. Knox. 1997. CD40-triggered protein tyrosine phosphorylation on Vav and on phosphatidylinositol 3-kinase correlates with survival of the Ramos-Burkitt lymphoma B cell line. Cell. Immunol. 177:119.
    • (1997) Cell. Immunol. , vol.177 , pp. 119
    • Padmore, L.1    An, S.2    Gunby, R.H.3    Kelly, K.4    Radda, G.K.5    Knox, K.A.6
  • 15
    • 0030917141 scopus 로고    scopus 로고
    • Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells
    • Hanissian, S. H., and R. S. Geha. 1997. Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells, immunity 6:379.
    • (1997) Immunity , vol.6 , pp. 379
    • Hanissian, S.H.1    Geha, R.S.2
  • 16
    • 0031278431 scopus 로고    scopus 로고
    • Induction of STAT protein signaling through the CD40 receptor in B lymphocytes
    • Karras, J. G., Z. Wang, L. Huo, D. A. Frank, and T. L. Rothstein. 1998. Induction of STAT protein signaling through the CD40 receptor in B lymphocytes. J. Immunol. 159:4350.
    • (1998) J. Immunol. , vol.159 , pp. 4350
    • Karras, J.G.1    Wang, Z.2    Huo, L.3    Frank, D.A.4    Rothstein, T.L.5
  • 18
    • 0030014424 scopus 로고    scopus 로고
    • Activation of mitogen-acttvated protein kinases via CD40 from that stimulated by surface IgM on B cells
    • Kashiwada, M., Y. Kaneko, H. Yagita, K. Okumura, and T. Takemori. 1996. Activation of mitogen-acttvated protein kinases via CD40 from that stimulated by surface IgM on B cells. Eur. J. Immunol. 26:1451.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1451
    • Kashiwada, M.1    Kaneko, Y.2    Yagita, H.3    Okumura, K.4    Takemori, T.5
  • 19
    • 0030586679 scopus 로고    scopus 로고
    • CD40 ligation results in protein kinase C-independent activation of ERK and JNK in resting murine splenic B cells
    • Li, Y.-Y., M. Baccam, S. B. Waters, J. E. Pessin, G. A. Bishop, and G. A. Koretzky. 1996. CD40 ligation results in protein kinase C-independent activation of ERK and JNK in resting murine splenic B cells. J. Immunol. 157: 1440.
    • (1996) J. Immunol. , vol.157 , pp. 1440
    • Li, Y.-Y.1    Baccam, M.2    Waters, S.B.3    Pessin, J.E.4    Bishop, G.A.5    Koretzky, G.A.6
  • 20
    • 0030069905 scopus 로고    scopus 로고
    • Cross-linking CD40 on B cells preferentially induces stress-activated protein kinases rather than mitogen-activated protein kinases
    • Berberich, I., G. Shu, F. Siebelt, J. R. Woodgrett, J. M. Kyriakis, and E. A. Clark. 1996. Cross-linking CD40 on B cells preferentially induces stress-activated protein kinases rather than mitogen-activated protein kinases. EMBO J. 15:92.
    • (1996) EMBO J. , vol.15 , pp. 92
    • Berberich, I.1    Shu, G.2    Siebelt, F.3    Woodgrett, J.R.4    Kyriakis, J.M.5    Clark, E.A.6
  • 21
    • 0029620212 scopus 로고
    • Selective activation of c-Jun kinase mitogen-activated protein kinase by CD40 on human B cells
    • Sakata, N., H. R. Patel, N. Terada, A. Aruffo, G. L. Johnson, and E. W. Gelfand. 1995. Selective activation of c-Jun kinase mitogen-activated protein kinase by CD40 on human B cells. J. Biol. Chem. 270:30823.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30823
    • Sakata, N.1    Patel, H.R.2    Terada, N.3    Aruffo, A.4    Johnson, G.L.5    Gelfand, E.W.6
  • 22
    • 0030587829 scopus 로고    scopus 로고
    • Differential activation of the ERK, JNK, and p38 mitogen-activated protein kinases by CD40 and the B cell antigen receptor
    • Sutherland, C. L., A. W. Heath, S. L. Pelech, P. R. Young, and M. R. Gold. 1996. Differential activation of the ERK, JNK, and p38 mitogen-activated protein kinases by CD40 and the B cell antigen receptor. J. Immunol. 157:3381.
