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Volumn 29, Issue 4, 2010, Pages 333-342

Abelson Virus Transformation Prevents TRAIL Expression by Inhibiting FoxO3a and NF-κB

Author keywords

Abelson murine leukemia virus; FoxO3a; NF kappaB; pro B cell leukemia; TRAIL

Indexed keywords

FORKHEAD TRANSCRIPTION FACTOR; FOXO3 PROTEIN, MOUSE; I KAPPA B KINASE; IMATINIB; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PIPERAZINE DERIVATIVE; PROTEIN KINASE B; PROTEIN KINASE INHIBITOR; PYRIMIDINE DERIVATIVE; TNFSF10 PROTEIN, MOUSE; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND;

EID: 77956052321     PISSN: 10168478     EISSN: 02191032     Source Type: Journal    
DOI: 10.1007/s10059-010-0029-8     Document Type: Article
Times cited : (8)

References (53)
  • 1
    • 0014837635 scopus 로고
    • Lymphosarcoma: virus-induced thymic-independent disease in mice.
    • Abelson, H.T., Rabstein, L.S., Lymphosarcoma: virus-induced thymic-independent disease in mice. Cancer Res. 30 (1970), 2213–2222.
    • (1970) Cancer Res. , vol.30 , pp. 2213-2222
    • Abelson, H.T.1    Rabstein, L.S.2
  • 2
    • 0036280235 scopus 로고    scopus 로고
    • Bcr-Abl variants: biological and clinical aspects.
    • Advani, A.S., Pendergast, A.M., Bcr-Abl variants: biological and clinical aspects. Leuk. Res. 26 (2002), 713–720.
    • (2002) Leuk. Res. , vol.26 , pp. 713-720
    • Advani, A.S.1    Pendergast, A.M.2
  • 4
    • 44049091757 scopus 로고    scopus 로고
    • Foxo1 directly regulates the transcription of recombination-activating genes during B cell development.
    • Amin, R.H., Schlissel, M.S., Foxo1 directly regulates the transcription of recombination-activating genes during B cell development. Nat. Immunol. 9 (2008), 613–622.
    • (2008) Nat. Immunol. , vol.9 , pp. 613-622
    • Amin, R.H.1    Schlissel, M.S.2
  • 5
    • 0035883162 scopus 로고    scopus 로고
    • Disruption of NF-kappaB signaling reveals a novel role for NF-kappaB in the regulation of TNF-related apoptosis-inducing ligand expression.
    • Baetu, T.M., Kwon, H., Sharma, S., Grandvaux, N., Hiscott, J., Disruption of NF-kappaB signaling reveals a novel role for NF-kappaB in the regulation of TNF-related apoptosis-inducing ligand expression. J. Immunol. 167 (2001), 3164–3173.
    • (2001) J. Immunol. , vol.167 , pp. 3164-3173
    • Baetu, T.M.1    Kwon, H.2    Sharma, S.3    Grandvaux, N.4    Hiscott, J.5
  • 6
    • 0032213263 scopus 로고    scopus 로고
    • IL-7 reconstitutes multiple aspects of v-Abl-mediated signaling.
    • Banerjee, A., Rothman, P., IL-7 reconstitutes multiple aspects of v-Abl-mediated signaling. J. Immunol. 161 (1998), 4611–4617.
    • (1998) J. Immunol. , vol.161 , pp. 4611-4617
    • Banerjee, A.1    Rothman, P.2
  • 7
    • 0033595011 scopus 로고    scopus 로고
    • Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1.
    • Biggs, W.H.3rd, Meisenhelder, J., Hunter, T., Cavenee, W.K., Arden, K.C., Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1. Proc. Natl. Acad. Sci. USA 96 (1999), 7421–7426.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7421-7426
    • Biggs, W.H.1    Meisenhelder, J.2    Hunter, T.3    Cavenee, W.K.4    Arden, K.C.5
  • 8
    • 0035135841 scopus 로고    scopus 로고
    • Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a).
