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Volumn 6, Issue 1, 2014, Pages 333-365

HspB1, HspB5 and HspB4 in human cancers: Potent oncogenic role of some of their client proteins

Author keywords

alphaA crystallin; alphaB crystallin; Cancer; Clients; Hsp27; HspB1; HspB4; HspB5; Human small Hsps

Indexed keywords


EID: 84893923808     PISSN: None     EISSN: 20726694     Source Type: Journal    
DOI: 10.3390/cancers6010333     Document Type: Review
Times cited : (79)

References (237)
  • 1
    • 35548970287 scopus 로고    scopus 로고
    • Heat shock proteins in cancer
    • Sherman, M.; Multhoff, G. Heat shock proteins in cancer. Ann. NY Acad. Sci. 2007, 1113, 192-201.
    • (2007) Ann. NY Acad. Sci , vol.1113 , pp. 192-201
    • Sherman, M.1    Multhoff, G.2
  • 2
    • 84872358363 scopus 로고    scopus 로고
    • Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development
    • Ciocca, D.R.; Arrigo, A.P.; Calderwood, S.K. Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: An update. Arch. Toxicol. 2013, 87, 19-48.
    • (2013) An Update. Arch. Toxicol , vol.87 , pp. 19-48
    • Ciocca, D.R.1    Arrigo, A.P.2    Calderwood, S.K.3
  • 4
    • 84867761627 scopus 로고    scopus 로고
    • HSF1, a versatile factor in tumorogenesis
    • Calderwood, S.K. HSF1, a versatile factor in tumorogenesis. Curr. Mol. Med. 2012, 12, 1102-1107.
    • (2012) Curr. Mol. Med , vol.12 , pp. 1102-1107
    • Calderwood, S.K.1
  • 7
    • 0030014643 scopus 로고    scopus 로고
    • Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death
    • Mehlen, P.; Schulze-Osthoff, K.; Arrigo, A.P. Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J. Biol. Chem. 1996, 271, 16510-16514.
    • (1996) J. Biol. Chem , vol.271 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 8
    • 0035844174 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin negatively regulates cytochrome cand caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation
    • Kamradt, M.C.; Chen, F.; Cryns, V.L. The small heat shock protein alpha B-crystallin negatively regulates cytochrome cand caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation. J. Biol. Chem. 2001, 276, 16059-16063.
    • (2001) J. Biol. Chem , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.2    Cryns, V.L.3
  • 9
    • 33751203833 scopus 로고    scopus 로고
    • Heat shock proteins 27 and 70: Anti-apoptotic proteins with tumorigenic properties
    • Garrido, C.; Brunet, M.; Didelot, C.; Zermati, Y.; Schmitt, E.; Kroemer, G. Heat shock proteins 27 and 70: Anti-apoptotic proteins with tumorigenic properties. Cell Cycle 2006, 5, 22.
    • (2006) Cell Cycle , vol.5 , pp. 22
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 10
    • 37549025455 scopus 로고    scopus 로고
    • Hsp27 modulates p53 signaling and suppresses cellular senescence
    • O'Callaghan-Sunol, C.; Gabai, V.L.; Sherman, M.Y. Hsp27 modulates p53 signaling and suppresses cellular senescence. Cancer Res. 2007, 67, 11779-11788.
    • (2007) Cancer Res , vol.67 , pp. 11779-11788
    • O'Callaghan-Sunol, C.1    Gabai, V.L.2    Sherman, M.Y.3
  • 13
    • 84860757279 scopus 로고    scopus 로고
    • Hsp27 silencing coordinately inhibits proliferation and promotes Fas-induced apoptosis by regulating the PEA-15 molecular switch
    • Hayashi, N.; Peacock, J.W.; Beraldi, E.; Zoubeidi, A.; Gleave, M.E.; Ong, C.J. Hsp27 silencing coordinately inhibits proliferation and promotes Fas-induced apoptosis by regulating the PEA-15 molecular switch. Cell Death Differ. 2012, 19, 990-1002.
    • (2012) Cell Death Differ , vol.19 , pp. 990-1002
    • Hayashi, N.1    Peacock, J.W.2    Beraldi, E.3    Zoubeidi, A.4    Gleave, M.E.5    Ong, C.J.6
  • 15
    • 0034609765 scopus 로고    scopus 로고
    • Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo
    • Bruey, J.M.; Paul, C.; Fromentin, A.; Hilpert, S.; Arrigo, A.P.; Solary, E.; Garrido, C. Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo. Oncogene 2000, 19, 4855-4863.
    • (2000) Oncogene , vol.19 , pp. 4855-4863
    • Bruey, J.M.1    Paul, C.2    Fromentin, A.3    Hilpert, S.4    Arrigo, A.P.5    Solary, E.6    Garrido, C.7
  • 18
    • 11444263900 scopus 로고    scopus 로고
    • Surface expression of Hsp25 and Hsp72 differentially regulates tumor growth and metastasis
    • Bausero, M.A.; Page, D.T.; Osinaga, E.; Asea, A. Surface expression of Hsp25 and Hsp72 differentially regulates tumor growth and metastasis. Tumour Biol. 2004, 25, 243-251.
    • (2004) Tumour Biol , vol.25 , pp. 243-251
    • Bausero, M.A.1    Page, D.T.2    Osinaga, E.3    Asea, A.4
  • 19
    • 84867782766 scopus 로고    scopus 로고
    • Role of human and mouse HspB1 in metastasis
    • Nagaraja, G.N.; Kaur, P.; Asea, A. Role of human and mouse HspB1 in metastasis. Curr. Mol. Med. 2012, 12, 1142-1150.
    • (2012) Curr. Mol. Med , vol.12 , pp. 1142-1150
    • Nagaraja, G.N.1    Kaur, P.2    Asea, A.3
  • 21
    • 84867772627 scopus 로고    scopus 로고
    • HspB1 dynamic phospho-oligomeric structure dependent interactome as cancer therapeutic target
    • Arrigo, A.P.; Gibert, B. HspB1 dynamic phospho-oligomeric structure dependent interactome as cancer therapeutic target. Curr. Mol. Med. 2012, 12, 1151-1163.