    • (1996) J. Immunol. , vol.157 , pp. 3381
    • Sutherland, C.L.1    Heath, A.W.2    Pelech, S.L.3    Young, P.R.4    Gold, M.R.5
  • 23
    • 0031297364 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase is activated by ligation of the T and B lymphocyte antigen receptors, Fas or CD40, but suppression of kinase activity does not inhibit apoptosis induced by antigen receptors
    • Salmon, R. A., I. N. Foltz, P. R. Young, and J. W. Schrader. 1997. The p38 mitogen-activated protein kinase is activated by ligation of the T and B lymphocyte antigen receptors, Fas or CD40, but suppression of kinase activity does not inhibit apoptosis induced by antigen receptors. J. Immunol. 159:5309.
    • (1997) J. Immunol. , vol.159 , pp. 5309
    • Salmon, R.A.1    Foltz, I.N.2    Young, P.R.3    Schrader, J.W.4
  • 24
    • 0028950221 scopus 로고
    • Induction of the transcription factors AP-1 and NF-AT during B cell stimulation through the CD40 receptor
    • Francis, D. A., J. G. Karras, X. Y. Ke, R. Sen, and T. L. Rothstein. 1995. Induction of the transcription factors AP-1 and NF-AT during B cell stimulation through the CD40 receptor. Int. Immunol. 7:151.
    • (1995) Int. Immunol. , vol.7 , pp. 151
    • Francis, D.A.1    Karras, J.G.2    Ke, X.Y.3    Sen, R.4    Rothstein, T.L.5
  • 25
    • 0028152658 scopus 로고
    • Cross-linking CD40 on B cells rapidly activates nuclear factor-κB
    • Berberich, I., G. L. Shu, and E. A. Clark. 1994. Cross-linking CD40 on B cells rapidly activates nuclear factor-κB. J. Immunol. 153:4357.
    • (1994) J. Immunol. , vol.153 , pp. 4357
    • Berberich, I.1    Shu, G.L.2    Clark, E.A.3
  • 27
    • 0028978626 scopus 로고
    • Traf2-mediated activation of NF-κB by TNF receptor 2 and CD40
    • Rothe, M., V. Sarma, V. M. Dixit, and D. V. Goeddel. 1995. Traf2-mediated activation of NF-κB by TNF receptor 2 and CD40. Science 269:1424.
    • (1995) Science , vol.269 , pp. 1424
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 30
    • 0027943499 scopus 로고
    • A novel RING finger protein interacts with the cytoplasmic domain of CD40
    • Hu, H. M., K. O'Rourke, M. S. Boguski, and V. M. Dixit. 1994. A novel RING finger protein interacts with the cytoplasmic domain of CD40. J. Biol. Chem. 269:30069.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30069
    • Hu, H.M.1    O'Rourke, K.2    Boguski, M.S.3    Dixit, V.M.4
  • 31
    • 0028809176 scopus 로고
    • A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40
    • Sato, T., S. Irie, and J. C. Reed. 1995. A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40. FEBS Lett. 358:113.
    • (1995) FEBS Lett. , vol.358 , pp. 113
    • Sato, T.1    Irie, S.2    Reed, J.C.3
  • 33
    • 0031975588 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates extracellular signal-regulated kinase (ERK) activity in CD40 signaling along a ras-independent pathway
    • Kashiwada, M., Y. Shirakata, J. -I. Inoue, H. Nakano, K. Okazaki, K. Okumura, T. Yamamoto, H. Nagaoka, and T. Takemori. 1998. Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates extracellular signal-regulated kinase (ERK) activity in CD40 signaling along a ras-independent pathway. J. Exp. Med 187:237.
