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Volumn 12, Issue 12, 2011, Pages 1023-1031

The heat shock proteins as targets for radiosensitization and chemosensitization in cancer

Author keywords

Cancer; Chemosensitization; Heat shock proteins; Radiosensitization

Indexed keywords

ALPHA CRYSTALLIN; ALVESPIMYCIN; BETA CRYSTALLIN; CISPLATIN; DOXORUBICIN; GELDANAMYCIN; GEMCITABINE; GLUCOSE REGULATED PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 10; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; IRINOTECAN; PACLITAXEL; PEPTIDE APTAMER; RADICICOL; TANESPIMYCIN; TRICHOSTATIN A;

EID: 84055190763     PISSN: 15384047     EISSN: 15558576     Source Type: Journal    
DOI: 10.4161/cbt.12.12.18374     Document Type: Review
Times cited : (24)

References (109)
  • 1
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature and DNP in Drosophila
    • Ritossa F. A new puffing pattern induced by temperature and DNP in Drosophila. Experimentia 1962; 18:571-3; http://dx.doi.org/10.1007/BF02172188
    • (1962) Experimentia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 2
    • 77952167700 scopus 로고    scopus 로고
    • Heat shock proteins as targets in oncology
    • PMID:20231121
    • Giménez Ortiz A, Montalar Salcedo J. Heat shock proteins as targets in oncology. Clin Transl Oncol 2010; 12:166-73; PMID:20231121; http://dx.doi.org/10.1007/s12094-010-0486-8
    • (2010) Clin Transl Oncol , vol.12 , pp. 166-173
    • Giménez Ortiz, A.1    Montalar Salcedo, J.2
  • 4
    • 36749002683 scopus 로고    scopus 로고
    • Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins
    • PMID:18045130
    • Didelot C, Lanneau D, Brunet M, Joly AL, De Thonel A, Chiosis G, et al. Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins. Curr Med Chem 2007; 14:2839-47; PMID:18045130; http://dx.doi.org/10.2174/092986707782360079
    • (2007) Curr Med Chem , vol.14 , pp. 2839-2847
    • Didelot, C.1    Lanneau, D.2    Brunet, M.3    Joly, A.L.4    De Thonel, A.5    Chiosis, G.6
  • 5
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • PMID:20628411
    • Akerfelt M, Morimoto RI, Sistonen L. Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 2010; 11:545-55; PMID:20628411; http://dx.doi.org/10.1038/nrm2938
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 6
    • 0024151897 scopus 로고
    • The heat-shock proteins
    • PMID:2853609
    • Lindquist S, Craig EA. The heat-shock proteins. Annu Rev Genet 1988; 22:631-77; PMID:2853609; http:// dx.doi.org/10.1146/annurev.ge.22.120188.003215
    • (1988) Annu Rev Genet , vol.22 , pp. 631-677
    • Lindquist, S.1    Craig, E.A.2
  • 7
    • 34248176724 scopus 로고    scopus 로고
    • Heat shock genes - Integrating cell survival and death
    • PMID:17536179
    • Arya R, Mallik M, Lakhotia SC. Heat shock genes - integrating cell survival and death. J Biosci 2007; 32:595-610; PMID:17536179; http://dx.doi.org/10.1007/s12038-007-0059-3
    • (2007) J Biosci , vol.32 , pp. 595-610
    • Arya, R.1    Mallik, M.2    Lakhotia, S.C.3
  • 8
    • 77955199612 scopus 로고    scopus 로고
    • Heat shock proteins: Cellular and molecular mechanisms in the central nervous system
    • PMID:20685377
    • Stetler RA, Gan Y, Zhang W, Liou AK, Gao Y, Cao G, et al. Heat shock proteins: cellular and molecular mechanisms in the central nervous system. Prog Neurobiol 2010; 92:184-211; PMID:20685377; http://dx.doi.org/10.1016/j. pneurobio.2010.05.002
    • (2010) Prog Neurobiol , vol.92 , pp. 184-211
    • Stetler, R.A.1    Gan, Y.2    Zhang, W.3    Liou, A.K.4    Gao, Y.5    Cao, G.6
  • 9
    • 33751203833 scopus 로고    scopus 로고
    • Heat shock proteins 27 and 70: Antiapoptotic proteins with tumorigenic properties
    • PMID:17106261
    • Garrido C, Brunet M, Didelot C, Zermati Y, Schmitt E, Kroemer G. Heat shock proteins 27 and 70: antiapoptotic proteins with tumorigenic properties. Cell Cycle 2006; 5:2592-601; PMID:17106261; http://dx.doi.org/10.4161/cc.5.22. 3448
    • (2006) Cell Cycle , vol.5 , pp. 2592-2601
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 10
    • 27744517366 scopus 로고    scopus 로고
    • Heat shock proteins as emerging therapeutic targets
    • PMID:16170327
    • Sõti C, Nagy E, Giricz Z, Vigh L, Csermely P, Ferdinandy P. Heat shock proteins as emerging therapeutic targets. Br J Pharmacol 2005; 146:769-80; PMID:16170327; http://dx.doi.org/10.1038/sj. bjp.0706396
    • (2005) Br J Pharmacol , vol.146 , pp. 769-780
    • Sõti, C.1    Nagy, E.2    Giricz, Z.3    Vigh, L.4    Csermely, P.5    Ferdinandy, P.6
  • 11
    • 77953576838 scopus 로고    scopus 로고
    • Targeting HSP70: The second potentially druggable heat shock protein and molecular chaperone?
