메뉴 건너뛰기




Volumn 121, Issue 1, 2015, Pages 83-89

Phosphorylation of AKT induced by phosphorylated Hsp27 confers the apoptosis-resistance in t-AUCB-treated glioblastoma cells in vitro

Author keywords

AKT; Chemotherapy; Glioma; Heat shock protein 27

Indexed keywords

4-(4-(3-ADAMANTAN-1-YLUREIDO)CYCLOHEXYLOXY)BENZOIC ACID; ANTINEOPLASTIC AGENT; BENZOIC ACID DERIVATIVE; CASP3 PROTEIN, HUMAN; CASPASE 3; HEAT SHOCK PROTEIN 27; HSPB1 PROTEIN, HUMAN; PROTEIN KINASE B; UREA;

EID: 84921021287     PISSN: 0167594X     EISSN: 15737373     Source Type: Journal    
DOI: 10.1007/s11060-014-1610-3     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 84863677229 scopus 로고    scopus 로고
    • Anisomycin induces glioma cell death via down-regulation of PP2A catalytic subunit in vitro
    • COI: 1:CAS:528:DC%2BC38XpsFOqt7k%3D, PID: 22684030
    • Li JY, Huang JY, Li M, Zhang H, Xing B, Chen G, Wei D, Gu PY, Hu WX (2012) Anisomycin induces glioma cell death via down-regulation of PP2A catalytic subunit in vitro. Acta Pharmacol Sin 33:935–940. doi:10.1038/aps.2012.46
    • (2012) Acta Pharmacol Sin , vol.33 , pp. 935-940
    • Li, J.Y.1    Huang, J.Y.2    Li, M.3    Zhang, H.4    Xing, B.5    Chen, G.6    Wei, D.7    Gu, P.Y.8    Hu, W.X.9
  • 2
    • 84871320678 scopus 로고    scopus 로고
    • ATM inhibitor KU-55933 increases the TMZ responsiveness of only inherently TMZ sensitive GBM cells
    • COI: 1:CAS:528:DC%2BC38Xhs12rs7bI, PID: 23054561
    • Nadkarni A, Shrivastav M, Mladek AC, Schwingler PM, Grogan PT, Chen J, Sarkaria JN (2012) ATM inhibitor KU-55933 increases the TMZ responsiveness of only inherently TMZ sensitive GBM cells. J Neurooncol 110:349–357. doi:10.1007/s11060-012-0979-0
    • (2012) J Neurooncol , vol.110 , pp. 349-357
    • Nadkarni, A.1    Shrivastav, M.2    Mladek, A.C.3    Schwingler, P.M.4    Grogan, P.T.5    Chen, J.6    Sarkaria, J.N.7
  • 3
    • 57349148269 scopus 로고    scopus 로고
    • Comparative analysis of temozolomide (TMZ) versus 1,3-bis (2-chloroethyl)-1 nitrosourea (BCNU) in newly diagnosed glioblastoma multiforme (GBM) patients
    • COI: 1:CAS:528:DC%2BD1MXjvFehsA%3D%3D, PID: 18813874
    • Vinjamuri M, Adumala RR, Altaha R, Hobbs GR, Crowell EB Jr (2009) Comparative analysis of temozolomide (TMZ) versus 1,3-bis (2-chloroethyl)-1 nitrosourea (BCNU) in newly diagnosed glioblastoma multiforme (GBM) patients. J Neurooncol 91:221–225. doi:10.1007/s11060-008-9702-6
    • (2009) J Neurooncol , vol.91 , pp. 221-225
    • Vinjamuri, M.1    Adumala, R.R.2    Altaha, R.3    Hobbs, G.R.4    Crowell, E.B.5
  • 4
    • 4444222498 scopus 로고    scopus 로고
    • Phase II study of concurrent continuous Temozolomide (TMZ) and Tamoxifen (TMX) for recurrent malignant astrocytic gliomas
    • PID: 15527114
    • Spence AM, Peterson RA, Scharnhorst JD, Silbergeld DL, Rostomily RC (2004) Phase II study of concurrent continuous Temozolomide (TMZ) and Tamoxifen (TMX) for recurrent malignant astrocytic gliomas. J Neurooncol 70:91–95
    • (2004) J Neurooncol , vol.70 , pp. 91-95
    • Spence, A.M.1    Peterson, R.A.2    Scharnhorst, J.D.3    Silbergeld, D.L.4    Rostomily, R.C.5
  • 5
    • 14044264295 scopus 로고    scopus 로고
    • Temozolomide (TMZ) combined with cisplatin (CDDP) in patients with brain metastases from solid tumors: a Hellenic Cooperative Oncology Group (HeCOG) phase II study
    • COI: 1:CAS:528:DC%2BD2MXhtlCjsLfK, PID: 15719277