    • (1998) J. Exp. Med , vol.187 , pp. 237
    • Kashiwada, M.1    Shirakata, Y.2    Inoue, J.I.3    Nakano, H.4    Okazaki, K.5    Okumura, K.6    Yamamoto, T.7    Nagaoka, H.8    Takemori, T.9
  • 34
    • 0031587929 scopus 로고    scopus 로고
    • Novel homologues of CSBP/p38 MAP kinase: Activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles
    • Kumar, S., P. C. McDonnell, R. J. Gum, A. T. Hand, J. C. Lee, and P. R. Young. 1997. Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles. Biochem. Biophys. Res. Commun. 235:533.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 533
    • Kumar, S.1    McDonnell, P.C.2    Gum, R.J.3    Hand, A.T.4    Lee, J.C.5    Young, P.R.6
  • 35
    • 0029982565 scopus 로고    scopus 로고
    • Characterization of the structure and function of a new mitogen-activated protein kinase (p38β)
    • Jiang, Y., C. Chen, Z. Li, W. Guo, J.A. Gegner, S. Lin, and J. Han. 1996. Characterization of the structure and function of a new mitogen-activated protein kinase (p38β). J. Biol. Chem. 27:17920.
    • (1996) J. Biol. Chem. , vol.27 , pp. 17920
    • Jiang, Y.1    Chen, C.2    Li, Z.3    Guo, W.4    Gegner, J.A.5    Lin, S.6    Han, J.7
  • 36
    • 0030581626 scopus 로고    scopus 로고
    • The primary structure of p38 γ: A new member of the p38 group of MAP kinases
    • Li, Z., Y. Jiang, R. J. Ulevitch, and J. Han. 1996. The primary structure of p38 γ: a new member of the p38 group of MAP kinases. Biochem. Biophys. Res. Commun. 228:334.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 334
    • Li, Z.1    Jiang, Y.2    Ulevitch, R.J.3    Han, J.4
  • 41
    • 0031939402 scopus 로고    scopus 로고
    • A fusion of the EBV latent membrane protein (LMP1) transmembrane domains to the CD40 cytoplasmic domain is similar to LMP1 in constitutive activation of epidermal growth factor receptor expression, nuclear factor-κB, and stress-activated protein kinase
    • Hatzivassiliou, W. E. Miller, N. Raub-Traub, E. Kieff, and G. Mosialos. 1998. A fusion of the EBV latent membrane protein (LMP1) transmembrane domains to the CD40 cytoplasmic domain is similar to LMP1 in constitutive activation of epidermal growth factor receptor expression, nuclear factor-κB, and stress-activated protein kinase. J. Immunol. 160:1116.
    • (1998) J. Immunol. , vol.160 , pp. 1116
    • Hatzivassiliou1    Miller, W.E.2    Raub-Traub, N.3    Kieff, E.4    Mosialos, G.5
  • 42
    • 0024497851 scopus 로고
    • A phenotypic study of cells from Burkitt lymphoma and EBV-B-lympho- blastoid lines and their relationship to cells in normal lymphoid tissue
    • Ling, M. R., D. Hardie, J. Lowe, G. D. Johnson, M. Khan, and I. C. MacLennan. 1989. A phenotypic study of cells from Burkitt lymphoma and EBV-B-lympho- blastoid lines and their relationship to cells in normal lymphoid tissue. Int. J. Cancer 43:112.
    • (1989) Int. J. Cancer , vol.43 , pp. 112
    • Ling, M.R.1    Hardie, D.2    Lowe, J.3    Johnson, G.D.4    Khan, M.5    MacLennan, I.C.6
  • 43
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle, P. A., and D. Baltimore. 1996. NF-κB: ten years after. Cell 87:13.
    • (1996) Cell , vol.87 , pp. 13
    • Baeuerle, P.A.1    Baltimore, D.2
  • 44
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • Baldwin, A. S. 1996. The NF-κB and IκB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:649.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649
    • Baldwin, A.S.1
  • 45
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB prevents cell death
    • Liu, Z. G., H. Hsu, D. V. Goeddel, and M. Karin. 1996. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB prevents cell death. Cell 87:565.
    • (1996) Cell , vol.87 , pp. 565
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 46
    • 0031048067 scopus 로고    scopus 로고
    • Tumor necrosis factor α-induced activation of c-jun N-terminal kinase is mediated by TRAF2
    • Reinhard, C., B. Shamoon, V. Shyamala, and L. T. Williams. 1997. Tumor necrosis factor α-induced activation of c-jun N-terminal kinase is mediated by TRAF2. EMBO J. 16:1080.
