메뉴 건너뛰기




Volumn 29, Issue 8, 2012, Pages 901-913

BTG2 suppresses cancer cell migration through inhibition of Src-FAK signaling by downregulation of reactive oxygen species generation in mitochondria

Author keywords

BTG2 TIS21 PC3; FAK; Mitochondria; ROS; Src

Indexed keywords

B CELL TRANSLOCATION GENE 2; CATALASE; FOCAL ADHESION KINASE; MANGANESE SUPEROXIDE DISMUTASE; MESSENGER RNA; PROTEIN TYROSINE KINASE; REACTIVE OXYGEN METABOLITE; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG; UVOMORULIN; BTG2 PROTEIN, HUMAN; FOCAL ADHESION KINASE 1; IMMEDIATE EARLY PROTEIN; PTK2 PROTEIN, HUMAN;

EID: 84872836189     PISSN: 02620898     EISSN: 15737276     Source Type: Journal    
DOI: 10.1007/s10585-012-9479-z     Document Type: Article
Times cited : (40)

References (41)
  • 1
    • 0029069922 scopus 로고
    • Differential expression of TIS21 and TIS1 genes in the various organs of Balb/c mice, thymic carcinoma tissues and human cancer cell lines
    • 7768965 10.1007/BF01209594 1:CAS:528:DyaK2MXnt1Okurs%3D
    • Lim IK, Lee MS, Lee SH, Kim NK, Jou I, Seo JS, Park SC (1995) Differential expression of TIS21 and TIS1 genes in the various organs of Balb/c mice, thymic carcinoma tissues and human cancer cell lines. J Cancer Res Clin Oncol 121:279-284
    • (1995) J Cancer Res Clin Oncol , vol.121 , pp. 279-284
    • Lim, I.K.1    Lee, M.S.2    Lee, S.H.3    Kim, N.K.4    Jou, I.5    Seo, J.S.6    Park, S.C.7
  • 2
    • 0034904215 scopus 로고    scopus 로고
    • Antiproliferative B cell translocation gene 2 protein is down-regulated post-transcriptionally as an early event in prostate carcinogenesis
    • 11470758 10.1093/carcin/22.8.1271 1:CAS:528:DC%2BD3MXlvVSqu7w%3D
    • Ficazzola MA, Fraiman M, Gitlin J, Woo K, Melamed J, Rubin MA, Walden PD (2001) Antiproliferative B cell translocation gene 2 protein is down-regulated post-transcriptionally as an early event in prostate carcinogenesis. Carcinogenesis 22:1271-1279
    • (2001) Carcinogenesis , vol.22 , pp. 1271-1279
    • Ficazzola, M.A.1    Fraiman, M.2    Gitlin, J.3    Woo, K.4    Melamed, J.5    Rubin, M.A.6    Walden, P.D.7
  • 3
    • 1642391547 scopus 로고    scopus 로고
    • Impaired expression of the cell cycle regulator BTG2 is common in clear cell renal cell carcinoma
    • 14996721 10.1158/0008-5472.CAN-03-1687 1:CAS:528:DC%2BD2cXhslektbg%3D
    • Struckmann K, Schraml P, Simon R, Elmenhorst K, Mirlacher M, Kononen J, Moch H (2004) Impaired expression of the cell cycle regulator BTG2 is common in clear cell renal cell carcinoma. Cancer Res 64:1632-1638
    • (2004) Cancer Res , vol.64 , pp. 1632-1638
    • Struckmann, K.1    Schraml, P.2    Simon, R.3    Elmenhorst, K.4    Mirlacher, M.5    Kononen, J.6    Moch, H.7
  • 4
    • 43949126233 scopus 로고    scopus 로고
    • TIS21 negatively regulates hepatocarcinogenesis by disruption of cyclin B1-Forkhead box M1 regulation loop
    • 18393292 10.1002/hep.22212 1:CAS:528:DC%2BD1cXmvVChs7c%3D
    • Park TJ, Kim JY, Oh SP, Kang SY, Kim BW, Wang HJ, Song KY, Kim HC, Lim IK (2008) TIS21 negatively regulates hepatocarcinogenesis by disruption of cyclin B1-Forkhead box M1 regulation loop. Hepatology 47:1533-1543
    • (2008) Hepatology , vol.47 , pp. 1533-1543
    • Park, T.J.1    Kim, J.Y.2    Oh, S.P.3    Kang, S.Y.4    Kim, B.W.5    Wang, H.J.6    Song, K.Y.7    Kim, H.C.8    Lim, I.K.9
  • 5
    • 0036231018 scopus 로고    scopus 로고
    • Expression of B-cell translocation gene 2 protein in normal human tissues
    • 11989967 10.1054/tice.2001.0220 1:CAS:528:DC%2BD38XjvFOjs7g%3D