    • (2012) Curr. Mol. Med , vol.12 , pp. 1151-1163
    • Arrigo, A.P.1    Gibert, B.2
  • 22
    • 84878897972 scopus 로고    scopus 로고
    • Dual, Beneficial and Deleterous, Roles of Small Stress Proteins in Human Diseases: Implications for Therapeutic Strategies
    • Book Serie: Protein Science Engineering; Arrigo, A.P., Simon, S., Eds.; Nova Sciences: New York, NY, USA
    • Arrigo, A.; Simon, S. Dual, Beneficial and Deleterous, Roles of Small Stress Proteins in Human Diseases: Implications for Therapeutic Strategies. In Small Stress Proteins in Human Diseases; Book Serie: Protein Science Engineering; Arrigo, A.P., Simon, S., Eds.; Nova Sciences: New York, NY, USA, 2010; pp. 457-476.
    • (2010) Small Stress Proteins In Human Diseases , pp. 457-476
    • Arrigo, A.1    Simon, S.2
  • 24
    • 84878912425 scopus 로고    scopus 로고
    • Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8
    • Arrigo, A.P.; Gibert, B. Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8. Int. J. Hyperth. 2013, 29, 409-422.
    • (2013) Int. J. Hyperth , vol.29 , pp. 409-422
    • Arrigo, A.P.1    Gibert, B.2
  • 25
    • 84878932295 scopus 로고    scopus 로고
    • Human small heat shock proteins: Protein interactomes of homo- and hetero-oligomeric complexes: An update
    • Arrigo, A.P. Human small heat shock proteins: Protein interactomes of homo- and hetero-oligomeric complexes: An update. FEBS Lett. 2013, 587, 1959-1969.
    • (2013) FEBS Lett , vol.587 , pp. 1959-1969
    • Arrigo, A.P.1
  • 26
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: Diagnostic, prognostic, predictive, and treatment implications
    • Ciocca, D.R.; Calderwood, S.K. Heat shock proteins in cancer: Diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 2005, 10, 86-103.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 27
    • 84878917797 scopus 로고    scopus 로고
    • Pathology-dependent effects linked to small heat shock proteins expression
    • Arrigo, A.P. Pathology-dependent effects linked to small heat shock proteins expression. Scientifica 2012, 2012, 19.
    • (2012) Scientifica , vol.2012 , pp. 19
    • Arrigo, A.P.1
  • 29
    • 0034624322 scopus 로고    scopus 로고
    • Heat shock protein expression in human tumours grown in severe combined immunodeficient mice
    • Katoh, M.; Koninkx, J.; Schumacher, U. Heat shock protein expression in human tumours grown in severe combined immunodeficient mice. Cancer Lett. 2000, 161, 113-120.
    • (2000) Cancer Lett , vol.161 , pp. 113-120
    • Katoh, M.1    Koninkx, J.2    Schumacher, U.3
  • 30
    • 79952825166 scopus 로고    scopus 로고
    • Chemoresistance of lung cancer stemlike cells depends on activation of Hsp27
    • Hsu, H.S.; Lin, J.H.; Huang, W.C.; Hsu, T.W.; Su, K.; Chiou, S.H.; Tsai, Y.T.; Hung, S.C. Chemoresistance of lung cancer stemlike cells depends on activation of Hsp27. Cancer 2011, 117, 1516-1528.
    • (2011) Cancer , vol.117 , pp. 1516-1528
    • Hsu, H.S.1    Lin, J.H.2    Huang, W.C.3    Hsu, T.W.4    Su, K.5    Chiou, S.H.6    Tsai, Y.T.7    Hung, S.C.8
  • 31
    • 80054814409 scopus 로고    scopus 로고
    • Hsp27 participates in the maintenance of breast cancer stem cells through regulation of epithelial-mesenchymal transition and nuclear factor-kappaB
    • Wei, L.; Liu, T.T.; Wang, H.H.; Hong, H.M.; Yu, A.L.; Feng, H.P.; Chang, W.W. Hsp27 participates in the maintenance of breast cancer stem cells through regulation of epithelial-mesenchymal transition and nuclear factor-kappaB. Breast Cancer Res. 2011, 13, R101.
    • (2011) Breast Cancer Res , vol.13
    • Wei, L.1    Liu, T.T.2    Wang, H.H.3    Hong, H.M.4    Yu, A.L.5    Feng, H.P.6    Chang, W.W.7
  • 35
    • 0025988318 scopus 로고
    • Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein
    • Huot, J.; Roy, G.; Lambert, H.; Chretien, P.; Landry, J. Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein. Cancer Res. 1991, 51, 5245-5252.
    • (1991) Cancer Res , vol.51 , pp. 5245-5252
    • Huot, J.1    Roy, G.2    Lambert, H.3    Chretien, P.4    Landry, J.5
  • 36
    • 0029882949 scopus 로고    scopus 로고
    • Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells
    • Richards, E.H.; Hickey, E.; Weber, L.A.; Master, J.R. Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells. Cancer Res. 1996, 56, 2446-2451.
    • (1996) Cancer Res , vol.56 , pp. 2446-2451
    • Richards, E.H.1    Hickey, E.2    Weber, L.A.3    Master, J.R.4
  • 37
    • 0034081704 scopus 로고    scopus 로고
    • Hsp as novel regulators of programmed cell death and tumorigenicity
    • Arrigo, A.P. Hsp as novel regulators of programmed cell death and tumorigenicity. Pathol. Biol. Paris 2000, 48, 280-288.
    • (2000) Pathol. Biol. Paris , vol.48 , pp. 280-288
    • Arrigo, A.P.1
  • 39
    • 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, 299-308.
    • (2007) Mol. Cancer Ther , vol.6 , pp. 299-308
    • Kamada, M.1    So, A.2    Muramaki, M.3    Rocchi, P.4    Beraldi, E.5    Gleave, M.6
  • 40
    • 54049100335 scopus 로고    scopus 로고
    • Upregulated HSP27 in human breast cancer cells reduces Herceptin susceptibility by increasing Her2 protein stability
    • Kang, S.H.; Kang, K.W.; Kim, K.H.; Kwon, B.; Kim, S.K.; Lee, H.Y.; Kong, S.Y.; Lee, E.S.; Jang, S.G.; Yoo, B.C. Upregulated HSP27 in human breast cancer cells reduces Herceptin susceptibility by increasing Her2 protein stability. BMC Cancer 2008, 8, 286.
