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Volumn 12, Issue , 2012, Pages

Effect of inhibition of the Ubiquitin-Proteasome System and Hsp90 on growth and survival of Rhabdomyosarcoma cells in vitro

Author keywords

[No Author keywords available]

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; ALVESPIMYCIN; BORTEZOMIB; CELL PROTEIN; CHLOROQUINE; FLUORESCEIN ISOTHIOCYANATE; HEAT SHOCK PROTEIN 90; LIPOCORTIN 5; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROPIDIUM IODIDE; PROTEASOME; PROTEIN LC3 I; RAPAMYCIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84861981005     PISSN: None     EISSN: 14712407     Source Type: Journal    
DOI: 10.1186/1471-2407-12-233     Document Type: Article
Times cited : (18)

References (60)
  • 2
    • 0033588883 scopus 로고    scopus 로고
    • Rhabdomyosarcoma-working out the pathways
    • 10.1038/sj.onc.1203038, 10498887
    • Merlino G, Helman LJ. Rhabdomyosarcoma-working out the pathways. Oncogene 1999, 18(38):5340-5348. 10.1038/sj.onc.1203038, 10498887.
    • (1999) Oncogene , vol.18 , Issue.38 , pp. 5340-5348
    • Merlino, G.1    Helman, L.J.2
  • 3
    • 0029181666 scopus 로고
    • Alveolar rhabdomyosarcoma: a prognostically unfavorable rhabdomyosarcoma type and its necessary distinction from embryonal rhabdomyosarcoma
    • 10.1007/978-3-642-77289-4_14, 7882714
    • Harms D. Alveolar rhabdomyosarcoma: a prognostically unfavorable rhabdomyosarcoma type and its necessary distinction from embryonal rhabdomyosarcoma. Curr Top Pathol 1995, 89:273-296. 10.1007/978-3-642-77289-4_14, 7882714.
    • (1995) Curr Top Pathol , vol.89 , pp. 273-296
    • Harms, D.1
  • 4
    • 0023867114 scopus 로고
    • Histopathology of childhood sarcomas, Intergroup Rhabdomyosarcoma Studies I and II: clinicopathologic correlation
    • Newton WA, Soule EH, Hamoudi AB, Reiman HM, Shimada H, Beltangady M, Maurer H. Histopathology of childhood sarcomas, Intergroup Rhabdomyosarcoma Studies I and II: clinicopathologic correlation. J Clin Oncol 1988, 6(1):67-75.
    • (1988) J Clin Oncol , vol.6 , Issue.1 , pp. 67-75
    • Newton, W.A.1    Soule, E.H.2    Hamoudi, A.B.3    Reiman, H.M.4    Shimada, H.5    Beltangady, M.6    Maurer, H.7
  • 5
    • 0028364374 scopus 로고
    • Fusion of PAX7 to FKHR by the variant t(1;13)(p36;q14) translocation in alveolar rhabdomyosarcoma
    • Davis RJ, D'Cruz CM, Lovell MA, Biegel JA, Barr FG. Fusion of PAX7 to FKHR by the variant t(1;13)(p36;q14) translocation in alveolar rhabdomyosarcoma. Cancer Res 1994, 54(11):2869-2872.
    • (1994) Cancer Res , vol.54 , Issue.11 , pp. 2869-2872
    • Davis, R.J.1    D'Cruz, C.M.2    Lovell, M.A.3    Biegel, J.A.4    Barr, F.G.5
  • 6
    • 0029980113 scopus 로고    scopus 로고
    • Mechanism for transcriptional gain of function resulting from chromosomal translocation in alveolar rhabdomyosarcoma
    • 10.1073/pnas.93.11.5455, 39267, 8643596
    • Bennicelli JL, Edwards RH, Barr FG. Mechanism for transcriptional gain of function resulting from chromosomal translocation in alveolar rhabdomyosarcoma. Proc Natl Acad Sci U S A 1996, 93(11):5455-5459. 10.1073/pnas.93.11.5455, 39267, 8643596.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.11 , pp. 5455-5459
    • Bennicelli, J.L.1    Edwards, R.H.2    Barr, F.G.3
  • 7
    • 41849086234 scopus 로고    scopus 로고
    • Bortezomib-mediated proteasome inhibition as a potential strategy for the treatment of rhabdomyosarcoma
    • 10.1016/j.ejca.2008.02.022, 18342500
    • Bersani F, Taulli R, Accornero P, Morotti A, Miretti S, Crepaldi T, Ponzetto C. Bortezomib-mediated proteasome inhibition as a potential strategy for the treatment of rhabdomyosarcoma. Eur J Cancer 2008, 44(6):876-884. 10.1016/j.ejca.2008.02.022, 18342500.
