메뉴 건너뛰기




Volumn 15, Issue 4, 2014, Pages 423-431

Hsp27 as a therapeutic target in cancers

Author keywords

Cancer; Heat shock protein Hsp27; Protein inhibition; Targeted therapy

Indexed keywords

APATORSEN; APOPTOSIS SIGNAL REGULATING KINASE 1; CHAPERONE; CISPLATIN; DAXX PROTEIN; DOXORUBICIN; GELATINASE A; GELATINASE B; GEMCITABINE; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN B10; HEAT SHOCK PROTEIN B11; HEAT SHOCK PROTEIN B2; HEAT SHOCK PROTEIN B4; HEAT SHOCK PROTEIN B5; HEAT SHOCK PROTEIN B7; HEAT SHOCK PROTEIN B8; HEAT SHOCK PROTEIN B9; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IRINOTECAN; MITOGEN ACTIVATED PROTEIN KINASE; PACLITAXEL; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN BAX; PROTEIN KINASE B; REACTIVE OXYGEN METABOLITE; RP 101; SOMATOMEDIN C; TRANSFORMING GROWTH FACTOR BETA; UBIQUITIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84896348569     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/13894501113146660230     Document Type: Review
Times cited : (48)

References (127)
  • 1
    • 0020067552 scopus 로고
    • Modulation of heat-shock polypeptide synthesis in HeLa cells during hyperthermia and recovery
    • Hickey ED, Weber LA. Modulation of heat-shock polypeptide synthesis in HeLa cells during hyperthermia and recovery. Biochemistry 1982; 21(7): 1513-21.
    • (1982) Biochemistry , vol.21 , Issue.7 , pp. 1513-1521
    • Hickey, E.D.1    Weber, L.A.2
  • 3
    • 0042825251 scopus 로고    scopus 로고
    • Heat shock protein 27 gene: Chromosomal and molecular location and relationship to Williams syndrome
    • Stock AD, Spallone PA, Dennis TR, et al. Heat shock protein 27 gene: chromosomal and molecular location and relationship to Williams syndrome. Am J Med Genet A 2003; 120A(3): 320-5.
    • (2003) Am J Med Genet A , vol.120 A , Issue.3 , pp. 320-325
    • Stock, A.D.1    Spallone, P.A.2    Dennis, T.R.3
  • 4
    • 0036809333 scopus 로고    scopus 로고
    • sHsps and their role in the chaperone network
    • Haslbeck M. sHsps and their role in the chaperone network. Cell Mol Life Sci 2002; 59(10): 1649-57.
    • (2002) Cell Mol Life Sci , vol.59 , Issue.10 , pp. 1649-1657
    • Haslbeck, M.1
  • 5
    • 33846945050 scopus 로고    scopus 로고
    • The small heat shock proteins and their clients
    • Nakamoto H, Vigh L. The small heat shock proteins and their clients. Cell Mol Life Sci 2007; 64(3): 294-306.
    • (2007) Cell Mol Life Sci , vol.64 , Issue.3 , pp. 294-306
    • Nakamoto, H.1    Vigh, L.2
  • 6
    • 0343742639 scopus 로고    scopus 로고
    • Binding of nonnative protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M, Graber S, Gaestel M, Buchner J. Binding of nonnative protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 1997 15; 16(2): 221-9.
    • (1997) EMBO J , vol.15-16 , Issue.2 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 7
    • 0036558366 scopus 로고    scopus 로고
    • Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
    • Gusev NB, Bogatcheva NV, Marston SB. Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins. Biochemistry (Mosc) 2002; 67(5): 511-9.
    • (2002) Biochemistry (Mosc) , vol.67 , Issue.5 , pp. 511-519
    • Gusev, N.B.1    Bogatcheva, N.V.2    Marston, S.B.3
  • 8
    • 77955665257 scopus 로고    scopus 로고
    • Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB
    • Kappe G, Boelens WC, de Jong WW. Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB. Cell Stress Chaperones 2010; 15(4): 457-61.
    • (2010) Cell Stress Chaperones , vol.15 , Issue.4 , pp. 457-461
    • Kappe, G.1    Boelens, W.C.2    de Jong, W.W.3
  • 9
    • 9644260484 scopus 로고    scopus 로고
    • Self-association of a small heat shock protein
    • Lelj-Garolla B, Mauk AG. Self-association of a small heat shock protein. J Mol Biol 2005; 345(3): 631-42.
    • (2005) J Mol Biol , vol.345 , Issue.3 , pp. 631-642
    • Lelj-Garolla, B.1    Mauk, A.G.2
  • 10
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim KK, Kim R, Kim SH. Crystal structure of a small heat-shock protein. Nature 1998; 394(6693): 595-9.
    • (1998) Nature , vol.394 , Issue.6693 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 12
    • 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
    • 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(2): 1035-42.
    • (2000) J Biol Chem , vol.275 , Issue.2 , pp. 1035-1042
    • Bova, M.P.1    McHaourab, H.S.2    Han, Y.3    Fung, B.K.4
  • 13
    • 79953235355 scopus 로고    scopus 로고
    • Crystal structures of Xanthomonas small heat shock protein provide a structural basis for an active molecular chaperone oligomer
    • Hilario E, Martin FJ, Bertolini MC, Fan L. Crystal structures of Xanthomonas small heat shock protein provide a structural basis for an active molecular chaperone oligomer. J Mol Biol 2011; 408(1): 74-86.
    • (2011) J Mol Biol , vol.408 , Issue.1 , pp. 74-86
    • Hilario, E.1    Martin, F.J.2    Bertolini, M.C.3    Fan, L.4
  • 14
    • 25144461582 scopus 로고    scopus 로고
    • Wrapping the alphacrystallin domain fold in a chaperone assembly
    • Stamler R, Kappe G, Boelens W, Slingsby C. Wrapping the alphacrystallin domain fold in a chaperone assembly. J Mol Biol 2005; 353(1): 68-79.
    • (2005) J Mol Biol , vol.353 , Issue.1 , pp. 68-79
    • Stamler, R.1    Kappe, G.2    Boelens, W.3    Slingsby, C.4
  • 15
    • 79953798740 scopus 로고    scopus 로고
    • Chaperone Hsp27 modulates AUF1 proteolysis and AU-rich element-mediated mRNA degradation
    • Knapinska AM, Gratacos FM, Krause CD, et al. Chaperone Hsp27 modulates AUF1 proteolysis and AU-rich element-mediated mRNA degradation. Mol Cell Biol 2011; 31(7): 1419-31.
    • (2011) Mol Cell Biol , vol.31 , Issue.7 , pp. 1419-1431
    • Knapinska, A.M.1    Gratacos, F.M.2    Krause, C.D.3
  • 16
    • 0037157161 scopus 로고    scopus 로고
    • The determinants of the oligomeric structure in Hsp16.5 are encoded in the alpha-crystallin domain
    • Koteiche HA, McHaourab HS. The determinants of the oligomeric structure in Hsp16.5 are encoded in the alpha-crystallin domain. FEBS Lett 2002; 519(1-3): 16-22.
    • (2002) FEBS Lett , vol.519 , Issue.1-3 , pp. 16-22
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 17
    • 40149107721 scopus 로고    scopus 로고
    • Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins
    • Ghosh JG, Houck SA, Clark JI. Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins. Int J Biochem Cell Biol 2008; 40(5): 954-67.