    • Brunet, A., Park, J., Tran, H., Hu, L.S., Hemmings, B.A., Greenberg, M.E., Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol. Cell. Biol. 21 (2001), 952–965.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 952-965
    • Brunet, A.1    Park, J.2    Tran, H.3    Hu, L.S.4    Hemmings, B.A.5    Greenberg, M.E.6
  • 9
    • 0036022407 scopus 로고    scopus 로고
    • Initiator caspases in apoptosis signaling pathways.
    • Chen, M., Wang, J., Initiator caspases in apoptosis signaling pathways. Apoptosis 7 (2002), 313–319.
    • (2002) Apoptosis , vol.7 , pp. 313-319
    • Chen, M.1    Wang, J.2
  • 10
    • 0344553913 scopus 로고
    • An active v-abl protein tyrosine kinase blocks immunoglobulin light-chain gene rearrangement.
    • Chen, Y.Y., Wang, L.C., Huang, M.S., Rosenberg, N., An active v-abl protein tyrosine kinase blocks immunoglobulin light-chain gene rearrangement. Genes Dev. 8 (1994), 688–697.
    • (1994) Genes Dev. , vol.8 , pp. 688-697
    • Chen, Y.Y.1    Wang, L.C.2    Huang, M.S.3    Rosenberg, N.4
  • 11
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: roles in cell survival and oncogenesis.
    • Cory, S., Huang, D.C., Adams, J.M., The Bcl-2 family: roles in cell survival and oncogenesis. Oncogene 22 (2003), 8590–8607.
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.2    Adams, J.M.3
  • 12
    • 0036141029 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO.
    • Deng, Y., Lin, Y., Wu, X., TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO. Genes Dev. 16 (2002), 33–45.
    • (2002) Genes Dev. , vol.16 , pp. 33-45
    • Deng, Y.1    Lin, Y.2    Wu, X.3
  • 15
    • 0028982230 scopus 로고
    • Bcl-xL rescues WEHI 231 B lymphocytes from oxidant-mediated death following diverse apoptotic stimuli.
    • Fang, W., Rivard, J.J., Ganser, J.A., LeBien, T.W., Nath, K.A., Mueller, D.L., Behrens, T.W., Bcl-xL rescues WEHI 231 B lymphocytes from oxidant-mediated death following diverse apoptotic stimuli. J. Immunol. 155 (1995), 66–75.
    • (1995) J. Immunol. , vol.155 , pp. 66-75
    • Fang, W.1    Rivard, J.J.2    Ganser, J.A.3    LeBien, T.W.4    Nath, K.A.5    Mueller, D.L.6    Behrens, T.W.7
  • 16
    • 0037975597 scopus 로고    scopus 로고
    • Cytokines and BCR-ABL mediate suppression of TRAIL-induced apoptosis through inhibition of forkhead FOXO3a transcription factor.
    • Ghaffari, S., Jagani, Z., Kitidis, C., Lodish, H.F., Khosravi-Far, R., Cytokines and BCR-ABL mediate suppression of TRAIL-induced apoptosis through inhibition of forkhead FOXO3a transcription factor. Proc. Natl. Acad. Sci. USA 100 (2003), 6523–6528.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6523-6528
    • Ghaffari, S.1    Jagani, Z.2    Kitidis, C.3    Lodish, H.F.4    Khosravi-Far, R.5
  • 17
    • 0024603007 scopus 로고
    • Multiple steps are required for the induction of tumors by Abelson murine leukemia virus.
    • Green, P.L., Kaehler, D.A., Bennett, L.M., Risser, R., Multiple steps are required for the induction of tumors by Abelson murine leukemia virus. J. Virol. 63 (1989), 1989–1994.
    • (1989) J. Virol. , vol.63 , pp. 1989-1994
    • Green, P.L.1    Kaehler, D.A.2    Bennett, L.M.3    Risser, R.4
  • 18
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKK-related kinases.
