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Volumn 180, Issue 5, 2008, Pages 3238-3249

The tumor suppressor death-associated protein kinase targets to TCR-stimulated NF-κB activation

Author keywords

[No Author keywords available]

Indexed keywords

DEATH ASSOCIATED PROTEIN KINASE; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 2; PROTEIN BCL 10; PROTEIN KINASE C; T LYMPHOCYTE RECEPTOR; APOPTOSIS REGULATORY PROTEIN; DEATH-ASSOCIATED PROTEIN KINASE; LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN KINASE (CALCIUM,CALMODULIN); SMALL INTERFERING RNA; TUMOR SUPPRESSOR PROTEIN;

EID: 49149091747     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.180.5.3238     Document Type: Article
Times cited : (50)

References (55)
  • 1
    • 0037020686 scopus 로고    scopus 로고
    • The DAP-kinase family of proteins: Study of a novel group of calcium-regulated death-promoting kinases
    • Shohat, G., G. Shani, M. Eisenstein, and A. Kimchi. 2002. The DAP-kinase family of proteins: study of a novel group of calcium-regulated death-promoting kinases. Biochim. Biophys. Acta 1600: 45-50.
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 45-50
    • Shohat, G.1    Shani, G.2    Eisenstein, M.3    Kimchi, A.4
  • 2
    • 3042515471 scopus 로고    scopus 로고
    • DAP-kinase as a target for drug design in cancer and diseases associated with accelerated cell death
    • Bialik, S., and A. Kimchi. 2004. DAP-kinase as a target for drug design in cancer and diseases associated with accelerated cell death. Semin. Cancer Biol. 14: 283-294.
    • (2004) Semin. Cancer Biol , vol.14 , pp. 283-294
    • Bialik, S.1    Kimchi, A.2
  • 3
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: Structure, function, and beyond
    • Bialik, S., and A. Kimchi. 2006. The death-associated protein kinases: structure, function, and beyond. Annu. Rev. Biochem. 75: 189-210.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 4
    • 0031056002 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity
    • 2+/calmodulin-dependent, cytoskeletal-associated protein kinase, with cell death-inducing functions that depend on its catalytic activity. EMBO J. 16: 998-1008.
    • (1997) EMBO J , vol.16 , pp. 998-1008
    • Cohen, O.1    Feinstein, E.2    Kimchi, A.3
  • 5
    • 0028831202 scopus 로고
    • Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the γ interferon-induced cell death
    • Deiss, L. P., E. Feinstein, H. Berissi, O. Cohen, and A. Kimchi. 1995. Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the γ interferon-induced cell death. Genes Dev. 9: 15-30.
    • (1995) Genes Dev , vol.9 , pp. 15-30
    • Deiss, L.P.1    Feinstein, E.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 7
    • 0036144377 scopus 로고    scopus 로고
    • TGF-β induces apoptosis through Smad-mediated expression of DAP-kinase
    • Jang, C. W., C. H. Chen, C. C. Chen, J. Y. Chen, Y. H. Su, and R. H. Chen. 2002. TGF-β induces apoptosis through Smad-mediated expression of DAP-kinase. Nat. Cell Biol. 4: 51-58.
    • (2002) Nat. Cell Biol , vol.4 , pp. 51-58
    • Jang, C.W.1    Chen, C.H.2    Chen, C.C.3    Chen, J.Y.4    Su, Y.H.5    Chen, R.H.6
  • 8
    • 0037127269 scopus 로고    scopus 로고
    • Death-associated protein (DAP) kinase plays a central role in ceramide-induced apoptosis in cultured hippocampal neurons
    • Pelled, D., T. Raveh, C. Riebeling, M. Fridkin, H. Berissi, A. H. Futerman, and A. Kimchi. 2002. Death-associated protein (DAP) kinase plays a central role in ceramide-induced apoptosis in cultured hippocampal neurons. J. Biol. Chem. 277: 1957-1961.
