메뉴 건너뛰기




Volumn 254, Issue 1, 2000, Pages 14-24

Tumor necrosis factor receptor-associated factor (TRAF) family: Adapter proteins that mediate cytokine signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CYTOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1 RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOTRANSFERASE; TRANSCRIPTION FACTOR AP 1; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0034627798     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4733     Document Type: Review
Times cited : (384)

References (105)
  • 1
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe M., Wong S. C., Henzel W. J., Goeddel D. V. A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell. 78:1994;681-692.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 2
    • 0027943499 scopus 로고
    • A novel RING finger protein interacts with the cytoplasmic domain of CD40
    • Hu H. M., O'Rourke K., Boguski M. S., Dixit V. M. A novel RING finger protein interacts with the cytoplasmic domain of CD40. J. Biol. Chem. 269:1994;30069-30072.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30069-30072
    • Hu, H.M.1    O'Rourke, K.2    Boguski, M.S.3    Dixit, V.M.4
  • 4
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos G., Birkenbach M., Yalamanchili R., VanArsdale T., Ware C., Kieff E. The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell. 80:1995;389-399.
    • (1995) Cell , vol.80 , pp. 389-399
    • Mosialos, G.1    Birkenbach, M.2    Yalamanchili, R.3    Vanarsdale, T.4    Ware, C.5    Kieff, E.6
  • 5
    • 0028809176 scopus 로고
    • A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40
    • Sato T., Irie S., Reed J. C. A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40. FEBS Lett. 358:1995;113-118.
    • (1995) FEBS Lett. , vol.358 , pp. 113-118
    • Sato, T.1    Irie, S.2    Reed, J.C.3
  • 6
    • 0028856787 scopus 로고
    • Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor-associated protein family, which is expressed in breast carcinoma
    • Regnier C. H., Tomasetto C., Moog-Lutz C., Chenard M. P., Wendling C., Basset P., Rio M. C. Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor-associated protein family, which is expressed in breast carcinoma. J. Biol. Chem. 270:1995;25715-25721.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25715-25721
    • Regnier, C.H.1    Tomasetto, C.2    Moog-Lutz, C.3    Chenard, M.P.4    Wendling, C.5    Basset, P.6    Rio, M.C.7
  • 10
    • 10544243364 scopus 로고    scopus 로고
    • Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region
    • Ishida T., Mizushima S., Azuma S., Kobayashi N., Tojo T., Suzuki K., Aizawa S., Watanabe T., Mosialos G., Kieff E., Yamamoto T., Inoue J. Identification of TRAF6, a novel tumor necrosis factor receptor-associated factor protein that mediates signaling from an amino-terminal domain of the CD40 cytoplasmic region. J. Biol. Chem. 271:1996;28745-28748.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28745-28748
    • Ishida, T.1    Mizushima, S.2    Azuma, S.3    Kobayashi, N.4    Tojo, T.5    Suzuki, K.6    Aizawa, S.7    Watanabe, T.8    Mosialos, G.9    Kieff, E.10    Yamamoto, T.11    Inoue, J.12
  • 11
    • 0344178160 scopus 로고    scopus 로고
    • Identification of a TRAF (TNF receptor-associated factor) gene in Caenorhabditis elegans
    • Wajant H., Muhlenbeck F., Scheurich P. Identification of a TRAF (TNF receptor-associated factor) gene in Caenorhabditis elegans. J. Mol. Evol. 47:1998;656-662.
    • (1998) J. Mol. Evol. , vol.47 , pp. 656-662
    • Wajant, H.1    Muhlenbeck, F.2    Scheurich, P.3
  • 12
    • 0033611551 scopus 로고    scopus 로고
    • A Drosophila TNF-receptor-associated factor (TRAF) binds the ste20 kinase Misshapen and activates Jun kinase
    • Liu H., Su Y. C., Becker E., Treisman J., Skolnik E. Y. A Drosophila TNF-receptor-associated factor (TRAF) binds the ste20 kinase Misshapen and activates Jun kinase. Curr. Biol. 9:1999;101-104.