    • PMID:20372081
    • Powers MV, Jones K, Barillari C, Westwood I, van Montfort RL, Workman P. Targeting HSP70: the second potentially druggable heat shock protein and molecular chaperone? Cell Cycle 2010; 9:1542-50; PMID:20372081; http://dx.doi.org/10.4161/cc.9.8.11204
    • (2010) Cell Cycle , vol.9 , pp. 1542-1550
    • Powers, M.V.1    Jones, K.2    Barillari, C.3    Westwood, I.4    Van Montfort, R.L.5    Workman, P.6
  • 12
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones, and proteotoxicity
    • PMID: 1855252
    • Hightower LE. Heat shock, stress proteins, chaperones, and proteotoxicity. Cell 1991; 66:191-7; PMID: 1855252; http://dx.doi.org/10.1016/ 0092-8674(91) 90611-2
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 13
    • 34447558236 scopus 로고    scopus 로고
    • ER chaperones in mammalian development and human diseases
    • PMID:17481612
    • Ni M, Lee AS. ER chaperones in mammalian development and human diseases. FEBS Lett 2007; 581:3641-51; PMID:17481612; http://dx.doi.org/10.1016/j.febslet. 2007.04.045
    • (2007) FEBS Lett , vol.581 , pp. 3641-3651
    • Ni, M.1    Lee, A.S.2
  • 14
    • 0034812599 scopus 로고    scopus 로고
    • Heat shock proteins: Endogenous modulators of apoptotic cell death
    • PMID:11511077
    • Garrido C, Gurbuxani S, Ravagnan L, Kroemer G. Heat shock proteins: endogenous modulators of apoptotic cell death. Biochem Biophys Res Commun 2001; 286:433-42; PMID:11511077; http://dx.doi.org/10.1006/bbrc.2001.5427
    • (2001) Biochem Biophys Res Commun , vol.286 , pp. 433-442
    • Garrido, C.1    Gurbuxani, S.2    Ravagnan, L.3    Kroemer, G.4
  • 15
    • 7744222195 scopus 로고    scopus 로고
    • Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
    • PMID: 15522909
    • Arispe N, Doh M, Simakova O, Kurganov B, De Maio A. Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J 2004; 18:1636-45; PMID: 15522909; http://dx.doi.org/10.1096/fj.04-2088com
    • (2004) FASEB J , vol.18 , pp. 1636-1645
    • Arispe, N.1    Doh, M.2    Simakova, O.3    Kurganov, B.4    De Maio, A.5
  • 16
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • PMID: 16175177
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005; 5:761-72; PMID: 16175177; http://dx.doi.org/10.1038/nrc1716
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 17
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • PMID:15177193
    • Kamal A, Boehm MF, Burrows FJ. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med 2004; 10:283-90; PMID:15177193; http://dx.doi.org/10.1016/j.molmed.2004.04.006
    • (2004) Trends Mol Med , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 18
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of hsp90 function results in degradation of the death domain kinase, receptorinteracting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation
    • PMID:10744744
    • Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L, et al. Disruption of hsp90 function results in degradation of the death domain kinase, receptorinteracting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem 2000; 275:10519-26; PMID:10744744; http://dx.doi.org/10.1074/jbc.275.14.10519
    • (2000) J Biol Chem , vol.275 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6
  • 19
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • PMID: 11864612
    • Chen G, Cao P, Goeddel DV. TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol Cell 2002; 9:401-10; PMID: 11864612; http://dx.doi.org/10.1016/S1097-2765(02) 00450-1
    • (2002) Mol Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 20
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • PMID:10995457
    • Sato S, Fujita N, Tsuruo T. Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci USA 2000; 97:10832-7; PMID:10995457; http://dx.doi.org/10.1073/pnas.170276797
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 21
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • PMID:12176997
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, Rosen N. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 2002; 277:39858-66; PMID:12176997; http://dx.doi.org/10.1074/jbc.M206322200
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 22
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
    • PMID:10944114
    • Pandey P, Saleh A, Nakazawa A, Kumar S, Srinivasula SM, Kumar V, et al. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J 2000; 19:4310-22; PMID:10944114; http://dx.doi.org/10.1093/emboj/19.16.4310
    • (2000) EMBO J , vol.19 , pp. 4310-4322
    • Pandey, P.1    Saleh, A.2    Nakazawa, A.3    Kumar, S.4    Srinivasula, S.M.5    Kumar, V.6
  • 23
    • 67650314916 scopus 로고    scopus 로고
    • Molecular parameters of hyperthermia for radiosensitization
    • PMID: 19883367
    • Pandita TK, Pandita S, Bhaumik SR. Molecular parameters of hyperthermia for radiosensitization. Crit Rev Eukaryot Gene Expr 2009; 19:235-51; PMID: 19883367
    • (2009) Crit Rev Eukaryot Gene Expr , vol.19 , pp. 235-251
    • Pandita, T.K.1    Pandita, S.2    Bhaumik, S.R.3
  • 24
    • 0035986356 scopus 로고    scopus 로고
    • Targeted disruption of hsf1 leads to lack of thermotolerance and defines tissue-specific regulation for stress-inducible Hsp molecular chaperones
    • PMID:12112007
    • Zhang Y, Huang L, Zhang J, Moskophidis D, Mivechi NF. Targeted disruption of hsf1 leads to lack of thermotolerance and defines tissue-specific regulation for stress-inducible Hsp molecular chaperones. J Cell Biochem 2002; 86:376-93; PMID:12112007; http://dx.doi.org/10.1002/jcb.10232
    • (2002) J Cell Biochem , vol.86 , pp. 376-393
    • Zhang, Y.1    Huang, L.2    Zhang, J.3    Moskophidis, D.4    Mivechi, N.F.5
  • 25
    • 33846682590 scopus 로고    scopus 로고
    • Heat shock protein 70 increases tumorigenicity and inhibits apoptosis in pancreatic adenocarcinoma
    • PMID:17234771
    • Aghdassi A, Phillips P, Dudeja V, Dhaulakhandi D, Sharif R, Dawra R, et al. Heat shock protein 70 increases tumorigenicity and inhibits apoptosis in pancreatic adenocarcinoma. Cancer Res 2007; 67: 616-25; PMID:17234771; http://dx.doi.org/10.1158/0008-5472.CAN-06-1567
    • (2007) Cancer Res , vol.67 , pp. 616-625
    • Aghdassi, A.1    Phillips, P.2    Dudeja, V.3    Dhaulakhandi, D.4    Sharif, R.5    Dawra, R.6
  • 26
    • 4344651318 scopus 로고    scopus 로고
    • Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization
    • PMID:15314073
    • Nylandsted J, Gyrd-Hansen M, Danielewicz A, Fehrenbacher N, Lademann U, Hoyer-Hansen M, et al. Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization. J Exp Med 2004; 200:425-35; PMID:15314073; http://dx.doi.org/10.1084/jem.20040531
    • (2004) J Exp Med , vol.200 , pp. 425-435