    • Hacker, H., Karin, M., Regulation and function of IKK and IKK-related kinases. Sci STKE, 2006, 2006, re13.
    • (2006) Sci STKE , vol.2006 , pp. re13
    • Hacker, H.1    Karin, M.2
  • 19
    • 40049090339 scopus 로고    scopus 로고
    • Gene expression analysis of BCR/ ABL1-dependent transcriptional response reveals enrichment for genes involved in negative feedback regulation.
    • Hakansson, P., Nilsson, B., Andersson, A., Lassen, C., Gullberg, U., Fioretos, T., Gene expression analysis of BCR/ ABL1-dependent transcriptional response reveals enrichment for genes involved in negative feedback regulation. Genes Chromosomes Cancer 47 (2008), 267–275.
    • (2008) Genes Chromosomes Cancer , vol.47 , pp. 267-275
    • Hakansson, P.1    Nilsson, B.2    Andersson, A.3    Lassen, C.4    Gullberg, U.5    Fioretos, T.6
  • 20
    • 38549132880 scopus 로고    scopus 로고
    • The role of TRAIL death receptors in the treatment of hematological malignancies.
    • Henson, E.S., Johnston, J.B., Gibson, S.B., The role of TRAIL death receptors in the treatment of hematological malignancies. Leuk. Lymphoma 49 (2008), 27–35.
    • (2008) Leuk. Lymphoma , vol.49 , pp. 27-35
    • Henson, E.S.1    Johnston, J.B.2    Gibson, S.B.3
  • 21
    • 1542267804 scopus 로고    scopus 로고
    • Disruption of forkhead transcription factor (FOXO) family members in mice reveals their functional diversification.
    • Hosaka, T., Biggs, W.H.3rd, Tieu, D., Boyer, A.D., Varki, N.M., Cavenee, W.K., Arden, K.C., Disruption of forkhead transcription factor (FOXO) family members in mice reveals their functional diversification. Proc. Natl. Acad. Sci. USA 101 (2004), 2975–2980.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2975-2980
    • Hosaka, T.1    Biggs, W.H.2    Tieu, D.3    Boyer, A.D.4    Varki, N.M.5    Cavenee, W.K.6    Arden, K.C.7
  • 23
    • 34548289502 scopus 로고    scopus 로고
    • Dynamic FoxO transcription factors.
    • Huang, H., Tindall, D.J., Dynamic FoxO transcription factors. J. Cell Sci. 120 (2007), 2479–2487.
    • (2007) J. Cell Sci. , vol.120 , pp. 2479-2487
    • Huang, H.1    Tindall, D.J.2
  • 24
    • 0040189996 scopus 로고    scopus 로고
    • A dominant negative Fas-associated death domain protein mutant inhibits proliferation and leads to impaired calcium mobilization in both T-cells and fibroblasts.
    • Hueber, A.O., Zornig, M., Bernard, A.M., Chautan, M., Evan, G., A dominant negative Fas-associated death domain protein mutant inhibits proliferation and leads to impaired calcium mobilization in both T-cells and fibroblasts. J. Biol. Chem. 275 (2000), 10453–10462.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10453-10462
    • Hueber, A.O.1    Zornig, M.2    Bernard, A.M.3    Chautan, M.4    Evan, G.5
  • 25
    • 0035933115 scopus 로고    scopus 로고
    • T cell-specific FADD-deficient mice: FADD is required for early T cell development.
    • Kabra, N.H., Kang, C., Hsing, L.C., Zhang, J., Winoto, A., T cell-specific FADD-deficient mice: FADD is required for early T cell development. Proc. Natl. Acad. Sci. USA 98 (2001), 6307–6312.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6307-6312
    • Kabra, N.H.1    Kang, C.2    Hsing, L.C.3    Zhang, J.4    Winoto, A.5
  • 26
    • 0035984188 scopus 로고    scopus 로고
    • Inactivation of NF-kappaB-dependent cell survival, a novel mechanism for the proapoptotic function of c-Abl.