    • (2008) Int J Biochem Cell Biol , vol.40 , Issue.5 , pp. 954-967
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 18
    • 0033515597 scopus 로고    scopus 로고
    • HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus
    • Lambert H, Charette SJ, Bernier AF, Guimond A, Landry J. HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus. J Biol Chem 1999; 274(14): 9378-85.
    • (1999) J Biol Chem , vol.274 , Issue.14 , pp. 9378-9385
    • Lambert, H.1    Charette, S.J.2    Bernier, A.F.3    Guimond, A.4    Landry, J.5
  • 19
    • 67650547950 scopus 로고    scopus 로고
    • Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function
    • Hayes D, Napoli V, Mazurkie A, Stafford WF, Graceffa P. Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function. J Biol Chem 2009; 284(28): 18801-7.
    • (2009) J Biol Chem , vol.284 , Issue.28 , pp. 18801-18807
    • Hayes, D.1    Napoli, V.2    Mazurkie, A.3    Stafford, W.F.4    Graceffa, P.5
  • 20
    • 0033516660 scopus 로고    scopus 로고
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation
    • Rogalla T, Ehrnsperger M, Preville X, et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem 1999; 274(27): 18947-56.
    • (1999) J Biol Chem , vol.274 , Issue.27 , pp. 18947-18956
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3
  • 21
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • Haley DA, Bova MP, Huang QL, McHaourab HS, Stewart PL. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. J Mol Biol 2000; 298(2): 261-72.
    • (2000) J Mol Biol , vol.298 , Issue.2 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.L.3    McHaourab, H.S.4    Stewart, P.L.5
  • 22
    • 0042820029 scopus 로고    scopus 로고
    • Enhancement of chaperone function of alpha-crystallin by methylglyoxal modification
    • Nagaraj RH, Oya-Ito T, Padayatti PS, et al. Enhancement of chaperone function of alpha-crystallin by methylglyoxal modification. Biochemistry 2003; 42(36): 10746-55.
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10746-10755
    • Nagaraj, R.H.1    Oya-Ito, T.2    Padayatti, P.S.3
  • 23
    • 33748087444 scopus 로고    scopus 로고
    • Effect of methylglyoxal modification and phosphorylation on the chaperone and antiapoptotic properties of heat shock protein 27
    • Oya-Ito T, Liu BF, Nagaraj RH. Effect of methylglyoxal modification and phosphorylation on the chaperone and antiapoptotic properties of heat shock protein 27. J Cell Biochem 2006; 99(1): 279-91.
    • (2006) J Cell Biochem , vol.99 , Issue.1 , pp. 279-291
    • Oya-Ito, T.1    Liu, B.F.2    Nagaraj, R.H.3
  • 24
    • 0037195845 scopus 로고    scopus 로고
    • Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification
    • Sakamoto H, Mashima T, Yamamoto K, Tsuruo T. Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification. J Biol Chem 2002; 277(48): 45770-5.
    • (2002) J Biol Chem , vol.277 , Issue.48 , pp. 45770-45775
    • Sakamoto, H.1    Mashima, T.2    Yamamoto, K.3    Tsuruo, T.4
  • 25
    • 33746741644 scopus 로고    scopus 로고
    • Argpyrimidine-modified Heat shock protein 27 in human non-small cell lung cancer: A possible mechanism for evasion of apoptosis
    • van Heijst JW, Niessen HW, Musters RJ, van Hinsbergh VW, Hoekman K, Schalkwijk CG. Argpyrimidine-modified Heat shock protein 27 in human non-small cell lung cancer: a possible mechanism for evasion of apoptosis. Cancer Lett 2006; 241(2): 309-19.
    • (2006) Cancer Lett , vol.241 , Issue.2 , pp. 309-319
    • van Heijst, J.W.1    Niessen, H.W.2    Musters, R.J.3    van Hinsbergh, V.W.4    Hoekman, K.5    Schalkwijk, C.G.6
  • 26
    • 0032517252 scopus 로고    scopus 로고
    • Thiol/disulfide exchange between small heat shock protein 25 and glutathione
    • Zavialov AV, Gaestel M, Korpela T, Zav'yalov VP. Thiol/disulfide exchange between small heat shock protein 25 and glutathione. Biochim Biophys Acta 1998; 1388(1): 123-32.
    • (1998) Biochim Biophys Acta , vol.1388 , Issue.1 , pp. 123-132
    • Zavialov, A.V.1    Gaestel, M.2    Korpela, T.3    Zav'yalov, V.P.4
  • 27
    • 0037077277 scopus 로고    scopus 로고
    • S-thiolation of HSP27 regulates its multimeric aggregate size independently of phosphorylation
    • Eaton P, Fuller W, Shattock MJ. S-thiolation of HSP27 regulates its multimeric aggregate size independently of phosphorylation. J Biol Chem 2002; 277(24): 21189-96.
    • (2002) J Biol Chem , vol.277 , Issue.24 , pp. 21189-21196
    • Eaton, P.1    Fuller, W.2    Shattock, M.J.3
  • 28
    • 0035831438 scopus 로고    scopus 로고
    • Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelets: Phosphorylation-induced actin polymerization caused by HSP27 mutants
    • Butt E, Immler D, Meyer HE, Kotlyarov A, Laass K, Gaestel M. Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelets: phosphorylation-induced actin polymerization caused by HSP27 mutants. J Biol Chem 2001; 276(10): 7108-13.
    • (2001) J Biol Chem , vol.276 , Issue.10 , pp. 7108-7113
    • Butt, E.1    Immler, D.2    Meyer, H.E.3    Kotlyarov, A.4    Laass, K.5    Gaestel, M.6
  • 29
    • 0026570931 scopus 로고
    • Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogenactivated kinases that recognize the same amino acid motif as S6 kinase II
    • Landry J, Lambert H, Zhou M, et al. Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogenactivated kinases that recognize the same amino acid motif as S6 kinase II. J Biol Chem 1992; 267(2): 794-803.
    • (1992) J Biol Chem , vol.267 , Issue.2 , pp. 794-803
    • Landry, J.1    Lambert, H.2    Zhou, M.3
  • 30
    • 0028346451 scopus 로고
    • Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
    • Kato K, Hasegawa K, Goto S, Inaguma Y. Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27. J Biol Chem 1994; 269(15): 11274-8.
    • (1994) J Biol Chem , vol.269 , Issue.15 , pp. 11274-11278
    • Kato, K.1    Hasegawa, K.2    Goto, S.3    Inaguma, Y.4
  • 31
    • 0034609765 scopus 로고    scopus 로고
    • Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo
    • Bruey JM, Paul C, Fromentin A, et al. Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo. Oncogene 2000; 19(42): 4855-63.
    • (2000) Oncogene , vol.19 , Issue.42 , pp. 4855-4863
    • Bruey, J.M.1    Paul, C.2    Fromentin, A.3
  • 32
    • 59349113370 scopus 로고    scopus 로고
    • Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20)
    • Bukach OV, Glukhova AE, Seit-Nebi AS, Gusev NB. Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20). Biochim Biophys Acta 2009; 1794(3): 486-95.
    • (2009) Biochim Biophys Acta , vol.1794 , Issue.3 , pp. 486-495
    • Bukach, O.V.1    Glukhova, A.E.2    Seit-Nebi, A.S.3    Gusev, N.B.4
  • 34
    • 0031056783 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by p38 map kinasemediated phosphorylation of heat shock protein 27
    • Guay J, Lambert H, Gingras-Breton G, Lavoie JN, Huot J, Landry J. Regulation of actin filament dynamics by p38 map kinasemediated phosphorylation of heat shock protein 27. J Cell Sci 1997; 110 (Pt 3): 357-68.