    • (1997) EMBO J. , vol.16 , pp. 1080
    • Reinhard, C.1    Shamoon, B.2    Shyamala, V.3    Williams, L.T.4
  • 48
    • 0008206988 scopus 로고    scopus 로고
    • TRAF2 is essential for JNK but not NF-κB activation and regulates proliferation and survival
    • Lee, S. Y., A. Reichlin, A. Santana, K. A. Sokol, M. C. Nussenzweig, and Y. Choi. 1997, TRAF2 is essential for JNK but not NF-κB activation and regulates proliferation and survival. Immunity 7:703.
    • (1997) Immunity , vol.7 , pp. 703
    • Lee, S.Y.1    Reichlin, A.2    Santana, A.3    Sokol, K.A.4    Nussenzweig, M.C.5    Choi, Y.6
  • 49
    • 12644272789 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-mediated kinase cascades: Bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2
    • Song, H. Y., C. H. Regnier, C. J. Kirschning, D. V. Goeddel, and M. Rothe. 1997. Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2. Proc. Natl. Acad. Sci. USA 94:9792.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9792
    • Song, H.Y.1    Regnier, C.H.2    Kirschning, C.J.3    Goeddel, D.V.4    Rothe, M.5
  • 50
    • 0030854040 scopus 로고    scopus 로고
    • Localization of the major NF-κB-activating site and the sole TRAF3 binding site of LMP-1 defines two distinct signaling motifs
    • Brodeur, S. R., G. Cheng, D. Baltimore, and D. A. Thorley-Lawson. 1997. Localization of the major NF-κB-activating site and the sole TRAF3 binding site of LMP-1 defines two distinct signaling motifs. J. Biol. Chem. 272:19777.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19777
    • Brodeur, S.R.1    Cheng, G.2    Baltimore, D.3    Thorley-Lawson, D.A.4
  • 51
    • 0031060448 scopus 로고    scopus 로고
    • Epstein-Barr virus LMP1 induction of the epidermal growth factor receptor is mediated through a TRAF signaling pathway distinct from NF-κB activation
    • Miller, W. E., G. Mosialos, E. Kieff, and N. Raab-Traub. 1997. Epstein-Barr virus LMP1 induction of the epidermal growth factor receptor is mediated through a TRAF signaling pathway distinct from NF-κB activation. J. Virol. 71:586.
    • (1997) J. Virol. , vol.71 , pp. 586
    • Miller, W.E.1    Mosialos, G.2    Kieff, E.3    Raab-Traub, N.4
  • 52
    • 0030747497 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded LMP1 and CD40 mediated IL6 production in epithelial cells via an NF-κB pathway involving TNF receptor-associated factors
    • Eliopoulos, A. G., M. Stack, C. W. Dawson, K. M. Kaye, L. Hodgkin, S. Sihota, M. Rowe, and L. S. Young. 1997. Epstein-Barr virus-encoded LMP1 and CD40 mediated IL6 production in epithelial cells via an NF-κB pathway involving TNF receptor-associated factors. Oncogene 14:2899.
    • (1997) Oncogene , vol.14 , pp. 2899
    • Eliopoulos, A.G.1    Stack, M.2    Dawson, C.W.3    Kaye, K.M.4    Hodgkin, L.5    Sihota, S.6    Rowe, M.7    Young, L.S.8
  • 53
    • 0030292777 scopus 로고    scopus 로고
    • Targeted disruption of TRAF3 leads to postnatal lethality and defective T-dependent immune responses
    • Xu, Y., G. Cheng, and D. Baltimore. 1996. Targeted disruption of TRAF3 leads to postnatal lethality and defective T-dependent immune responses. Immunity 5:407.
    • (1996) Immunity , vol.5 , pp. 407
    • Xu, Y.1    Cheng, G.2    Baltimore, D.3
  • 55
    • 0029917841 scopus 로고    scopus 로고
    • TANK, a co-inducer with TRAF2 of TNF-and CD40L-mediated NF-κB activation
    • Cheng, G., and D. Baltimore. 1996. TANK, a co-inducer with TRAF2 of TNF-and CD40L-mediated NF-κB activation. Genes Dev. 10:963.