    • Nylandsted, J.1    Gyrd-Hansen, M.2    Danielewicz, A.3    Fehrenbacher, N.4    Lademann, U.5    Hoyer-Hansen, M.6
  • 27
    • 0036234472 scopus 로고    scopus 로고
    • Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis
    • PMID:11971973
    • Gabai VL, Mabuchi K, Mosser DD, Sherman MY. Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis. Mol Cell Biol 2002; 22:3415-24; PMID:11971973; http://dx.doi.org/10.1128/ MCB.22.10.3415-3424.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 3415-3424
    • Gabai, V.L.1    Mabuchi, K.2    Mosser, D.D.3    Sherman, M.Y.4
  • 28
    • 0242606282 scopus 로고    scopus 로고
    • Heat shock protein 70 binding inhibits the nuclear import of apoptosisinducing factor
    • PMID: 14555980
    • Gurbuxani S, Schmitt E, Cande C, Parcellier A, Hammann A, Daugas E, et al. Heat shock protein 70 binding inhibits the nuclear import of apoptosisinducing factor. Oncogene 2003; 22:6669-78; PMID: 14555980; http://dx.doi.org/10.1038/sj.onc.1206794
    • (2003) Oncogene , vol.22 , pp. 6669-6678
    • Gurbuxani, S.1    Schmitt, E.2    Cande, C.3    Parcellier, A.4    Hammann, A.5    Daugas, E.6
  • 29
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • PMID: 16175177
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005; 5:761-72; PMID: 16175177; http://dx.doi.org/10.1038/nrc1716
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 30
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • PMID:15177193
    • Kamal A, Boehm MF, Burrows FJ. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med 2004; 10:283-90; PMID:15177193; http://dx.doi.org/10.1016/j.molmed.2004.04.006
    • (2004) Trends Mol Med , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 31
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of hsp90 function results in degradation of the death domain kinase, receptorinteracting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation
    • PMID:10744744
    • Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L, et al. Disruption of hsp90 function results in degradation of the death domain kinase, receptorinteracting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem 2000; 275:10519-26; PMID:10744744; http://dx.doi.org/10.1074/jbc.275.14.10519
    • (2000) J Biol Chem , vol.275 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6
  • 32
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • PMID: 11864612
    • Chen G, Cao P, Goeddel DV. TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol Cell 2002; 9:401-10; PMID: 11864612; http://dx.doi.org/10.1016/S1097-2765(02) 00450-1
    • (2002) Mol Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 33
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • PMID:10995457
    • Sato S, Fujita N, Tsuruo T. Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci USA 2000; 97:10832-7; PMID:10995457; http://dx.doi.org/10.1073/pnas.170276797
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 34
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • PMID:12176997
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, Rosen N. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 2002; 277:39858-66; PMID:12176997; http://dx.doi.org/10.1074/jbc.M206322200
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 35
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
    • PMID:10944114
    • Pandey P, Saleh A, Nakazawa A, Kumar S, Srinivasula SM, Kumar V, et al. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J 2000; 19:4310-22; PMID:10944114; http://dx.doi.org/10.1093/emboj/19.16.4310
    • (2000) EMBO J , vol.19 , pp. 4310-4322
    • Pandey, P.1    Saleh, A.2    Nakazawa, A.3    Kumar, S.4    Srinivasula, S.M.5    Kumar, V.6
  • 36
    • 67650314916 scopus 로고    scopus 로고
    • Molecular parameters of hyperthermia for radiosensitization
    • PMID: 19883367
    • Pandita TK, Pandita S, Bhaumik SR. Molecular parameters of hyperthermia for radiosensitization. Crit Rev Eukaryot Gene Expr 2009; 19:235-51; PMID: 19883367
    • (2009) Crit Rev Eukaryot Gene Expr , vol.19 , pp. 235-251
    • Pandita, T.K.1    Pandita, S.2    Bhaumik, S.R.3
  • 37
    • 0035986356 scopus 로고    scopus 로고
    • Targeted disruption of hsf1 leads to lack of thermotolerance and defines tissue-specific regulation for stress-inducible Hsp molecular chaperones
    • PMID:12112007
    • Zhang Y, Huang L, Zhang J, Moskophidis D, Mivechi NF. Targeted disruption of hsf1 leads to lack of thermotolerance and defines tissue-specific regulation for stress-inducible Hsp molecular chaperones. J Cell Biochem 2002; 86:376-93; PMID:12112007; http://dx.doi.org/10.1002/jcb.10232
    • (2002) J Cell Biochem , vol.86 , pp. 376-393
    • Zhang, Y.1    Huang, L.2    Zhang, J.3    Moskophidis, D.4    Mivechi, N.F.5
  • 38
    • 33846682590 scopus 로고    scopus 로고
    • Heat shock protein 70 increases tumorigenicity and inhibits apoptosis in pancreatic adenocarcinoma
    • PMID:17234771
    • Aghdassi A, Phillips P, Dudeja V, Dhaulakhandi D, Sharif R, Dawra R, et al. Heat shock protein 70 increases tumorigenicity and inhibits apoptosis in pancreatic adenocarcinoma. Cancer Res 2007; 67: 616-25; PMID:17234771; http://dx.doi.org/10.1158/ 0008-5472.CAN-06-1567
    • (2007) Cancer Res , vol.67 , pp. 616-625
    • Aghdassi, A.1    Phillips, P.2    Dudeja, V.3    Dhaulakhandi, D.4    Sharif, R.5    Dawra, R.6
  • 39
    • 4344651318 scopus 로고    scopus 로고
    • Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization
    • PMID:15314073
    • Nylandsted J, Gyrd-Hansen M, Danielewicz A, Fehrenbacher N, Lademann U, Hoyer-Hansen M, et al. Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization. J Exp Med 2004; 200:425-35; PMID:15314073; http://dx.doi.org/10.1084/jem.20040531
    • (2004) J Exp Med , vol.200 , pp. 425-435
    • Nylandsted, J.1    Gyrd-Hansen, M.2    Danielewicz, A.3    Fehrenbacher, N.4    Lademann, U.5    Hoyer-Hansen, M.6
  • 40
    • 0036234472 scopus 로고    scopus 로고
    • Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis
    • PMID:11971973
    • Gabai VL, Mabuchi K, Mosser DD, Sherman MY. Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis. Mol Cell Biol 2002; 22:3415-24; PMID:11971973; http://dx.doi.org/10.1128/ MCB.22.10.3415-3424.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 3415-3424
    • Gabai, V.L.1    Mabuchi, K.2    Mosser, D.D.3    Sherman, M.Y.4
  • 41
    • 0242606282 scopus 로고    scopus 로고
    • Heat shock protein 70 binding inhibits the nuclear import of apoptosisinducing factor
    • PMID: 14555980
    • Gurbuxani S, Schmitt E, Cande C, Parcellier A, Hammann A, Daugas E, et al. Heat shock protein 70 binding inhibits the nuclear import of apoptosisinducing factor. Oncogene 2003; 22:6669-78; PMID: 14555980; http://dx.doi.org/10.1038/sj.onc.1206794
    • (2003) Oncogene , vol.22 , pp. 6669-6678