    • (1997) J Cell Sci , vol.110 , Issue.PART 3 , pp. 357-368
    • Guay, J.1    Lambert, H.2    Gingras-Breton, G.3    Lavoie, J.N.4    Huot, J.5    Landry, J.6
  • 35
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • 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(1): 505-16.
    • (1995) Mol Cell Biol , vol.15 , Issue.1 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 36
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of Daxxmediated apoptosis by heat shock protein 27
    • Charette SJ, Lavoie JN, Lambert H, Landry J. Inhibition of Daxxmediated apoptosis by heat shock protein 27. Mol Cell Biol 2000; 20(20): 7602-12.
    • (2000) Mol Cell Biol , vol.20 , Issue.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3    Landry, J.4
  • 37
    • 33845623275 scopus 로고    scopus 로고
    • HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells
    • Parcellier A, Brunet M, Schmitt E, et al. HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells. FASEB J 2006; 20(8): 1179-81.
    • (2006) FASEB J , vol.20 , Issue.8 , pp. 1179-1181
    • Parcellier, A.1    Brunet, M.2    Schmitt, E.3
  • 38
    • 0043133793 scopus 로고    scopus 로고
    • HSP27 is a ubiquitinbinding protein involved in I-kappaBalpha proteasomal degradation
    • Parcellier A, Schmitt E, Gurbuxani S, et al. HSP27 is a ubiquitinbinding protein involved in I-kappaBalpha proteasomal degradation. Mol Cell Biol 2003; 23(16): 5790-802.
    • (2003) Mol Cell Biol , vol.23 , Issue.16 , pp. 5790-5802
    • Parcellier, A.1    Schmitt, E.2    Gurbuxani, S.3
  • 39
    • 33646345849 scopus 로고    scopus 로고
    • Self-association and chaperone activity of Hsp27 are thermally activated
    • Lelj-Garolla B, Mauk AG. Self-association and chaperone activity of Hsp27 are thermally activated. J Biol Chem 2006; 281(12): 8169-74.
    • (2006) J Biol Chem , vol.281 , Issue.12 , pp. 8169-8174
    • Lelj-Garolla, B.1    Mauk, A.G.2
  • 40
    • 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
    • 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(7): 5281-9.
    • (2005) J Biol Chem , vol.280 , Issue.7 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 41
    • 57349114099 scopus 로고    scopus 로고
    • Heat shock protein expression in diabetic nephropathy
    • Barutta F, Pinach S, Giunti S, et al. Heat shock protein expression in diabetic nephropathy. Am J Physiol Renal Physiol 2008; 295(6): F1817-24.
    • (2008) Am J Physiol Renal Physiol , vol.295 , Issue.6
    • Barutta, F.1    Pinach, S.2    Giunti, S.3
  • 42
    • 57149087666 scopus 로고    scopus 로고
    • Autoantibodies in the autoimmune disease pemphigus foliaceus induce blistering via p38 mitogen-activated protein kinase-dependent signaling in the skin
    • Berkowitz P, Chua M, Liu Z, Diaz LA, Rubenstein DS. Autoantibodies in the autoimmune disease pemphigus foliaceus induce blistering via p38 mitogen-activated protein kinase-dependent signaling in the skin. Am J Pathol 2008; 173(6): 1628-36.
    • (2008) Am J Pathol , vol.173 , Issue.6 , pp. 1628-1636
    • Berkowitz, P.1    Chua, M.2    Liu, Z.3    Diaz, L.A.4    Rubenstein, D.S.5
  • 43
    • 39149110925 scopus 로고    scopus 로고
    • Induction of p38MAPK and HSP27 phosphorylation in pemphigus patient skin
    • Berkowitz P, Diaz LA, Hall RP, Rubenstein DS. Induction of p38MAPK and HSP27 phosphorylation in pemphigus patient skin. J Invest Dermatol 2008; 128(3): 738-40.
    • (2008) J Invest Dermatol , vol.128 , Issue.3 , pp. 738-740
    • Berkowitz, P.1    Diaz, L.A.2    Hall, R.P.3    Rubenstein, D.S.4
  • 45
    • 55549122292 scopus 로고    scopus 로고
    • Pyrrolo-pyrimidones: A novel class of MK2 inhibitors with potent cellular activity
    • Schlapbach A, Feifel R, Hawtin S, et al. Pyrrolo-pyrimidones: a novel class of MK2 inhibitors with potent cellular activity. Bioorg Med Chem Lett 2008 1; 18(23): 6142-6.
    • (2008) Bioorg Med Chem Lett , vol.18 , Issue.23 , pp. 6142-6146
    • Schlapbach, A.1    Feifel, R.2    Hawtin, S.3
  • 46
    • 33749436432 scopus 로고    scopus 로고
    • Inhibitors of signal transduction protein kinases as targets for cancer therapy
    • Mikalsen T, Gerits N, Moens U. Inhibitors of signal transduction protein kinases as targets for cancer therapy. Biotechnol Annu Rev 2006; 12: 153-223.
    • (2006) Biotechnol Annu Rev , vol.12 , pp. 153-223
    • Mikalsen, T.1    Gerits, N.2    Moens, U.3
  • 48
    • 0026774629 scopus 로고
    • Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle
    • Kato K, Shinohara H, Goto S, Inaguma Y, Morishita R, Asano T. Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle. J Biol Chem 1992; 267(11): 7718-25.
    • (1992) J Biol Chem , vol.267 , Issue.11 , pp. 7718-7725
    • Kato, K.1    Shinohara, H.2    Goto, S.3    Inaguma, Y.4    Morishita, R.5    Asano, T.6
  • 49
    • 0034004638 scopus 로고    scopus 로고
    • The expression of small heat shock proteins in seeds responds to discrete developmental signals and suggests a general protective role in desiccation tolerance
    • Wehmeyer N, Vierling E. The expression of small heat shock proteins in seeds responds to discrete developmental signals and suggests a general protective role in desiccation tolerance. Plant Physiol 2000; 122(4): 1099-108.
    • (2000) Plant Physiol , vol.122 , Issue.4 , pp. 1099-1108
    • Wehmeyer, N.1    Vierling, E.2
  • 50
    • 77954338941 scopus 로고    scopus 로고
    • Pulmonary vascular remodeling in congenital heart disease: Enhanced expression of heat shock proteins
    • Geiger R, Sharma HS, Mooi WJ, Berger RM. Pulmonary vascular remodeling in congenital heart disease: enhanced expression of heat shock proteins. Indian J Biochem Biophys 2009; 46(6): 482-90.
    • (2009) Indian J Biochem Biophys , vol.46 , Issue.6 , pp. 482-490
    • Geiger, R.1    Sharma, H.S.2    Mooi, W.J.3    Berger, R.M.4
  • 51
    • 0030862335 scopus 로고    scopus 로고
    • Abundance and location of the small heat shock proteins HSP25 and alphaB-crystallin in rat and human heart
    • Lutsch G, Vetter R, Offhauss U, et al. Abundance and location of the small heat shock proteins HSP25 and alphaB-crystallin in rat and human heart. Circulation 1997; 96(10): 3466-76.
    • (1997) Circulation , vol.96 , Issue.10 , pp. 3466-3476
    • Lutsch, G.1    Vetter, R.2    Offhauss, U.3
  • 52
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: Diagnostic, prognostic, predictive, and treatment implications
    • Ciocca DR, Calderwood SK. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 2005; 10(2): 86-103.