    • Christodoulou C, Bafaloukos D, Linardou H, Aravantinos G, Bamias A, Carina M, Klouvas G, Skarlos D, Hellenic Cooperative Oncology G (2005) Temozolomide (TMZ) combined with cisplatin (CDDP) in patients with brain metastases from solid tumors: a Hellenic Cooperative Oncology Group (HeCOG) phase II study. J Neurooncol 71:61–65. doi:10.1007/s11060-004-9176-0
    • (2005) J Neurooncol , vol.71 , pp. 61-65
    • Christodoulou, C.1    Bafaloukos, D.2    Linardou, H.3    Aravantinos, G.4    Bamias, A.5    Carina, M.6    Klouvas, G.7    Skarlos, D.8
  • 6
    • 75749084460 scopus 로고    scopus 로고
    • Inhibition of soluble epoxide hydrolase by trans-4- [4-(3-adamantan-1-yl-ureido)-cyclohexyloxy]-benzoic acid is protective against ischemia-reperfusion injury
    • COI: 1:CAS:528:DC%2BC3cXos1Wjsw%3D%3D, PID: 19834332
    • Chaudhary KR, Abukhashim M, Hwang SH, Hammock BD, Seubert JM (2010) Inhibition of soluble epoxide hydrolase by trans-4- [4-(3-adamantan-1-yl-ureido)-cyclohexyloxy]-benzoic acid is protective against ischemia-reperfusion injury. J Cardiovasc Pharmacol 55:67–73. doi:10.1097/FJC.0b013e3181c37d69
    • (2010) J Cardiovasc Pharmacol , vol.55 , pp. 67-73
    • Chaudhary, K.R.1    Abukhashim, M.2    Hwang, S.H.3    Hammock, B.D.4    Seubert, J.M.5
  • 7
    • 67650228182 scopus 로고    scopus 로고
    • Pharmacokinetic optimization of four soluble epoxide hydrolase inhibitors for use in a murine model of inflammation
    • COI: 1:CAS:528:DC%2BD1MXpt1Wmu7k%3D, PID: 19154430
    • Liu JY, Tsai HJ, Hwang SH, Jones PD, Morisseau C, Hammock BD (2009) Pharmacokinetic optimization of four soluble epoxide hydrolase inhibitors for use in a murine model of inflammation. Br J Pharmacol 156:284–296. doi:10.1111/j.1476-5381.2008.00009.x
    • (2009) Br J Pharmacol , vol.156 , pp. 284-296
    • Liu, J.Y.1    Tsai, H.J.2    Hwang, S.H.3    Jones, P.D.4    Morisseau, C.5    Hammock, B.D.6
  • 8
    • 84864039219 scopus 로고    scopus 로고
    • t-AUCB, an improved sEH inhibitor, suppresses human glioblastoma cell growth by activating NF-kappaB-p65
    • COI: 1:CAS:528:DC%2BC38Xot1Oksb4%3D, PID: 22382785
    • Li J, Liu H, Xing B, Yu Y, Wang H, Chen G, Gu B, Zhang G, Wei D, Gu P, Li M, Hu W (2012) t-AUCB, an improved sEH inhibitor, suppresses human glioblastoma cell growth by activating NF-kappaB-p65. J Neurooncol 108:385–393. doi:10.1007/s11060-012-0841-4
    • (2012) J Neurooncol , vol.108 , pp. 385-393
    • Li, J.1    Liu, H.2    Xing, B.3    Yu, Y.4    Wang, H.5    Chen, G.6    Gu, B.7    Zhang, G.8    Wei, D.9    Gu, P.10    Li, M.11    Hu, W.12
  • 9
    • 84867843684 scopus 로고    scopus 로고
    • The apoptosis-resistance in t-AUCB-treated glioblastoma cells depends on activation of Hsp27
    • PID: 22903412
    • Li J, Hu W, Lan Q (2012) The apoptosis-resistance in t-AUCB-treated glioblastoma cells depends on activation of Hsp27. J Neurooncol 110:187–194. doi:10.1007/s11060-012-0963-8
    • (2012) J Neurooncol , vol.110 , pp. 187-194
    • Li, J.1    Hu, W.2    Lan, Q.3
  • 10
    • 0030907987 scopus 로고    scopus 로고
    • PI3 K: downstream AKTion blocks apoptosis
    • COI: 1:CAS:528:DyaK2sXhtlKqs70%3D, PID: 9038334
    • Franke TF, Kaplan DR, Cantley LC (1997) PI3 K: downstream AKTion blocks apoptosis. Cell 88:435–437
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 11
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • COI: 1:CAS:528:DyaK2MXns1SjtLw%3D, PID: 7637810