    • (2008) Eur J Cancer , vol.44 , Issue.6 , pp. 876-884
    • Bersani, F.1    Taulli, R.2    Accornero, P.3    Morotti, A.4    Miretti, S.5    Crepaldi, T.6    Ponzetto, C.7
  • 8
    • 34748826129 scopus 로고    scopus 로고
    • HSP90 antagonist, geldanamycin, inhibits proliferation, induces apoptosis and blocks migration of rhabdomyosarcoma cells in vitro and seeding into bone marrow in vivo
    • 10.1097/CAD.0b013e3282ef532d, 17893518
    • Lesko E, Gozdzik J, Kijowski J, Jenner B, Wiecha O, Majka M. HSP90 antagonist, geldanamycin, inhibits proliferation, induces apoptosis and blocks migration of rhabdomyosarcoma cells in vitro and seeding into bone marrow in vivo. Anticancer Drugs 2007, 18(10):1173-1181. 10.1097/CAD.0b013e3282ef532d, 17893518.
    • (2007) Anticancer Drugs , vol.18 , Issue.10 , pp. 1173-1181
    • Lesko, E.1    Gozdzik, J.2    Kijowski, J.3    Jenner, B.4    Wiecha, O.5    Majka, M.6
  • 9
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: a suitable antineoplastic target
    • 10.1038/nrc1361, 15122206
    • Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer 2004, 4(5):349-360. 10.1038/nrc1361, 15122206.
    • (2004) Nat Rev Cancer , vol.4 , Issue.5 , pp. 349-360
    • Adams, J.1
  • 10
    • 34247125164 scopus 로고    scopus 로고
    • The proteasome: a worthwhile target for the treatment of solid tumours?
    • 10.1016/j.ejca.2007.01.038, 17379504
    • Milano A, Iaffaioli RV, Caponigro F. The proteasome: a worthwhile target for the treatment of solid tumours?. Eur J Cancer 2007, 43(7):1125-1133. 10.1016/j.ejca.2007.01.038, 17379504.
    • (2007) Eur J Cancer , vol.43 , Issue.7 , pp. 1125-1133
    • Milano, A.1    Iaffaioli, R.V.2    Caponigro, F.3
  • 11
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima T, Richardson P, Chauhan D, Palombella VJ, Elliott PJ, Adams J, Anderson KC. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res 2001, 61(7):3071-3076.
    • (2001) Cancer Res , vol.61 , Issue.7 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3    Palombella, V.J.4    Elliott, P.J.5    Adams, J.6    Anderson, K.C.7
  • 12
    • 21244466289 scopus 로고    scopus 로고
    • Comparison of 17-dimethylaminoethylamino-17-demethoxy-geldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: effects on Hsp90 and client proteins in melanoma models
    • 10.1007/s00280-004-0947-2, 15841378
    • Smith V, Sausville EA, Camalier RF, Fiebig HH, Burger AM. Comparison of 17-dimethylaminoethylamino-17-demethoxy-geldanamycin (17DMAG) and 17-allylamino-17-demethoxygeldanamycin (17AAG) in vitro: effects on Hsp90 and client proteins in melanoma models. Cancer Chemother Pharmacol 2005, 56(2):126-137. 10.1007/s00280-004-0947-2, 15841378.
    • (2005) Cancer Chemother Pharmacol , vol.56 , Issue.2 , pp. 126-137
    • Smith, V.1    Sausville, E.A.2    Camalier, R.F.3    Fiebig, H.H.4    Burger, A.M.5
  • 13
    • 0034452730 scopus 로고    scopus 로고
    • Kinetics of absorbance and anisotropy upon excited state relaxation in the reaction center core complex of a green sulfur bacterium
    • 10.1023/A:1010647205220, 16228492
    • Neerken S, Ma YZ, Aschenbrucker J, Schmidt KA, Nowak FR, Permentier HP, Aartsma TJ, Gillbro T, Amesz J. Kinetics of absorbance and anisotropy upon excited state relaxation in the reaction center core complex of a green sulfur bacterium. Photosynth Res 2000, 65(3):261-268. 10.1023/A:1010647205220, 16228492.
    • (2000) Photosynth Res , vol.65 , Issue.3 , pp. 261-268
    • Neerken, S.1    Ma, Y.Z.2    Aschenbrucker, J.3    Schmidt, K.A.4    Nowak, F.R.5    Permentier, H.P.6    Aartsma, T.J.7    Gillbro, T.8    Amesz, J.9
  • 14
    • 0034983973 scopus 로고    scopus 로고
    • Geldanamycin: the prototype of a class of antitumor drugs targeting the heat shock protein 90 family of molecular chaperones
    • 10.1379/1466-1268(2001)006<0105:GTPOAC>2.0.CO;2, 434387, 11599571
    • Ochel HJ, Eichhorn K, Gademann G. Geldanamycin: the prototype of a class of antitumor drugs targeting the heat shock protein 90 family of molecular chaperones. Cell Stress Chaperones 2001, 6(2):105-112. 10.1379/1466-1268(2001)006<0105:GTPOAC>2.0.CO;2, 434387, 11599571.