    • Melamed J, Kernizan S, Walden PD (2002) Expression of B-cell translocation gene 2 protein in normal human tissues. Tissue Cell 34:28-32
    • (2002) Tissue Cell , vol.34 , pp. 28-32
    • Melamed, J.1    Kernizan, S.2    Walden, P.D.3
  • 9
    • 67650588774 scopus 로고    scopus 로고
    • Characterisation of fibronectin-mediated FAK signalling pathways in lung cancer cell migration and invasion
    • 19568240 10.1038/sj.bjc.6605154 1:CAS:528:DC%2BD1MXoslOmu7g%3D
    • Meng XN, Jin Y, Yu Y, Bai J, Liu GY, Zhu J, Zhao YZ, Wang Z, Chen F, Lee KY (2009) Characterisation of fibronectin-mediated FAK signalling pathways in lung cancer cell migration and invasion. Br J Cancer 101:327-334
    • (2009) Br J Cancer , vol.101 , pp. 327-334
    • Meng, X.N.1    Jin, Y.2    Yu, Y.3    Bai, J.4    Liu, G.Y.5    Zhu, J.6    Zhao, Y.Z.7    Wang, Z.8    Chen, F.9    Lee, K.Y.10
  • 10
    • 21744435478 scopus 로고    scopus 로고
    • The role of focal-adhesion kinase in cancer - A new therapeutic opportunity
    • 16069815 10.1038/nrc1647 1:CAS:528:DC%2BD2MXmtFOns7k%3D
    • McLean GW, Carragher NO, Avizienyte E, Evans J, Brunton VG, Frame MC (2005) The role of focal-adhesion kinase in cancer - a new therapeutic opportunity. Nat Rev Cancer 5:505-515
    • (2005) Nat Rev Cancer , vol.5 , pp. 505-515
    • McLean, G.W.1    Carragher, N.O.2    Avizienyte, E.3    Evans, J.4    Brunton, V.G.5    Frame, M.C.6
  • 11
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • 15246681 10.1016/j.bbamcr.2004.04.008 1:CAS:528:DC%2BD2cXlsFymt7o%3D
    • Schlaepfer DD, Mitra SK, Ilic D (2004) Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim Biophys Acta 1692:77-102
    • (2004) Biochim Biophys Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3
  • 12
    • 11144285417 scopus 로고    scopus 로고
    • Differential expression of protease activated receptor 1 (Par1) and pY397FAK in benign and malignant human ovarian tissue samples
    • 15455382 10.1002/ijc.20607 1:CAS:528:DC%2BD2MXhsFWj
    • Grisaru-Granovsky S, Salah Z, Maoz M, Pruss D, Beller U, Bar-Shavit R (2005) Differential expression of protease activated receptor 1 (Par1) and pY397FAK in benign and malignant human ovarian tissue samples. Int J Cancer 113:372-378
    • (2005) Int J Cancer , vol.113 , pp. 372-378
    • Grisaru-Granovsky, S.1    Salah, Z.2    Maoz, M.3    Pruss, D.4    Beller, U.5    Bar-Shavit, R.6
  • 14
    • 0028342938 scopus 로고
    • Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain
    • 8054685 1:CAS:528:DyaK2MXht12msQ%3D%3D
    • Xing Z, Chen HC, Nowlen JK, Taylor SJ, Shalloway D, Guan JL (1994) Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain. Mol Biol Cell 5:413-421
    • (1994) Mol Biol Cell , vol.5 , pp. 413-421
    • Xing, Z.1    Chen, H.C.2    Nowlen, J.K.3    Taylor, S.J.4    Shalloway, D.5    Guan, J.L.6
  • 15
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • 7509446 1:CAS:528:DyaK2cXitl2jurg%3D
    • Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, Parsons JT (1994) Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 14:1680-1688
    • (1994) Mol Cell Biol , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 16
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • 7529876 1:CAS:528:DyaK2MXjtlant7o%3D
    • Calalb MB, Polte TR, Hanks SK (1995) Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol Cell Biol 15:954-963
    • (1995) Mol Cell Biol , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 17
    • 0029834447 scopus 로고    scopus 로고
    • Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases
    • 8816475 1:CAS:528:DyaK28XlvFamurY%3D
    • Schlaepfer DD, Hunter T (1996) Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases. Mol Cell Biol 16:5623-5633