    • Burgering BM, Coffer PJ (1995) Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599–602. doi:10.1038/376599a0
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 12
    • 33846000629 scopus 로고    scopus 로고
    • MAPK-activated protein kinase-2 (MK2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, MK2, Akt, and Hsp27
    • COI: 1:CAS:528:DC%2BD28Xht1elt7zO, PID: 17015449
    • Zheng C, Lin Z, Zhao ZJ, Yang Y, Niu H, Shen X (2006) MAPK-activated protein kinase-2 (MK2)-mediated formation and phosphorylation-regulated dissociation of the signal complex consisting of p38, MK2, Akt, and Hsp27. J Biol Chem 281:37215–37226. doi:10.1074/jbc.M603622200
    • (2006) J Biol Chem , vol.281 , pp. 37215-37226
    • Zheng, C.1    Lin, Z.2    Zhao, Z.J.3    Yang, Y.4    Niu, H.5    Shen, X.6
  • 13
    • 34547588567 scopus 로고    scopus 로고
    • Hsp27 regulates Akt activation and polymorphonuclear leukocyte apoptosis by scaffolding MK2 to Akt signal complex
    • COI: 1:CAS:528:DC%2BD2sXotVGmsbk%3D, PID: 17510053
    • Wu R, Kausar H, Johnson P, Montoya-Durango DE, Merchant M, Rane MJ (2007) Hsp27 regulates Akt activation and polymorphonuclear leukocyte apoptosis by scaffolding MK2 to Akt signal complex. J Biol Chem 282:21598–21608. doi:10.1074/jbc.M611316200
    • (2007) J Biol Chem , vol.282 , pp. 21598-21608
    • Wu, R.1    Kausar, H.2    Johnson, P.3    Montoya-Durango, D.E.4    Merchant, M.5    Rane, M.J.6
  • 14
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of Daxx-mediated apoptosis by heat shock protein 27
    • COI: 1:CAS:528:DC%2BD3cXnt1ait7o%3D, PID: 11003656
    • Charette SJ, Lavoie JN, Lambert H, Landry J (2000) Inhibition of Daxx-mediated apoptosis by heat shock protein 27. Mol Cell Biol 20:7602–7612
    • (2000) Mol Cell Biol , vol.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3    Landry, J.4
  • 15
    • 0036143720 scopus 로고    scopus 로고
    • Hsp27 as a negative regulator of cytochrome C release
    • COI: 1:CAS:528:DC%2BD38Xmt12gtQ%3D%3D, PID: 11784858
    • Paul C, Manero F, Gonin S, Kretz-Remy C, Virot S, Arrigo AP (2002) Hsp27 as a negative regulator of cytochrome C release. Mol Cell Biol 22:816–834
    • (2002) Mol Cell Biol , vol.22 , pp. 816-834
    • Paul, C.1    Manero, F.2    Gonin, S.3    Kretz-Remy, C.4    Virot, S.5    Arrigo, A.P.6
  • 16
    • 0032722324 scopus 로고    scopus 로고
    • HSP27 inhibits cytochrome c-dependent activation of procaspase-9
    • COI: 1:CAS:528:DyaK1MXnt1Gnuro%3D, PID: 10544189
    • Garrido C, Bruey JM, Fromentin A, Hammann A, Arrigo AP, Solary E (1999) HSP27 inhibits cytochrome c-dependent activation of procaspase-9. FASEB J 13:2061–2070
    • (1999) FASEB J , vol.13 , pp. 2061-2070
    • Garrido, C.1    Bruey, J.M.2    Fromentin, A.3    Hammann, A.4    Arrigo, A.P.5    Solary, E.6
  • 17
    • 0034963578 scopus 로고    scopus 로고
    • Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c
    • COI: 1:CAS:528:DC%2BD3MXltlKisr8%3D, PID: 11444529
    • Concannon CG, Orrenius S, Samali A (2001) Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c. Gene Expr 9:195–201
    • (2001) Gene Expr , vol.9 , pp. 195-201
    • Concannon, C.G.1    Orrenius, S.2    Samali, A.3
  • 18
    • 34248176724 scopus 로고    scopus 로고
    • Heat shock genes - integrating cell survival and death
    • COI: 1:CAS:528:DC%2BD2sXmsFalsrs%3D, PID: 17536179