    • (2008) BMC Cancer , vol.8 , pp. 286
    • Kang, S.H.1    Kang, K.W.2    Kim, K.H.3    Kwon, B.4    Kim, S.K.5    Lee, H.Y.6    Kong, S.Y.7    Lee, E.S.8    Jang, S.G.9    Yoo, B.C.10
  • 41
    • 64849112707 scopus 로고    scopus 로고
    • Expression of heat shock protein 27 and alpha-crystallins in human retinoblastoma after chemoreduction
    • Kase, S.; Parikh, J.G.; Rao, N.A. Expression of heat shock protein 27 and alpha-crystallins in human retinoblastoma after chemoreduction. Br. J. Ophthalmol. 2009, 93, 541-544.
    • (2009) Br. J. Ophthalmol , vol.93 , pp. 541-544
    • Kase, S.1    Parikh, J.G.2    Rao, N.A.3
  • 42
    • 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, 2855-2864.
    • (2007) Clin. Cancer Res , vol.13 , pp. 2855-2864
    • Zhang, Y.1    Shen, X.2
  • 43
    • 84855405100 scopus 로고    scopus 로고
    • Unfolded protein response suppresses cisplatin-induced apoptosis via autophagy regulation in human hepatocellular carcinoma cells
    • Chen, R.; Dai, R.Y.; Duan, C.Y.; Liu, Y.P.; Chen, S.K.; Yan, D.M.; Chen, C.N.; Wei, M.; Li, H. Unfolded protein response suppresses cisplatin-induced apoptosis via autophagy regulation in human hepatocellular carcinoma cells. Folia Biol. Praha 2011, 57, 87-95.
    • (2011) Folia Biol. Praha , vol.57 , pp. 87-95
    • Chen, R.1    Dai, R.Y.2    Duan, C.Y.3    Liu, Y.P.4    Chen, S.K.5    Yan, D.M.6    Chen, C.N.7    Wei, M.8    Li, H.9
  • 44
    • 80052463873 scopus 로고    scopus 로고
    • Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment
    • Fujita, R.; Ounzain, S.; Wang, A.C.; Heads, R.J.; Budhram-Mahadeo, V.S. Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment. Cell Stress Chaperones 2011, 16, 427-439.
    • (2011) Cell Stress Chaperones , vol.16 , pp. 427-439
    • Fujita, R.1    Ounzain, S.2    Wang, A.C.3    Heads, R.J.4    Budhram-Mahadeo, V.S.5
  • 45
    • 84860389155 scopus 로고    scopus 로고
    • Proliferation-associated POU4F2/Brn-3b transcription factor expression is regulated by oestrogen through ERalpha and growth factors via MAPK pathway
    • Ounzain, S.; Bowen, S.; Patel, C.; Fujita, R.; Heads, R.J.; Budhram-Mahadeo, V.S. Proliferation-associated POU4F2/Brn-3b transcription factor expression is regulated by oestrogen through ERalpha and growth factors via MAPK pathway. Breast Cancer Res. 2011, 13, R5
    • (2011) Breast Cancer Res , vol.13
    • Ounzain, S.1    Bowen, S.2    Patel, C.3    Fujita, R.4    Heads, R.J.5    Budhram-Mahadeo, V.S.6
  • 46
    • 0025934067 scopus 로고
    • Cisplatin induces the small heat shock protein hsp25 and thermotolerance in Ehrlich ascites tumor cells
    • Oesterreich, S.; Schunck, H.; Benndorf, R.; Bielka, H. Cisplatin induces the small heat shock protein hsp25 and thermotolerance in Ehrlich ascites tumor cells. Biochem. Biophys. Res. Commun. 1991, 180, 243-248.
    • (1991) Biochem. Biophys. Res. Commun , vol.180 , pp. 243-248
    • Oesterreich, S.1    Schunck, H.2    Benndorf, R.3    Bielka, H.4
  • 50
    • 34548731917 scopus 로고    scopus 로고
    • Phosphorylation of Ser78 of Hsp27 correlated with HER-2/neu status and lymph node positivity in breast cancer
    • Zhang, D.; Wong, L.L.; Koay, E.S. Phosphorylation of Ser78 of Hsp27 correlated with HER-2/neu status and lymph node positivity in breast cancer. Mol. Cancer 2007, 6, 52.
    • (2007) Mol. Cancer , vol.6 , pp. 52
    • Zhang, D.1    Wong, L.L.2    Koay, E.S.3
  • 51
    • 77952890212 scopus 로고    scopus 로고
    • Dynamic processes that reflect anti-apoptotic strategies set up by HspB1 (Hsp27)
    • Paul, C.; Simon, S.; Gibert, B.; Virot, S.; Manero, F.; Arrigo, A.P. Dynamic processes that reflect anti-apoptotic strategies set up by HspB1 (Hsp27). Exp. Cell Res. 2010, 316, 1535-1552.
    • (2010) Exp. Cell Res , vol.316 , pp. 1535-1552
    • Paul, C.1    Simon, S.2    Gibert, B.3    Virot, S.4    Manero, F.5    Arrigo, A.P.6
  • 55
    • 2642553016 scopus 로고    scopus 로고
    • alphaB-crystallin as a marker of lymph node involvement in breast carcinoma
    • Chelouche-Lev, D.; Kluger, H.M.; Berger, A.J.; Rimm, D.L.; Price, J.E. alphaB-crystallin as a marker of lymph node involvement in breast carcinoma. Cancer 2004, 100, 2543-2548.
    • (2004) Cancer , vol.100 , pp. 2543-2548
    • Chelouche-Lev, D.1    Kluger, H.M.2    Berger, A.J.3    Rimm, D.L.4    Price, J.E.5
  • 56
    • 79955393339 scopus 로고    scopus 로고
    • AlphaB-crystallin is a novel oncoprotein associated with poor prognosis in breast cancer
    • Kim, H.S.; Lee, Y.; Lim, Y.A.; Kang, H.J.; Kim, L.S. AlphaB-crystallin is a novel oncoprotein associated with poor prognosis in breast cancer. J. Breast Cancer 2011, 14, 14-19.