    • (2001) Cell Stress Chaperones , vol.6 , Issue.2 , pp. 105-112
    • Ochel, H.J.1    Eichhorn, K.2    Gademann, G.3
  • 15
    • 0037454761 scopus 로고    scopus 로고
    • Geldanamycin decreases Raf-1 and Akt levels and induces apoptosis in neuroblastomas
    • 10.1002/ijc.10820, 12471618
    • Kim S, Kang J, Hu W, Evers BM, Chung DH. Geldanamycin decreases Raf-1 and Akt levels and induces apoptosis in neuroblastomas. Int J Cancer 2003, 103(3):352-359. 10.1002/ijc.10820, 12471618.
    • (2003) Int J Cancer , vol.103 , Issue.3 , pp. 352-359
    • Kim, S.1    Kang, J.2    Hu, W.3    Evers, B.M.4    Chung, D.H.5
  • 16
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • 10.1038/nrc1716, 16175177
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005, 5(10):761-772. 10.1038/nrc1716, 16175177.
    • (2005) Nat Rev Cancer , vol.5 , Issue.10 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 17
    • 4444311881 scopus 로고    scopus 로고
    • Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity
    • Mimnaugh EG, Xu W, Vos M, Yuan X, Isaacs JS, Bisht KS, Gius D, Neckers L. Simultaneous inhibition of hsp 90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances antitumor activity. Mol Cancer Ther 2004, 3(5):551-566.
    • (2004) Mol Cancer Ther , vol.3 , Issue.5 , pp. 551-566
    • Mimnaugh, E.G.1    Xu, W.2    Vos, M.3    Yuan, X.4    Isaacs, J.S.5    Bisht, K.S.6    Gius, D.7    Neckers, L.8
  • 19
    • 77957021127 scopus 로고    scopus 로고
    • Autophagy inhibition sensitizes multiple myeloma cells to17-dimethylaminoethylamino-17-demethoxygeldanamycin-induced apoptosis
    • Palacios C, Martin-Perez R, Lopez-Perez AI, Pandiella A, Lopez-Rivas A. Autophagy inhibition sensitizes multiple myeloma cells to17-dimethylaminoethylamino-17-demethoxygeldanamycin-induced apoptosis. Leuk Res 34(11):1533-1538.
    • Leuk Res , vol.34 , Issue.11 , pp. 1533-1538
    • Palacios, C.1    Martin-Perez, R.2    Lopez-Perez, A.I.3    Pandiella, A.4    Lopez-Rivas, A.5
  • 20
    • 33645812852 scopus 로고    scopus 로고
    • Effects of small molecules on chaperone-mediated autophagy
    • 10.4161/auto.1.3.2000, 16874031
    • Finn PF, Mesires NT, Vine M, Dice JF. Effects of small molecules on chaperone-mediated autophagy. Autophagy 2005, 1(3):141-145. 10.4161/auto.1.3.2000, 16874031.
    • (2005) Autophagy , vol.1 , Issue.3 , pp. 141-145
    • Finn, P.F.1    Mesires, N.T.2    Vine, M.3    Dice, J.F.4
  • 21
    • 48249091611 scopus 로고    scopus 로고
    • Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy
    • 10.1091/mbc.E07-11-1155, 2366850, 18337468
    • Kaushik S, Massey AC, Mizushima N, Cuervo AM. Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol Biol Cell 2008, 19(5):2179-2192. 10.1091/mbc.E07-11-1155, 2366850, 18337468.
    • (2008) Mol Biol Cell , vol.19 , Issue.5 , pp. 2179-2192
    • Kaushik, S.1    Massey, A.C.2    Mizushima, N.3    Cuervo, A.M.4
  • 22
    • 33645829816 scopus 로고    scopus 로고
    • Consequences of the selective blockage of chaperone-mediated autophagy
    • 10.1073/pnas.0507436103, 1458654, 16585521
    • Massey AC, Kaushik S, Sovak G, Kiffin R, Cuervo AM. Consequences of the selective blockage of chaperone-mediated autophagy. Proc Natl Acad Sci U S A 2006, 103(15):5805-5810. 10.1073/pnas.0507436103, 1458654, 16585521.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.15 , pp. 5805-5810
    • Massey, A.C.1    Kaushik, S.2    Sovak, G.3    Kiffin, R.4    Cuervo, A.M.5
  • 23
    • 79951580982 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: machinery, regulation and biological consequences
    • 10.1007/s00018-010-0565-6, 20976518
    • Li W, Yang Q, Mao Z. Chaperone-mediated autophagy: machinery, regulation and biological consequences. Cell Mol Life Sci 2011, 68(5):749-763. 10.1007/s00018-010-0565-6, 20976518.