    • Gurbuxani, S.1    Schmitt, E.2    Cande, C.3    Parcellier, A.4    Hammann, A.5    Daugas, E.6
  • 42
    • 0034253474 scopus 로고    scopus 로고
    • Negative regulation of the Apaf-1 apoptosome by Hsp70
    • PMID:10934467
    • Saleh A, Srinivasula SM, Balkir L, Robbins PD, Alnemri ES. Negative regulation of the Apaf-1 apoptosome by Hsp70. Nat Cell Biol 2000; 2:476-83; PMID:10934467; http://dx.doi.org/10.1038/35019510
    • (2000) Nat Cell Biol , vol.2 , pp. 476-483
    • Saleh, A.1    Srinivasula, S.M.2    Balkir, L.3    Robbins, P.D.4    Alnemri, E.S.5
  • 43
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • PMID:9799222
    • Jäättelä M, Wissing D, Kokholm K, Kallunki T, Egeblad M. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J 1998; 17:6124-34; PMID:9799222; http://dx.doi.org/10.1093/emboj/17.21. 6124
    • (1998) EMBO J , vol.17 , pp. 6124-6134
    • Jäättelä, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 44
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • PMID:11282911
    • Lin KM, Lin B, Lian IY, Mestril R, Scheffler IE, Dillmann WH. Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation. Circulation 2001; 103:1787-92; PMID:11282911
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 45
    • 0037129860 scopus 로고    scopus 로고
    • Cytosolic heat shock protein 60, apoptosis, and myocardial injury
    • PMID:12070120
    • Kirchhoff SR, Gupta S, Knowlton AA. Cytosolic heat shock protein 60, apoptosis, and myocardial injury. Circulation 2002; 105:2899-904; PMID:12070120; http://dx.doi.org/10.1161/01.CIR.0000019403.35847.23
    • (2002) Circulation , vol.105 , pp. 2899-2904
    • Kirchhoff, S.R.1    Gupta, S.2    Knowlton, A.A.3
  • 46
    • 9644281610 scopus 로고    scopus 로고
    • Expression of heat-shock protein Hsp60 correlated with the apoptotic index and patient prognosis in human oesophageal squamous cell carcinoma
    • PMID:15571964
    • Faried A, Sohda M, Nakajima M, Miyazaki T, Kato H, Kuwano H. Expression of heat-shock protein Hsp60 correlated with the apoptotic index and patient prognosis in human oesophageal squamous cell carcinoma. Eur J Cancer 2004; 40:2804-11; PMID:15571964; http://dx.doi.org/10.1016/j.ejca.2004.08.013
    • (2004) Eur J Cancer , vol.40 , pp. 2804-2811
    • Faried, A.1    Sohda, M.2    Nakajima, M.3    Miyazaki, T.4    Kato, H.5    Kuwano, H.6
  • 47
    • 59649118541 scopus 로고    scopus 로고
    • Hsp60D is essential for caspasemediated induced apoptosis in Drosophila melanogaster
    • PMID: 18506601
    • Arya R, Lakhotia SC. Hsp60D is essential for caspasemediated induced apoptosis in Drosophila melanogaster. Cell Stress Chaperones 2008; 13:509-26; PMID: 18506601; http://dx.doi.org/10.1007/s12192-008-0051-3
    • (2008) Cell Stress Chaperones , vol.13 , pp. 509-526
    • Arya, R.1    Lakhotia, S.C.2
  • 48
    • 77951715190 scopus 로고    scopus 로고
    • Small heat shock proteins: Recent advances in neuropathy
    • PMID:20438447
    • Zeng L, Hu Z, Lu W, Tang X, Zhang J, Li T, et al. Small heat shock proteins: recent advances in neuropathy. Curr Neurovasc Res 2010; 7:155-66; PMID:20438447; http://dx.doi.org/10.2174/156720210791184934
    • (2010) Curr Neurovasc Res , vol.7 , pp. 155-166
    • Zeng, L.1    Hu, Z.2    Lu, W.3    Tang, X.4    Zhang, J.5    Li, T.6
  • 49
    • 67649262170 scopus 로고    scopus 로고
    • Dysregulation of heat shock protein 27 expression in oral tongue squamous cell carcinoma
    • PMID:19497117
    • Wang A, Liu X, Sheng S, Ye H, Peng T, Shi F, et al. Dysregulation of heat shock protein 27 expression in oral tongue squamous cell carcinoma. BMC Cancer 2009; 9:167; PMID:19497117; http://dx.doi.org/10.1186/1471-2407-9-167
    • (2009) BMC Cancer , vol.9 , pp. 167
    • Wang, A.1    Liu, X.2    Sheng, S.3    Ye, H.4    Peng, T.5    Shi, F.6
  • 50
    • 33645823223 scopus 로고    scopus 로고
    • Prognostic value of HSP27 in head and neck squamous cell carcinoma: A retrospective analysis of 57 tumours
    • PMID:16619543
    • Lo Muzio L, Campisi G, Farina A, Rubini C, Ferrari F, Falaschini S, et al. Prognostic value of HSP27 in head and neck squamous cell carcinoma: a retrospective analysis of 57 tumours. Anticancer Res 2006; 26:1343-9; PMID:16619543
    • (2006) Anticancer Res , vol.26 , pp. 1343-1349
    • Lo Muzio, L.1    Campisi, G.2    Farina, A.3    Rubini, C.4    Ferrari, F.5    Falaschini, S.6
  • 51
    • 0036092428 scopus 로고    scopus 로고
    • Size matters: Of the small HSP27 and its large oligomers
    • PMID:11973606
    • Garrido C. Size matters: of the small HSP27 and its large oligomers. Cell Death Differ 2002; 9:483-5; PMID:11973606; http://dx.doi.org/10.1038/sj.cdd. 4401005
    • (2002) Cell Death Differ , vol.9 , pp. 483-485
    • Garrido, C.1
  • 52
    • 0033972325 scopus 로고    scopus 로고
    • Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
    • PMID: 10625643
    • Bova MP, McHaourab HS, Han Y, Fung BK. Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations. J Biol Chem 2000; 275:1035-42; PMID: 10625643; http://dx.doi.org/10.1074/jbc.275.2.1035
    • (2000) J Biol Chem , vol.275 , pp. 1035-1042
    • Bova, M.P.1    McHaourab, H.S.2    Han, Y.3    Fung, B.K.4
  • 53
    • 9644260484 scopus 로고    scopus 로고
    • Self-association of a small heat shock protein
    • PMID:15581903
    • Lelj-Garolla B, Mauk AG. Self-association of a small heat shock protein. J Mol Biol 2005; 345:631-42; PMID:15581903; http://dx.doi.org/10.1016/j.jmb. 2004.10.056
    • (2005) J Mol Biol , vol.345 , pp. 631-642
    • Lelj-Garolla, B.1    Mauk, A.G.2
  • 55
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of Daxx-mediated apoptosis by heat shock protein 27
    • PMID: 11003656
    • Charette SJ, Lavoie JN, Lambert H, Landry J. Inhibition of Daxx-mediated apoptosis by heat shock protein 27. Mol Cell Biol 2000; 20:7602-12; PMID: 11003656; http://dx.doi.org/10.1128/MCB.20.20.7602-7612.2000
    • (2000) Mol Cell Biol , vol.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3    Landry, J.4
  • 56
    • 0034282104 scopus 로고    scopus 로고
    • Hsp27 negatively regulates cell death by interacting with cytochrome c
    • PMID:10980706
    • Bruey JM, Ducasse C, Bonniaud P, Ravagnan L, Susin SA, Diaz-Latoud C, et al. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2000; 2:645-52; PMID:10980706; http://dx.doi. org/10.1038/35023595
    • (2000) Nat Cell Biol , vol.2 , pp. 645-652
    • Bruey, J.M.1    Ducasse, C.2    Bonniaud, P.3    Ravagnan, L.4    Susin, S.A.5    Diaz-Latoud, C.6
  • 57
    • 79951876376 scopus 로고    scopus 로고
    • Altered cross-linking of HSP27 by zerumbone as a novel strategy for overcoming HSP27-mediated radioresistance
    • PMID:21353161