    • (2011) J. Breast Cancer , vol.14 , pp. 14-19
    • Kim, H.S.1    Lee, Y.2    Lim, Y.A.3    Kang, H.J.4    Kim, L.S.5
  • 60
    • 33845633819 scopus 로고    scopus 로고
    • Biomarker discovery: A proteomic approach for brain cancer profiling
    • Khalil, A.A. Biomarker discovery: A proteomic approach for brain cancer profiling. Cancer Sci. 2007, 98, 201-213.
    • (2007) Cancer Sci , vol.98 , pp. 201-213
    • Khalil, A.A.1
  • 61
    • 59049100372 scopus 로고    scopus 로고
    • Expression and prognostic significance of the alpha B-crystallin gene in human hepatocellular carcinoma
    • Tang, Q.; Liu, Y.F.; Zhu, X.J.; Li, Y.H.; Zhu, J.; Zhang, J.P.; Feng, Z.Q.; Guan, X.H. Expression and prognostic significance of the alpha B-crystallin gene in human hepatocellular carcinoma. Hum. Pathol. 2009, 40, 300-305.
    • (2009) Hum. Pathol , vol.40 , pp. 300-305
    • Tang, Q.1    Liu, Y.F.2    Zhu, X.J.3    Li, Y.H.4    Zhu, J.5    Zhang, J.P.6    Feng, Z.Q.7    Guan, X.H.8
  • 62
    • 34548603481 scopus 로고    scopus 로고
    • Expression profile of heat shock proteins in tissues and cells of lung adenocarcinoma
    • Liu, X.L.; Guo, K.P.; Ma, F.; Xie, G.Y.; He, Y.; Hu, C.H. Expression profile of heat shock proteins in tissues and cells of lung adenocarcinoma. Zhong Nan Da Xue Xue Bao Yi Xue Ban 2007, 32, 660-664.
    • (2007) Zhong Nan Da Xue Xue Bao Yi Xue Ban , vol.32 , pp. 660-664
    • Liu, X.L.1    Guo, K.P.2    Ma, F.3    Xie, G.Y.4    He, Y.5    Hu, C.H.6
  • 63
    • 0031647626 scopus 로고    scopus 로고
    • Different concentrations of two small stress proteins, alphaB crystallin and HSP27 in human urological tumor tissues
    • Takashi, M.; Katsuno, S.; Sakata, T.; Ohshima, S.; Kato, K. Different concentrations of two small stress proteins, alphaB crystallin and HSP27 in human urological tumor tissues. Urol. Res. 1998, 26, 395-399.
    • (1998) Urol. Res , vol.26 , pp. 395-399
    • Takashi, M.1    Katsuno, S.2    Sakata, T.3    Ohshima, S.4    Kato, K.5
  • 64
    • 0141591735 scopus 로고    scopus 로고
    • Hyperproliferation and p53 status of lens epithelial cells derived from alphaB-crystallin knockout mice
    • Bai, F.; Xi, J.H.; Wawrousek, E.F.; Fleming, T.P.; Andley, U.P. Hyperproliferation and p53 status of lens epithelial cells derived from alphaB-crystallin knockout mice. J. Biol. Chem. 2003, 278, 36876-36886.
    • (2003) J. Biol. Chem , vol.278 , pp. 36876-36886
    • Bai, F.1    Xi, J.H.2    Wawrousek, E.F.3    Fleming, T.P.4    Andley, U.P.5
  • 66
    • 26944481201 scopus 로고    scopus 로고
    • Differential expression of alphaB-crystallin and Hsp27-1 in anaplastic thyroid carcinomas because of tumor-specific alphaB-crystallin gene (CRYAB) silencing
    • Mineva, I.; Gartner, W.; Hauser, P.; Kainz, A.; Loffler, M.; Wolf, G.; Oberbauer, R.; Weissel, M.; Wagner, L. Differential expression of alphaB-crystallin and Hsp27-1 in anaplastic thyroid carcinomas because of tumor-specific alphaB-crystallin gene (CRYAB) silencing. Cell Stress Chaperones 2005, 10, 171-184.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 171-184
    • Mineva, I.1    Gartner, W.2    Hauser, P.3    Kainz, A.4    Loffler, M.5    Wolf, G.6    Oberbauer, R.7    Weissel, M.8    Wagner, L.9
  • 67
    • 39649108844 scopus 로고    scopus 로고
    • Identification of tumor suppressive activity by irradiation microcell-mediated chromosome transfer and involvement of alpha B-crystallin in nasopharyngeal carcinoma
    • Lung, H.L.; Lo, C.C.; Wong, C.C.; Cheung, A.K.; Cheong, K.F.; Wong, N.; Kwong, F.M.; Chan, K.C.; Law, E.W.; Tsao, S.W.; et al. Identification of tumor suppressive activity by irradiation microcell-mediated chromosome transfer and involvement of alpha B-crystallin in nasopharyngeal carcinoma. Int. J. Cancer 2008, 122, 1288-1296.
    • (2008) Int. J. Cancer , vol.122 , pp. 1288-1296
    • Lung, H.L.1    Lo, C.C.2    Wong, C.C.3    Cheung, A.K.4    Cheong, K.F.5    Wong, N.6    Kwong, F.M.7    Chan, K.C.8    Law, E.W.9    Tsao, S.W.10
  • 68
    • 76749138385 scopus 로고    scopus 로고
    • Reduced alphaB-crystallin staining in perineural invasion of head and neck cutaneous squamous cell carcinoma
    • Solares, C.A.; Boyle, G.M.; Brown, I.; Parsons, P.G.; Panizza, B. Reduced alphaB-crystallin staining in perineural invasion of head and neck cutaneous squamous cell carcinoma. Otolaryngol. Head. Neck. Surg. 2010, 142, S15-S19.