    • Arya R, Mallik M, Lakhotia SC (2007) Heat shock genes - integrating cell survival and death. J Biosci 32:595–610
    • (2007) J Biosci , vol.32 , pp. 595-610
    • Arya, R.1    Mallik, M.2    Lakhotia, S.C.3
  • 20
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
    • COI: 1:CAS:528:DC%2BD2MXmsFymur4%3D, PID: 16038406
    • Ciocca DR, Calderwood SK (2005) Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 10:86–103
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 21
    • 54049100335 scopus 로고    scopus 로고
    • Upregulated HSP27 in human breast cancer cells reduces Herceptin susceptibility by increasing Her2 protein stability
    • PID: 18834540
    • Kang SH, Kang KW, Kim KH, Kwon B, Kim SK, Lee HY, Kong SY, Lee ES, Jang SG, Yoo BC (2008) Upregulated HSP27 in human breast cancer cells reduces Herceptin susceptibility by increasing Her2 protein stability. BMC Cancer 8:286. doi:10.1186/1471-2407-8-286
    • (2008) BMC Cancer , vol.8 , pp. 286
    • Kang, S.H.1    Kang, K.W.2    Kim, K.H.3    Kwon, B.4    Kim, S.K.5    Lee, H.Y.6    Kong, S.Y.7    Lee, E.S.8    Jang, S.G.9    Yoo, B.C.10
  • 22
    • 0032990651 scopus 로고    scopus 로고
    • Heat-shock-protein-27 (Hsp27) expression in ovarian carcinoma: relation in response to chemotherapy and prognosis
    • COI: 1:CAS:528:DyaK1MXkt1altrk%3D, PID: 10371339
    • Arts HJ, Hollema H, Lemstra W, Willemse PH, De Vries EG, Kampinga HH, Van der Zee AG (1999) Heat-shock-protein-27 (Hsp27) expression in ovarian carcinoma: relation in response to chemotherapy and prognosis. Int J Cancer 84:234–238. doi:10.1002/(SICI)1097-0215(19990621)84
    • (1999) Int J Cancer , vol.84 , pp. 234-238
    • Arts, H.J.1    Hollema, H.2    Lemstra, W.3    Willemse, P.H.4    De Vries, E.G.5    Kampinga, H.H.6    Van der Zee, A.G.7
  • 23
    • 0034213832 scopus 로고    scopus 로고
    • Prognostic significance of heat shock protein-27 expression in hepatocellular carcinoma and its relation to histologic grading and survival
    • COI: 1:CAS:528:DC%2BD3cXktFGjs78%3D, PID: 10861421
    • King KL, Li AF, Chau GY, Chi CW, Wu CW, Huang CL, Lui WY (2000) Prognostic significance of heat shock protein-27 expression in hepatocellular carcinoma and its relation to histologic grading and survival. Cancer 88:2464–2470. doi:10.1002/1097-0142(20000601)88
    • (2000) Cancer , vol.88 , pp. 2464-2470
    • King, K.L.1    Li, A.F.2    Chau, G.Y.3    Chi, C.W.4    Wu, C.W.5    Huang, C.L.6    Lui, W.Y.7
  • 25
    • 79952825166 scopus 로고    scopus 로고
    • Chemoresistance of lung cancer stemlike cells depends on activation of Hsp27
    • COI: 1:CAS:528:DC%2BC3MXkslWhsr0%3D, PID: 21425153
    • Hsu HS, Lin JH, Huang WC, Hsu TW, Su K, Chiou SH, Tsai YT, Hung SC (2011) Chemoresistance of lung cancer stemlike cells depends on activation of Hsp27. Cancer 117:1516–1528. doi:10.1002/cncr.25599
    • (2011) Cancer , vol.117 , pp. 1516-1528
    • Hsu, H.S.1    Lin, J.H.2    Huang, W.C.3    Hsu, T.W.4    Su, K.5    Chiou, S.H.6    Tsai, Y.T.7    Hung, S.C.8
  • 26
    • 23844517377 scopus 로고    scopus 로고
    • Heat shock protein 27 is the major differentially phosphorylated protein involved in renal epithelial cellular stress response and controls focal adhesion organization and apoptosis
    • PID: 15944157