    • (1999) Curr. Biol. , vol.9 , pp. 101-104
    • Liu, H.1    Su, Y.C.2    Becker, E.3    Treisman, J.4    Skolnik, E.Y.5
  • 14
    • 0030292777 scopus 로고    scopus 로고
    • Targeted disruption of TRAF3 leads to postnatal lethality and defective T-dependent immune responses
    • Xu Y., Cheng G., Baltimore D. Targeted disruption of TRAF3 leads to postnatal lethality and defective T-dependent immune responses. Immunity. 5:1996;407-415.
    • (1996) Immunity , vol.5 , pp. 407-415
    • Xu, Y.1    Cheng, G.2    Baltimore, D.3
  • 15
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κ B activation
    • Hsu H., Xiong J., Goeddel D. V. The TNF receptor 1-associated protein TRADD signals cell death and NF-κ B activation. Cell. 81:1995;495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 17
    • 0031423761 scopus 로고    scopus 로고
    • MyD88: An adapter that recruits IRAK to the IL-1 receptor complex
    • Wesche H., Henzel W. J., Shillinglaw W., Li S., Cao Z. MyD88: An adapter that recruits IRAK to the IL-1 receptor complex. Immunity. 7:1997;837-847.
    • (1997) Immunity , vol.7 , pp. 837-847
    • Wesche, H.1    Henzel, W.J.2    Shillinglaw, W.3    Li, S.4    Cao, Z.5
  • 19
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 340:1989;245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 20
    • 0029786304 scopus 로고    scopus 로고
    • Anatomy of TRAF2: Distinct domains for nuclear factor-κB activation and association with tumor necrosis factor signaling proteins
    • Takeuchi M., Rothe M., Goeddel D. V. Anatomy of TRAF2: Distinct domains for nuclear factor-κB activation and association with tumor necrosis factor signaling proteins. J. Biol. Chem. 271:1996;19935-19942.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19935-19942
    • Takeuchi, M.1    Rothe, M.2    Goeddel, D.V.3
  • 21
    • 0001033803 scopus 로고    scopus 로고
    • Structural basis for self-association and receptor recognition of human TRAF2
    • Park Y. C., Burkitt V., Villa A. R., Tong L., Wu H. Structural basis for self-association and receptor recognition of human TRAF2. Nature. 398:1999;533-538.
    • (1999) Nature , vol.398 , pp. 533-538
    • Park, Y.C.1    Burkitt, V.2    Villa, A.R.3    Tong, L.4    Wu, H.5
  • 23
    • 0040084598 scopus 로고    scopus 로고
    • CD30/TNF receptor-associated factor interaction: NF-κB activation and binding specificity
    • Lee S. Y., Lee S. Y., Kandala G., Liou M. L., Liou H. C., Choi Y. CD30/TNF receptor-associated factor interaction: NF-κB activation and binding specificity. Proc. Natl. Acad. Sci. USA. 93:1996;9699-9703.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9699-9703
    • Lee, S.Y.1    Lee, S.Y.2    Kandala, G.3    Liou, M.L.4    Liou, H.C.5    Choi, Y.6
  • 24
    • 0030661665 scopus 로고    scopus 로고
    • Dominant negative mutants of TRAF3 reveal an important role for the coiled coil domains in cell death signaling by the lymphotoxin-β receptor
    • Force W. R., Cheung T. C., Ware C. F. Dominant negative mutants of TRAF3 reveal an important role for the coiled coil domains in cell death signaling by the lymphotoxin-β receptor. J. Biol. Chem. 272:1997;30835-30840.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30835-30840
    • Force, W.R.1    Cheung, T.C.2    Ware, C.F.3
  • 25
    • 0032493737 scopus 로고    scopus 로고
    • Characterization of the intracellular domain of receptor activator of NF-κB (RANK): Interaction with tumor necrosis factor receptor-associated factors and activation of NF-κB and c-Jun N-terminal kinase
    • Darnay B. G., Haridas V., Ni J., Moore P. A., Aggarwal B. B. Characterization of the intracellular domain of receptor activator of NF-κB (RANK): Interaction with tumor necrosis factor receptor-associated factors and activation of NF-κB and c-Jun N-terminal kinase. J. Biol. Chem. 273:1998;20551-20555.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20551-20555
    • Darnay, B.G.1    Haridas, V.2    Ni, J.3    Moore, P.A.4    Aggarwal, B.B.5
  • 26
    • 0029956392 scopus 로고    scopus 로고
    • Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: Role in NF-κB activation
    • Devergne O., Hatzivassiliou E., Izumi K. M., Kaye K. M., Kleijnen M. F., Kieff E., Mosialos G. Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: Role in NF-κB activation. Mol. Cell. Biol. 16:1996;7098-7108.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7098-7108