    • (1996) Genes Dev. , vol.10 , pp. 963
    • Cheng, G.1    Baltimore, D.2
  • 56
    • 0029039180 scopus 로고
    • Evidence for multiple activators for stress-activated protein kinase/c-Jun amino terminal kinases: Evidence of novel activators
    • Moriguchi, T., H. Kawasaki, S. Matsuda, Y. Gotoh, and E. Nishida. 1995. Evidence for multiple activators for stress-activated protein kinase/c-Jun amino terminal kinases: evidence of novel activators. J. Biol. Chem. 270:12969.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12969
    • Moriguchi, T.1    Kawasaki, H.2    Matsuda, S.3    Gotoh, Y.4    Nishida, E.5
  • 57
    • 0030908341 scopus 로고    scopus 로고
    • Targeted disruption of the MKK4 gene causes embryonic death, inhibition of c-Jun NH2-terminal kinase activation, and defects in AP-1 transcriptional activity
    • Yang, D., C. Tournier, M. Wysk, H.-T. Lu, J. Xu, R. J. Davis, and R. A. Flavell. 1997. Targeted disruption of the MKK4 gene causes embryonic death, inhibition of c-Jun NH2-terminal kinase activation, and defects in AP-1 transcriptional activity. Proc. Natl. Acad. Sci. USA 94:3004.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3004
    • Yang, D.1    Tournier, C.2    Wysk, M.3    Lu, H.-T.4    Xu, J.5    Davis, R.J.6    Flavell, R.A.7
  • 58
    • 0031047962 scopus 로고    scopus 로고
    • Identification and characterization of a predominant isoform of human MKK3
    • Han, J., X. Wang, Y. Jiang, R. J. Ulevitch, and S. Lin. 1997. Identification and characterization of a predominant isoform of human MKK3. FEBS Lett. 403:19.
    • (1997) FEBS Lett. , vol.403 , pp. 19
    • Han, J.1    Wang, X.2    Jiang, Y.3    Ulevitch, R.J.4    Lin, S.5
  • 59
    • 0029782176 scopus 로고    scopus 로고
    • Purification and cDNA cloning of SAPKK3, the major activator of RK/p38 in stress- and cytokine-stimulated monocytes and epithelial cells
    • Cuenda, A., G. Alonso, N. Morrice, M. Jones, R. Meier, P. Cohen, and A. R. Nebreda. 1996. Purification and cDNA cloning of SAPKK3, the major activator of RK/p38 in stress- and cytokine-stimulated monocytes and epithelial cells. EMBO J. 15:4156.
    • (1996) EMBO J. , vol.15 , pp. 4156
    • Cuenda, A.1    Alonso, G.2    Morrice, N.3    Jones, M.4    Meier, R.5    Cohen, P.6    Nebreda, A.R.7
  • 60
    • 10244241798 scopus 로고    scopus 로고
    • Purification and identification of a major activator for p38 from osmotically shocked cells: Activation of mitogen-activated protein kinase kinase 6 by osmotic shock, TNF-α, and H202
    • Moriguchi, T., F. Toyoshima, Y. Gotoh, A. Iwamatsu, K. Irie, E. Mori, N. Kuroyanagi, M. Hagiwara, K. Matsumoto, and E. Nishida. 1996. Purification and identification of a major activator for p38 from osmotically shocked cells: activation of mitogen-activated protein kinase kinase 6 by osmotic shock, TNF-α, and H202. J. Biol. Chem. 271:26981.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26981
    • Moriguchi, T.1    Toyoshima, F.2    Gotoh, Y.3    Iwamatsu, A.4    Irie, K.5    Mori, E.6    Kuroyanagi, N.7    Hagiwara, M.8    Matsumoto, K.9    Nishida, E.10
  • 63
    • 0030051528 scopus 로고    scopus 로고
    • MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway
    • Raingeaud, J., A. J. Whitmarsh, T. Barren, B. Derijard, and R. J. Davis. 1996. MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell. Biol. 16:1247.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1247
    • Raingeaud, J.1    Whitmarsh, A.J.2    Barren, T.3    Derijard, B.4    Davis, R.J.5
  • 64
    • 0030044182 scopus 로고    scopus 로고