    • Choi SH, Lee YJ, Seo WD, Lee HJ, Nam JW, Kim J, et al. Altered cross-linking of HSP27 by zerumbone as a novel strategy for overcoming HSP27-mediated radioresistance. Int J Radiat Oncol Biol Phys 2011; 79:1196-205; PMID:21353161; http://dx.doi.org/10.1016/j.ijrobp.2010.10.025
    • (2011) Int J Radiat Oncol Biol Phys , vol.79 , pp. 1196-1205
    • Choi, S.H.1    Lee, Y.J.2    Seo, W.D.3    Lee, H.J.4    Nam, J.W.5    Kim, J.6
  • 58
    • 38149112827 scopus 로고    scopus 로고
    • Protective role of Hsp27 protein against gamma radiation-induced apoptosis and radiosensitization effects of Hsp27 gene silencing in different human tumor cells
    • PMID:17980509
    • Aloy MT, Hadchity E, Bionda C, Diaz-Latoud C, Claude L, Rousson R, et al. Protective role of Hsp27 protein against gamma radiation-induced apoptosis and radiosensitization effects of Hsp27 gene silencing in different human tumor cells. Int J Radiat Oncol Biol Phys 2008; 70:543-53; PMID:17980509; http://dx.doi.org/10.1016/j.ijrobp.2007.08.061
    • (2008) Int J Radiat Oncol Biol Phys , vol.70 , pp. 543-553
    • Aloy, M.T.1    Hadchity, E.2    Bionda, C.3    Diaz-Latoud, C.4    Claude, L.5    Rousson, R.6
  • 59
    • 14044272992 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins: Dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme
    • PMID:15542604
    • Shashidharamurthy R, Koteiche HA, Dong J, McHaourab HS. Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme. J Biol Chem 2005; 280:5281-9; PMID:15542604; http://dx.doi.org/10.1074/ jbc.M407236200
    • (2005) J Biol Chem , vol.280 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 60
    • 0041344614 scopus 로고    scopus 로고
    • Heat shock protein 27 controls apoptosis by regulating Akt activation
    • PMID:12740362
    • Rane MJ, Pan Y, Singh S, Powell DW, Wu R, Cummins T, et al. Heat shock protein 27 controls apoptosis by regulating Akt activation. J Biol Chem 2003; 278:27828-35; PMID:12740362; http://dx.doi.org/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
  • 61
    • 45549088083 scopus 로고    scopus 로고
    • Hsp27 inhibits Bax activation and apoptosis via a phosphatidylinositol 3-kinasedependent mechanism
    • PMID:18299320
    • Havasi A, Li Z, Wang Z, Martin JL, Botla V, Ruchalski K, et al. Hsp27 inhibits Bax activation and apoptosis via a phosphatidylinositol 3-kinasedependent mechanism. J Biol Chem 2008; 283:12305-13; PMID:18299320; http://dx.doi.org/10.1074/jbc.M801291200
    • (2008) J Biol Chem , vol.283 , pp. 12305-12313
    • Havasi, A.1    Li, Z.2    Wang, Z.3    Martin, J.L.4    Botla, V.5    Ruchalski, K.6
  • 62
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human alphaBcrystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha-induced cell death
    • PMID:8654367
    • Mehlen P, Kretz-Remy C, Preville X, Arrigo AP. Human hsp27, Drosophila hsp27 and human alphaBcrystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha-induced cell death. EMBO J 1996; 15:2695-706; PMID:8654367
    • (1996) EMBO J , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Kretz-Remy, C.2    Preville, X.3    Arrigo, A.P.4
  • 63
    • 14044250859 scopus 로고    scopus 로고
    • Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels
    • PMID: 15706088
    • Arrigo AP, Virot S, Chaufour S, Firdaus W, Kretz- Remy C, Diaz-Latoud C. Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels. Antioxid Redox Signal 2005; 7:414-22; PMID: 15706088; http://dx.doi.org/10.1089/ars.2005.7.414
    • (2005) Antioxid Redox Signal , vol.7 , pp. 414-422
    • Arrigo, A.P.1    Virot, S.2    Chaufour, S.3    Firdaus, W.4    Kretz- Remy, C.5    Diaz-Latoud, C.6
  • 64
    • 0036143720 scopus 로고    scopus 로고
    • Hsp27 as a negative regulator of cytochrome C release
    • PMID:11784858
    • Paul C, Manero F, Gonin S, Kretz-Remy C, Virot S, Arrigo AP. Hsp27 as a negative regulator of cytochrome C release. Mol Cell Biol 2002; 22:816-34; PMID:11784858; http://dx.doi.org/10.1128/MCB.22.3.816-834.2002
    • (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
  • 66
    • 33751523271 scopus 로고    scopus 로고
    • Overexpression of human 27 kDa heat shock protein in laryngeal cancer cells confers chemoresistance associated with cell growth delay
    • PMID:16906418
    • Lee JH, Sun D, Cho KJ, Kim MS, Hong MH, Kim IK, et al. Overexpression of human 27 kDa heat shock protein in laryngeal cancer cells confers chemoresistance associated with cell growth delay. J Cancer Res Clin Oncol 2007; 133:37-46; PMID:16906418; http://dx.doi.org/10.1007/s00432-006-0143-3
    • (2007) J Cancer Res Clin Oncol , vol.133 , pp. 37-46
    • Lee, J.H.1    Sun, D.2    Cho, K.J.3    Kim, M.S.4    Hong, M.H.5    Kim, I.K.6
  • 67
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • PMID: 7799959
    • Lavoie JN, Lambert H, Hickey E, Weber LA, Landry J. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol 1995; 15:505-16; PMID: 7799959
    • (1995) Mol Cell Biol , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 68
    • 0043133793 scopus 로고    scopus 로고
    • HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation
    • PMID:12897149
    • Parcellier A, Schmitt E, Gurbuxani S, Seigneurin- Berny D, Pance A, Chantome A, et al. HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation. Mol Cell Biol 2003; 23:5790-802; PMID:12897149; http://dx.doi.org/10.1128/ MCB.23.16.5790-5802.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 5790-5802
    • Parcellier, A.1    Schmitt, E.2    Gurbuxani, S.3    Seigneurin- Berny, D.4    Pance, A.5    Chantome, A.6
  • 69
    • 33644835965 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: Chaperones of tumorigenesis
    • PMID:16483782
    • Calderwood SK, Khaleque MA, Sawyer DB, Ciocca DR. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci 2006; 31:164-72; PMID:16483782; http://dx.doi.org/10.1016/j.tibs.2006.01.006
    • (2006) Trends Biochem Sci , vol.31 , pp. 164-172
    • Calderwood, S.K.1    Khaleque, M.A.2    Sawyer, D.B.3    Ciocca, D.R.4
  • 70
    • 77649147755 scopus 로고    scopus 로고
    • Heat shock cognate protein 70 is essential for Akt signaling in endothelial function
    • PMID:20018937
    • Shiota M, Kusakabe H, Izumi Y, Hikita Y, Nakao T, Funae Y, et al. Heat shock cognate protein 70 is essential for Akt signaling in endothelial function. Arterioscler Thromb Vasc Biol 2010; 30:491-7; PMID:20018937; http://dx.doi.org/10.1161/ ATVBAHA.109.193631
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , pp. 491-497
    • Shiota, M.1    Kusakabe, H.2    Izumi, Y.3    Hikita, Y.4    Nakao, T.5    Funae, Y.6
  • 71
    • 20944433868 scopus 로고    scopus 로고
    • Proteomic analysis of mantle-cell lymphoma by protein microarray
    • PMID:15650054