    • (2005) Cell Stress Chaperones , vol.10 , Issue.2 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 53
    • 0037439058 scopus 로고    scopus 로고
    • Administration of brain-derived neurotrophic factor suppresses the expression of heat shock protein 27 in rat retinal ganglion cells following axotomy
    • Krueger-Naug AM, Emsley JG, Myers TL, Currie RW, Clarke DB. Administration of brain-derived neurotrophic factor suppresses the expression of heat shock protein 27 in rat retinal ganglion cells following axotomy. Neuroscience 2003; 116(1): 49-58.
    • (2003) Neuroscience , vol.116 , Issue.1 , pp. 49-58
    • Krueger-Naug, A.M.1    Emsley, J.G.2    Myers, T.L.3    Currie, R.W.4    Clarke, D.B.5
  • 54
    • 0038805383 scopus 로고    scopus 로고
    • Induction of Hsp27 and Hsp32 stress proteins and vimentin in glial cells of the rat hippocampus following hyperthermia
    • Bechtold DA, Brown IR. Induction of Hsp27 and Hsp32 stress proteins and vimentin in glial cells of the rat hippocampus following hyperthermia. Neurochem Res 2003; 28(8): 1163-73.
    • (2003) Neurochem Res , vol.28 , Issue.8 , pp. 1163-1173
    • Bechtold, D.A.1    Brown, I.R.2
  • 55
    • 0027158545 scopus 로고
    • Structure and organisation of a murine gene encoding small heat-shock protein Hsp25
    • Gaestel M, Gotthardt R, Muller T. Structure and organisation of a murine gene encoding small heat-shock protein Hsp25. Gene 1993; 128(2): 279-83.
    • (1993) Gene , vol.128 , Issue.2 , pp. 279-283
    • Gaestel, M.1    Gotthardt, R.2    Muller, T.3
  • 56
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • Mosser DD, Kotzbauer PT, Sarge KD, Morimoto RI. In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc Natl Acad Sci USA 1990; 87(10): 3748-52.
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.10 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 57
    • 0024371485 scopus 로고
    • Induction of the estrogen-regulated "24K" protein by heat shock
    • Fuqua SA, Blum-Salingaros M, McGuire WL. Induction of the estrogen-regulated "24K" protein by heat shock. Cancer Res 1989; 49(15): 4126-9.
    • (1989) Cancer Res , vol.49 , Issue.15 , pp. 4126-4129
    • Fuqua, S.A.1    Blum-Salingaros, M.2    McGuire, W.L.3
  • 58
    • 78751562690 scopus 로고    scopus 로고
    • Heat shock protein 27 differentiates tolerogenic macrophages that may support human breast cancer progression
    • Banerjee S, Lin CF, Skinner KA, et al. Heat shock protein 27 differentiates tolerogenic macrophages that may support human breast cancer progression. Cancer Res 2011; 71(2): 318-27.
    • (2011) Cancer Res , vol.71 , Issue.2 , pp. 318-327
    • Banerjee, S.1    Lin, C.F.2    Skinner, K.A.3
  • 59
    • 35348856923 scopus 로고    scopus 로고
    • Exogenous heat shock protein 27 uniquely blocks differentiation of monocytes to dendritic cells
    • Laudanski K, De A, Miller-Graziano C. Exogenous heat shock protein 27 uniquely blocks differentiation of monocytes to dendritic cells. Eur J Immunol 2007; 37(10): 2812-24.
    • (2007) Eur J Immunol , vol.37 , Issue.10 , pp. 2812-2824
    • Laudanski, K.1    De, A.2    Miller-Graziano, C.3
  • 60
    • 84863571573 scopus 로고    scopus 로고
    • Plasma Hsp72 (HSPA1A) and Hsp27 (HSPB1) expression under heat stress: Influence of exercise intensity
    • Jan 6
    • Periard JD, Ruell P, Caillaud C, Thompson MW. Plasma Hsp72 (HSPA1A) and Hsp27 (HSPB1) expression under heat stress: influence of exercise intensity. Cell Stress Chaperones 2012 Jan 6.
    • (2012) Cell Stress Chaperones
    • Periard, J.D.1    Ruell, P.2    Caillaud, C.3    Thompson, M.W.4
  • 61
    • 42049123241 scopus 로고    scopus 로고
    • Small heat shock protein Hsp27 protects myosin S1 from heatinduced aggregation, but not from thermal denaturation and ATPase inactivation
    • Markov DI, Pivovarova AV, Chernik IS, Gusev NB, Levitsky DI. Small heat shock protein Hsp27 protects myosin S1 from heatinduced aggregation, but not from thermal denaturation and ATPase inactivation. FEBS Lett 2008; 582(10): 1407-12.
    • (2008) FEBS Lett , vol.582 , Issue.10 , pp. 1407-1412
    • Markov, D.I.1    Pivovarova, A.V.2    Chernik, I.S.3    Gusev, N.B.4    Levitsky, D.I.5
  • 62
    • 35748965834 scopus 로고    scopus 로고
    • Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin
    • Pivovarova AV, Chebotareva NA, Chernik IS, Gusev NB, Levitsky DI. Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin. FEBS J 2007; 274(22): 5937-48.
    • (2007) FEBS J , vol.274 , Issue.22 , pp. 5937-5948
    • Pivovarova, A.V.1    Chebotareva, N.A.2    Chernik, I.S.3    Gusev, N.B.4    Levitsky, D.I.5
  • 63
    • 66149117827 scopus 로고    scopus 로고
    • Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins
    • McHaourab HS, Godar JA, Stewart PL. Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins. Biochemistry 2009; 48(18): 3828-37.
    • (2009) Biochemistry , vol.48 , Issue.18 , pp. 3828-3837
    • McHaourab, H.S.1    Godar, J.A.2    Stewart, P.L.3
  • 64
    • 69449088004 scopus 로고    scopus 로고
    • Modification and reorganization of the cytoprotective cellular chaperone Hsp27 during herpes simplex virus type 1 infection
    • Mathew SS, Della Selva MP, Burch AD. Modification and reorganization of the cytoprotective cellular chaperone Hsp27 during herpes simplex virus type 1 infection. J Virol 2009; 83(18): 9304-12.
    • (2009) J Virol , vol.83 , Issue.18 , pp. 9304-9312
    • Mathew, S.S.1    Della Selva, M.P.2    Burch, A.D.3
  • 65
    • 70350474677 scopus 로고    scopus 로고
    • Heat shock protein 27 phosphorylation: Kinases, phosphatases, functions and pathology
    • Kostenko S, Moens U. Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology. Cell Mol Life Sci 2009; 66(20): 3289-307.
    • (2009) Cell Mol Life Sci , vol.66 , Issue.20 , pp. 3289-3307
    • Kostenko, S.1    Moens, U.2
  • 66
    • 84934439863 scopus 로고    scopus 로고
    • The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis
    • Arrigo AP. The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis. Adv Exp Med Biol 2007; 594: 14-26.
    • (2007) Adv Exp Med Biol , vol.594 , pp. 14-26
    • Arrigo, A.P.1
  • 67
    • 0030785821 scopus 로고    scopus 로고
    • HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs
    • Jul 1
    • Garrido C, Ottavi P, Fromentin A, et al. HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs. Cancer Res 1997 Jul 1; 57(13): 2661-7.
    • (1997) Cancer Res , vol.57 , Issue.13 , pp. 2661-2667
    • Garrido, C.1    Ottavi, P.2    Fromentin, A.3
  • 69
    • 0034643424 scopus 로고    scopus 로고
    • Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3
    • Pandey P, Farber R, Nakazawa A, et al. Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3. Oncogene 2000; 19(16): 1975-81.