    • Characterization of the structure and function of a novel MAP kinase kinase (MKK6)
    • Han, J., J. D. Lee, Y. Jiang, Z. Li, L. Feng, and R. J. Ulevitch. 1996. Characterization of the structure and function of a novel MAP kinase kinase (MKK6). J. Biol. Chem. 271:2886.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2886
    • Han, J.1    Lee, J.D.2    Jiang, Y.3    Li, Z.4    Feng, L.5    Ulevitch, R.J.6
  • 65
    • 0030006618 scopus 로고    scopus 로고
    • Cloning and characterization of MEK6, a novel member of the mitogen-activated protein kinase kinase cascade
    • Stein, B., H. Brady, M. X. Yang, D. B. Young, and M. S. Barbosa. 1996. Cloning and characterization of MEK6, a novel member of the mitogen-activated protein kinase kinase cascade. J. Biol. Chem. 271:11427.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11427
    • Stein, B.1    Brady, H.2    Yang, M.X.3    Young, D.B.4    Barbosa, M.S.5
  • 67
    • 0030825190 scopus 로고    scopus 로고
    • MKK7 is a stress-activated mitogen-activated protein kinase kinase functionally related to hemipterous
    • Holland, P. M., M. Suzanne, J. S. Campbell, S. Noselli, and J. A. Cooper. 1997. MKK7 is a stress-activated mitogen-activated protein kinase kinase functionally related to hemipterous. J. Biol. Chem. 272:24994.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24994
    • Holland, P.M.1    Suzanne, M.2    Campbell, J.S.3    Noselli, S.4    Cooper, J.A.5
  • 68
    • 0030863983 scopus 로고    scopus 로고
    • SKK4, a novel activator of stress-activated protein kinase-1 (SAPK1/JNK)
    • Lawler, S., A. Cuenda, M. Goedert, and P. Cohen. 1997. SKK4, a novel activator of stress-activated protein kinase-1 (SAPK1/JNK). FEBS Lett. 414:153.
    • (1997) FEBS Lett. , vol.414 , pp. 153
    • Lawler, S.1    Cuenda, A.2    Goedert, M.3    Cohen, P.4
  • 69
    • 0029808748 scopus 로고    scopus 로고
    • Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
    • Whitmarsh, A. J., and R. J. Davis. 1996. Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways. J. Mol. Med. 74: 589.
    • (1996) J. Mol. Med. , vol.74 , pp. 589
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 71
  • 72
    • 0031573678 scopus 로고    scopus 로고
    • Immunohistochemical analysis of in vivo patterns of TRAF3 expression, a member of the TNF-receptor-associated factor family
    • Krajewski, S., J. M. Zapata, M. Krajewska, T. VanArsdale, A. Shabaik, R. D. Gascoyne, and J. C. Reed. 1997. Immunohistochemical analysis of in vivo patterns of TRAF3 expression, a member of the TNF-receptor-associated factor family. J. Immunol. 159:5841.
    • (1997) J. Immunol. , vol.159 , pp. 5841
    • Krajewski, S.1    Zapata, J.M.2    Krajewska, M.3    Vanarsdale, T.4    Shabaik, A.5    Gascoyne, R.D.6    Reed, J.C.7
  • 73
    • 0030210233 scopus 로고    scopus 로고
    • Different CD40-mediated signaling events require distinct CD40 structural features
    • Hostager, B. S., Y. Hsing, D.E. Harms, and G. A. Bishop. 1996. Different CD40-mediated signaling events require distinct CD40 structural features. J. Immunol. 157:1047.
    • (1996) J. Immunol. , vol.157 , pp. 1047
    • Hostager, B.S.1    Hsing, Y.2    Harms, D.E.3    Bishop, G.A.4
  • 75
    • 0031985287 scopus 로고    scopus 로고
    • Nuclear factor (NF)-κB2 (p100/p52) is required for normal splenic microarchitecture and B cell-mediated immune responses
    • Caamano, J. H., C. A. Rizzo, S. K. Durham, D. S. Barton, C. Raventos-Suarez, C. M. Snapper, and R. Bravo. 1998. Nuclear factor (NF)-κB2 (p100/p52) is required for normal splenic microarchitecture and B cell-mediated immune responses. J. Exp. Med. 187:185.