    • (2011) Cell Mol Life Sci , vol.68 , Issue.5 , pp. 749-763
    • Li, W.1    Yang, Q.2    Mao, Z.3
  • 24
    • 33845417678 scopus 로고    scopus 로고
    • Retrospective study of five-year clinical performance of direct composite restorations using a self-etching primer adhesive system
    • 10.4012/dmj.25.611, 17076335
    • Nikaido T, Takada T, Kitasako Y, Ogata M, Shimada Y, Yoshikawa T, Nakajima M, Otsuki M, Tagami J, Burrow MF. Retrospective study of five-year clinical performance of direct composite restorations using a self-etching primer adhesive system. Dent Mater J 2006, 25(3):611-615. 10.4012/dmj.25.611, 17076335.
    • (2006) Dent Mater J , vol.25 , Issue.3 , pp. 611-615
    • Nikaido, T.1    Takada, T.2    Kitasako, Y.3    Ogata, M.4    Shimada, Y.5    Yoshikawa, T.6    Nakajima, M.7    Otsuki, M.8    Tagami, J.9    Burrow, M.F.10
  • 25
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • 10.1093/emboj/19.21.5720, 305793, 11060023
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, Kominami E, Ohsumi Y, Yoshimori T. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000, 19(21):5720-5728. 10.1093/emboj/19.21.5720, 305793, 11060023.
    • (2000) EMBO J , vol.19 , Issue.21 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6    Kominami, E.7    Ohsumi, Y.8    Yoshimori, T.9
  • 27
    • 15044350668 scopus 로고    scopus 로고
    • The expanding TOR signaling network
    • 10.1016/j.ceb.2005.02.008, 15780592
    • Martin DE, Hall MN. The expanding TOR signaling network. Curr Opin Cell Biol 2005, 17(2):158-166. 10.1016/j.ceb.2005.02.008, 15780592.
    • (2005) Curr Opin Cell Biol , vol.17 , Issue.2 , pp. 158-166
    • Martin, D.E.1    Hall, M.N.2
  • 28
    • 64749103447 scopus 로고    scopus 로고
    • Inhibition of lysosomal functions reduces proteasomal activity
    • 10.1016/j.neulet.2009.03.085, 19429125
    • Qiao L, Zhang J. Inhibition of lysosomal functions reduces proteasomal activity. Neurosci Lett 2009, 456(1):15-19. 10.1016/j.neulet.2009.03.085, 19429125.
    • (2009) Neurosci Lett , vol.456 , Issue.1 , pp. 15-19
    • Qiao, L.1    Zhang, J.2
  • 29
    • 51549086469 scopus 로고    scopus 로고
    • Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement
    • 10.1016/j.nbd.2008.06.003, 18640276
    • Pan T, Kondo S, Zhu W, Xie W, Jankovic J, Le W. Neuroprotection of rapamycin in lactacystin-induced neurodegeneration via autophagy enhancement. Neurobiol Dis 2008, 32(1):16-25. 10.1016/j.nbd.2008.06.003, 18640276.
    • (2008) Neurobiol Dis , vol.32 , Issue.1 , pp. 16-25
    • Pan, T.1    Kondo, S.2    Zhu, W.3    Xie, W.4    Jankovic, J.5    Le, W.6
  • 30
    • 67650267785 scopus 로고    scopus 로고
    • An insight into the mechanistic role of p53-mediated autophagy induction in response to proteasomal inhibition-induced neurotoxicity
    • 10.4161/auto.5.5.8377, 19337030
    • Du Y, Yang D, Li L, Luo G, Li T, Fan X, Wang Q, Zhang X, Wang Y, Le W. An insight into the mechanistic role of p53-mediated autophagy induction in response to proteasomal inhibition-induced neurotoxicity. Autophagy 2009, 5(5):663-675. 10.4161/auto.5.5.8377, 19337030.
    • (2009) Autophagy , vol.5 , Issue.5 , pp. 663-675
    • Du, Y.1    Yang, D.2    Li, L.3    Luo, G.4    Li, T.5    Fan, X.6    Wang, Q.7    Zhang, X.8    Wang, Y.9    Le, W.10
  • 31
    • 33746533874 scopus 로고    scopus 로고
    • Heat shock protein 90: a unique chemotherapeutic target
    • 10.1053/j.seminoncol.2006.04.001, 16890800
    • Cullinan SB, Whitesell L. Heat shock protein 90: a unique chemotherapeutic target. Semin Oncol 2006, 33(4):457-465. 10.1053/j.seminoncol.2006.04.001, 16890800.
    • (2006) Semin Oncol , vol.33 , Issue.4 , pp. 457-465
    • Cullinan, S.B.1    Whitesell, L.2
  • 32
    • 33747517230 scopus 로고    scopus 로고
    • The proteasome: a novel target for anticancer therapy
    • 10.1007/s12094-006-0176-8, 16760005
    • Montagut C, Rovira A, Albanell J. The proteasome: a novel target for anticancer therapy. Clin Transl Oncol 2006, 8(5):313-317. 10.1007/s12094-006-0176-8, 16760005.