    • (2002) J. Biol. Chem , vol.277 , pp. 1957-1961
    • Pelled, D.1    Raveh, T.2    Riebeling, C.3    Fridkin, M.4    Berissi, H.5    Futerman, A.H.6    Kimchi, A.7
  • 10
    • 0037078325 scopus 로고    scopus 로고
    • DAP-kinase induces apoptosis by suppressing integrin activity and disrupting matrix survival signals
    • Wang, W. J., J. C. Kuo, C. C. Yao, and R. H. Chen. 2002. DAP-kinase induces apoptosis by suppressing integrin activity and disrupting matrix survival signals. J. Cell Biol. 159: 169-179.
    • (2002) J. Cell Biol , vol.159 , pp. 169-179
    • Wang, W.J.1    Kuo, J.C.2    Yao, C.C.3    Chen, R.H.4
  • 12
    • 27144458235 scopus 로고    scopus 로고
    • Death-associated protein kinase as a sensor of mitochondrial membrane potential: Role of lysosome in mitochondrial toxin-induced cell death
    • Shang, T., J. Joseph, C. J. Hillard, and B. Kalyanaraman. 2005. Death-associated protein kinase as a sensor of mitochondrial membrane potential: role of lysosome in mitochondrial toxin-induced cell death. J. Biol. Chem. 280: 34644-34653.
    • (2005) J. Biol. Chem , vol.280 , pp. 34644-34653
    • Shang, T.1    Joseph, J.2    Hillard, C.J.3    Kalyanaraman, B.4
  • 15
    • 0035835823 scopus 로고    scopus 로고
    • DAP kinase-a proapoptotic gene that functions as a tumor suppressor
    • Raveh, T., and A. Kimchi. 2001. DAP kinase-a proapoptotic gene that functions as a tumor suppressor. Exp. Cell Res. 264: 185-192.
    • (2001) Exp. Cell Res , vol.264 , pp. 185-192
    • Raveh, T.1    Kimchi, A.2
  • 17
    • 0035955620 scopus 로고    scopus 로고
    • Identification of a new form of death-associated protein kinase that promotes cell survival
    • Jin, Y., E. K. Blue, S. Dixon, L. Hou, R. B. Wysolmerski, and P. J. Gallagher. 2001. Identification of a new form of death-associated protein kinase that promotes cell survival. J. Biol. Chem. 276: 39667-39678.
    • (2001) J. Biol. Chem , vol.276 , pp. 39667-39678
    • Jin, Y.1    Blue, E.K.2    Dixon, S.3    Hou, L.4    Wysolmerski, R.B.5    Gallagher, P.J.6
  • 18
    • 0346121431 scopus 로고    scopus 로고
    • Uncoordinated regulation of stress fibers and focal adhesions by DAP kinase
    • Kuo, J. C., J. R. Lin, J. M. Staddon, H. Hosoya, and R. H. Chen. 2003. Uncoordinated regulation of stress fibers and focal adhesions by DAP kinase. J. Cell Sci. 116: 4777-4790.
    • (2003) J. Cell Sci , vol.116 , pp. 4777-4790
    • Kuo, J.C.1    Lin, J.R.2    Staddon, J.M.3    Hosoya, H.4    Chen, R.H.5
  • 19
    • 2942740790 scopus 로고    scopus 로고
    • DAP-kinase-mediated morphological changes are localization dependent and involve myosin-II phosphorylation
    • Bialik, S., A. R. Bresnick, and A. Kimchi. 2004. DAP-kinase-mediated morphological changes are localization dependent and involve myosin-II phosphorylation. Cell Death Differ. 11: 631-644.
    • (2004) Cell Death Differ , vol.11 , pp. 631-644
    • Bialik, S.1    Bresnick, A.R.2    Kimchi, A.3
  • 20
    • 0032931786 scopus 로고    scopus 로고
    • ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells
    • Murata-Hori, M., F. Suizu, T. Iwasaki, A. Kikuchi, and H. Hosoya. 1999. ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells. FEBS Lett. 451: 81-84.