    • de Graauw M, Tijdens I, Cramer R, Corless S, Timms JF, van de Water B (2005) Heat shock protein 27 is the major differentially phosphorylated protein involved in renal epithelial cellular stress response and controls focal adhesion organization and apoptosis. J Biol Chem 280:29885–29898. doi:10.1074/jbc.M412708200
    • (2005) J Biol Chem , vol.280 , pp. 29885-29898
    • de Graauw, M.1    Tijdens, I.2    Cramer, R.3    Corless, S.4    Timms, J.F.5    van de Water, B.6
  • 27
    • 0035793574 scopus 로고    scopus 로고
    • p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils
    • COI: 1:CAS:528:DC%2BD3MXhtFWisL4%3D, PID: 11042204
    • Rane MJ, Coxon PY, Powell DW, Webster R, Klein JB, Pierce W, Ping P, McLeish KR (2001) p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils. J Biol Chem 276:3517–3523. doi:10.1074/jbc.M005953200
    • (2001) J Biol Chem , vol.276 , pp. 3517-3523
    • Rane, M.J.1    Coxon, P.Y.2    Powell, D.W.3    Webster, R.4    Klein, J.B.5    Pierce, W.6    Ping, P.7    McLeish, K.R.8
  • 28
    • 0041344614 scopus 로고    scopus 로고
    • Heat shock protein 27 controls apoptosis by regulating Akt activation
    • COI: 1:CAS:528:DC%2BD3sXlsFKktbY%3D, PID: 12740362
    • Rane MJ, Pan Y, Singh S, Powell DW, Wu R, Cummins T, Chen Q, McLeish KR, Klein JB (2003) Heat shock protein 27 controls apoptosis by regulating Akt activation. J Biol Chem 278:27828–27835. doi:10.1074/jbc.M303417200
    • (2003) J Biol Chem , vol.278 , pp. 27828-27835
    • Rane, M.J.1    Pan, Y.2    Singh, S.3    Powell, D.W.4    Wu, R.5    Cummins, T.6    Chen, Q.7    McLeish, K.R.8    Klein, J.B.9
  • 29
    • 0035511787 scopus 로고    scopus 로고
    • Cytokine-induced p38 activation feedback regulates the prolonged activation of AKT cell survival pathway initiated by reactive oxygen species in response to UV irradiation in human keratinocytes
    • COI: 1:CAS:528:DC%2BD3MXotlGit74%3D, PID: 11605009
    • Zhang QS, Maddock DA, Chen JP, Heo S, Chiu C, Lai D, Souza K, Mehta S, Wan YS (2001) Cytokine-induced p38 activation feedback regulates the prolonged activation of AKT cell survival pathway initiated by reactive oxygen species in response to UV irradiation in human keratinocytes. Int J Oncol 19:1057–1061
    • (2001) Int J Oncol , vol.19 , pp. 1057-1061
    • Zhang, Q.S.1    Maddock, D.A.2    Chen, J.P.3    Heo, S.4    Chiu, C.5    Lai, D.6    Souza, K.7    Mehta, S.8    Wan, Y.S.9
  • 30
    • 12544256432 scopus 로고    scopus 로고
    • Akt2 phosphorylates ezrin to trigger NHE3 translocation and activation
    • COI: 1:CAS:528:DC%2BD2MXitFGjsw%3D%3D, PID: 15531580
    • Shiue H, Musch MW, Wang Y, Chang EB, Turner JR (2005) Akt2 phosphorylates ezrin to trigger NHE3 translocation and activation. J Biol Chem 280:1688–1695. doi:10.1074/jbc.M409471200
    • (2005) J Biol Chem , vol.280 , pp. 1688-1695
    • Shiue, H.1    Musch, M.W.2    Wang, Y.3    Chang, E.B.4    Turner, J.R.5
  • 31
    • 4644310423 scopus 로고    scopus 로고
    • The p38 pathway regulates Akt both at the protein and transcriptional activation levels during myogenesis
    • COI: 1:CAS:528:DC%2BD2cXnslenur8%3D, PID: 15381256
    • Cabane C, Coldefy AS, Yeow K, Derijard B (2004) The p38 pathway regulates Akt both at the protein and transcriptional activation levels during myogenesis. Cell Signal 16:1405–1415. doi:10.1016/j.cellsig.2004.05.003
    • (2004) Cell Signal , vol.16 , pp. 1405-1415
    • Cabane, C.1    Coldefy, A.S.2    Yeow, K.3    Derijard, B.4
  • 32
    • 17644385160 scopus 로고    scopus 로고