    • (2000) Oncogene , vol.19 , Issue.16 , pp. 1975-1981
    • Pandey, P.1    Farber, R.2    Nakazawa, A.3
  • 70
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells
    • Mehlen P, Hickey E, Weber LA, Arrigo AP. Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells. Biochem Biophys Res Commun 1997; 241(1): 187-92.
    • (1997) Biochem Biophys Res Commun , vol.241 , Issue.1 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.A.3    Arrigo, A.P.4
  • 71
    • 0345410965 scopus 로고    scopus 로고
    • Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery
    • Preville X, Salvemini F, Giraud S, et al. Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery. Exp Cell Res 1999; 247(1): 61-78.
    • (1999) Exp Cell Res , vol.247 , Issue.1 , pp. 61-78
    • Preville, X.1    Salvemini, F.2    Giraud, S.3
  • 72
    • 1442300779 scopus 로고    scopus 로고
    • Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions
    • Koh TJ, Escobedo J. Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions. Am J Physiol Cell Physiol 2004; 286(3): C713-22.
    • (2004) Am J Physiol Cell Physiol , vol.286 , Issue.3
    • Koh, T.J.1    Escobedo, J.2
  • 73
    • 33745887473 scopus 로고    scopus 로고
    • Heat shock protein 27: Its potential role in vascular disease
    • Ferns G, Shams S, Shafi S. Heat shock protein 27: its potential role in vascular disease. Int J Exp Pathol 2006; 87(4): 253-74.
    • (2006) Int J Exp Pathol , vol.87 , Issue.4 , pp. 253-274
    • Ferns, G.1    Shams, S.2    Shafi, S.3
  • 74
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • Mounier N, Arrigo AP. Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones 2002; 7(2): 167-76.
    • (2002) Cell Stress Chaperones , vol.7 , Issue.2 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 75
    • 2342557359 scopus 로고    scopus 로고
    • Role of heat shock protein 27 in cytoskeletal remodeling of the airway smooth muscle cell
    • An SS, Fabry B, Mellema M, et al. Role of heat shock protein 27 in cytoskeletal remodeling of the airway smooth muscle cell. J Appl Physiol 2004; 96(5): 1701-13.
    • (2004) J Appl Physiol , vol.96 , Issue.5 , pp. 1701-1713
    • An, S.S.1    Fabry, B.2    Mellema, M.3
  • 76
    • 0032858218 scopus 로고    scopus 로고
    • HSP27 in signal transduction and association with contractile proteins in smooth muscle cells
    • Ibitayo AI, Sladick J, Tuteja S, et al. HSP27 in signal transduction and association with contractile proteins in smooth muscle cells. Am J Physiol 1999; 277(2 Pt 1): G445-54.
    • (1999) Am J Physiol , vol.277 , Issue.2 PART 1
    • Ibitayo, A.I.1    Sladick, J.2    Tuteja, S.3
  • 77
    • 2442610624 scopus 로고    scopus 로고
    • Tropomyosin interacts with phosphorylated HSP27 in agonist-induced contraction of smooth muscle
    • Somara S, Bitar KN. Tropomyosin interacts with phosphorylated HSP27 in agonist-induced contraction of smooth muscle. Am J Physiol Cell Physiol 2004; 286(6): C1290-301.
    • (2004) Am J Physiol Cell Physiol , vol.286 , Issue.6
    • Somara, S.1    Bitar, K.N.2
  • 78
    • 77950366991 scopus 로고    scopus 로고
    • Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton
    • Jia Y, Wu SL, Isenberg JS, et al. Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton. Cell Stress Chaperones 2010; 15(2): 165-81.
    • (2010) Cell Stress Chaperones , vol.15 , Issue.2 , pp. 165-181
    • Jia, Y.1    Wu, S.L.2    Isenberg, J.S.3
  • 79
    • 27744607883 scopus 로고    scopus 로고
    • Heat shock protein 27 interacts with vimentin and prevents insolubilization of vimentin subunits induced by cadmium
    • Lee JS, Zhang MH, Yun EK, et al. Heat shock protein 27 interacts with vimentin and prevents insolubilization of vimentin subunits induced by cadmium. Exp Mol Med 2005; 37(5): 427-35.
    • (2005) Exp Mol Med , vol.37 , Issue.5 , pp. 427-435
    • Lee, J.S.1    Zhang, M.H.2    Yun, E.K.3
  • 80
    • 29244474560 scopus 로고    scopus 로고
    • Silencing the hsp25 gene eliminates migration capability of the highly metastatic murine 4T1 breast adenocarcinoma cell
    • Bausero MA, Bharti A, Page DT, et al. Silencing the hsp25 gene eliminates migration capability of the highly metastatic murine 4T1 breast adenocarcinoma cell. Tumour Biol 2006; 27(1): 17-26.
    • (2006) Tumour Biol , vol.27 , Issue.1 , pp. 17-26
    • Bausero, M.A.1    Bharti, A.2    Page, D.T.3
  • 81
    • 43049173697 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces heat shock protein (HSP) 27 serine 82 phosphorylation and endothelial tubulogenesis via protein kinase D and independent of p38 kinase
    • Evans IM, Britton G, Zachary IC. Vascular endothelial growth factor induces heat shock protein (HSP) 27 serine 82 phosphorylation and endothelial tubulogenesis via protein kinase D and independent of p38 kinase. Cell Signal 2008; 20(7): 1375-84.
    • (2008) Cell Signal , vol.20 , Issue.7 , pp. 1375-1384
    • Evans, I.M.1    Britton, G.2    Zachary, I.C.3
  • 82
    • 34249338080 scopus 로고    scopus 로고
    • MMP-2, MMP-9 and activin A blood levels in patients with breast cancer or prostate cancer metastatic to the bone
    • Incorvaia L, Badalamenti G, Rini G, et al. MMP-2, MMP-9 and activin A blood levels in patients with breast cancer or prostate cancer metastatic to the bone. Anticancer Res 2007; 27(3B): 1519-25.
    • (2007) Anticancer Res , vol.27 , Issue.3 B , pp. 1519-1525
    • Incorvaia, L.1    Badalamenti, G.2    Rini, G.3
  • 83
    • 0030785701 scopus 로고    scopus 로고
    • Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27
    • Konishi H, Matsuzaki H, Tanaka M, et al. Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27. FEBS Lett 1997; 410(2-3): 493-8.
    • (1997) FEBS Lett , vol.410 , Issue.2-3 , pp. 493-498
    • Konishi, H.1    Matsuzaki, H.2    Tanaka, M.3
  • 84
    • 0041344614 scopus 로고    scopus 로고
    • Heat shock protein 27 controls apoptosis by regulating Akt activation
    • Rane MJ, Pan Y, Singh S, et al. Heat shock protein 27 controls apoptosis by regulating Akt activation. J Biol Chem 2003; 278(30): 27828-35.
    • (2003) J Biol Chem , vol.278 , Issue.30 , pp. 27828-27835
    • Rane, M.J.1    Pan, Y.2    Singh, S.3
  • 85
    • 45549088083 scopus 로고    scopus 로고
    • Hsp27 inhibits Bax activation and apoptosis via a phosphatidylinositol 3-kinase-dependent mechanism
    • Havasi A, Li Z, Wang Z, et al. Hsp27 inhibits Bax activation and apoptosis via a phosphatidylinositol 3-kinase-dependent mechanism. J Biol Chem 2008; 283(18): 12305-13.