    • (1996) Mol Cell Biol , vol.16 , pp. 5623-5633
    • Schlaepfer, D.D.1    Hunter, T.2
  • 18
    • 27144547509 scopus 로고    scopus 로고
    • Action of the Src family kinase inhibitor, dasatinib (BMS-354825), on human prostate cancer cells
    • 16230377 10.1158/0008-5472.CAN-05-1731 1:CAS:528:DC%2BD2MXhtFWmu77K
    • Nam S, Kim D, Cheng JQ, Zhang S, Lee JH, Buettner R, Mirosevich J, Lee FY, Jove R (2005) Action of the Src family kinase inhibitor, dasatinib (BMS-354825), on human prostate cancer cells. Cancer Res 65:9185-9189
    • (2005) Cancer Res , vol.65 , pp. 9185-9189
    • Nam, S.1    Kim, D.2    Cheng, J.Q.3    Zhang, S.4    Lee, J.H.5    Buettner, R.6    Mirosevich, J.7    Lee, F.Y.8    Jove, R.9
  • 19
    • 33745243692 scopus 로고    scopus 로고
    • Dasatinib (BMS-354825) selectively induces apoptosis in lung cancer cells dependent on epidermal growth factor receptor signaling for survival
    • 16740687 10.1158/0008-5472.CAN-05-4620 1:CAS:528:DC%2BD28XltFyjtr8%3D
    • Song L, Morris M, Bagui T, Lee FY, Jove R, Haura EB (2006) Dasatinib (BMS-354825) selectively induces apoptosis in lung cancer cells dependent on epidermal growth factor receptor signaling for survival. Cancer Res 66:5542-5548
    • (2006) Cancer Res , vol.66 , pp. 5542-5548
    • Song, L.1    Morris, M.2    Bagui, T.3    Lee, F.Y.4    Jove, R.5    Haura, E.B.6
  • 20
    • 0027340192 scopus 로고
    • Redistribution of activated pp60c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets
    • 7680100 1:CAS:528:DyaK3sXitlSqtL8%3D
    • Clark EA, Brugge JS (1993) Redistribution of activated pp60c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets. Mol Cell Biol 13:1863-1871
    • (1993) Mol Cell Biol , vol.13 , pp. 1863-1871
    • Clark, E.A.1    Brugge, J.S.2
  • 21
    • 0027300619 scopus 로고
    • The when and how of Src regulation
    • 7685656 10.1016/0092-8674(93)90634-3 1:CAS:528:DyaK3sXkvV2msrY%3D
    • Cooper JA, Howell B (1993) The when and how of Src regulation. Cell 73:1051-1054
    • (1993) Cell , vol.73 , pp. 1051-1054
    • Cooper, J.A.1    Howell, B.2
  • 22
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • 8672527
    • Brown MT, Cooper JA (1996) Regulation, substrates and functions of src. Biochim Biophys Acta 1287:121-149
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 23
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • 9024657 10.1038/385595a0 1:CAS:528:DyaK2sXht1ymtL8%3D
    • Xu W, Harrison SC, Eck MJ (1997) Three-dimensional structure of the tyrosine kinase c-Src. Nature 385:595-602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 24
    • 22544453858 scopus 로고    scopus 로고
    • Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth
    • 16024778 10.1128/MCB.25.15.6391-6403.2005 1:CAS:528:DC%2BD2MXntVShtbY%3D
    • Giannoni E, Buricchi F, Raugei G, Ramponi G, Chiarugi P (2005) Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth. Mol Cell Biol 25:6391-6403
    • (2005) Mol Cell Biol , vol.25 , pp. 6391-6403
    • Giannoni, E.1    Buricchi, F.2    Raugei, G.3    Ramponi, G.4    Chiarugi, P.5
  • 25
    • 0023755783 scopus 로고
    • Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity
    • 2463476 1:CAS:528:DyaL1cXlt1eis7o%3D
    • Gould KL, Hunter T (1988) Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity. Mol Cell Biol 8:3345-3356
    • (1988) Mol Cell Biol , vol.8 , pp. 3345-3356
    • Gould, K.L.1    Hunter, T.2
  • 26
    • 0032967101 scopus 로고    scopus 로고
    • Chemoattractant- and mitogen-induced generation of reactive oxygen species in human lymphocytes: The role of calcium