    • Devergne, O.1    Hatzivassiliou, E.2    Izumi, K.M.3    Kaye, K.M.4    Kleijnen, M.F.5    Kieff, E.6    Mosialos, G.7
  • 27
    • 15844369897 scopus 로고    scopus 로고
    • CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins
    • Gedrich R. W., Gilfillan M. C., Duckett C. S., Van Dongen J. L., Thompson C. B. CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins. J. Biol. Chem. 271:1996;12852-12858.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12852-12858
    • Gedrich, R.W.1    Gilfillan, M.C.2    Duckett, C.S.3    Van Dongen, J.L.4    Thompson, C.B.5
  • 28
    • 0033574060 scopus 로고    scopus 로고
    • Specificities of CD40 signaling: Involvement of TRAF2 in CD40-induced NF-κB activation and intercellular adhesion molecule-1 up-regulation
    • Lee H. H., Dempsey P. W., Parks T. P., Zhu X., Baltimore D., Cheng G. Specificities of CD40 signaling: involvement of TRAF2 in CD40-induced NF-κB activation and intercellular adhesion molecule-1 up-regulation. Proc. Natl. Acad. Sci. USA. 96:1999;1421-1426.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1421-1426
    • Lee, H.H.1    Dempsey, P.W.2    Parks, T.P.3    Zhu, X.4    Baltimore, D.5    Cheng, G.6
  • 29
    • 0033574051 scopus 로고    scopus 로고
    • Two differently regulated nuclear factor κb activation pathways triggered by the cytoplasmic tail of CD40
    • Tsukamoto N., Kobayashi N., Azuma S., Yamamoto T., Inoue J. Two differently regulated nuclear factor κB activation pathways triggered by the cytoplasmic tail of CD40. Proc. Natl. Acad. Sci. USA. 96:1999;1234-1239.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1234-1239
    • Tsukamoto, N.1    Kobayashi, N.2    Azuma, S.3    Yamamoto, T.4    Inoue, J.5
  • 30
    • 0032561198 scopus 로고    scopus 로고
    • The TRAF family of signal transducers mediates NF-κB activation by the TRANCE receptor
    • Wong B. R., Josien R., Lee S. Y., Vologodskaia M., Steinman R. M., Choi Y. The TRAF family of signal transducers mediates NF-κB activation by the TRANCE receptor. J. Biol. Chem. 273:1998;28355-28359.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28355-28359
    • Wong, B.R.1    Josien, R.2    Lee, S.Y.3    Vologodskaia, M.4    Steinman, R.M.5    Choi, Y.6
  • 31
    • 0032545465 scopus 로고    scopus 로고
    • The involvement of multiple tumor necrosis factor receptor (TNFR)-associated factors in the signaling mechanisms of receptor activator of NF-κB, a member of the TNFR superfamily
    • Galibert L., Tometsko M. E., Anderson D. M., Cosman D., Dougall W. C. The involvement of multiple tumor necrosis factor receptor (TNFR)-associated factors in the signaling mechanisms of receptor activator of NF-κB, a member of the TNFR superfamily. J. Biol. Chem. 273:1998;34120-34127.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34120-34127
    • Galibert, L.1    Tometsko, M.E.2    Anderson, D.M.3    Cosman, D.4    Dougall, W.C.5
  • 32
    • 0033582819 scopus 로고    scopus 로고
    • Activation of NF-κB by RANK requires tumor necrosis factor receptor-associated factor (TRAF) 6 and NF-κB-inducing kinase: Identification of a novel TRAF6 interaction motif
    • Darnay B. G., Ni J., Moore P. A., Aggarwal B. B. Activation of NF-κB by RANK requires tumor necrosis factor receptor-associated factor (TRAF) 6 and NF-κB-inducing kinase: Identification of a novel TRAF6 interaction motif. J. Biol. Chem. 274:1999;7724-7731.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7724-7731
    • Darnay, B.G.1    Ni, J.2    Moore, P.A.3    Aggarwal, B.B.4
  • 33
    • 0033613831 scopus 로고    scopus 로고
    • Association of the p75 neurotrophin receptor with TRAF6
    • Khursigara G., Orlinick J. R., Chao M. V. Association of the p75 neurotrophin receptor with TRAF6. J. Biol. Chem. 274:1999;2597-2600.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2597-2600
    • Khursigara, G.1    Orlinick, J.R.2    Chao, M.V.3
  • 36
    • 0033166472 scopus 로고    scopus 로고
    • Unresponsiveness of MyD88-deficient mice to endotoxin
    • Kawai T., Adachi O., Ogawa T., Takeda K., Akira S. Unresponsiveness of MyD88-deficient mice to endotoxin. Immunity. 11:1999;115-122.