    • (2006) Clin Transl Oncol , vol.8 , Issue.5 , pp. 313-317
    • Montagut, C.1    Rovira, A.2    Albanell, J.3
  • 33
    • 0043166366 scopus 로고    scopus 로고
    • Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb
    • 10.1038/sj.cdd.4401251, 12868001
    • Lauricella M, D'Anneo A, Giuliano M, Calvaruso G, Emanuele S, Vento R, Tesoriere G. Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb. Cell Death Differ 2003, 10(8):930-932. 10.1038/sj.cdd.4401251, 12868001.
    • (2003) Cell Death Differ , vol.10 , Issue.8 , pp. 930-932
    • Lauricella, M.1    D'Anneo, A.2    Giuliano, M.3    Calvaruso, G.4    Emanuele, S.5    Vento, R.6    Tesoriere, G.7
  • 34
    • 45349092269 scopus 로고    scopus 로고
    • Proteasome inhibitor Bortezomib induces cell cycle arrest and apoptosis in cell lines derived from Ewing's sarcoma family of tumors and synergizes with TRAIL
    • 10.4161/cbt.7.4.5564, 18223318
    • Lu G, Punj V, Chaudhary PM. Proteasome inhibitor Bortezomib induces cell cycle arrest and apoptosis in cell lines derived from Ewing's sarcoma family of tumors and synergizes with TRAIL. Cancer Biol Ther 2008, 7(4):603-608. 10.4161/cbt.7.4.5564, 18223318.
    • (2008) Cancer Biol Ther , vol.7 , Issue.4 , pp. 603-608
    • Lu, G.1    Punj, V.2    Chaudhary, P.M.3
  • 35
    • 34447108737 scopus 로고    scopus 로고
    • Caspase-8 dependent osteosarcoma cell apoptosis induced by proteasome inhibitor MG132
    • 10.1016/j.cellbi.2007.03.037, 17493842
    • Yan XB, Yang DS, Gao X, Feng J, Shi ZL, Ye Z. Caspase-8 dependent osteosarcoma cell apoptosis induced by proteasome inhibitor MG132. Cell Biol Int 2007, 31(10):1136-1143. 10.1016/j.cellbi.2007.03.037, 17493842.
    • (2007) Cell Biol Int , vol.31 , Issue.10 , pp. 1136-1143
    • Yan, X.B.1    Yang, D.S.2    Gao, X.3    Feng, J.4    Shi, Z.L.5    Ye, Z.6
  • 36
    • 15744364211 scopus 로고    scopus 로고
    • A multicenter Phase II study of bortezomib in recurrent or metastatic sarcomas
    • 10.1002/cncr.20968, 15739208
    • Maki RG, Kraft AS, Scheu K, Yamada J, Wadler S, Antonescu CR, Wright JJ, Schwartz GK. A multicenter Phase II study of bortezomib in recurrent or metastatic sarcomas. Cancer 2005, 103(7):1431-1438. 10.1002/cncr.20968, 15739208.
    • (2005) Cancer , vol.103 , Issue.7 , pp. 1431-1438
    • Maki, R.G.1    Kraft, A.S.2    Scheu, K.3    Yamada, J.4    Wadler, S.5    Antonescu, C.R.6    Wright, J.J.7    Schwartz, G.K.8
  • 37
    • 79954614811 scopus 로고    scopus 로고
    • Phase I trial of weekly and twiceweekly bortezomib with rituximab, cyclophosphamide, and prednisone in relapsed or refractory non-hodgkin lymphoma
    • 10.1158/1078-0432.CCR-10-1498, 21346146
    • Gerecitano J, Portlock C, Hamlin P, Moskowitz CH, Noy A, Straus D, Schulman P, Dumitrescu O, Sarasohn D, Pappanicholaou J. Phase I trial of weekly and twiceweekly bortezomib with rituximab, cyclophosphamide, and prednisone in relapsed or refractory non-hodgkin lymphoma. Clin Cancer Res 2011, 17(8):2493-2501. 10.1158/1078-0432.CCR-10-1498, 21346146.
    • (2011) Clin Cancer Res , vol.17 , Issue.8 , pp. 2493-2501
    • Gerecitano, J.1    Portlock, C.2    Hamlin, P.3    Moskowitz, C.H.4    Noy, A.5    Straus, D.6    Schulman, P.7    Dumitrescu, O.8    Sarasohn, D.9    Pappanicholaou, J.10
  • 38
    • 78649594306 scopus 로고    scopus 로고
    • Phase 1 trial of bortezomib plus R-CHOP in previously untreated patients with aggressive non-Hodgkin lymphoma
    • 10.1002/cncr.25509, 20665890
    • Furman RR, Martin P, Ruan J, Cheung YK, Vose JM, LaCasce AS, Elstrom R, Coleman M, Leonard JP. Phase 1 trial of bortezomib plus R-CHOP in previously untreated patients with aggressive non-Hodgkin lymphoma. Cancer 2010, 116(23):5432-5439. 10.1002/cncr.25509, 20665890.