    • Kawai, H., Nie, L., Yuan, Z.M., Inactivation of NF-kappaB-dependent cell survival, a novel mechanism for the proapoptotic function of c-Abl. Mol. Cell. Biol. 22 (2002), 6079–6088.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6079-6088
    • Kawai, H.1    Nie, L.2    Yuan, Z.M.3
  • 27
    • 35548932785 scopus 로고    scopus 로고
    • Active FKHRL1 overcomes imatinib resistance in chronic myelogenous leukemia-derived cell lines via the production of tumor necrosis factor-related apoptosis-inducing ligand.
    • Kikuchi, S., Nagai, T., Kunitama, M., Kirito, K., Ozawa, K., Komatsu, N., Active FKHRL1 overcomes imatinib resistance in chronic myelogenous leukemia-derived cell lines via the production of tumor necrosis factor-related apoptosis-inducing ligand. Cancer Sci. 98 (2007), 1949–1958.
    • (2007) Cancer Sci. , vol.98 , pp. 1949-1958
    • Kikuchi, S.1    Nagai, T.2    Kunitama, M.3    Kirito, K.4    Ozawa, K.5    Komatsu, N.6
  • 28
    • 0028299725 scopus 로고
    • The v-abl tyrosine kinase negatively regulates NF-kappa B/Rel factors and blocks kappa gene transcription in pre-B lymphocytes.
    • Klug, C.A., Gerety, S.J., Shah, P.C., Chen, Y.Y., Rice, N.R., Rosenberg, N., Singh, H., The v-abl tyrosine kinase negatively regulates NF-kappa B/Rel factors and blocks kappa gene transcription in pre-B lymphocytes. Genes Dev. 8 (1994), 678–687.
    • (1994) Genes Dev. , vol.8 , pp. 678-687
    • Klug, C.A.1    Gerety, S.J.2    Shah, P.C.3    Chen, Y.Y.4    Rice, N.R.5    Rosenberg, N.6    Singh, H.7
  • 29
    • 0037458609 scopus 로고    scopus 로고
    • A member of Forkhead transcription factor FKHRL1 is a downstream effector of STI571-induced cell cycle arrest in BCR-ABL-expressing cells.
    • Komatsu, N., Watanabe, T., Uchida, M., Mori, M., Kirito, K., Kikuchi, S., Liu, Q., Tauchi, T., Miyazawa, K., Endo, H., et al. A member of Forkhead transcription factor FKHRL1 is a downstream effector of STI571-induced cell cycle arrest in BCR-ABL-expressing cells. J. Biol. Chem. 278 (2003), 6411–6419.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6411-6419
    • Komatsu, N.1    Watanabe, T.2    Uchida, M.3    Mori, M.4    Kirito, K.5    Kikuchi, S.6    Liu, Q.7    Tauchi, T.8    Miyazawa, K.9    Endo, H.10
  • 30
    • 41049112098 scopus 로고    scopus 로고
    • TRAIL and cancer therapy.
    • Kruyt, F.A., TRAIL and cancer therapy. Cancer Lett. 263 (2008), 14–25.
    • (2008) Cancer Lett. , vol.263 , pp. 14-25
    • Kruyt, F.A.1
  • 32
    • 0020464847 scopus 로고
    • Continuing kappa-gene rearrangement in a cell line transformed by Abelson murine leukemia virus.
    • Lewis, S., Rosenberg, N., Alt, F., Baltimore, D., Continuing kappa-gene rearrangement in a cell line transformed by Abelson murine leukemia virus. Cell 30 (1982), 807–816.