    • (1999) FEBS Lett , vol.451 , pp. 81-84
    • Murata-Hori, M.1    Suizu, F.2    Iwasaki, T.3    Kikuchi, A.4    Hosoya, H.5
  • 21
    • 32644448252 scopus 로고    scopus 로고
    • The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway
    • Kuo, J. C., W. J. Wang, C. C. Yao, P. R. Wu, and R. H. Chen. 2006. The tumor suppressor DAPK inhibits cell motility by blocking the integrin-mediated polarity pathway. J. Cell Biol. 172: 619-631.
    • (2006) J. Cell Biol , vol.172 , pp. 619-631
    • Kuo, J.C.1    Wang, W.J.2    Yao, C.C.3    Wu, P.R.4    Chen, R.H.5
  • 22
    • 13444311622 scopus 로고    scopus 로고
    • Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK
    • Chen, C. H., W. J. Wang, J. C. Kuo, H. C. Tsai, J. R. Lin, Z. F. Chang, and R. H. Chen. 2005. Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK. EMBO J. 24: 294-304.
    • (2005) EMBO J , vol.24 , pp. 294-304
    • Chen, C.H.1    Wang, W.J.2    Kuo, J.C.3    Tsai, H.C.4    Lin, J.R.5    Chang, Z.F.6    Chen, R.H.7
  • 23
    • 26244449244 scopus 로고    scopus 로고
    • The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling
    • Anjum, R., P. P. Roux, B. A. Ballif, S. P. Gygi, and J. Blenis. 2005. The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling. Curr. Biol. 15: 1762-1767.
    • (2005) Curr. Biol , vol.15 , pp. 1762-1767
    • Anjum, R.1    Roux, P.P.2    Ballif, B.A.3    Gygi, S.P.4    Blenis, J.5
  • 24
    • 0036009115 scopus 로고    scopus 로고
    • NF-κB at the crossroads of life and death
    • Karin, M., and A. Lin. 2002. NF-κB at the crossroads of life and death. Nat. Immunol. 3: 221-227.
    • (2002) Nat. Immunol , vol.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 25
    • 0033637216 scopus 로고    scopus 로고
    • NF-κB activation by the pre-T cell receptor serves as a selective survival signal in T lymphocyte development
    • Voll, R. E., E. Jimi, R. J. Phillips, D. F. Barber, M. Rincon, A. C. Hayday, R. A. Flavell, and S. Ghosh. 2000. NF-κB activation by the pre-T cell receptor serves as a selective survival signal in T lymphocyte development. Immunity 13: 677-689.
    • (2000) Immunity , vol.13 , pp. 677-689
    • Voll, R.E.1    Jimi, E.2    Phillips, R.J.3    Barber, D.F.4    Rincon, M.5    Hayday, A.C.6    Flavell, R.A.7    Ghosh, S.8
  • 27
    • 20644455960 scopus 로고    scopus 로고
    • Control of lymphocyte development by nuclear factor-κB
    • Siebenlist, U., Brown, K., and Claudio, E. 2005. Control of lymphocyte development by nuclear factor-κB. Nat. Rev. Immunol. 5: 435-445.
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 435-445
    • Siebenlist, U.1    Brown, K.2    Claudio, E.3
  • 28
  • 29
    • 0043268731 scopus 로고    scopus 로고
    • TCR-induced NF-κB activation: A crucial role for Carma1, Bcl10 and MALT1
    • Thome, M., and J. Tschopp. 2003. TCR-induced NF-κB activation: a crucial role for Carma1, Bcl10 and MALT1. Trends Immunol. 24: 419-424.