    • 10362849 10.1017/S0958067099018618 1:CAS:528:DyaK1MXktVyntL4%3D
    • Orie NN, Zidek W, Tepel M (1999) Chemoattractant- and mitogen-induced generation of reactive oxygen species in human lymphocytes: the role of calcium. Exp Physiol 84:515-520
    • (1999) Exp Physiol , vol.84 , pp. 515-520
    • Orie, N.N.1    Zidek, W.2    Tepel, M.3
  • 27
    • 0029311281 scopus 로고
    • Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
    • 7552174 10.1016/S0960-9822(95)00128-X 1:CAS:528:DyaK2MXmtlOntbg%3D
    • Rizzuto R, Brini M, Pizzo P, Murgia M, Pozzan T (1995) Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells. Curr Biol 5:635-642
    • (1995) Curr Biol , vol.5 , pp. 635-642
    • Rizzuto, R.1    Brini, M.2    Pizzo, P.3    Murgia, M.4    Pozzan, T.5
  • 28
    • 77954534974 scopus 로고    scopus 로고
    • Src redox regulation: Again in the front line
    • 20434540 10.1016/j.freeradbiomed.2010.04.025 1:CAS:528: DC%2BC3cXoslWrs7o%3D
    • Giannoni E, Taddei ML, Chiarugi P (2010) Src redox regulation: again in the front line. Free Radic Biol Med 49:516-527
    • (2010) Free Radic Biol Med , vol.49 , pp. 516-527
    • Giannoni, E.1    Taddei, M.L.2    Chiarugi, P.3
  • 29
    • 0027957613 scopus 로고
    • Synthesis, degradation, and subcellular localization of proteins encoded by the primary response genes TIS7/PC4 and TIS21/PC3
    • 8263025 10.1002/jcp.1041580125 1:CAS:528:DyaK2cXhtlSgu70%3D
    • Varnum BC, Reddy ST, Koski RA, Herschman HR (1994) Synthesis, degradation, and subcellular localization of proteins encoded by the primary response genes TIS7/PC4 and TIS21/PC3. J Cell Physiol 158:205-213
    • (1994) J Cell Physiol , vol.158 , pp. 205-213
    • Varnum, B.C.1    Reddy, S.T.2    Koski, R.A.3    Herschman, H.R.4
  • 30
    • 0033976110 scopus 로고    scopus 로고
    • Arrest of G(1)-S progression by the p53-inducible gene PC3 is Rb dependent and relies on the inhibition of cyclin D1 transcription
    • 10669755 10.1128/MCB.20.5.1797-1815.2000 1:CAS:528:DC%2BD3cXhtF2ntLs%3D
    • Guardavaccaro D, Corrente G, Covone F, Micheli L, D'Agnano I, Starace G, Caruso M, Tirone F (2000) Arrest of G(1)-S progression by the p53-inducible gene PC3 is Rb dependent and relies on the inhibition of cyclin D1 transcription. Mol Cell Biol 20:1797-1815
    • (2000) Mol Cell Biol , vol.20 , pp. 1797-1815
    • Guardavaccaro, D.1    Corrente, G.2    Covone, F.3    Micheli, L.4    D'Agnano, I.5    Starace, G.6    Caruso, M.7    Tirone, F.8
  • 31
    • 0041034370 scopus 로고    scopus 로고
    • The leukemia-associated protein Btg1 and the p53-regulated protein Btg2 interact with the homeoprotein Hoxb9 and enhance its transcriptional activation
    • 10617598 10.1074/jbc.275.1.147 1:CAS:528:DC%2BD3cXjvVGktA%3D%3D
    • Prevot D, Voeltzel T, Birot AM, Morel AP, Rostan MC, Magaud JP, Corbo L (2000) The leukemia-associated protein Btg1 and the p53-regulated protein Btg2 interact with the homeoprotein Hoxb9 and enhance its transcriptional activation. J Biol Chem 275:147-153
    • (2000) J Biol Chem , vol.275 , pp. 147-153
    • Prevot, D.1    Voeltzel, T.2    Birot, A.M.3    Morel, A.P.4    Rostan, M.C.5    Magaud, J.P.6    Corbo, L.7
  • 32
    • 79151481567 scopus 로고    scopus 로고
    • BTG2 is an LXXLL-dependent co-repressor for androgen receptor transcriptional activity
    • 21172304 10.1016/j.bbrc.2010.12.064 1:CAS:528:DC%2BC3MXhtlCrtr4%3D
    • Hu XD, Meng QH, Xu JY, Jiao Y, Ge CM, Jacob A, Wang P, Rosen EM, Fan S (2011) BTG2 is an LXXLL-dependent co-repressor for androgen receptor transcriptional activity. Biochem Biophys Res Commun 404:903-909