    • (1982) Cell , vol.30 , pp. 807-816
    • Lewis, S.1    Rosenberg, N.2    Alt, F.3    Baltimore, D.4
  • 33
    • 0032402316 scopus 로고    scopus 로고
    • Modulation of the IL-7 dose-response threshold during pro-B cell differentiation is dependent on pre-B cell receptor expression.
    • Marshall, A.J., Fleming, H.E., Wu, G.E., Paige, C.J., Modulation of the IL-7 dose-response threshold during pro-B cell differentiation is dependent on pre-B cell receptor expression. J. Immunol. 161 (1998), 6038–6045.
    • (1998) J. Immunol. , vol.161 , pp. 6038-6045
    • Marshall, A.J.1    Fleming, H.E.2    Wu, G.E.3    Paige, C.J.4
  • 34
    • 0028694423 scopus 로고
    • Regulation of protein activities by fusion to steroid binding domains.
    • Mattioni, T., Louvion, J.F., Picard, D., Regulation of protein activities by fusion to steroid binding domains. Methods Cell Biol. 43 Pt A (1994), 335–352.
    • (1994) Methods Cell Biol. , vol.43 Pt A , pp. 335-352
    • Mattioni, T.1    Louvion, J.F.2    Picard, D.3
  • 35
    • 0034951384 scopus 로고    scopus 로고
    • STI571: targeting BCR-ABL as therapy for CML.
    • Mauro, M.J., Druker, B.J., STI571: targeting BCR-ABL as therapy for CML. Oncologist 6 (2001), 233–238.
    • (2001) Oncologist , vol.6 , pp. 233-238
    • Mauro, M.J.1    Druker, B.J.2
  • 36
    • 0037033005 scopus 로고    scopus 로고
    • FOXO proteins regulate tumor necrosis factor-related apoptosis inducing ligand expression. Implications for PTEN mutation in prostate cancer.
    • Modur, V., Nagarajan, R., Evers, B.M., Milbrandt, J., FOXO proteins regulate tumor necrosis factor-related apoptosis inducing ligand expression. Implications for PTEN mutation in prostate cancer. J. Biol. Chem. 277 (2002), 47928–47937.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47928-47937
    • Modur, V.1    Nagarajan, R.2    Evers, B.M.3    Milbrandt, J.4
  • 37
    • 0037232230 scopus 로고    scopus 로고
    • A small molecule Abl kinase inhibitor induces differentiation of Abelson virus-transformed pre-B cell lines.
    • Muljo, S.A., Schlissel, M.S., A small molecule Abl kinase inhibitor induces differentiation of Abelson virus-transformed pre-B cell lines. Nat. Immunol. 4 (2003), 31–37.
    • (2003) Nat. Immunol. , vol.4 , pp. 31-37
    • Muljo, S.A.1    Schlissel, M.S.2
  • 38
    • 0032472916 scopus 로고    scopus 로고
    • A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes.
    • Newton, K., Harris, A.W., Bath, M.L., Smith, K.G., Strasser, A., A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes. Embo J. 17 (1998), 706–718.
    • (1998) Embo J. , vol.17 , pp. 706-718
    • Newton, K.1    Harris, A.W.2    Bath, M.L.3    Smith, K.G.4    Strasser, A.5
  • 39
    • 27544432516 scopus 로고    scopus 로고
    • Nonapoptotic functions of FADD-binding death receptors and their signaling molecules.
    • Park, S.M., Schickel, R., Peter, M.E., Nonapoptotic functions of FADD-binding death receptors and their signaling molecules. Curr. Opin. Cell Biol. 17 (2005), 610–616.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 610-616
    • Park, S.M.1    Schickel, R.2    Peter, M.E.3
  • 40
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-kappaB and IKK function.
    • Perkins, N.D., Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat. Rev. Mol. Cell Biol. 8 (2007), 49–62.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 41
    • 0036651790 scopus 로고    scopus 로고
    • A novel mechanism of gene regulation and tumor suppression by the transcription factor FKHR.