    • (1999) Immunity , vol.11 , pp. 115-122
    • Kawai, T.1    Adachi, O.2    Ogawa, T.3    Takeda, K.4    Akira, S.5
  • 37
    • 0032526861 scopus 로고    scopus 로고
    • The human toll signaling pathway: Divergence of nuclear factor κb and JNK/SAPK activation upstream of tumor necrosis factor receptor-associated factor 6 (TRAF6)
    • Muzio M., Natoli G., Saccani S., Levrero M., Mantovani A. The human toll signaling pathway: Divergence of nuclear factor κB and JNK/SAPK activation upstream of tumor necrosis factor receptor-associated factor 6 (TRAF6). J. Exp. Med. 187:1998;2097-2101.
    • (1998) J. Exp. Med. , vol.187 , pp. 2097-2101
    • Muzio, M.1    Natoli, G.2    Saccani, S.3    Levrero, M.4    Mantovani, A.5
  • 38
    • 0030694108 scopus 로고    scopus 로고
    • IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling
    • Muzio M., Ni J., Feng P., Dixit V. M. IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. Science. 278:1997;1612-1615.
    • (1997) Science , vol.278 , pp. 1612-1615
    • Muzio, M.1    Ni, J.2    Feng, P.3    Dixit, V.M.4
  • 40
    • 0030911873 scopus 로고    scopus 로고
    • Lymphotoxin-β receptor signaling complex: Role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor κb
    • VanArsdale T. L., VanArsdale S. L., Force W. R., Walter B. N., Mosialos G., Kieff E., Reed J. C., Ware C. F. Lymphotoxin-β receptor signaling complex: Role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor κB. Proc. Natl. Acad. Sci. USA. 94:1997;2460-2465.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2460-2465
    • 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
  • 42
    • 0023192180 scopus 로고
    • The active form of tumor necrosis factor is a trimer
    • Smith R. A., Baglioni C. The active form of tumor necrosis factor is a trimer. J. Biol. Chem. 262:1987;6951-6954.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6951-6954
    • Smith, R.A.1    Baglioni, C.2
  • 43
    • 0030055168 scopus 로고    scopus 로고
    • Human pro-tumor necrosis factor is a homotrimer
    • Tang P., Hung M. C., Klostergaard J. Human pro-tumor necrosis factor is a homotrimer. Biochemistry. 35:1996;8216-8225.
    • (1996) Biochemistry , vol.35 , pp. 8216-8225
    • Tang, P.1    Hung, M.C.2    Klostergaard, J.3
  • 44
    • 0033563101 scopus 로고    scopus 로고
    • Signaling by proinflammatory cytokines: Oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain
    • Baud V., Liu Z. G., Bennett B., Suzuki N., Xia Y., Karin M. Signaling by proinflammatory cytokines: Oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain. Genes Dev. 13:1999;1297-1308.
    • (1999) Genes Dev. , vol.13 , pp. 1297-1308
    • Baud, V.1    Liu, Z.G.2    Bennett, B.3    Suzuki, N.4    Xia, Y.5    Karin, M.6
  • 45
    • 0028670788 scopus 로고
    • Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
    • Yan M., Dai T., Deak J. C., Kyriakis J. M., Zon L. I., Woodgett J. R., Templeton D. J. Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1. Nature. 372:1994;798-800.
    • (1994) Nature , vol.372 , pp. 798-800
    • Yan, M.1    Dai, T.2    Deak, J.C.3    Kyriakis, J.M.4    Zon, L.I.5    Woodgett, J.R.6    Templeton, D.J.7
  • 49
    • 0033580466 scopus 로고    scopus 로고
    • The kinase TAK1 can activate the NIK-I κb as well as the MAP kinase cascade in the IL-1 signalling pathway
    • Ninomiya T. J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K. The kinase TAK1 can activate the NIK-I κB as well as the MAP kinase cascade in the IL-1 signalling pathway. Nature. 398:1999;252-256.