    • (1998) J. Exp. Med. , vol.187 , pp. 185
    • Caamano, J.H.1    Rizzo, C.A.2    Durham, S.K.3    Barton, D.S.4    Raventos-Suarez, C.5    Snapper, C.M.6    Bravo, R.7
  • 76
    • 0029150389 scopus 로고
    • Mice lacking the c-rel proto-oncogene exhibit defects in lymphocyte proliferation, humoral immunity, and interleukin-2 expression
    • Kontgen, F., R. J. Grumont, A. Strasser, D. Metcalf, R. Li, D. Tarlinton, and S. Gerondakis. 1995. Mice lacking the c-rel proto-oncogene exhibit defects in lymphocyte proliferation, humoral immunity, and interleukin-2 expression. Genes Dev 9:1965.
    • (1995) Genes Dev , vol.9 , pp. 1965
    • Kontgen, F.1    Grumont, R.J.2    Strasser, A.3    Metcalf, D.4    Li, R.5    Tarlinton, D.6    Gerondakis, S.7
  • 77
    • 0029903486 scopus 로고    scopus 로고
    • B cells lacking RelB are defective in proliferative responses, but undergo normal B cell maturation to Ig secretion and Ig class switching
    • Snapper, C. M., F. R. Rosas, P. Zeiazowski, M. A. Moorman, M. R. Kehry, R. Bravo, and F. Weih. 1996. B cells lacking RelB are defective in proliferative responses, but undergo normal B cell maturation to Ig secretion and Ig class switching. J. Exp. Med. 184:1537.
    • (1996) J. Exp. Med. , vol.184 , pp. 1537
    • Snapper, C.M.1    Rosas, F.R.2    Zeiazowski, P.3    Moorman, M.A.4    Kehry, M.R.5    Bravo, R.6    Weih, F.7
  • 78
    • 0030048494 scopus 로고    scopus 로고
    • Apoptosis mediated by the TNF-related cytokine and receptor families
    • Ware, C. F., S. VanArsdale, and T. L. VanArsdale. 1996. Apoptosis mediated by the TNF-related cytokine and receptor families. J. Cell Biochem. 60:47.
    • (1996) J. Cell Biochem. , vol.60 , pp. 47
    • Ware, C.F.1    Vanarsdale, S.2    Vanarsdale, T.L.3
  • 79
    • 0030746740 scopus 로고    scopus 로고
    • Casper is a FADD- and capase-related inducer of apoptosis
    • Shu, H.-B., D. R. Halphin, and D. V. Goeddel. 1997. Casper is a FADD- and capase-related inducer of apoptosis. Immunity 7:751.
    • (1997) Immunity , vol.7 , pp. 751
    • Shu, H.-B.1    Halphin, D.R.2    Goeddel, D.V.3
  • 81
    • 0030911873 scopus 로고    scopus 로고
    • Lymphotoxin-β receptor signaling complex: Role of TNF receptor-associated factor 3 recruitment in cell death and activation of nuclear factor κB
    • VanArsdale, T. L., S. L. VanArsdale, W. R. Force, B. N. Walter, G. Mosialos, E. Kieff, J. C. Reed, and C. F. Ware. 1997. Lymphotoxin-β receptor signaling complex: role of TNF receptor-associated factor 3 recruitment in cell death and activation of nuclear factor κB. Proc. Natl. Acad. Sci. USA 94:2460.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2460
    • Vanarsdale, T.L.1    Vanarsdale, S.L.2    Force, W.R.3    Walter, B.N.4    Mosialos, G.5    Kieff, E.6    Reed, J.C.7    Ware, C.F.8
  • 83
    • 0030741166 scopus 로고    scopus 로고
    • Production of cytokines by human B cells in health and disease
    • Pistoia, V. 1997. Production of cytokines by human B cells in health and disease. Immunol. Today 18:343.
    • (1997) Immunol. Today , vol.18 , pp. 343
    • Pistoia, V.1
  • 84
    • 0028837901 scopus 로고
    • The ability of synoviocytes to support terminal differentiation of activated B cells may explain plasma cell accumulation in rheumatoid synovium
    • Dechanet, J., P. Merville, I. Durand, J. Banchereau, and P. Miossec. 1995. The ability of synoviocytes to support terminal differentiation of activated B cells may explain plasma cell accumulation in rheumatoid synovium. J. Clin. Invest. 95:456.