    • (2008) J Biol Chem , vol.283 , Issue.18 , pp. 12305-12313
    • Havasi, A.1    Li, Z.2    Wang, Z.3
  • 86
    • 70350537407 scopus 로고    scopus 로고
    • HSP27: Mechanisms of cellular protection against neuronal injury
    • Stetler RA, Gao Y, Signore AP, Cao G, Chen J. HSP27: mechanisms of cellular protection against neuronal injury. Curr Mol Med 2009; 9(7): 863-72.
    • (2009) Curr Mol Med , vol.9 , Issue.7 , pp. 863-872
    • Stetler, R.A.1    Gao, Y.2    Signore, A.P.3    Cao, G.4    Chen, J.5
  • 87
    • 0034282104 scopus 로고    scopus 로고
    • Hsp27 negatively regulates cell death by interacting with cytochrome c
    • Bruey JM, Ducasse C, Bonniaud P, et al. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2000; 2(9): 645-52.
    • (2000) Nat Cell Biol , vol.2 , Issue.9 , pp. 645-652
    • Bruey, J.M.1    Ducasse, C.2    Bonniaud, P.3
  • 88
    • 0034963578 scopus 로고    scopus 로고
    • Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c
    • Concannon CG, Orrenius S, Samali A. Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c. Gene Expr 2001; 9(4-5): 195-201.
    • (2001) Gene Expr , vol.9 , Issue.4-5 , pp. 195-201
    • Concannon, C.G.1    Orrenius, S.2    Samali, A.3
  • 89
    • 0142245588 scopus 로고    scopus 로고
    • Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance
    • Chauhan D, Li G, Hideshima T, et al. Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance. Blood 2003; 102(9): 3379-86.
    • (2003) Blood , vol.102 , Issue.9 , pp. 3379-3386
    • Chauhan, D.1    Li, G.2    Hideshima, T.3
  • 90
    • 77950267783 scopus 로고    scopus 로고
    • Hsp27 promotes insulin-like growth factor-I survival signaling in prostate cancer via p90Rsk-dependent phosphorylation and inactivation of BAD
    • Zoubeidi A, Zardan A, Wiedmann RM, et al. Hsp27 promotes insulin-like growth factor-I survival signaling in prostate cancer via p90Rsk-dependent phosphorylation and inactivation of BAD. Cancer Res 2010; 70(6): 2307-17.
    • (2010) Cancer Res , vol.70 , Issue.6 , pp. 2307-2317
    • Zoubeidi, A.1    Zardan, A.2    Wiedmann, R.M.3
  • 91
    • 34248176724 scopus 로고    scopus 로고
    • Heat shock genes-integrating cell survival and death
    • Arya R, Mallik M, Lakhotia SC. Heat shock genes-integrating cell survival and death. J Biosci 2007; 32(3): 595-610.
    • (2007) J Biosci , vol.32 , Issue.3 , pp. 595-610
    • Arya, R.1    Mallik, M.2    Lakhotia, S.C.3
  • 92
    • 0034512869 scopus 로고    scopus 로고
    • The interaction of HSP27 with Daxx identifies a potential regulatory role of HSP27 in Fas-induced apoptosis
    • Charette SJ, Landry J. The interaction of HSP27 with Daxx identifies a potential regulatory role of HSP27 in Fas-induced apoptosis. Ann N Y Acad Sci 2000; 926: 126-31.
    • (2000) Ann N Y Acad Sci , vol.926 , pp. 126-131
    • Charette, S.J.1    Landry, J.2
  • 93
    • 0032990651 scopus 로고    scopus 로고
    • Heat-shock-protein-27 (hsp27) expression in ovarian carcinoma: Relation in response to chemotherapy and prognosis
    • Arts HJ, Hollema H, Lemstra W, et al. Heat-shock-protein-27 (hsp27) expression in ovarian carcinoma: relation in response to chemotherapy and prognosis. Int J Cancer 1999; 84(3): 234-8.
    • (1999) Int J Cancer , vol.84 , Issue.3 , pp. 234-238
    • Arts, H.J.1    Hollema, H.2    Lemstra, W.3
  • 94
    • 0033761328 scopus 로고    scopus 로고
    • Immunohistochemical changes in prostate cancer after androgen deprivation therapy
    • discussion 7
    • Bostwick DG. Immunohistochemical changes in prostate cancer after androgen deprivation therapy. Mol Urol 2000; 4(3): 101-6; discussion 7.
    • (2000) Mol Urol , vol.4 , Issue.3 , pp. 101-106
    • Bostwick, D.G.1
  • 95
    • 0035013496 scopus 로고    scopus 로고
    • Expression of heat shock proteins HSP70 and HSP27 in primary non-small cell lung carcinomas. An immunohistochemical study
    • Malusecka E, Zborek A, Krzyzowska-Gruca S, Krawczyk Z. Expression of heat shock proteins HSP70 and HSP27 in primary non-small cell lung carcinomas. An immunohistochemical study. Anticancer Res 2001; 21(2A): 1015-21.
    • (2001) Anticancer Res , vol.21 , Issue.2 A , pp. 1015-1021
    • Malusecka, E.1    Zborek, A.2    Krzyzowska-Gruca, S.3    Krawczyk, Z.4
  • 96
    • 0032404094 scopus 로고    scopus 로고
    • Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones
    • Garrido C, Fromentin A, Bonnotte B, et al. Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones. Cancer Res 1998; 58(23): 5495-9.
    • (1998) Cancer Res , vol.58 , Issue.23 , pp. 5495-5499
    • Garrido, C.1    Fromentin, A.2    Bonnotte, B.3
  • 97
    • 0012127775 scopus 로고    scopus 로고
    • The small heat shock protein hsp27 increases invasiveness but decreases motility of breast cancer cells
    • Lemieux P, Oesterreich S, Lawrence JA, et al. The small heat shock protein hsp27 increases invasiveness but decreases motility of breast cancer cells. Invasion Metastasis 1997; 17(3): 113-23.
    • (1997) Invasion Metastasis , vol.17 , Issue.3 , pp. 113-123
    • Lemieux, P.1    Oesterreich, S.2    Lawrence, J.A.3
  • 98
    • 34047132772 scopus 로고    scopus 로고
    • Heat shock protein 27 is associated with irinotecan resistance in human colorectal cancer cells
    • Choi DH, Ha JS, Lee WH, et al. Heat shock protein 27 is associated with irinotecan resistance in human colorectal cancer cells. FEBS Lett 2007; 581(8): 1649-56.
    • (2007) FEBS Lett , vol.581 , Issue.8 , pp. 1649-1656
    • Choi, D.H.1    Ha, J.S.2    Lee, W.H.3
  • 99
    • 4644237335 scopus 로고    scopus 로고
    • Heat shock protein 27 increases after androgen ablation and plays a cytoprotective role in hormonerefractory prostate cancer
    • Rocchi P, So A, Kojima S, et al. Heat shock protein 27 increases after androgen ablation and plays a cytoprotective role in hormonerefractory prostate cancer. Cancer Res 2004; 64(18): 6595-602.
    • (2004) Cancer Res , vol.64 , Issue.18 , pp. 6595-6602
    • Rocchi, P.1    So, A.2    Kojima, S.3
  • 100
    • 34249801769 scopus 로고    scopus 로고
    • Heat shock protein 27 protects L929 cells from cisplatin-induced apoptosis by enhancing Akt activation and abating suppression of thioredoxin reductase activity
    • Zhang Y, Shen X. Heat shock protein 27 protects L929 cells from cisplatin-induced apoptosis by enhancing Akt activation and abating suppression of thioredoxin reductase activity. Clin Cancer Res 2007; 13(10): 2855-64.