    • (1999) Nature , vol.398 , pp. 252-256
    • Ninomiya, T.J.1    Kishimoto, K.2    Hiyama, A.3    Inoue, J.4    Cao, Z.5    Matsumoto, K.6
  • 50
    • 0032575591 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase (JNK) and p38: Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/ERK kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38
    • Yuasa T., Ohno S., Kehrl J. H., Kyriakis J. M. Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase (JNK) and p38: Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/ERK kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38. J. Biol. Chem. 273:1998;22681-22692.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22681-22692
    • Yuasa, T.1    Ohno, S.2    Kehrl, J.H.3    Kyriakis, J.M.4
  • 51
    • 0031437885 scopus 로고    scopus 로고
    • Activation of stress-activated protein kinase/c-Jun N-terminal kinase, but not NF-κB, by the tumor necrosis factor (TNF) receptor 1 through a TNF receptor-associated factor 2-and germinal center kinase related-dependent pathway
    • Shi C. S., Kehrl J. H. Activation of stress-activated protein kinase/c-Jun N-terminal kinase, but not NF-κB, by the tumor necrosis factor (TNF) receptor 1 through a TNF receptor-associated factor 2-and germinal center kinase related-dependent pathway. J. Biol. Chem. 272:1997;32102-32107.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32102-32107
    • Shi, C.S.1    Kehrl, J.H.2
  • 52
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1
    • Malinin N. L., Boldin M. P., Kovalenko A. V., Wallach D. MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature. 385:1997;540-544.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 53
    • 0033611544 scopus 로고    scopus 로고
    • TPL-2 kinase regulates the proteolysis of the NF-κB-inhibitory protein NF-κB1 p105
    • Belich M. P., Salmeron A., Johnston L. H., Ley S. C. TPL-2 kinase regulates the proteolysis of the NF-κB-inhibitory protein NF-κB1 p105. Nature. 397:1999;363-368.
    • (1999) Nature , vol.397 , pp. 363-368
    • Belich, M.P.1    Salmeron, A.2    Johnston, L.H.3    Ley, S.C.4
  • 54
    • 0033082990 scopus 로고    scopus 로고
    • The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-κB acting through the NF-κB-inducing kinase and IκB kinases
    • Lin X., Cunningham E. T. Jr., Mu Y., Geleziunas R., Greene W. C. The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-κB acting through the NF-κB-inducing kinase and IκB kinases. Immunity. 10:1999;271-280.
    • (1999) Immunity , vol.10 , pp. 271-280
    • Lin, X.1    Cunningham E.T., Jr.2    Mu, Y.3    Geleziunas, R.4    Greene, W.C.5
  • 55
    • 0027332498 scopus 로고
    • The IκB proteins: Multifunctional regulators of Rel/NF-κB transcription factors
    • Beg A. A., Baldwin A. S. Jr. The IκB proteins: Multifunctional regulators of Rel/NF-κB transcription factors. Genes Dev. 7:1993;2064-2070.
    • (1993) Genes Dev. , vol.7 , pp. 2064-2070
    • Beg, A.A.1    Baldwin A.S., Jr.2
  • 56
    • 0027333044 scopus 로고
    • The IκB proteins: Members of a multifunctional family
    • Gilmore T. D., Morin P. J. The IκB proteins: Members of a multifunctional family. Trends Genet. 9:1993;427-433.
    • (1993) Trends Genet. , vol.9 , pp. 427-433
    • Gilmore, T.D.1    Morin, P.J.2
  • 58
    • 0027446955 scopus 로고
    • The oncoprotein Bcl-3 directly transactivates through κb motifs via association with DNA-binding p50B homodimers
    • Bours V., Franzoso G., Azarenko V., Park S., Kanno T., Brown K., Siebenlist U. The oncoprotein Bcl-3 directly transactivates through κB motifs via association with DNA-binding p50B homodimers. Cell. 72:1993;729-739.