    • (2010) Otolaryngol. Head. Neck. Surg , vol.142
    • Solares, C.A.1    Boyle, G.M.2    Brown, I.3    Parsons, P.G.4    Panizza, B.5
  • 69
    • 3543055313 scopus 로고    scopus 로고
    • Proteomics of buccal squamous cell carcinoma: The involvement of multiple pathways in tumorigenesis
    • Chen, J.; He, Q.Y.; Yuen, A.P.; Chiu, J.F. Proteomics of buccal squamous cell carcinoma: The involvement of multiple pathways in tumorigenesis. Proteomics 2004, 4, 2465-2475.
    • (2004) Proteomics , vol.4 , pp. 2465-2475
    • Chen, J.1    He, Q.Y.2    Yuen, A.P.3    Chiu, J.F.4
  • 70
    • 0942297968 scopus 로고    scopus 로고
    • Identification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomics
    • He, Q.Y.; Chen, J.; Kung, H.F.; Yuen, A.P.; Chiu, J.F. Identification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomics. Proteomics 2004, 4, 271-278.
    • (2004) Proteomics , vol.4 , pp. 271-278
    • He, Q.Y.1    Chen, J.2    Kung, H.F.3    Yuen, A.P.4    Chiu, J.F.5
  • 72
    • 72449208135 scopus 로고    scopus 로고
    • Regulation of alphaB-crystallin gene expression by the transcription factor Ets1 in breast cancer
    • Bosman, J.D.; Yehiely, F.; Evans, J.R.; Cryns, V.L. Regulation of alphaB-crystallin gene expression by the transcription factor Ets1 in breast cancer. Breast Cancer Res Treat 2010, 119, 63-70.
    • (2010) Breast Cancer Res Treat , vol.119 , pp. 63-70
    • Bosman, J.D.1    Yehiely, F.2    Evans, J.R.3    Cryns, V.L.4
  • 73
    • 77953806476 scopus 로고    scopus 로고
    • The small heat shock protein alphaA-crystallin is expressed in pancreas and acts as a negative regulator of carcinogenesis
    • Deng, M.; Chen, P.C.; Xie, S.; Zhao, J.; Gong, L.; Liu, J.; Zhang, L.; Sun, S.; Liu, J.; Ma, H.; et al. The small heat shock protein alphaA-crystallin is expressed in pancreas and acts as a negative regulator of carcinogenesis. Biochim. Biophys. Acta 2010, 1802, 621-631.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 621-631
    • Deng, M.1    Chen, P.C.2    Xie, S.3    Zhao, J.4    Gong, L.5    Liu, J.6    Zhang, L.7    Sun, S.8    Liu, J.9    Ma, H.10
  • 75
    • 70549102151 scopus 로고    scopus 로고
    • Expression of alpha-crystallins in human sebaceous carcinoma of the eyelid
    • Rigas, P.K.; Kase, S.; Rao, N.A. Expression of alpha-crystallins in human sebaceous carcinoma of the eyelid. Eur. J. Ophthalmol. 2009, 19, 702-707.
    • (2009) Eur. J. Ophthalmol , vol.19 , pp. 702-707
    • Rigas, P.K.1    Kase, S.2    Rao, N.A.3
  • 76
    • 84858003372 scopus 로고    scopus 로고
    • Small heat shock proteins and alpha-crystallins: Dynamic proteins with flexible functions
    • Basha, E.; O'Neill, H.; Vierling, E. Small heat shock proteins and alpha-crystallins: Dynamic proteins with flexible functions. Trends Biochem. Sci. 2011, 37, 106-117.
    • (2011) Trends Biochem. Sci , vol.37 , pp. 106-117
    • Basha, E.1    O'Neill, H.2    Vierling, E.3
  • 77
    • 80054772211 scopus 로고    scopus 로고
    • Structure-functions of HspB1 (Hsp27)
    • Arrigo, A.P. Structure-functions of HspB1 (Hsp27). Methods Mol. Biol. 2011, 787, 105-119.
    • (2011) Methods Mol. Biol , vol.787 , pp. 105-119
    • Arrigo, A.P.1
  • 79
    • 0023697402 scopus 로고
    • Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein
    • Arrigo, A.-P.; Suhan, J.P.; Welch, W.J. Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein. Mol. Cell. Biol. 1988, 8, 5059-5071.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 5059-5071
    • Arrigo, A.-P.1    Suhan, J.P.2    Welch, W.J.3
  • 80
    • 0028263008 scopus 로고
    • The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization
    • Mehlen, P.; Arrigo, A.-P. The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization. Eur. J. Biochem. 1994, 221, 327-334.
    • (1994) Eur. J. Biochem , vol.221 , pp. 327-334
    • Mehlen, P.1    Arrigo, A.-P.2
  • 81
    • 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 TNFα in NIH-3T3-ras cells
    • Mehlen, P.; Hickey, E.; Weber, L.; Arrigo, A.-P. Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFα in NIH-3T3-ras cells. Biochem. Biophys. Res. Comm. 1997, 241, 187-192.
    • (1997) Biochem. Biophys. Res. Comm , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.3    Arrigo, A.-P.4
  • 82
    • 0036092428 scopus 로고    scopus 로고
    • Size matters: Of the small HSP27 and its large oligomers
    • Garrido, C. Size matters: Of the small HSP27 and its large oligomers. Cell Death Differ. 2002, 9, 483-485.
    • (2002) Cell Death Differ , vol.9 , pp. 483-485
    • Garrido, C.1
  • 83
    • 84934439863 scopus 로고    scopus 로고
    • The cellular -networking{norm of matrix} of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis
    • Arrigo, A.P. The cellular -networking{norm of matrix} 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
  • 85
    • 0026330838 scopus 로고
    • Immunological evidence for the identity between the hsp27 estrogenregulated heat shock protein and the p29 estrogen receptor-associated protein in breast and endometrial cancer
    • Ciocca, D.R.; Luque, E.H. Immunological evidence for the identity between the hsp27 estrogenregulated heat shock protein and the p29 estrogen receptor-associated protein in breast and endometrial cancer. Breast. Cancer Res. Treat. 1991, 20, 33-42.
    • (1991) Breast. Cancer Res. Treat , vol.20 , pp. 33-42
    • Ciocca, D.R.1    Luque, E.H.2
  • 86
    • 34247602460 scopus 로고    scopus 로고
    • The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation
    • Al-Madhoun, A.S.; Chen, Y.X.; Haidari, L.; Rayner, K.; Gerthoffer, W.; McBride, H.; O'Brien, E.R. The interaction and cellular localization of HSP27 and ERbeta are modulated by 17beta-estradiol and HSP27 phosphorylation. Mol. Cell Endocrinol. 2007, 270, 33-42.