    • (2007) Clin Cancer Res , vol.13 , Issue.10 , pp. 2855-2864
    • Zhang, Y.1    Shen, X.2
  • 101
    • 33645824981 scopus 로고    scopus 로고
    • Enhanced expression of heat shock protein 27 following neoadjuvant hormonal therapy is associated with poor clinical outcome in patients undergoing radical prostatectomy for prostate cancer
    • Miyake H, Muramaki M, Kurahashi T, Yamanaka K, Hara I, Fujisawa M. Enhanced expression of heat shock protein 27 following neoadjuvant hormonal therapy is associated with poor clinical outcome in patients undergoing radical prostatectomy for prostate cancer. Anticancer Res 2006; 26(2B): 1583-7.
    • (2006) Anticancer Res , vol.26 , Issue.2 B , pp. 1583-1587
    • Miyake, H.1    Muramaki, M.2    Kurahashi, T.3    Yamanaka, K.4    Hara, I.5    Fujisawa, M.6
  • 102
    • 0034671358 scopus 로고    scopus 로고
    • Heat shock protein expression independently predicts clinical outcome in prostate cancer
    • Cornford PA, Dodson AR, Parsons KF, et al. Heat shock protein expression independently predicts clinical outcome in prostate cancer. Cancer Res 2000; 60(24): 7099-105.
    • (2000) Cancer Res , vol.60 , Issue.24 , pp. 7099-7105
    • Cornford, P.A.1    Dodson, A.R.2    Parsons, K.F.3
  • 103
    • 28244456529 scopus 로고    scopus 로고
    • Increased Hsp27 after androgen ablation facilitates androgen-independent progression in prostate cancer via signal transducers and activators of transcription 3-mediated suppression of apoptosis
    • Rocchi P, Beraldi E, Ettinger S, et al. Increased Hsp27 after androgen ablation facilitates androgen-independent progression in prostate cancer via signal transducers and activators of transcription 3-mediated suppression of apoptosis. Cancer Res 2005; 65(23): 11083-93.
    • (2005) Cancer Res , vol.65 , Issue.23 , pp. 11083-11093
    • Rocchi, P.1    Beraldi, E.2    Ettinger, S.3
  • 104
    • 0033899869 scopus 로고    scopus 로고
    • A novel association between the human heat shock transcription factor 1 (HSF1) and prostate adenocarcinoma
    • Hoang AT, Huang J, Rudra-Ganguly N, et al. A novel association between the human heat shock transcription factor 1 (HSF1) and prostate adenocarcinoma. Am J Pathol 2000; 156(3): 857-64.
    • (2000) Am J Pathol , vol.156 , Issue.3 , pp. 857-864
    • Hoang, A.T.1    Huang, J.2    Rudra-Ganguly, N.3
  • 105
    • 0347986522 scopus 로고    scopus 로고
    • Stat3 modulates heat shock 27kDa protein expression in breast epithelial cells
    • Song H, Ethier SP, Dziubinski ML, Lin J. Stat3 modulates heat shock 27kDa protein expression in breast epithelial cells. Biochem Biophys Res Commun 2004; 314(1): 143-50.
    • (2004) Biochem Biophys Res Commun , vol.314 , Issue.1 , pp. 143-150
    • Song, H.1    Ethier, S.P.2    Dziubinski, M.L.3    Lin, J.4
  • 106
    • 0027942180 scopus 로고
    • Constitutive overexpression of the 27,000 dalton heat shock protein in late passage human breast cancer cells
    • Fuqua SA, Benedix MG, Krieg S, Weng CN, Chamness GC, Oesterreich S. Constitutive overexpression of the 27,000 dalton heat shock protein in late passage human breast cancer cells. Breast Cancer Res Treat 1994; 32(2): 177-86.
    • (1994) Breast Cancer Res Treat , vol.32 , Issue.2 , pp. 177-186
    • Fuqua, S.A.1    Benedix, M.G.2    Krieg, S.3    Weng, C.N.4    Chamness, G.C.5    Oesterreich, S.6
  • 107
    • 84864462281 scopus 로고    scopus 로고
    • Small heat shock proteins in cancer therapy and prognosis
    • Zoubeidi A, Gleave M. Small heat shock proteins in cancer therapy and prognosis. Int J Biochem Cell Biol 2012; 44(10): 1646-56.
    • (2012) Int J Biochem Cell Biol , vol.44 , Issue.10 , pp. 1646-1656
    • Zoubeidi, A.1    Gleave, M.2
  • 108
    • 48749115689 scopus 로고    scopus 로고
    • Intravesically administered antisense oligonucleotides targeting heat-shock protein-27 inhibit the growth of non-muscle-invasive bladder cancer
    • Hadaschik BA, Jackson J, Fazli L, et al. Intravesically administered antisense oligonucleotides targeting heat-shock protein-27 inhibit the growth of non-muscle-invasive bladder cancer. BJU Int 2008; 102(5): 610-6.
    • (2008) BJU Int , vol.102 , Issue.5 , pp. 610-616
    • Hadaschik, B.A.1    Jackson, J.2    Fazli, L.3
  • 109
    • 68249119157 scopus 로고    scopus 로고
    • Heat shock protein 27 as a new therapeutic target for radiation sensitization of head and neck squamous cell carcinoma
    • Hadchity E, Aloy MT, Paulin C, 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(8): 1387-94.
    • (2009) Mol Ther , vol.17 , Issue.8 , pp. 1387-1394
    • Hadchity, E.1    Aloy, M.T.2    Paulin, C.3
  • 110
    • 33846821658 scopus 로고    scopus 로고
    • Hsp27 knockdown using nucleotide-based therapies inhibit tumor growth and enhance chemotherapy in human bladder cancer cells
    • Kamada M, So A, Muramaki M, Rocchi P, Beraldi E, Gleave M. Hsp27 knockdown using nucleotide-based therapies inhibit tumor growth and enhance chemotherapy in human bladder cancer cells. Mol Cancer Ther 2007; 6(1): 299-308.
    • (2007) Mol Cancer Ther , vol.6 , Issue.1 , pp. 299-308
    • Kamada, M.1    So, A.2    Muramaki, M.3    Rocchi, P.4    Beraldi, E.5    Gleave, M.6
  • 111
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire A, Xu S, Montgomery MK, Kostas SA, Driver SE, Mello CC. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 1998; 391(6669): 806-11.
    • (1998) Nature , vol.391 , Issue.6669 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5    Mello, C.C.6
  • 112
    • 84863229706 scopus 로고    scopus 로고
    • Efficient Delivery of Sticky siRNA and Potent Gene Silencing in a Prostate Cancer Model Using a Generation 5 Triethanolamine-Core PAMAM Dendrimer
    • Liu X, Liu C, Laurini E, et al. Efficient Delivery of Sticky siRNA and Potent Gene Silencing in a Prostate Cancer Model Using a Generation 5 Triethanolamine-Core PAMAM Dendrimer. Mol Pharm 2012; 9(3): 470-81.