    • (1993) Cell , vol.72 , pp. 729-739
    • Bours, V.1    Franzoso, G.2    Azarenko, V.3    Park, S.4    Kanno, T.5    Brown, K.6    Siebenlist, U.7
  • 59
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato J., Mercurio F., Rosette C., Wu-Li J., Suyang H., Ghosh S., Karin M. Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16:1996;1295-1304.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • Didonato, J.1    Mercurio, F.2    Rosette, C.3    Wu-Li, J.4    Suyang, H.5    Ghosh, S.6    Karin, M.7
  • 61
    • 0028986075 scopus 로고
    • Control of IκBα proteolysis by site-specific, signal-induced phosphorylation
    • Brown K., Gerstberger S., Carlson L., Franzoso G., Siebenlist U. Control of IκBα proteolysis by site-specific, signal-induced phosphorylation. Science. 267:1995;1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 62
    • 0028978032 scopus 로고
    • Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli
    • Traenckner E. B., Pahl H. L., Henkel T., Schmidt K. N., Wilk S., Baeuerle P. A. Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14:1995;2876-2883.
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 63
    • 0029122799 scopus 로고
    • N- And C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity
    • Whiteside S. T., Ernst M. K., LeBail O., Laurent-Winter C., Rice N.m, Israel A. N- and C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity. Mol. Cell. Biol. 15:1995;5339-5345.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5339-5345
    • Whiteside, S.T.1    Ernst, M.K.2    Lebail, O.3    Laurent-Winter, C.4    Rice, N.M.5    Israel, A.6
  • 64
    • 0028557348 scopus 로고
    • Tumor necrosis factor α-induced phosphorylation of IκBα is a signal for its degradation but not dissociation from NF-κB
    • Miyamoto S., Maki M., Schmitt M. J., Hatanaka M., Verma I. M. Tumor necrosis factor α-induced phosphorylation of IκBα is a signal for its degradation but not dissociation from NF-κB. Proc. Natl. Acad. Sci. USA. 91:1994;12740-12744.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12740-12744
    • Miyamoto, S.1    Maki, M.2    Schmitt, M.J.3    Hatanaka, M.4    Verma, I.M.5
  • 66
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP
    • Spencer E., Jiang J., Chen Z. J. Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP. Genes Dev. 13:1999;284-294.
    • (1999) Genes Dev , vol.13 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 68
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity
    • Chen Z. J., Parent L., Maniatis T. Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell. 84:1996;853-862.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 69
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato J. A., Hayakawa M., Rothwarf D. M., Zandi E., Karin M. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature. 388:1997;548-554.
    • (1997) Nature , vol.388 , pp. 548-554
    • Didonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 71
    • 0030611595 scopus 로고    scopus 로고
    • IκB kinase-β: NF-κB activation and complex formation with IκB kinase-α And NIK
    • Woronicz J. D., Gao X., Cao Z., Rothe M., Goeddel D. V. IκB kinase-β: NF-κB activation and complex formation with IκB kinase-α and NIK. Science. 278:1997;866-869.
    • (1997) Science , vol.278 , pp. 866-869
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 72
    • 0030613551 scopus 로고    scopus 로고
    • The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation
    • Zandi E., Rothwarf D. M., Delhase M., Hayakawa M., Karin M. The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation. Cell. 91:1997;243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 74
    • 0032583949 scopus 로고    scopus 로고
    • Differential regulation of IκB kinase α and β by two upstream kinases, NF-κB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1
    • Nakano H., Shindo M., Sakon S., Nishinaka S., Mihara M., Yagita H., Okumura K. Differential regulation of IκB kinase α and β by two upstream kinases, NF-κB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1. Proc. Natl. Acad. Sci. USA. 95:1998;3537-3542.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3537-3542
    • Nakano, H.1    Shindo, M.2    Sakon, S.3    Nishinaka, S.4    Mihara, M.5    Yagita, H.6    Okumura, K.7
  • 75
    • 0033567388 scopus 로고    scopus 로고
    • ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway
    • Kopp E., Medzhitov R., Carothers J., Xiao C., Douglas I., Janeway C. A., Ghosh S. ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway. Genes Dev. 13:1999;2059-2071.