    • Ramaswamy, S., Nakamura, N., Sansal, I., Bergeron, L., Sellers, W.R., A novel mechanism of gene regulation and tumor suppression by the transcription factor FKHR. Cancer Cell 2 (2002), 81–91.
    • (2002) Cancer Cell , vol.2 , pp. 81-91
    • Ramaswamy, S.1    Nakamura, N.2    Sansal, I.3    Bergeron, L.4    Sellers, W.R.5
  • 42
    • 0036130889 scopus 로고    scopus 로고
    • Apoptosis and cancer: when BAX is TRAILing away.
    • Roth, W., Reed, J.C., Apoptosis and cancer: when BAX is TRAILing away. Nat. Med. 8 (2002), 216–218.
    • (2002) Nat. Med. , vol.8 , pp. 216-218
    • Roth, W.1    Reed, J.C.2
  • 45
    • 0022930702 scopus 로고
    • Inducibility of kappa immunoglobulin enhancer-binding protein Nf-kappa B by a posttranslational mechanism.
    • Sen, R., Baltimore, D., Inducibility of kappa immunoglobulin enhancer-binding protein Nf-kappa B by a posttranslational mechanism. Cell 47 (1986), 921–928.
    • (1986) Cell , vol.47 , pp. 921-928
    • Sen, R.1    Baltimore, D.2
  • 46
    • 0033605572 scopus 로고    scopus 로고
    • Overexpression of RelA causes G1 arrest and apoptosis in a pro-B cell line.
    • Sheehy, A.M., Schlissel, M.S., Overexpression of RelA causes G1 arrest and apoptosis in a pro-B cell line. J. Biol. Chem. 274 (1999), 8708–8716.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8708-8716
    • Sheehy, A.M.1    Schlissel, M.S.2
  • 48
    • 34548686289 scopus 로고    scopus 로고
    • Apoptosis signaling pathways and lymphocyte homeostasis.
    • Xu, G., Shi, Y., Apoptosis signaling pathways and lymphocyte homeostasis. Cell Res. 17 (2007), 759–771.
    • (2007) Cell Res. , vol.17 , pp. 759-771
    • Xu, G.1    Shi, Y.2
  • 49
    • 14644437742 scopus 로고    scopus 로고
    • Mechanisms of resistance to TRAIL-induced apoptosis in cancer.
    • Zhang, L., Fang, B., Mechanisms of resistance to TRAIL-induced apoptosis in cancer. Cancer Gene Ther. 12 (2005), 228–237.
    • (2005) Cancer Gene Ther. , vol.12 , pp. 228-237
    • Zhang, L.1    Fang, B.2
  • 50
    • 0030001051 scopus 로고    scopus 로고
    • A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis.
    • Zhang, J., Winoto, A., A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis. Mol. Cell. Biol. 16 (1996), 2756–2763.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2756-2763
    • Zhang, J.1    Winoto, A.2
  • 51
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1.
    • Zhang, J., Cado, D., Chen, A., Kabra, N.H., Winoto, A., Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 392 (1998), 296–300.
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 52
    • 0035839640 scopus 로고    scopus 로고
    • FADD-deficient T cells exhibit a disaccord in regulation of the cell cycle machinery.
    • Zhang, J., Kabra, N.H., Cado, D., Kang, C., Winoto, A., FADD-deficient T cells exhibit a disaccord in regulation of the cell cycle machinery. J. Biol. Chem. 276 (2001), 29815–29818.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29815-29818
    • Zhang, J.1    Kabra, N.H.2    Cado, D.3    Kang, C.4    Winoto, A.5
  • 53
    • 0033603435 scopus 로고    scopus 로고
    • Signaling pathways activated by oncogenic forms of Abl tyrosine kinase.
    • Zou, X., Calame, K., Signaling pathways activated by oncogenic forms of Abl tyrosine kinase. J. Biol. Chem. 274 (1999), 18141–18144.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18141-18144
    • Zou, X.1    Calame, K.2


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