    • Ghobrial IM, McCormick DJ, Kaufmann SH, Leontovich AA, Loegering DA, Dai NT, et al. Proteomic analysis of mantle-cell lymphoma by protein microarray. Blood 2005; 105:3722-30; PMID:15650054; http://dx.doi.org/10.1182/blood-2004-10- 3999
    • (2005) Blood , vol.105 , pp. 3722-3730
    • Ghobrial, I.M.1    McCormick, D.J.2    Kaufmann, S.H.3    Leontovich, A.A.4    Loegering, D.A.5    Dai, N.T.6
  • 72
    • 34248195608 scopus 로고    scopus 로고
    • High HSP90 expression is associated with decreased survival in breast cancer
    • PMID:17409397
    • Pick E, Kluger Y, Giltnane JM, Moeder C, Camp RL, Rimm DL, et al. High HSP90 expression is associated with decreased survival in breast cancer. Cancer Res 2007; 67:2932-7; PMID:17409397; http://dx.doi.org/10.1158/0008-5472.CAN-06- 4511
    • (2007) Cancer Res , vol.67 , pp. 2932-2937
    • Pick, E.1    Kluger, Y.2    Giltnane, J.M.3    Moeder, C.4    Camp, R.L.5    Rimm, D.L.6
  • 73
    • 0031708908 scopus 로고    scopus 로고
    • Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy
    • PMID: 9761114
    • Vargas-Roig LM, Gago FE, Tello O, Aznar JC, Ciocca DR. Heat shock protein expression and drug resistance in breast cancer patients treated with induction chemotherapy. Int J Cancer 1998; 79:468-75; PMID: 9761114; http://dx.doi.org/ 10.1002/(SICI)1097-0215 (19981023)79:5,468::AID-IJC4.3.0.CO;2-Z
    • (1998) Int J Cancer , vol.79 , pp. 468-475
    • Vargas-Roig, L.M.1    Gago, F.E.2    Tello, O.3    Aznar, J.C.4    Ciocca, D.R.5
  • 75
    • 3442878404 scopus 로고    scopus 로고
    • Plasma levels of heat shock protein 70 in patients with prostate cancer: A potential biomarker for prostate cancer
    • PMID:15279691
    • Abe M, Manola JB, Oh WK, Parslow DL, George DJ, Austin CL, et al. Plasma levels of heat shock protein 70 in patients with prostate cancer: a potential biomarker for prostate cancer. Clin Prostate Cancer 2004; 3:49-53; PMID:15279691
    • (2004) Clin Prostate Cancer , vol.3 , pp. 49-53
    • Abe, M.1    Manola, J.B.2    Oh, W.K.3    Parslow, D.L.4    George, D.J.5    Austin, C.L.6
  • 76
    • 4143151967 scopus 로고    scopus 로고
    • Genomic mechanisms of p210BCRABL signaling: Induction of heat shock protein 70 through the GATA response element confers resistance to paclitaxel-induced apoptosis
    • PMID:15155749
    • Ray S, Lu Y, Kaufmann SH, Gustafson WC, Karp JE, Boldogh I, et al. Genomic mechanisms of p210BCRABL signaling: induction of heat shock protein 70 through the GATA response element confers resistance to paclitaxel-induced apoptosis. J Biol Chem 2004; 279:35604-15; PMID:15155749; http://dx.doi.org/10. 1074/jbc.M401851200
    • (2004) J Biol Chem , vol.279 , pp. 35604-35615
    • Ray, S.1    Lu, Y.2    Kaufmann, S.H.3    Gustafson, W.C.4    Karp, J.E.5    Boldogh, I.6
  • 77
    • 33845525384 scopus 로고    scopus 로고
    • Overexpression of the heat-shock protein 70 is associated to imatinib resistance in chronic myeloid leukemia
    • PMID: 17109025
    • Pocaly M, Lagarde V, Etienne G, Ribeil JA, Claverol S, Bonneu M, et al. Overexpression of the heat-shock protein 70 is associated to imatinib resistance in chronic myeloid leukemia. Leukemia 2007; 21:93-101; PMID: 17109025; http://dx.doi.org/10.1038/sj.leu.2404463
    • (2007) Leukemia , vol.21 , pp. 93-101
    • Pocaly, M.1    Lagarde, V.2    Etienne, G.3    Ribeil, J.A.4    Claverol, S.5    Bonneu, M.6
  • 78
    • 79952825166 scopus 로고    scopus 로고
    • Chemoresistance of lung cancer stemlike cells depends on activation of Hsp27
    • PMID:21425153
    • Hsu HS, Lin JH, Huang WC, Hsu TW, Su K, Chiou SH, et al. Chemoresistance of lung cancer stemlike cells depends on activation of Hsp27. Cancer 2011; 117:1516-28; PMID:21425153; http://dx.doi.org/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
  • 79
    • 0030785821 scopus 로고    scopus 로고
    • HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs
    • PMID:9205074
    • Garrido C, Ottavi P, Fromentin A, Hammann A, Arrigo AP, Chauffert B, et al. HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs. Cancer Res 1997; 57:2661-7; PMID:9205074
    • (1997) Cancer Res , vol.57 , pp. 2661-2667
    • Garrido, C.1    Ottavi, P.2    Fromentin, A.3    Hammann, A.4    Arrigo, A.P.5    Chauffert, B.6
  • 80
    • 77955241980 scopus 로고    scopus 로고
    • Silencing heat shock protein 27 decreases metastatic behavior of human head and neck squamous cell cancer cells in vitro
    • PMID:20540527
    • Zhu Z, Xu X, Yu Y, Graham M, Prince ME, Carey TE, et al. Silencing heat shock protein 27 decreases metastatic behavior of human head and neck squamous cell cancer cells in vitro. Mol Pharm 2010; 7: 1283-90; PMID:20540527; http://dx.doi.org/10.1021/mp100073s
    • (2010) Mol Pharm , vol.7 , pp. 1283-1290
    • Zhu, Z.1    Xu, X.2    Yu, Y.3    Graham, M.4    Prince, M.E.5    Carey, T.E.6
  • 81
    • 33645066349 scopus 로고    scopus 로고
    • Proteomic analysis reveals a novel role for the actin cytoskeleton in vincristine resistant childhood leukemia-an in vivo study
    • PMID:16456880
    • Verrills NM, Liem NL, Liaw TY, Hood BD, Lock RB, Kavallaris M. Proteomic analysis reveals a novel role for the actin cytoskeleton in vincristine resistant childhood leukemia-an in vivo study. Proteomics 2006; 6:1681-94; PMID:16456880; http://dx.doi.org/10.1002/pmic.200500417
    • (2006) Proteomics , vol.6 , pp. 1681-1694
    • Verrills, N.M.1    Liem, N.L.2    Liaw, T.Y.3    Hood, B.D.4    Lock, R.B.5    Kavallaris, M.6
  • 82
    • 77953454825 scopus 로고    scopus 로고
    • Identification of potential therapeutic targets in human head & neck squamous cell carcinoma
    • PMID:19602232
    • Han J, Kioi M, Chu WS, Kasperbauer JL, Strome SE, Puri RK. Identification of potential therapeutic targets in human head & neck squamous cell carcinoma. Head Neck Oncol 2009; 1:27; PMID:19602232; http://dx. doi.org/10.1186/1758-3284-1-27
    • (2009) Head Neck Oncol , vol.1 , pp. 27
    • Han, J.1    Kioi, M.2    Chu, W.S.3    Kasperbauer, J.L.4    Strome, S.E.5    Puri, R.K.6
  • 83
    • 77951255162 scopus 로고    scopus 로고
    • Hsp90 inhibitors as promising agents for radiotherapy
    • (Berl) PMID:19946660
    • Kabakov AE, Kudryavtsev VA, Gabai VL. Hsp90 inhibitors as promising agents for radiotherapy. J Mol Med (Berl) 2010; 88:241-7; PMID:19946660
    • (2010) J Mol Med , vol.88 , pp. 241-247
    • Kabakov, A.E.1    Kudryavtsev, V.A.2    Gabai, V.L.3
  • 84
    • 33749469341 scopus 로고    scopus 로고
    • Inhibition of hsp90 compromises the DNA damage response to radiation
    • PMID:16982765
    • Dote H, Burgan WE, Camphausen K, Tofilon PJ. Inhibition of hsp90 compromises the DNA damage response to radiation. Cancer Res 2006; 66:9211-20; PMID:16982765; http://dx.doi.org/10.1158/0008-5472.CAN-06-2181
    • (2006) Cancer Res , vol.66 , pp. 9211-9220