    • (2010) Cancer , vol.116 , Issue.23 , pp. 5432-5439
    • Furman, R.R.1    Martin, P.2    Ruan, J.3    Cheung, Y.K.4    Vose, J.M.5    LaCasce, A.S.6    Elstrom, R.7    Coleman, M.8    Leonard, J.P.9
  • 39
    • 10344225631 scopus 로고    scopus 로고
    • Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin
    • 10.1002/ijc.20611, 15455381
    • Bagatell R, Beliakoff J, David CL, Marron MT, Whitesell L. Hsp90 inhibitors deplete key anti-apoptotic proteins in pediatric solid tumor cells and demonstrate synergistic anticancer activity with cisplatin. Int J Cancer 2005, 113(2):179-188. 10.1002/ijc.20611, 15455381.
    • (2005) Int J Cancer , vol.113 , Issue.2 , pp. 179-188
    • Bagatell, R.1    Beliakoff, J.2    David, C.L.3    Marron, M.T.4    Whitesell, L.5
  • 40
    • 51049098720 scopus 로고    scopus 로고
    • A pivotal role for heat shock protein 90 in Ewing sarcoma resistance to anti-insulin-like growth factor 1 receptor treatment: in vitro and in vivo study
    • 10.1158/0008-5472.CAN-07-3074, 18676850
    • Martins AS, Ordonez JL, Garcia-Sanchez A, Herrero D, Sevillano V, Osuna D, Mackintosh C, Caballero G, Otero AP, Poremba C. A pivotal role for heat shock protein 90 in Ewing sarcoma resistance to anti-insulin-like growth factor 1 receptor treatment: in vitro and in vivo study. Cancer Res 2008, 68(15):6260-6270. 10.1158/0008-5472.CAN-07-3074, 18676850.
    • (2008) Cancer Res , vol.68 , Issue.15 , pp. 6260-6270
    • Martins, A.S.1    Ordonez, J.L.2    Garcia-Sanchez, A.3    Herrero, D.4    Sevillano, V.5    Osuna, D.6    Mackintosh, C.7    Caballero, G.8    Otero, A.P.9    Poremba, C.10
  • 41
    • 78851472038 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 90 (HSP90) as a therapeutic strategy for the treatment of myeloma and other cancers
    • 10.1111/j.1365-2141.2010.08360.x, 21219297
    • Richardson PG, Mitsiades CS, Laubach JP, Lonial S, Chanan-Khan AA, Anderson KC. Inhibition of heat shock protein 90 (HSP90) as a therapeutic strategy for the treatment of myeloma and other cancers. Br J Haematol 2011, 152(4):367-379. 10.1111/j.1365-2141.2010.08360.x, 21219297.
    • (2011) Br J Haematol , vol.152 , Issue.4 , pp. 367-379
    • Richardson, P.G.1    Mitsiades, C.S.2    Laubach, J.P.3    Lonial, S.4    Chanan-Khan, A.A.5    Anderson, K.C.6
  • 42
    • 33747679267 scopus 로고    scopus 로고
    • Analysis of expression of heat shock protein-90 (HSP90) and the effects of HSP90 inhibitor (17-AAG) in multiple myeloma
    • 10.1080/10428190500472123, 16923571
    • Duus J, Bahar HI, Venkataraman G, Ozpuyan F, Izban KF, Al-Masri H, Maududi T, Toor A, Alkan S. Analysis of expression of heat shock protein-90 (HSP90) and the effects of HSP90 inhibitor (17-AAG) in multiple myeloma. Leuk Lymphoma 2006, 47(7):1369-1378. 10.1080/10428190500472123, 16923571.
    • (2006) Leuk Lymphoma , vol.47 , Issue.7 , pp. 1369-1378
    • Duus, J.1    Bahar, H.I.2    Venkataraman, G.3    Ozpuyan, F.4    Izban, K.F.5    Al-Masri, H.6    Maududi, T.7    Toor, A.8    Alkan, S.9
  • 43
    • 79251545172 scopus 로고    scopus 로고
    • The Hsp90 inhibitor IPI-504 overcomes bortezomib resistance in mantle cell lymphoma in vitro and in vivo by down-regulation of the prosurvival ER chaperone BiP/Grp78
    • 10.1182/blood-2010-04-278853, 21106982
    • Roue G, Perez-Galan P, Mozos A, Lopez-Guerra M, Xargay-Torrent S, Rosich L, Saborit-Villarroya I, Normant E, Campo E, Colomer D. The Hsp90 inhibitor IPI-504 overcomes bortezomib resistance in mantle cell lymphoma in vitro and in vivo by down-regulation of the prosurvival ER chaperone BiP/Grp78. Blood 2011, 117(4):1270-1279. 10.1182/blood-2010-04-278853, 21106982.