    • (2003) Trends Immunol , vol.24 , pp. 419-424
    • Thome, M.1    Tschopp, J.2
  • 30
    • 0346993668 scopus 로고    scopus 로고
    • CD3/CD28 costimulation-induced NF-κB activation is mediated by recruitment of protein kinase C-θ, Bcl10, and IκB kinase β to the immunological synapse through CARMA1
    • Wang, D., R. Matsumoto, Y. You, T. Che, X. Y. Lin, S. L. Gaffen, and X. Lin. 2004. CD3/CD28 costimulation-induced NF-κB activation is mediated by recruitment of protein kinase C-θ, Bcl10, and IκB kinase β to the immunological synapse through CARMA1. Mol. Cell. Biol. 24: 164-171.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 164-171
    • Wang, D.1    Matsumoto, R.2    You, Y.3    Che, T.4    Lin, X.Y.5    Gaffen, S.L.6    Lin, X.7
  • 31
    • 33645975534 scopus 로고    scopus 로고
    • Deciphering the pathway from the TCR to NF-κB
    • Weil, R., and A. Israel. 2006. Deciphering the pathway from the TCR to NF-κB. Cell Death Diff. 13: 826-833.
    • (2006) Cell Death Diff , vol.13 , pp. 826-833
    • Weil, R.1    Israel, A.2
  • 32
    • 15944410614 scopus 로고    scopus 로고
    • PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation
    • Lee, K. Y., F. D'Acquisto, M. S. Hayden, J. H. Shim, and S. Ghosh. 2005. PDK1 nucleates T cell receptor-induced signaling complex for NF-κB activation. Science 308: 114-118.
    • (2005) Science , vol.308 , pp. 114-118
    • Lee, K.Y.1    D'Acquisto, F.2    Hayden, M.S.3    Shim, J.H.4    Ghosh, S.5
  • 33
    • 28844499919 scopus 로고    scopus 로고
    • Phosphorylation of CARMA1 plays a critical role in T cell receptor-mediated NF-κB activation
    • Matsumoto, R., D. Wang, M. Blonska, H. Li, M. Kobayashi, B. Pappu, Y. Chen, D. Wang, and X. Lin. 2005. Phosphorylation of CARMA1 plays a critical role in T cell receptor-mediated NF-κB activation. Immunity 23: 575-585.
    • (2005) Immunity , vol.23 , pp. 575-585
    • Matsumoto, R.1    Wang, D.2    Blonska, M.3    Li, H.4    Kobayashi, M.5    Pappu, B.6    Chen, Y.7    Wang, D.8    Lin, X.9
  • 34
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • Hayden, M. S., and S. Ghosh. 2004. Signaling to NF-κB. Genes Dev. 18: 2195-2224.
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 35
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signaling in the NF-κB pathway
    • Chen, Z. J. 2005. Ubiquitin signaling in the NF-κB pathway. Nat. Cell Biol. 7: 758-765.
    • (2005) Nat. Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 36
    • 0020601431 scopus 로고
    • Antigen recognition by H-2-restricted T cells. I. Cell-free antigen processing
    • Shimonkevitz, R., J. Kappler, P. Marrack, and H. Grey. 1983. Antigen recognition by H-2-restricted T cells. I. Cell-free antigen processing. J. Exp. Med. 158: 303-316.
    • (1983) J. Exp. Med , vol.158 , pp. 303-316
    • Shimonkevitz, R.1    Kappler, J.2    Marrack, P.3    Grey, H.4
  • 37
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti, I., G. Migliorati, M. C. Pagliacci, F. Grignani, and C. Riccardi. 1991. A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J. Immunol. Methods 139: 271-279.
    • (1991) J. Immunol. Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 38
    • 0029037960 scopus 로고
    • Improved version of a human CD2 minigene based vector for T cell-specific expression in transgenic mice
    • Zhumabekov, T., P. Corbella, M. Tolaini, and D. Kioussis. 1995. Improved version of a human CD2 minigene based vector for T cell-specific expression in transgenic mice. J. Immunol. Methods 185: 133-140.