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 903-909
    • Hu, X.D.1    Meng, Q.H.2    Xu, J.Y.3    Jiao, Y.4    Ge, C.M.5    Jacob, A.6    Wang, P.7    Rosen, E.M.8    Fan, S.9
  • 33
    • 33745461938 scopus 로고    scopus 로고
    • Btg2 enhances retinoic acid-induced differentiation by modulating histone H4 methylation and acetylation
    • 16782888 10.1128/MCB.01360-05 1:CAS:528:DC%2BD28XmsVSlurg%3D
    • Passeri D, Marcucci A, Rizzo G, Billi M, Panigada M, Leonardi L, Tirone F, Grignani F (2006) Btg2 enhances retinoic acid-induced differentiation by modulating histone H4 methylation and acetylation. Mol Cell Biol 26:5023-5032
    • (2006) Mol Cell Biol , vol.26 , pp. 5023-5032
    • Passeri, D.1    Marcucci, A.2    Rizzo, G.3    Billi, M.4    Panigada, M.5    Leonardi, L.6    Tirone, F.7    Grignani, F.8
  • 34
    • 0035971242 scopus 로고    scopus 로고
    • Relationships of the antiproliferative proteins BTG1 and BTG2 with CAF1, the human homolog of a component of the yeast CCR4 transcriptional complex: Involvement in estrogen receptor alpha signaling pathway
    • 11136725 10.1074/jbc.M008201200
    • Prévôt D, Morel AP, Voeltzel T, Rostan MC, Rimokh R, Magaud JP, Corbo L (2001) Relationships of the antiproliferative proteins BTG1 and BTG2 with CAF1, the human homolog of a component of the yeast CCR4 transcriptional complex: involvement in estrogen receptor alpha signaling pathway. J Biol Chem 276:9640-9648
    • (2001) J Biol Chem , vol.276 , pp. 9640-9648
    • Prévôt, D.1    Morel, A.P.2    Voeltzel, T.3    Rostan, M.C.4    Rimokh, R.5    Magaud, J.P.6    Corbo, L.7
  • 35
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • 8663146 10.1074/jbc.271.25.15034 1:CAS:528:DyaK28XjvVWmtb0%3D
    • Lin WJ, Gary JD, Yang MC, Clarke S, Herschman HR (1996) The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J Biol Chem 271:15034-15044
    • (1996) J Biol Chem , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 37
    • 0032575653 scopus 로고    scopus 로고
    • Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex
    • 9712883 10.1074/jbc.273.35.22563 1:CAS:528:DyaK1cXlvValtLk%3D
    • Rouault JP, Prevot D, Berthet C, Birot AM, Billaud M, Magaud JP, Corbo L (1998) Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex. J Biol Chem 273:22563-22569
    • (1998) J Biol Chem , vol.273 , pp. 22563-22569
    • Rouault, J.P.1    Prevot, D.2    Berthet, C.3    Birot, A.M.4    Billaud, M.5    Magaud, J.P.6    Corbo, L.7
  • 38
  • 39
    • 41949099124 scopus 로고    scopus 로고
    • The BTG2 protein is a general activator of mRNA deadenylation
    • 18337750 10.1038/emboj.2008.43 1:CAS:528:DC%2BD1cXksVagtLc%3D
    • Mauxion F, Faux C, Séraphin B (2008) The BTG2 protein is a general activator of mRNA deadenylation. EMBO J 27:1039-1048
    • (2008) EMBO J , vol.27 , pp. 1039-1048
    • Mauxion, F.1    Faux, C.2    Séraphin, B.3
  • 40
    • 34547616284 scopus 로고    scopus 로고
    • Dual role of mitochondrial reactive oxygen species in hypoxia signaling: Activation of nuclear factor-{kappa}B via c-SRC and oxidant-dependent cell death
    • 17671207 10.1158/0008-5472.CAN-07-0515 1:CAS:528:DC%2BD2sXosVemtL4%3D
    • Lluis JM, Buricchi F, Chiarugi P, Morales A, Fernandez-Checa JC (2007) Dual role of mitochondrial reactive oxygen species in hypoxia signaling: activation of nuclear factor-{kappa}B via c-SRC and oxidant-dependent cell death. Cancer Res 67:7368-7377
    • (2007) Cancer Res , vol.67 , pp. 7368-7377
    • Lluis, J.M.1    Buricchi, F.2    Chiarugi, P.3    Morales, A.4    Fernandez-Checa, J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.