    • (2011) Blood , vol.117 , Issue.4 , pp. 1270-1279
    • Roue, G.1    Perez-Galan, P.2    Mozos, A.3    Lopez-Guerra, M.4    Xargay-Torrent, S.5    Rosich, L.6    Saborit-Villarroya, I.7    Normant, E.8    Campo, E.9    Colomer, D.10
  • 44
    • 33751258297 scopus 로고    scopus 로고
    • Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI 504), an anti-cancer agent directed against Hsp90
    • 10.1073/pnas.0608372103, 1635022, 17090671
    • Sydor JR, Normant E, Pien CS, Porter JR, Ge J, Grenier L, Pak RH, Ali JA, Dembski MS, Hudak J. Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI 504), an anti-cancer agent directed against Hsp90. Proc Natl Acad Sci U S A 2006, 103(46):17408-17413. 10.1073/pnas.0608372103, 1635022, 17090671.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.46 , pp. 17408-17413
    • Sydor, J.R.1    Normant, E.2    Pien, C.S.3    Porter, J.R.4    Ge, J.5    Grenier, L.6    Pak, R.H.7    Ali, J.A.8    Dembski, M.S.9    Hudak, J.10
  • 45
    • 44149091042 scopus 로고    scopus 로고
    • Stage 1 testing and pharmacodynamic evaluation of the HSP90 inhibitor alvespimycin (17-DMAG, KOS-1022) by the pediatric preclinical testing program
    • 10.1002/pbc.21508, 18260120
    • Smith MA, Morton CL, Phelps DA, Kolb EA, Lock R, Carol H, Reynolds CP, Maris JM, Keir ST, Wu J. Stage 1 testing and pharmacodynamic evaluation of the HSP90 inhibitor alvespimycin (17-DMAG, KOS-1022) by the pediatric preclinical testing program. Pediatr Blood Cancer 2008, 51(1):34-41. 10.1002/pbc.21508, 18260120.
    • (2008) Pediatr Blood Cancer , vol.51 , Issue.1 , pp. 34-41
    • Smith, M.A.1    Morton, C.L.2    Phelps, D.A.3    Kolb, E.A.4    Lock, R.5    Carol, H.6    Reynolds, C.P.7    Maris, J.M.8    Keir, S.T.9    Wu, J.10
  • 47
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers
    • 10.1016/S0002-9440(10)62994-X, 1603556, 16049336
    • Fratta P, Engel WK, McFerrin J, Davies KJ, Lin SW, Askanas V. Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers. Am J Pathol 2005, 167(2):517-526. 10.1016/S0002-9440(10)62994-X, 1603556, 16049336.
    • (2005) Am J Pathol , vol.167 , Issue.2 , pp. 517-526
    • Fratta, P.1    Engel, W.K.2    McFerrin, J.3    Davies, K.J.4    Lin, S.W.5    Askanas, V.6
  • 48
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • 10.1016/j.molcel.2009.04.026, 19450525
    • Kirkin V, McEwan DG, Novak I, Dikic I. A role for ubiquitin in selective autophagy. Mol Cell 2009, 34(3):259-269. 10.1016/j.molcel.2009.04.026, 19450525.
    • (2009) Mol Cell , vol.34 , Issue.3 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 49
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes FA, Dice JF. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 2001, 114(Pt 13):2491-2499.
    • (2001) J Cell Sci , vol.114 , Issue.PART 13 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 50
    • 0034282931 scopus 로고    scopus 로고
    • Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state
    • Salvador N, Aguado C, Horst M, Knecht E. Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J Biol Chem 2000, 275(35):27447-27456.
    • (2000) J Biol Chem , vol.275 , Issue.35 , pp. 27447-27456
    • Salvador, N.1    Aguado, C.2    Horst, M.3    Knecht, E.4
  • 51
    • 4344673498 scopus 로고    scopus 로고
    • Mechanisms of chaperone-mediated autophagy
    • 10.1016/j.biocel.2004.02.013, 15325583
    • Majeski AE, Dice JF. Mechanisms of chaperone-mediated autophagy. Int J Biochem Cell Biol 2004, 36(12):2435-2444. 10.1016/j.biocel.2004.02.013, 15325583.
    • (2004) Int J Biochem Cell Biol , vol.36 , Issue.12 , pp. 2435-2444
    • Majeski, A.E.1    Dice, J.F.2
  • 52
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • 10.1128/MCB.02070-07, 2546938, 18644871
    • Bandyopadhyay U, Kaushik S, Varticovski L, Cuervo AM. The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 2008, 28(18):5747-5763. 10.1128/MCB.02070-07, 2546938, 18644871.