    • (1995) J. Immunol. Methods , vol.185 , pp. 133-140
    • Zhumabekov, T.1    Corbella, P.2    Tolaini, M.3    Kioussis, D.4
  • 39
    • 0035861546 scopus 로고    scopus 로고
    • The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism
    • Shohat, G., T. Spivak-Kroizman, O. Cohen, S. Bialik, G. Shani, H. Berrisi, M. Eisenstein, and A. Kimchi. 2001. The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism. J. Biol. Chem. 276: 47460-47467.
    • (2001) J. Biol. Chem , vol.276 , pp. 47460-47467
    • Shohat, G.1    Spivak-Kroizman, T.2    Cohen, O.3    Bialik, S.4    Shani, G.5    Berrisi, H.6    Eisenstein, M.7    Kimchi, A.8
  • 40
    • 33845984960 scopus 로고    scopus 로고
    • Control of death-associated protein kinase (DAPK) activity by phosphorylation and proteasomal degradation
    • Jin, Y., E. K. Blue, and P. J. Gallagher. 2006. Control of death-associated protein kinase (DAPK) activity by phosphorylation and proteasomal degradation. J. Biol. Chem. 281: 39033-39040.
    • (2006) J. Biol. Chem , vol.281 , pp. 39033-39040
    • Jin, Y.1    Blue, E.K.2    Gallagher, P.J.3
  • 41
    • 29644433255 scopus 로고    scopus 로고
    • Death-associated protein kinase is activated by dephosphorylation in response to cerebral ischemia
    • Shamloo, M., L. Soriano, T. Wieloch, K. Nikolich, R. Urfer, R., and D. Oksenberg. 2005. Death-associated protein kinase is activated by dephosphorylation in response to cerebral ischemia. J. Biol. Chem. 280: 42290-42299.
    • (2005) J. Biol. Chem , vol.280 , pp. 42290-42299
    • Shamloo, M.L.1    Soriano, T.2    Wieloch, K.3    Nikolich, R.4    Urfer, R.5    Oksenberg, D.6
  • 42
    • 2942564711 scopus 로고    scopus 로고
    • Tumor necrosis factor α-induced apoptosis requires p73 and c-ABL activation downstream of RB degradation
    • Chau, B. N., T. T. Chen, Y. Y. Wan, J. DeGregori, and J. Y. Wang. 2004. Tumor necrosis factor α-induced apoptosis requires p73 and c-ABL activation downstream of RB degradation. Mol. Cell. Biol. 24: 4438-4447.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 4438-4447
    • Chau, B.N.1    Chen, T.T.2    Wan, Y.Y.3    DeGregori, J.4    Wang, J.Y.5
  • 43
    • 4544374632 scopus 로고    scopus 로고
    • Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions
    • Shani, G., L. Marash, D. Gozuacik, S. Bialik, L. Teitelbaum, G. Shohat, and A. Kimchi. 2004. Death-associated protein kinase phosphorylates ZIP kinase, forming a unique kinase hierarchy to activate its cell death functions. Mol. Cell. Biol. 24: 8611-8626.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 8611-8626
    • Shani, G.1    Marash, L.2    Gozuacik, D.3    Bialik, S.4    Teitelbaum, L.5    Shohat, G.6    Kimchi, A.7
  • 44
    • 0037033026 scopus 로고    scopus 로고
    • A death-associated protein kinase (DAPK)-interacting protein, DIP-1, is an E3 ubiquitin ligase that promotes tumor necrosis factor-induced apoptosis and regulates the cellular levels of DAPK
    • Jin, Y., E. K. Blue, S. Dixon, Z. Shao, and P. J. Gallagher. 2002. A death-associated protein kinase (DAPK)-interacting protein, DIP-1, is an E3 ubiquitin ligase that promotes tumor necrosis factor-induced apoptosis and regulates the cellular levels of DAPK. J. Biol. Chem. 277: 46980-46986.