    • (2012) Mol Pharm , vol.9 , Issue.3 , pp. 470-481
    • Liu, X.1    Liu, C.2    Laurini, E.3
  • 113
    • 84555186724 scopus 로고    scopus 로고
    • Structurally flexible triethanolamine core PAMAM dendrimers are effective nanovectors for DNA transfection in vitro and in vivo to the mouse thymus
    • Liu X, Wu J, Yammine M, et al. Structurally flexible triethanolamine core PAMAM dendrimers are effective nanovectors for DNA transfection in vitro and in vivo to the mouse thymus. Bioconjug Chem 2011; 22(12): 2461-73.
    • (2011) Bioconjug Chem , vol.22 , Issue.12 , pp. 2461-2473
    • Liu, X.1    Wu, J.2    Yammine, M.3
  • 114
    • 68149163646 scopus 로고    scopus 로고
    • PAMAM dendrimers mediate siRNA delivery to target Hsp27 and produce potent antiproliferative effects on prostate cancer cells
    • Liu XX, Rocchi P, Qu FQ, et al. PAMAM dendrimers mediate siRNA delivery to target Hsp27 and produce potent antiproliferative effects on prostate cancer cells. ChemMedChem 2009; 4(8): 1302-10.
    • (2009) ChemMedChem , vol.4 , Issue.8 , pp. 1302-1310
    • Liu, X.X.1    Rocchi, P.2    Qu, F.Q.3
  • 115
    • 80054764372 scopus 로고    scopus 로고
    • Combined lentiviral and RNAi technologies for the delivery and permanent silencing of the hsp25 gene
    • Kaur P, Nagaraja GM, Asea A. Combined lentiviral and RNAi technologies for the delivery and permanent silencing of the hsp25 gene. Methods Mol Biol 2011; 787: 121-36.
    • (2011) Methods Mol Biol , vol.787 , pp. 121-136
    • Kaur, P.1    Nagaraja, G.M.2    Asea, A.3
  • 116
    • 79955592687 scopus 로고    scopus 로고
    • Can non-viral technologies knockdown the barriers to siRNA delivery and achieve the next generation of cancer therapeutics?
    • Guo J, Bourre L, Soden DM, O'Sullivan GC, O'Driscoll C. Can non-viral technologies knockdown the barriers to siRNA delivery and achieve the next generation of cancer therapeutics? Biotechnol Adv 2011; 29(4): 402-17.
    • (2011) Biotechnol Adv , vol.29 , Issue.4 , pp. 402-417
    • Guo, J.1    Bourre, L.2    Soden, D.M.3    O'Sullivan, G.C.4    O'Driscoll, C.5
  • 117
    • 79959967622 scopus 로고    scopus 로고
    • Bio-inspired, bioengineered and biomimetic drug delivery carriers
    • Yoo JW, Irvine DJ, Discher DE, Mitragotri S. Bio-inspired, bioengineered and biomimetic drug delivery carriers. Nat Rev Drug Discov 2011; 10(7): 521-35.
    • (2011) Nat Rev Drug Discov , vol.10 , Issue.7 , pp. 521-535
    • Yoo, J.W.1    Irvine, D.J.2    Discher, D.E.3    Mitragotri, S.4
  • 118
    • 84862816694 scopus 로고    scopus 로고
    • Targeting heat shock factor 1 with a triazole nucleoside analog to elicit potent anticancer activity on drug-resistant pancreatic cancer
    • Xia Y, Liu Y, Rocchi P, et al. Targeting heat shock factor 1 with a triazole nucleoside analog to elicit potent anticancer activity on drug-resistant pancreatic cancer. Cancer Lett 2012; 318(2): 145-53.
    • (2012) Cancer Lett , vol.318 , Issue.2 , pp. 145-153
    • Xia, Y.1    Liu, Y.2    Rocchi, P.3
  • 119
    • 70349650214 scopus 로고    scopus 로고
    • Novel triazole ribonucleoside downregulates heat shock protein 27 and induces potent anticancer activity on drug-resistant pancreatic cancer
    • Xia Y, Liu Y, Wan J, et al. Novel triazole ribonucleoside downregulates heat shock protein 27 and induces potent anticancer activity on drug-resistant pancreatic cancer. J Med Chem 2009; 52(19): 6083-96.
    • (2009) J Med Chem , vol.52 , Issue.19 , pp. 6083-6096
    • Xia, Y.1    Liu, Y.2    Wan, J.3
  • 120
    • 84855847704 scopus 로고    scopus 로고
    • Targeting heat shock response pathways to treat pancreatic cancer
    • Xia Y, Rocchi P, Iovanna JL, Peng L. Targeting heat shock response pathways to treat pancreatic cancer. Drug Discov Today 2012; 17(1-2): 35-43.
    • (2012) Drug Discov Today , vol.17 , Issue.1-2 , pp. 35-43
    • Xia, Y.1    Rocchi, P.2    Iovanna, J.L.3    Peng, L.4
  • 121
    • 80054720155 scopus 로고    scopus 로고
    • RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients
    • Heinrich JC, Tuukkanen A, Schroeder M, Fahrig T, Fahrig R. RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients. J Cancer Res Clin Oncol 2011; 137(9): 1349-61.
    • (2011) J Cancer Res Clin Oncol , vol.137 , Issue.9 , pp. 1349-1361
    • Heinrich, J.C.1    Tuukkanen, A.2    Schroeder, M.3    Fahrig, T.4    Fahrig, R.5
  • 122
    • 84875209931 scopus 로고    scopus 로고
    • Heat shock proteins 27, 40, and 70 as combinational and dual therapeutic cancer targets
    • McConnell JR, McAlpine SR. Heat shock proteins 27, 40, and 70 as combinational and dual therapeutic cancer targets. Bioorg Med Chem Lett 2013; 23(7): 1923-8.
    • (2013) Bioorg Med Chem Lett , vol.23 , Issue.7 , pp. 1923-1928
    • McConnell, J.R.1    McAlpine, S.R.2
  • 123
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclindependent kinase 2
    • Colas P, Cohen B, Jessen T, Grishina I, McCoy J, Brent R. Genetic selection of peptide aptamers that recognize and inhibit cyclindependent kinase 2. Nature 1996; 380(6574): 548-50.
    • (1996) Nature , vol.380 , Issue.6574 , pp. 548-550
    • Colas, P.1    Cohen, B.2    Jessen, T.3    Grishina, I.4    McCoy, J.5    Brent, R.6
  • 124
    • 0033748710 scopus 로고    scopus 로고
    • Selection of genetic agents from random peptide aptamer expression libraries
    • Geyer CR, Brent R. Selection of genetic agents from random peptide aptamer expression libraries. Methods Enzymol 2000; 328: 171-208.
    • (2000) Methods Enzymol , vol.328 , pp. 171-208
    • Geyer, C.R.1    Brent, R.2
  • 126
    • 33846847966 scopus 로고    scopus 로고
    • Modulation of Nr-13 antideath activity by peptide aptamers
    • Nouvion AL, Thibaut J, Lohez OD, et al. Modulation of Nr-13 antideath activity by peptide aptamers. Oncogene 2007; 26(5): 701-10.
    • (2007) Oncogene , vol.26 , Issue.5 , pp. 701-710
    • Nouvion, A.L.1    Thibaut, J.2    Lohez, O.D.3
  • 127
    • 80052049395 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 27 (HspB1) tumorigenic functions by peptide aptamers
    • Gibert B, Hadchity E, Czekalla A, et al. Inhibition of heat shock protein 27 (HspB1) tumorigenic functions by peptide aptamers. Oncogene 2011; 30(34): 3672-81.
    • (2011) Oncogene , vol.30 , Issue.34 , pp. 3672-3681
    • Gibert, B.1    Hadchity, E.2    Czekalla, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.