    • (1995) J. Clin. Invest. , vol.95 , pp. 456
    • Dechanet, J.1    Merville, P.2    Durand, I.3    Banchereau, J.4    Miossec, P.5
  • 86
    • 0029837669 scopus 로고    scopus 로고
    • Cell-type-specific regulation of the human TNF-α gene in B cells and T cells by NFATp and ATF-2/JUN
    • Tsai, E. Y., J. Yie, D. Thanos, and A. E. Goldfeld. 1996. Cell-type-specific regulation of the human TNF-α gene in B cells and T cells by NFATp and ATF-2/JUN. Mol. Cell Biol. 16:5232.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5232
    • Tsai, E.Y.1    Yie, J.2    Thanos, D.3    Goldfeld, A.E.4
  • 87
    • 0029786684 scopus 로고    scopus 로고
    • Characterization of a new isoform of the NFAT (nuclear factor of activated T cells) gene family member NFATc
    • Park, J., A. Takeuchi, and S. Sharma. 1996. Characterization of a new isoform of the NFAT (nuclear factor of activated T cells) gene family member NFATc. J. Biol. Chem. 271:20914.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20914
    • Park, J.1    Takeuchi, A.2    Sharma, S.3
  • 88
    • 0029156958 scopus 로고
    • CD40-mediated lymphotoxin α expression in human B cells is tyrosine kinase dependent
    • Worm, M., and R. S. Geha. 1995. CD40-mediated lymphotoxin α expression in human B cells is tyrosine kinase dependent. Eur. J. Immunol. 25:2438.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 2438
    • Worm, M.1    Geha, R.S.2
  • 90
    • 0030910899 scopus 로고    scopus 로고
    • Mapping of the human IL10 gene and further characterization of the 5′ flanking sequence
    • Eskdale, J., D. Kube, H. Tesch, and G. Gallagher. 1997. Mapping of the human IL10 gene and further characterization of the 5′ flanking sequence. Immunogenetics 46:120.
    • (1997) Immunogenetics , vol.46 , pp. 120
    • Eskdale, J.1    Kube, D.2    Tesch, H.3    Gallagher, G.4
  • 93
    • 0029818395 scopus 로고    scopus 로고
    • Two distinct regions in the 3′ untranslated region of TNF-α mRNA form complexes with macrophage proteins
    • Hel, Z., E. Skamene, and D. Radzioch. 1996. Two distinct regions in the 3′ untranslated region of TNF-α mRNA form complexes with macrophage proteins. Mol. Cell. Biol. 16:5579.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5579
    • Hel, Z.1    Skamene, E.2    Radzioch, D.3
  • 94
    • 0028900073 scopus 로고
    • The nonamer UUAUUUAUU is the key AU-rich sequence motif that mediates mRNA degradation
    • Zubiaga, A. M., J. G. Belasco, and M. E. Greenberg. 1995. The nonamer UUAUUUAUU is the key AU-rich sequence motif that mediates mRNA degradation. Mol. Cell. Biol. 15:2219.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2219
    • Zubiaga, A.M.1    Belasco, J.G.2    Greenberg, M.E.3
  • 95
    • 0030881742 scopus 로고    scopus 로고
    • JNK/stress-activated protein kinase (SAPK) is required for lipopolysaccharide stimulation of TNF-α (TNFα) translation: Glucocorticoids inhibit TNFα translation by blocking JNK/SAPK
    • Swantek, J. L., M. H. Cobb, and T. Geppert. 1997. JNK/stress-activated protein kinase (SAPK) is required for lipopolysaccharide stimulation of TNF-α (TNFα) translation: glucocorticoids inhibit TNFα translation by blocking JNK/SAPK. Mol. Cell. Biol. 17:6274.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6274
    • Swantek, J.L.1    Cobb, M.H.2    Geppert, T.3
  • 96
    • 0029664650 scopus 로고    scopus 로고
    • Role of CSB/p38/RK stress response kinase in LPS and cytokine signaling mechanisms
    • Lee, J. C., and P. R. Young. 1996. Role of CSB/p38/RK stress response kinase in LPS and cytokine signaling mechanisms. J. Leukocyte Biol. 59:152.
    • (1996) J. Leukocyte Biol. , vol.59 , pp. 152
    • Lee, J.C.1    Young, P.R.2


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