    • (2007) Mol. Cell Endocrinol , vol.270 , pp. 33-42
    • Al-Madhoun, A.S.1    Chen, Y.X.2    Haidari, L.3    Rayner, K.4    Gerthoffer, W.5    McBride, H.6    O'Brien, E.R.7
  • 87
    • 77951491586 scopus 로고    scopus 로고
    • alphaB-crystallin: A novel VEGF chaperone
    • Kerr, B.A.; Byzova, T.V. alphaB-crystallin: A novel VEGF chaperone. Blood 2010, 115, 3181-3183.
    • (2010) Blood , vol.115 , pp. 3181-3183
    • Kerr, B.A.1    Byzova, T.V.2
  • 88
    • 34249749409 scopus 로고    scopus 로고
    • Interactions between important regulatory proteins and human alphaB crystallin
    • Ghosh, J.G.; Shenoy, A.K., Jr.; Clark, J.I. Interactions between important regulatory proteins and human alphaB crystallin. Biochemistry 2007, 46, 6308-6317.
    • (2007) Biochemistry , vol.46 , pp. 6308-6317
    • Ghosh, J.G.1    Shenoy Jr., A.K.2    Clark, J.I.3
  • 89
    • 35948950583 scopus 로고    scopus 로고
    • Cooperative interactions between androgen receptor (AR) and heat-shock protein 27 facilitate AR transcriptional activity
    • Zoubeidi, A.; Zardan, A.; Beraldi, E.; Fazli, L.; Sowery, R.; Rennie, P.; Nelson, C.; Gleave, M. Cooperative interactions between androgen receptor (AR) and heat-shock protein 27 facilitate AR transcriptional activity. Cancer Res. 2007, 67, 10455-10465.
    • (2007) Cancer Res , vol.67 , pp. 10455-10465
    • Zoubeidi, A.1    Zardan, A.2    Beraldi, E.3    Fazli, L.4    Sowery, R.5    Rennie, P.6    Nelson, C.7    Gleave, M.8
  • 90
    • 79959362400 scopus 로고    scopus 로고
    • alphaB-crystallin, a small heat shock protein, modulates NF-kappaB activity in a phosphorylation-dependent manner and protects muscle myoblasts from TNF-alpha induced cytotoxicity
    • Adhikari, A.S.; Singh, B.N.; Rao, K.S.; Rao Ch, M. alphaB-crystallin, a small heat shock protein, modulates NF-kappaB activity in a phosphorylation-dependent manner and protects muscle myoblasts from TNF-alpha induced cytotoxicity. Biochim. Biophys. Acta 2011, 1813, 1532-1542
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1532-1542
    • Adhikari, A.S.1    Singh, B.N.2    Rao, K.S.3    Rao, C.M.4
  • 91
    • 56949099411 scopus 로고    scopus 로고
    • HSP27 regulates IL-1 stimulated IKK activation through interacting with TRAF6 and affecting its ubiquitination
    • Wu, Y.; Liu, J.; Zhang, Z.; Huang, H.; Shen, J.; Zhang, S.; Jiang, Y.; Luo, L.; Yin, Z. HSP27 regulates IL-1 stimulated IKK activation through interacting with TRAF6 and affecting its ubiquitination. Cell. Signal. 2009, 21, 143-150.
    • (2009) Cell. Signal , vol.21 , pp. 143-150
    • Wu, Y.1    Liu, J.2    Zhang, Z.3    Huang, H.4    Shen, J.5    Zhang, S.6    Jiang, Y.7    Luo, L.8    Yin, Z.9
  • 92
    • 0034512869 scopus 로고    scopus 로고
    • The interaction of HSP27 with Daxx identifies a potential regulatory role of HSP27 in Fas-induced apoptosis
    • Charette, S.J.; Landry, J. The interaction of HSP27 with Daxx identifies a potential regulatory role of HSP27 in Fas-induced apoptosis. Ann. NY Acad. Sci. 2000, 926, 126-131.
    • (2000) Ann. NY Acad. Sci , vol.926 , pp. 126-131
    • Charette, S.J.1    Landry, J.2
  • 93
    • 77953269378 scopus 로고    scopus 로고
    • Repeated-dose toxicity of HSP27-binding heptapeptide in mice
    • Lee, H.J.; Lee, Y.S. Repeated-dose toxicity of HSP27-binding heptapeptide in mice. Drug Chem. Toxicol. 2010, 33, 284-290.
    • (2010) Drug Chem. Toxicol , vol.33 , pp. 284-290
    • Lee, H.J.1    Lee, Y.S.2
  • 95
    • 34547588567 scopus 로고    scopus 로고
    • Hsp27 regulates Akt activation and polymorphonuclear leukocyte apoptosis by scaffolding MK2 to Akt signal complex
    • Wu, R.; Kausar, H.; Johnson, P.; Montoya-Durango, D.E.; Merchant, M.; Rane, M.J. Hsp27 regulates Akt activation and polymorphonuclear leukocyte apoptosis by scaffolding MK2 to Akt signal complex. J. Biol. Chem. 2007, 282, 21598-21608.
    • (2007) J. Biol. Chem , vol.282 , pp. 21598-21608
    • Wu, R.1    Kausar, H.2    Johnson, P.3    Montoya-Durango, D.E.4    Merchant, M.5    Rane, M.J.6
  • 96
    • 4444281383 scopus 로고    scopus 로고
    • Human alphaA- and alphaB-crystallins prevent UVA-induced apoptosis through regulation of PKCalpha, RAF/MEK/ERK and AKT signaling pathways
    • Liu, J.P.; Schlosser, R.; Ma, W.Y.; Dong, Z.; Feng, H.; Lui, L.; Huang, X.Q.; Liu, Y.; Li, D.W. Human alphaA- and alphaB-crystallins prevent UVA-induced apoptosis through regulation of PKCalpha, RAF/MEK/ERK and AKT signaling pathways. Exp. Eye Res. 2004, 79, 393-403.