    • (1999) Genes Dev. , vol.13 , pp. 2059-2071
    • Kopp, E.1    Medzhitov, R.2    Carothers, J.3    Xiao, C.4    Douglas, I.5    Janeway, C.A.6    Ghosh, S.7
  • 76
    • 0029858387 scopus 로고    scopus 로고
    • TNF- And cancer therapy-induced apoptosis: Potentiation by inhibition of NF-κB
    • Wang C. Y., Mayo M. W., Baldwin A. S. Jr. TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-κB. Science. 274:1996;784-787.
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin A.S., Jr.3
  • 78
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-α-induced cell death
    • Beg A. A., Baltimore D. An essential role for NF-κB in preventing TNF-α-induced cell death. Science. 274:1996;782-784.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 79
    • 0030885421 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control
    • Chu Z. L., McKinsey T. A., Liu L., Gentry J. J., Malim M. H., Ballard D. W. Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control. Proc. Natl. Acad. Sci. USA. 94:1997;10057-10062.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10057-10062
    • Chu, Z.L.1    McKinsey, T.A.2    Liu, L.3    Gentry, J.J.4    Malim, M.H.5    Ballard, D.W.6
  • 80
    • 0032508414 scopus 로고    scopus 로고
    • NF-κB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c- IAP2 to suppress caspase-8 activation
    • Wang C. Y., Mayo M. W., Korneluk R. G., Goeddel D. V., Baldwin A. S. Jr. NF-κB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c- IAP2 to suppress caspase-8 activation. Science. 281:1998;1680-1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin A.S., Jr.5
  • 81
    • 0029073035 scopus 로고
    • Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis
    • Sarma V., Lin Z., Clark L., Rust B. M., Tewari M., Noelle R. J., Dixit V. M. Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis. J. Biol. Chem. 270:1995;12343-12346.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12343-12346
    • Sarma, V.1    Lin, Z.2    Clark, L.3    Rust, B.M.4    Tewari, M.5    Noelle, R.J.6    Dixit, V.M.7
  • 82
    • 0025179989 scopus 로고
    • The A20 cDNA induced by tumor necrosis factor α encodes a novel type of zinc finger protein
    • Opipari A. W. Jr., Boguski M. S., Dixit V. M. The A20 cDNA induced by tumor necrosis factor α encodes a novel type of zinc finger protein. J. Biol. Chem. 265:1990;14705-14708.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14705-14708
    • Opipari A.W., Jr.1    Boguski, M.S.2    Dixit, V.M.3
  • 83
    • 0029917841 scopus 로고    scopus 로고
    • TANK, a co-inducer with TRAF2 of TNF- And CD 40L-mediated NF-κB activation
    • Cheng G., Baltimore D. TANK, a co-inducer with TRAF2 of TNF- and CD 40L-mediated NF-κB activation. Genes Dev. 10:1996;963-973.
    • (1996) Genes Dev. , vol.10 , pp. 963-973
    • Cheng, G.1    Baltimore, D.2
  • 85
    • 0000564581 scopus 로고    scopus 로고
    • The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-κB activation
    • Song H. Y., Rothe M., Goeddel D. V. The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-κB activation. Proc. Natl. Acad. Sci. USA. 93:1996;6721-6725.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6721-6725
    • Song, H.Y.1    Rothe, M.2    Goeddel, D.V.3
  • 86
    • 0032939356 scopus 로고    scopus 로고
    • The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-κB activation at the level of TRAF6
    • Heyninck K., Beyaert R. The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-κB activation at the level of TRAF6. FEBS Lett. 442:1999;147-150.
    • (1999) FEBS Lett. , vol.442 , pp. 147-150
    • Heyninck, K.1    Beyaert, R.2
  • 87
    • 0347667234 scopus 로고    scopus 로고
    • TRAF-interacting protein (TRIP): A novel component of the tumor necrosis factor receptor (TNFR)- And CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-κB activation
    • Lee S. Y., Lee S. Y., Choi Y. TRAF-interacting protein (TRIP): A novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-κB activation. J. Exp. Med. 185:1997;1275-1285.
    • (1997) J. Exp. Med. , vol.185 , pp. 1275-1285
    • Lee, S.Y.1    Lee, S.Y.2    Choi, Y.3
  • 88
    • 0031906851 scopus 로고    scopus 로고
    • Peg3/Pw1 is an imprinted gene involved in the TNF-NFκB signal transduction pathway
    • Relaix F., Wei X. J., Wu X., Sassoon D. A. Peg3/Pw1 is an imprinted gene involved in the TNF-NFκB signal transduction pathway. Nature Genet. 18:1998;287-291.