    • Antiapoptotic role of p38 mitogen activated protein kinase in Jurkat T cells and normal human T lymphocytes treated with 8-methoxypsoralen and ultraviolet-A radiation
    • COI: 1:CAS:528:DC%2BD2MXhsVWmsLY%3D, PID: 15711930
    • Cappellini A, Tazzari PL, Mantovani I, Billi AM, Tassi C, Ricci F, Conte R, Martelli AM (2005) Antiapoptotic role of p38 mitogen activated protein kinase in Jurkat T cells and normal human T lymphocytes treated with 8-methoxypsoralen and ultraviolet-A radiation. Apoptosis 10:141–152. doi:10.1007/s10495-005-6069-4
    • (2005) Apoptosis , vol.10 , pp. 141-152
    • Cappellini, A.1    Tazzari, P.L.2    Mantovani, I.3    Billi, A.M.4    Tassi, C.5    Ricci, F.6    Conte, R.7    Martelli, A.M.8
  • 33
    • 20244368231 scopus 로고    scopus 로고
    • Akt regulates thrombin-induced HSP27 phosphorylation in aortic smooth muscle cells: function at a point downstream from p38 MAP kinase
    • COI: 1:CAS:528:DC%2BD2MXjsVersrY%3D, PID: 15848222
    • Nakajima K, Hirade K, Ishisaki A, Matsuno H, Suga H, Kanno Y, Shu E, Kitajima Y, Katagiri Y, Kozawa O (2005) Akt regulates thrombin-induced HSP27 phosphorylation in aortic smooth muscle cells: function at a point downstream from p38 MAP kinase. Life Sci 77:96–107. doi:10.1016/j.lfs.2004.12.017
    • (2005) Life Sci , vol.77 , pp. 96-107
    • Nakajima, K.1    Hirade, K.2    Ishisaki, A.3    Matsuno, H.4    Suga, H.5    Kanno, Y.6    Shu, E.7    Kitajima, Y.8    Katagiri, Y.9    Kozawa, O.10
  • 35
    • 84859331722 scopus 로고    scopus 로고
    • Inhibition of HSP27 alone or in combination with pAKT inhibition as therapeutic approaches to target SPARC-induced glioma cell survival
    • COI: 1:CAS:528:DC%2BC38Xnslyhs7w%3D, PID: 22480225
    • Schultz CR, Golembieski WA, King DA, Brown SL, Brodie C, Rempel SA (2012) Inhibition of HSP27 alone or in combination with pAKT inhibition as therapeutic approaches to target SPARC-induced glioma cell survival. Mol Cancer 11:20. doi:10.1186/1476-4598-11-20
    • (2012) Mol Cancer , vol.11 , pp. 20
    • Schultz, C.R.1    Golembieski, W.A.2    King, D.A.3    Brown, S.L.4    Brodie, C.5    Rempel, S.A.6
  • 36
    • 78149500836 scopus 로고    scopus 로고
    • Activation of Nippostrongylus brasiliensis infective larvae is regulated by a pathway distinct from the hookworm Ancylostoma caninum
    • COI: 1:CAS:528:DC%2BC3cXhsVWmt7fK, PID: 20654619
    • Huang SC, Chan DT, Smyth DJ, Ball G, Gounaris K, Selkirk ME (2010) Activation of Nippostrongylus brasiliensis infective larvae is regulated by a pathway distinct from the hookworm Ancylostoma caninum. Int J Parasitol 40:1619–1628. doi:10.1016/j.ijpara.2010.06.004
    • (2010) Int J Parasitol , vol.40 , pp. 1619-1628
    • Huang, S.C.1    Chan, D.T.2    Smyth, D.J.3    Ball, G.4    Gounaris, K.5    Selkirk, M.E.6
  • 37
    • 77954710908 scopus 로고    scopus 로고
    • Akt signaling pathway: a target for radiosensitizing human malignant glioma
    • COI: 1:CAS:528:DC%2BC3cXotVWmsb8%3D, PID: 20406894
    • Chautard E, Loubeau G, Tchirkov A, Chassagne J, Vermot-Desroches C, Morel L, Verrelle P (2010) Akt signaling pathway: a target for radiosensitizing human malignant glioma. Neuro Oncol 12:434–443. doi:10.1093/neuonc/nop059
    • (2010) Neuro Oncol , vol.12 , pp. 434-443
    • Chautard, E.1    Loubeau, G.2    Tchirkov, A.3    Chassagne, J.4    Vermot-Desroches, C.5    Morel, L.6    Verrelle, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.