    • (2004) Exp. Eye Res , vol.79 , pp. 393-403
    • Liu, J.P.1    Schlosser, R.2    Ma, W.Y.3    Dong, Z.4    Feng, H.5    Lui, L.6    Huang, X.Q.7    Liu, Y.8    Li, D.W.9
  • 98
    • 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, R.M.; Locke, J.; Beraldi, E.; Fazli, L.; Gleave, M.E. Hsp27 promotes insulin-like growth factor-I survival signaling in prostate cancer via p90Rsk-dependent phosphorylation and inactivation of BAD. Cancer Res. 2010, 70, 2307-2317.
    • (2010) Cancer Res , vol.70 , pp. 2307-2317
    • Zoubeidi, A.1    Zardan, A.2    Wiedmann, R.M.3    Locke, J.4    Beraldi, E.5    Fazli, L.6    Gleave, M.E.7
  • 100
    • 17644370387 scopus 로고    scopus 로고
    • A phosphorylation state-specific antibody recognizes Hsp27, a novel substrate of protein kinase D
    • Doppler, H.; Storz, P.; Li, J.; Comb, M.J.; Toker, A. A phosphorylation state-specific antibody recognizes Hsp27, a novel substrate of protein kinase D. J. Biol. Chem. 2005, 280, 15013-15019.
    • (2005) J. Biol. Chem , vol.280 , pp. 15013-15019
    • Doppler, H.1    Storz, P.2    Li, J.3    Comb, M.J.4    Toker, A.5
  • 102
    • 24344508124 scopus 로고    scopus 로고
    • Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by alpha B-crystallin through inhibition of RAS activation
    • Li, D.W.; Liu, J.P.; Mao, Y.W.; Xiang, H.; Wang, J.; Ma, W.Y.; Dong, Z.; Pike, H.M.; Brown, R.E.; Reed, J.C. Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by alpha B-crystallin through inhibition of RAS activation. Mol. Biol. Cell. 2005, 16, 4437-4453.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4437-4453
    • Li, D.W.1    Liu, J.P.2    Mao, Y.W.3    Xiang, H.4    Wang, J.5    Ma, W.Y.6    Dong, Z.7    Pike, H.M.8    Brown, R.E.9    Reed, J.C.10
  • 103
    • 34248163076 scopus 로고    scopus 로고
    • HSP27 and HSP70 interact with CD10 in C4-2 prostate cancer cells
    • Dall'Era, M.A.; Oudes, A.; Martin, D.B.; Liu, A.Y. HSP27 and HSP70 interact with CD10 in C4-2 prostate cancer cells. Prostate 2007, 67, 714-721.
    • (2007) Prostate , vol.67 , pp. 714-721
    • Dall'Era, M.A.1    Oudes, A.2    Martin, D.B.3    Liu, A.Y.4
  • 104
    • 84868458674 scopus 로고    scopus 로고
    • Activation of an immune-regulatory macrophage response and inhibition of lung inflammation in a mouse model of COPD using heat-shock protein alpha B-crystallin-loaded PLGA microparticles
    • Van Noort, J.M.; Bsibsi, M.; Nacken, P.J.; Gerritsen, W.H.; Amor, S.; Holtman, I.R.; Boddeke, E.; van Ark, I.; Leusink-Muis, T.; Folkerts, G.; et al. Activation of an immune-regulatory macrophage response and inhibition of lung inflammation in a mouse model of COPD using heat-shock protein alpha B-crystallin-loaded PLGA microparticles. Biomaterials 2013, 34, 831-840.
    • (2013) Biomaterials , vol.34 , pp. 831-840
    • van Noort, J.M.1    Bsibsi, M.2    Nacken, P.J.3    Gerritsen, W.H.4    Amor, S.5    Holtman, I.R.6    Boddeke, E.7    van Ark, I.8    Leusink-Muis, T.9    Folkerts, G.10
  • 107
    • 84862939518 scopus 로고    scopus 로고
    • alphaA- and alphaB-crystallins interact with caspase-3 and Bax to guard mouse lens development
    • Hu, W.F.; Gong, L.; Cao, Z.; Ma, H.; Ji, W.; Deng, M.; Liu, M.; Hu, X.H.; Chen, P.; Yan, Q.; et al. alphaA- and alphaB-crystallins interact with caspase-3 and Bax to guard mouse lens development. Curr. Mol. Med. 2012, 12, 177-187.
    • (2012) Curr. Mol. Med , vol.12 , pp. 177-187
    • Hu, W.F.1    Gong, L.2    Cao, Z.3    Ma, H.4    Ji, W.5    Deng, M.6    Liu, M.7    Hu, X.H.8    Chen, P.9    Yan, Q.10
  • 109
    • 0142102552 scopus 로고    scopus 로고
    • Methylglyoxal modifies heat shock protein 27 in glomerular mesangial cells
    • Padival, A.K.; Crabb, J.W.; Nagaraj, R.H. Methylglyoxal modifies heat shock protein 27 in glomerular mesangial cells. FEBS Lett. 2003, 551, 113-118.
    • (2003) FEBS Lett , vol.551 , pp. 113-118
    • Padival, A.K.1    Crabb, J.W.2    Nagaraj, R.H.3
  • 110
    • 2442681777 scopus 로고    scopus 로고
    • Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis
    • Mao, Y.W.; Liu, J.P.; Xiang, H.; Li, D.W. Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ. 2004, 11, 512-526.
    • (2004) Cell Death Differ , vol.11 , pp. 512-526
    • Mao, Y.W.1    Liu, J.P.2    Xiang, H.3    Li, D.W.4
  • 111
    • 33846297971 scopus 로고    scopus 로고
    • Small heat shock protein alphaB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis
    • Liu, S.; Li, J.; Tao, Y.; Xiao, X. Small heat shock protein alphaB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis. Biochem. Biophys. Res. Commun. 2007, 354, 109-114.