    • (1998) Nature Genet. , vol.18 , pp. 287-291
    • Relaix, F.1    Wei, X.J.2    Wu, X.3    Sassoon, D.A.4
  • 89
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M., Pan M. G., Henzel W. J., Ayres T. M., Goeddel D. V. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell. 83:1995;1243-1252.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 90
    • 0030746740 scopus 로고    scopus 로고
    • Casper is a FADD- And caspase-related inducer of apoptosis
    • Shu H. B., Halpin D. R., Goeddel D. V. Casper is a FADD- and caspase-related inducer of apoptosis. Immunity. 6:1997;751-763.
    • (1997) Immunity , vol.6 , pp. 751-763
    • Shu, H.B.1    Halpin, D.R.2    Goeddel, D.V.3
  • 91
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger B. Z., Leder P., Lee T. H., Kim E., Seed B. RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell. 81:1995;513-523.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 92
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H., Huang J., Shu H. B., Baichwal V., Goeddel D. V. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity. 4:1996;387-396.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 94
    • 0008206988 scopus 로고    scopus 로고
    • TRAF2 is essential for JNK but not NF-κB activation and regulates lymphocyte proliferation and survival
    • Lee S. Y., Reichlin A., Santana A., Sokol K. A., Nussenzweig M. C., Choi Y. TRAF2 is essential for JNK but not NF-κB activation and regulates lymphocyte proliferation and survival. Immunity. 7:1997;703-713.
    • (1997) Immunity , vol.7 , pp. 703-713
    • Lee, S.Y.1    Reichlin, A.2    Santana, A.3    Sokol, K.A.4    Nussenzweig, M.C.5    Choi, Y.6
  • 96
    • 15444346943 scopus 로고    scopus 로고
    • CD27, a member of the tumor necrosis factor receptor superfamily, activates NF-κB and stress-activated protein kinase/c-Jun N-terminal kinase via TRAF2, TRAF5, and NF-κB-inducing kinase
    • Akiba H., Nakano H., Nishinaka S., Shindo M., Kobata T., Atsuta M., Morimoto C., Ware C. F., Malinin N. L., Wallach D., Yagita H., Okumura K. CD27, a member of the tumor necrosis factor receptor superfamily, activates NF-κB and stress-activated protein kinase/c-Jun N-terminal kinase via TRAF2, TRAF5, and NF-κB-inducing kinase. J. Biol. Chem. 273:1998;13353-13358.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13353-13358
    • Akiba, H.1    Nakano, H.2    Nishinaka, S.3    Shindo, M.4    Kobata, T.5    Atsuta, M.6    Morimoto, C.7    Ware, C.F.8    Malinin, N.L.9    Wallach, D.10    Yagita, H.11    Okumura, K.12
  • 98
    • 0032127301 scopus 로고    scopus 로고
    • The lymphotoxin β receptor controls organogenesis and affinity maturation in peripheral lymphoid tissues
    • Futterer A., Mink K., Luz A., Kosco-Vilbois M. H., Pfeffer K. The lymphotoxin β receptor controls organogenesis and affinity maturation in peripheral lymphoid tissues. Immunity. 9:1998;59-70.
    • (1998) Immunity , vol.9 , pp. 59-70
    • Futterer, A.1    Mink, K.2    Luz, A.3    Kosco-Vilbois, M.H.4    Pfeffer, K.5
  • 105
    • 0031439265 scopus 로고    scopus 로고
    • TRANCE (tumor necrosis factor [TNF]-related activation-induced cytokine), a new TNF family member predominantly expressed in T cells, is a dendritic cell-specific survival factor
    • Wong B. R., Josien R., Lee S. Y., Sauter B., Li H. L., Steinman R. M., Choi Y. TRANCE (tumor necrosis factor [TNF]-related activation-induced cytokine), a new TNF family member predominantly expressed in T cells, is a dendritic cell-specific survival factor. J. Exp. Med. 186:1997;2075-2080.
    • (1997) J. Exp. Med. , vol.186 , pp. 2075-2080
    • Wong, B.R.1    Josien, R.2    Lee, S.Y.3    Sauter, B.4    Li, H.L.5    Steinman, R.M.6    Choi, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.