    • (2008) Mol Cell Biol , vol.28 , Issue.18 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 53
    • 77951248828 scopus 로고    scopus 로고
    • Autophagy: links with the proteasome
    • 10.1016/j.ceb.2009.11.002, 19962293
    • Lamark T, Johansen T. Autophagy: links with the proteasome. Curr Opin Cell Biol 2010, 22(2):192-198. 10.1016/j.ceb.2009.11.002, 19962293.
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.2 , pp. 192-198
    • Lamark, T.1    Johansen, T.2
  • 54
    • 48349087467 scopus 로고    scopus 로고
    • Induction of autophagy by proteasome inhibitor is associated with proliferative arrest in colon cancer cells
    • 10.1016/j.bbrc.2008.07.031, 18638451
    • Wu WK, Wu YC, Yu L, Li ZJ, Sung JJ, Cho CH. Induction of autophagy by proteasome inhibitor is associated with proliferative arrest in colon cancer cells. Biochem Biophys Res Commun 2008, 374(2):258-263. 10.1016/j.bbrc.2008.07.031, 18638451.
    • (2008) Biochem Biophys Res Commun , vol.374 , Issue.2 , pp. 258-263
    • Wu, W.K.1    Wu, Y.C.2    Yu, L.3    Li, Z.J.4    Sung, J.J.5    Cho, C.H.6
  • 55
    • 67651146579 scopus 로고    scopus 로고
    • Inhibition of autophagy induced by proteasome inhibition increases cell death in human SHG-44 glioma cells
    • 10.1038/aps.2009.71, 19575007
    • Ge PF, Zhang JZ, Wang XF, Meng FK, Li WC, Luan YX, Ling F, Luo YN. Inhibition of autophagy induced by proteasome inhibition increases cell death in human SHG-44 glioma cells. Acta Pharmacol Sin 2009, 30(7):1046-1052. 10.1038/aps.2009.71, 19575007.
    • (2009) Acta Pharmacol Sin , vol.30 , Issue.7 , pp. 1046-1052
    • Ge, P.F.1    Zhang, J.Z.2    Wang, X.F.3    Meng, F.K.4    Li, W.C.5    Luan, Y.X.6    Ling, F.7    Luo, Y.N.8
  • 56
    • 67651155954 scopus 로고    scopus 로고
    • Oncogenic transformation confers a selective susceptibility to the combined suppression of the proteasome and autophagy
    • 10.1158/1535-7163.MCT-08-1169, 2711219, 19584239
    • Ding WX, Ni HM, Gao W, Chen X, Kang JH, Stolz DB, Liu J, Yin XM. Oncogenic transformation confers a selective susceptibility to the combined suppression of the proteasome and autophagy. Mol Cancer Ther 2009, 8(7):2036-2045. 10.1158/1535-7163.MCT-08-1169, 2711219, 19584239.
    • (2009) Mol Cancer Ther , vol.8 , Issue.7 , pp. 2036-2045
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Chen, X.4    Kang, J.H.5    Stolz, D.B.6    Liu, J.7    Yin, X.M.8
  • 57
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • 10.1016/j.cell.2007.12.018, 2696814, 18191218
    • Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008, 132(1):27-42. 10.1016/j.cell.2007.12.018, 2696814, 18191218.
    • (2008) Cell , vol.132 , Issue.1 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 58
    • 53549089861 scopus 로고    scopus 로고
    • Dual role of JNK1-mediated phosphorylation of Bcl-2 in autophagy and apoptosis regulation
    • 2677707, 18769111
    • Wei Y, Sinha S, Levine B. Dual role of JNK1-mediated phosphorylation of Bcl-2 in autophagy and apoptosis regulation. Autophagy 2008, 4(7):949-951. 2677707, 18769111.
    • (2008) Autophagy , vol.4 , Issue.7 , pp. 949-951
    • Wei, Y.1    Sinha, S.2    Levine, B.3
  • 59
    • 53549113031 scopus 로고    scopus 로고
    • The role of TOR in autophagy regulation from yeast to plants and mammals
    • Diaz-Troya S, Perez-Perez ME, Florencio FJ, Crespo JL. The role of TOR in autophagy regulation from yeast to plants and mammals. Autophagy 2008, 4(7):851-865.
    • (2008) Autophagy , vol.4 , Issue.7 , pp. 851-865
    • Diaz-Troya, S.1    Perez-Perez, M.E.2    Florencio, F.J.3    Crespo, J.L.4
  • 60
    • 38349074872 scopus 로고    scopus 로고
    • Hydrophobic statins induce autophagy in cultured human rhabdomyosarcoma cells
    • 10.1016/j.bbrc.2007.12.166, 18178158
    • Araki M, Motojima K. Hydrophobic statins induce autophagy in cultured human rhabdomyosarcoma cells. Biochem Biophys Res Commun 2008, 367(2):462-467. 10.1016/j.bbrc.2007.12.166, 18178158.
    • (2008) Biochem Biophys Res Commun , vol.367 , Issue.2 , pp. 462-467
    • Araki, M.1    Motojima, K.2


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