    • Dote, H.1    Burgan, W.E.2    Camphausen, K.3    Tofilon, P.J.4
  • 85
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • PMID:11850835
    • Basso AD, Solit DB, Munster PN, Rosen N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 2002; 21:1159-66; PMID:11850835; http://dx.doi.org/10.1038/sj. onc.1205184
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 86
    • 4644237335 scopus 로고    scopus 로고
    • Heat shock protein 27 increases after androgen ablation and plays a cytoprotective role in hormone-refractory prostate cancer
    • PMID:15374973
    • Rocchi P, So A, Kojima S, Signaevsky M, Beraldi E, Fazli L, et al. Heat shock protein 27 increases after androgen ablation and plays a cytoprotective role in hormone-refractory prostate cancer. Cancer Res 2004; 64:6595-602; PMID:15374973; http://dx.doi.org/10.1158/0008-5472.CAN-03-3998
    • (2004) Cancer Res , vol.64 , pp. 6595-6602
    • Rocchi, P.1    So, A.2    Kojima, S.3    Signaevsky, M.4    Beraldi, E.5    Fazli, L.6
  • 87
    • 34047132772 scopus 로고    scopus 로고
    • Heat shock protein 27 is associated with irinotecan resistance in human colorectal cancer cells
    • PMID:17395183
    • Choi DH, Ha JS, Lee WH, Song JK, Kim GY, Park JH, et al. Heat shock protein 27 is associated with irinotecan resistance in human colorectal cancer cells. FEBS Lett 2007; 581:1649-56; PMID:17395183; http://dx.doi.org/10.1016/j. febslet.2007.02.075
    • (2007) FEBS Lett , vol.581 , pp. 1649-1656
    • Choi, D.H.1    Ha, J.S.2    Lee, W.H.3    Song, J.K.4    Kim, G.Y.5    Park, J.H.6
  • 88
    • 33845301225 scopus 로고    scopus 로고
    • Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism
    • PMID:17108135
    • McCollum AK, Teneyck CJ, Sauer BM, Toft DO, Erlichman C. Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism. Cancer Res 2006; 66:10967-75; PMID:17108135; http://dx.doi.org/10.1158/0008-5472.CAN-06-1629
    • (2006) Cancer Res , vol.66 , pp. 10967-10975
    • McCollum, A.K.1    Teneyck, C.J.2    Sauer, B.M.3    Toft, D.O.4    Erlichman, C.5
  • 89
    • 68849099328 scopus 로고    scopus 로고
    • Intravesical combination treatment with antisense oligonucleotides targeting heat shock protein-27 and HTI-286 as a novel strategy for high-grade bladder cancer
    • PMID:19625496
    • Matsui Y, Hadaschik BA, Fazli L, Andersen RJ, Gleave ME, So AI. Intravesical combination treatment with antisense oligonucleotides targeting heat shock protein-27 and HTI-286 as a novel strategy for high-grade bladder cancer. Mol Cancer Ther 2009; 8:2402-11; PMID:19625496; http://dx.doi.org/10. 1158/1535-7163.MCT-09-0148
    • (2009) Mol Cancer Ther , vol.8 , pp. 2402-2411
    • Matsui, Y.1    Hadaschik, B.A.2    Fazli, L.3    Andersen, R.J.4    Gleave, M.E.5    So, A.I.6
  • 90
    • 0742304429 scopus 로고    scopus 로고
    • Geldanamycin, an inhibitor of Hsp90, sensitizes human tumour cells to radiation
    • PMID:14713575
    • Machida H, Matsumoto Y, Shirai M, Kubota N. Geldanamycin, an inhibitor of Hsp90, sensitizes human tumour cells to radiation. Int J Radiat Biol 2003; 79:973-80; PMID:14713575; http://dx.doi.org/10.1080/09553000310001626135
    • (2003) Int J Radiat Biol , vol.79 , pp. 973-980
    • Machida, H.1    Matsumoto, Y.2    Shirai, M.3    Kubota, N.4
  • 91
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • PMID:14508491
    • Kamal A, Thao L, Sensintaffar J, Zhang L, Boehm MF, Fritz LC, et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003; 425:407-10; PMID:14508491; http://dx.doi.org/10.1038/ nature01913
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3    Zhang, L.4    Boehm, M.F.5    Fritz, L.C.6
  • 92
    • 64549140105 scopus 로고    scopus 로고
    • Inhibition of heat shock induction of heat shock protein 70 and enhancement of heat shock protein 27 phosphorylation by quercetin derivatives
    • PMID: 19296652
    • Wang RE, Kao JL, Hilliard CA, Pandita RK, Roti Roti JL, Hunt CR, et al. Inhibition of heat shock induction of heat shock protein 70 and enhancement of heat shock protein 27 phosphorylation by quercetin derivatives. J Med Chem 2009; 52:1912-21; PMID: 19296652; http://dx.doi.org/10.1021/jm801445c
    • (2009) J Med Chem , vol.52 , pp. 1912-1921
    • Wang, R.E.1    Kao, J.L.2    Hilliard, C.A.3    Pandita, R.K.4    Roti Roti, J.L.5    Hunt, C.R.6
  • 93
    • 33646900838 scopus 로고    scopus 로고
    • Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death
    • PMID:16469748
    • Westerheide SD, Kawahara TL, Orton K, Morimoto RI. Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death. J Biol Chem 2006; 281:9616-22; PMID:16469748; http:// dx.doi.org/10.1074/jbc.M512044200
    • (2006) J Biol Chem , vol.281 , pp. 9616-9622
    • Westerheide, S.D.1    Kawahara, T.L.2    Orton, K.3    Morimoto, R.I.4
  • 94
    • 33748760880 scopus 로고    scopus 로고
    • Down-regulation of Hsp27 radiosensitizes human prostate cancer cells
    • PMID:16984557
    • Teimourian S, Jalal R, Sohrabpour M, Goliaei B. Down-regulation of Hsp27 radiosensitizes human prostate cancer cells. Int J Urol 2006; 13:1221-5; PMID:16984557; http://dx.doi.org/10.1111/j.1442-2042.2006.01483.x
    • (2006) Int J Urol , vol.13 , pp. 1221-1225
    • Teimourian, S.1    Jalal, R.2    Sohrabpour, M.3    Goliaei, B.4
  • 95
    • 68249119157 scopus 로고    scopus 로고
    • Heat shock protein 27 as a new therapeutic target for radiation sensitization of head and neck squamous cell carcinoma
    • PMID:19436268
    • Hadchity E, Aloy MT, Paulin C, Armandy E, Watkin E, Rousson R, et al. Heat shock protein 27 as a new therapeutic target for radiation sensitization of head and neck squamous cell carcinoma. Mol Ther 2009; 17:1387-94; PMID:19436268; http://dx.doi.org/10.1038/mt.2009.90
    • (2009) Mol Ther , vol.17 , pp. 1387-1394
    • Hadchity, E.1    Aloy, M.T.2    Paulin, C.3    Armandy, E.4    Watkin, E.5    Rousson, R.6
  • 96
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • PMID: 7592678
    • Schulte TW, Blagosklonny MV, Ingui C, Neckers L. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J Biol Chem 1995; 270:24585-8; PMID: 7592678; http://dx.doi.org/10.1074/jbc.270.41.24585
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 97
    • 23044480581 scopus 로고    scopus 로고
    • ErbB3 expression predicts tumor cell radiosensitization induced by Hsp90 inhibition
    • PMID:16061682
    • Dote H, Cerna D, Burgan WE, Camphausen K, Tofilon PJ. ErbB3 expression predicts tumor cell radiosensitization induced by Hsp90 inhibition. Cancer Res 2005; 65:6967-75; PMID:16061682; http://dx.doi.org/10.1158/0008-5472.CAN-05-1304
    • (2005) Cancer Res , vol.65 , pp. 6967-6975
    • Dote, H.1    Cerna, D.2    Burgan, W.E.3    Camphausen, K.4    Tofilon, P.J.5
  • 99
    • 68849126662 scopus 로고    scopus 로고