    • (2002) J. Biol. Chem , vol.277 , pp. 46980-46986
    • Jin, Y.1    Blue, E.K.2    Dixon, S.3    Shao, Z.4    Gallagher, P.J.5
  • 46
    • 34249717858 scopus 로고    scopus 로고
    • Regulation of death-associated protein kinase: Stabilization by HSP90 heterocomplexes
    • Zhang, L., K. P. Nephew, and P. J. Gallagher. 2007. Regulation of death-associated protein kinase: stabilization by HSP90 heterocomplexes. J. Biol. Chem. 282: 11795-11804.
    • (2007) J. Biol. Chem , vol.282 , pp. 11795-11804
    • Zhang, L.1    Nephew, K.P.2    Gallagher, P.J.3
  • 47
    • 34447132228 scopus 로고    scopus 로고
    • Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis
    • Lin, Y., C. Stevens, and T. Hupp. 2007. Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis. J. Biol. Chem. 282: 16792-16802.
    • (2007) J. Biol. Chem , vol.282 , pp. 16792-16802
    • Lin, Y.1    Stevens, C.2    Hupp, T.3
  • 48
    • 33744959237 scopus 로고    scopus 로고
    • Transgenic drak2 overexpression in mice leads to increased T cell apoptosis and compromised memory T cell development
    • Mao, J., X. Qiao, H. Luo, and J. Wu. 2006. Transgenic drak2 overexpression in mice leads to increased T cell apoptosis and compromised memory T cell development. J. Biol. Chem. 281: 12587-12595.
    • (2006) J. Biol. Chem , vol.281 , pp. 12587-12595
    • Mao, J.1    Qiao, X.2    Luo, H.3    Wu, J.4
  • 49
    • 10344250951 scopus 로고    scopus 로고
    • A deficiency in Drak2 results in a T cell hypersensitivity and an unexpected resistance to autoimmunity
    • McGargill, M. A., B. G. Wen, C. M. Walsh, and S. M. Hedrick. 2004. A deficiency in Drak2 results in a T cell hypersensitivity and an unexpected resistance to autoimmunity. Immunity 21: 781-791.
    • (2004) Immunity , vol.21 , pp. 781-791
    • McGargill, M.A.1    Wen, B.G.2    Walsh, C.M.3    Hedrick, S.M.4
  • 50
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., R. P. Trible, and L. E. Samelson. 1998. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 9: 239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 52
    • 9644268146 scopus 로고    scopus 로고
    • Lipid rafts and the initiation of T cell receptor signaling
    • He, H. T., A. Lellouch, and D. Marguet. 2005. Lipid rafts and the initiation of T cell receptor signaling. Semin. Immunol. 17: 23-33.
    • (2005) Semin. Immunol , vol.17 , pp. 23-33
    • He, H.T.1    Lellouch, A.2    Marguet, D.3
  • 54
    • 0030012566 scopus 로고    scopus 로고
    • T-cell receptor stimulation elicits an early phase of activation and a later phase of deactivation of the transcription factor NFAT1
    • Loh, C., J. A. Carew, J. Kim, P. G. Hogan, and A. Rao. 1996. T-cell receptor stimulation elicits an early phase of activation and a later phase of deactivation of the transcription factor NFAT1. Mol. Cell. Biol. 16: 3945-3954.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 3945-3954
    • Loh, C.1    Carew, J.A.2    Kim, J.3    Hogan, P.G.4    Rao, A.5
  • 55
    • 61849099638 scopus 로고    scopus 로고
    • NFATc is a target of p38 mitogen activated protein kinase in T cells
    • Wu, C. C., S. C. Hsu, H. M. Shih, and M. Z. Lai. 2003. NFATc is a target of p38 mitogen activated protein kinase in T cells. Mol. Cell. Biol. 23: 8442-6454.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 8442-6454
    • Wu, C.C.1    Hsu, S.C.2    Shih, H.M.3    Lai, M.Z.4


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