    • Enhanced radiosensitization of human glioma cells by combining inhibition of poly(ADP-ribose) polymerase with inhibition of heat shock protein 90
    • PMID:19671736
    • Dungey FA, Caldecott KW, Chalmers AJ. Enhanced radiosensitization of human glioma cells by combining inhibition of poly(ADP-ribose) polymerase with inhibition of heat shock protein 90. Mol Cancer Ther 2009; 8:2243-54; PMID:19671736; http://dx.doi.org/10.1158/1535-7163.MCT-09-0201
    • (2009) Mol Cancer Ther , vol.8 , pp. 2243-2254
    • Dungey, F.A.1    Caldecott, K.W.2    Chalmers, A.J.3
  • 100
    • 37549000210 scopus 로고    scopus 로고
    • Proteomic analysis of two head and neck cancer cell lines presenting different radiation sensitivity
    • PMID:17917836
    • Lee YS, Chang HW, Jeong JE, Lee SW, Kim SY. Proteomic analysis of two head and neck cancer cell lines presenting different radiation sensitivity. Acta Otolaryngol 2008; 128:86-92; PMID:17917836; http://dx.doi.org/10.1080/ 00016480601110196
    • (2008) Acta Otolaryngol , vol.128 , pp. 86-92
    • Lee, Y.S.1    Chang, H.W.2    Jeong, J.E.3    Lee, S.W.4    Kim, S.Y.5
  • 101
    • 0029610424 scopus 로고
    • Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (hsp27) structural organization and phosphorylation in basal and tumour necrosis factor alpha-treated T47D human carcinoma cells
    • PMID: 8526844
    • Mehlen P, Kretz-Remy C, Briolay J, Fostan P, Mirault ME, Arrigo AP. Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (hsp27) structural organization and phosphorylation in basal and tumour necrosis factor alpha-treated T47D human carcinoma cells. Biochem J 1995; 312:367-75; PMID: 8526844
    • (1995) Biochem J , vol.312 , pp. 367-375
    • Mehlen, P.1    Kretz-Remy, C.2    Briolay, J.3    Fostan, P.4    Mirault, M.E.5    Arrigo, A.P.6
  • 102
    • 51049088872 scopus 로고    scopus 로고
    • HSP90 inhibitor, DMAG, synergizes with radiation of lung cancer cells by interfering with base excision and ATM-mediated DNA repair
    • PMID:18645008
    • Koll TT, Feis SS, Wright MH, Teniola MM, Richardson MM, Robles AI, et al. HSP90 inhibitor, DMAG, synergizes with radiation of lung cancer cells by interfering with base excision and ATM-mediated DNA repair. Mol Cancer Ther 2008; 7:1985-92; PMID:18645008; http://dx.doi.org/10.1158/1535-7163.MCT-07-2104
    • (2008) Mol Cancer Ther , vol.7 , pp. 1985-1992
    • Koll, T.T.1    Feis, S.S.2    Wright, M.H.3    Teniola, M.M.4    Richardson, M.M.5    Robles, A.I.6
  • 103
    • 33750696349 scopus 로고    scopus 로고
    • Inhibition of homologous recombination repair in irradiated tumor cells pretreated with Hsp90 inhibitor 17-allylamino-17- Demethoxygeldanamycin
    • PMID:17083915
    • Noguchi M, Yu D, Hirayama R, Ninomiya Y, Sekine E, Kubota N, et al. Inhibition of homologous recombination repair in irradiated tumor cells pretreated with Hsp90 inhibitor 17-allylamino-17- demethoxygeldanamycin. Biochem Biophys Res Commun 2006; 351:658-63; PMID:17083915; http://dx.doi.org/10.1016/ j.bbrc.2006.10.094
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 658-663
    • Noguchi, M.1    Yu, D.2    Hirayama, R.3    Ninomiya, Y.4    Sekine, E.5    Kubota, N.6
  • 104
    • 2342611976 scopus 로고    scopus 로고
    • Radiation activates HIF-1 to regulate vascular radiosensitivity in tumors: Role of reoxygenation, free radicals, and stress granules
    • PMID: 15144951
    • Moeller BJ, Cao Y, Li CY, Dewhirst MW. Radiation activates HIF-1 to regulate vascular radiosensitivity in tumors: role of reoxygenation, free radicals, and stress granules. Cancer Cell 2004; 5:429-41; PMID: 15144951; http://dx.doi.org/10.1016/S1535-6108(04) 00115-1
    • (2004) Cancer Cell , vol.5 , pp. 429-441
    • Moeller, B.J.1    Cao, Y.2    Li, C.Y.3    Dewhirst, M.W.4
  • 105
    • 33746191768 scopus 로고    scopus 로고
    • Inhibitors of the HSP90 molecular chaperone: Current status
    • PMID:16860662
    • Sharp S, Workman P. Inhibitors of the HSP90 molecular chaperone: current status. Adv Cancer Res 2006; 95:323-48; PMID:16860662; http://dx.doi.org/10. 1016/S0065-230X(06)95009-X
    • (2006) Adv Cancer Res , vol.95 , pp. 323-348
    • Sharp, S.1    Workman, P.2
  • 106
    • 60549083336 scopus 로고    scopus 로고
    • Targeting heat shock protein 90 overrides the resistance of lung cancer cells by blocking radiation-induced stabilization of hypoxia-inducible factor-1alpha
    • PMID:19176399
    • Kim WY, Oh SH, Woo JK, Hong WK, Lee HY. Targeting heat shock protein 90 overrides the resistance of lung cancer cells by blocking radiation-induced stabilization of hypoxia-inducible factor-1alpha. Cancer Res 2009; 69:1624-32; PMID:19176399; http://dx. doi.org/10.1158/0008-5472.CAN-08-0505
    • (2009) Cancer Res , vol.69 , pp. 1624-1632
    • Kim, W.Y.1    Oh, S.H.2    Woo, J.K.3    Hong, W.K.4    Lee, H.Y.5
  • 107
    • 9144261127 scopus 로고    scopus 로고
    • Geldanamycin and 17- Allylamino-17-demethoxygeldanamycin potentiate the in vitro and in vivo radiation response of cervical tumor cells via the heat shock protein 90-mediated intracellular signaling and cytotoxicity
    • PMID:14695217
    • Bisht KS, Bradbury CM, Mattson D, Kaushal A, Sowers A, Markovina S, et al. Geldanamycin and 17- allylamino-17-demethoxygeldanamycin potentiate the in vitro and in vivo radiation response of cervical tumor cells via the heat shock protein 90-mediated intracellular signaling and cytotoxicity. Cancer Res 2003; 63:8984-95; PMID:14695217
    • (2003) Cancer Res , vol.63 , pp. 8984-8995
    • Bisht, K.S.1    Bradbury, C.M.2    Mattson, D.3    Kaushal, A.4    Sowers, A.5    Markovina, S.6
  • 108
    • 79960985832 scopus 로고    scopus 로고
    • Current state of knowledge regarding the use of antiangiogenic agents with radiation therapy
    • PMID:21546163
    • Mazeron R, Anderson B, Supiot S, Paris F, Deutsch E. Current state of knowledge regarding the use of antiangiogenic agents with radiation therapy. Cancer Treat Rev 2011; 37:476-86; PMID:21546163
    • (2011) Cancer Treat Rev , vol.37 , pp. 476-486
    • Mazeron, R.1    Anderson, B.2    Supiot, S.3    Paris, F.4    Deutsch, E.5
  • 109
    • 0034306974 scopus 로고    scopus 로고
    • Anti-Vascular endothelial growth factor treatment augments tumor radiation response under normoxic or hypoxic conditions
    • PMID:11034104
    • Lee CG, Heijn M, di Tomaso E, Griffon-Etienne G, Ancukiewicz M, Koike C, et al. Anti-Vascular endothelial growth factor treatment augments tumor radiation response under normoxic or hypoxic conditions. Cancer Res 2000; 60:5565-70; PMID:11034104
    • (2000) Cancer Res , vol.60 , pp. 5565-5570
    • Lee, C.G.1    Heijn, M.2    Di Tomaso, E.3    Griffon-Etienne, G.4    Ancukiewicz, M.5    Koike, C.6


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