    • (2007) Biochem. Biophys. Res. Commun , vol.354 , pp. 109-114
    • Liu, S.1    Li, J.2    Tao, Y.3    Xiao, X.4
  • 114
    • 84872673278 scopus 로고    scopus 로고
    • Cisplatin enhances interaction between p66Shc and HSP27: Its role in reorganization of the actin cytoskeleton in renal proximal tubule cells
    • Arany, I.; Clark, J.S.; Reed, D.K.; Ember, I.; Juncos, L.A. Cisplatin enhances interaction between p66Shc and HSP27: Its role in reorganization of the actin cytoskeleton in renal proximal tubule cells. Anticancer Res. 2012, 32, 4759-4763.
    • (2012) Anticancer Res , vol.32 , pp. 4759-4763
    • Arany, I.1    Clark, J.S.2    Reed, D.K.3    Ember, I.4    Juncos, L.A.5
  • 115
    • 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.; Chaufour, S.; Paul, C.; Stepien, G.; Ursini, M.V.; Arrigo, A.P. 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, 61-78.
    • (1999) Exp. Cell Res , vol.247 , pp. 61-78
    • Preville, X.1    Salvemini, F.2    Giraud, S.3    Chaufour, S.4    Paul, C.5    Stepien, G.6    Ursini, M.V.7    Arrigo, A.P.8
  • 116
    • 79551580561 scopus 로고    scopus 로고
    • ATM activates the pentose phosphate pathway promoting anti-oxidant defence and DNA repair
    • Cosentino, C.; Grieco, D.; Costanzo, V. ATM activates the pentose phosphate pathway promoting anti-oxidant defence and DNA repair. EMBO J. 2011, 30, 546-555.
    • (2011) EMBO J , vol.30 , pp. 546-555
    • Cosentino, C.1    Grieco, D.2    Costanzo, V.3
  • 118
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • Mounier, N.; Arrigo, A.P. Actin cytoskeleton and small heat shock proteins: How do they. interact? Cell Stress Chaperones 2002, 7, 167-176
    • (2002) Cell Stress Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 120
    • 84872316472 scopus 로고    scopus 로고
    • Commentary on paper: Small heat shock proteins and the cytoskeleton: An essential interplay for cell integrity?
    • (Wettstein et al.)
    • Seit-Nebi, A.S.; Datskevich, P.; Gusev, N.B. Commentary on paper: Small heat shock proteins and the cytoskeleton: An essential interplay for cell integrity? (Wettstein et al.). Int. J. Biochem. Cell Biol. 2013, 45, 344-346.
    • (2013) Int. J. Biochem. Cell Biol , vol.45 , pp. 344-346
    • Seit-Nebi, A.S.1    Datskevich, P.2    Gusev, N.B.3
  • 121
    • 0021199252 scopus 로고
    • Association of alpha-crystallin with actin in cultured lens cells
    • Del Vecchio, P.J.; MacElroy, K.S.; Rosser, M.P.; Church, R.L. Association of alpha-crystallin with actin in cultured lens cells. Curr. Eye Res. 1984, 3, 1213-1219.
    • (1984) Curr. Eye Res , vol.3 , pp. 1213-1219
    • Del Vecchio, P.J.1    Macelroy, K.S.2    Rosser, M.P.3    Church, R.L.4
  • 122
    • 0029658123 scopus 로고    scopus 로고
    • alpha-Crystallin stabilizes actin filaments and prevents cytochalasininduced depolymerization in a phosphorylation-dependent manner
    • Wang, K.; Spector, A. alpha-Crystallin stabilizes actin filaments and prevents cytochalasininduced depolymerization in a phosphorylation-dependent manner. Eur. J. Biochem. 1996, 242, 56-66.
    • (1996) Eur. J. Biochem , vol.242 , pp. 56-66
    • Wang, K.1    Spector, A.2
  • 123
    • 33846618592 scopus 로고    scopus 로고
    • Association of alphab-crystallin, a small heat shock protein, with actin: Role in modulating actin filament dynamics in vivo
    • Singh, B.N.; Rao, K.S.; Ramakrishna, T.; Rangaraj, N.; Rao Ch, M. Association of alphab-crystallin, a small heat shock protein, with actin: Role in modulating actin filament dynamics in vivo. J. Mol. Biol. 2007, 366, 756-767.
    • (2007) J. Mol. Biol , vol.366 , pp. 756-767
    • Singh, B.N.1    Rao, K.S.2    Ramakrishna, T.3    Rangaraj, N.4    Rao, C.M.5
  • 124
    • 34548241302 scopus 로고    scopus 로고
    • Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments
    • Ghosh, J.G.; Houck, S.A.; Clark, J.I. Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments. Int. J. Biochem. Cell Biol. 2007, 39, 1804-1815.
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 1804-1815
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 125
    • 0034728761 scopus 로고    scopus 로고
    • Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells
    • Hino, M.; Kurogi, K.; Okubo, M.A.; Murata-Hori, M.; Hosoya, H. Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells. Biochem. Biophys. Res. Commun. 2000, 271, 164-169.
    • (2000) Biochem. Biophys. Res. Commun , vol.271 , pp. 164-169
    • Hino, M.1    Kurogi, K.2    Okubo, M.A.3    Murata-Hori, M.4    Hosoya, H.5
  • 126
    • 34548028021 scopus 로고    scopus 로고
    • Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregation
    • Ohto-Fujita, E.; Fujita, Y.; Atomi, Y. Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregation. Cell Stress Chaperones 2007, 12, 163-171.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 163-171
    • Ohto-Fujita, E.1    Fujita, Y.2    Atomi, Y.3
  • 127
    • 40149111037 scopus 로고    scopus 로고
    • Interactive domains in the molecular chaperone human alphaB crystallin modulate microtubule assembly and disassembly
    • Ghosh, J.G.; Houck, S.A.; Clark, J.I. Interactive domains in the molecular chaperone human alphaB crystallin modulate microtubule assembly and disassembly. PLoS One 2007, 2, e498.
    • (2007) PLoS One , vol.2
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 128
    • 33744475377 scopus 로고    scopus 로고
    • Alpha-crystallin expression affects microtubule assembly and prevents their aggregation
    • Xi, J.H.; Bai, F.; McGaha, R.; Andley, U.P. Alpha-crystallin expression affects microtubule assembly and prevents their aggregation. FASEB J. 2006, 20, 846-857.
    • (2006) FASEB J , vol.20 , pp. 846-857
    • Xi, J.H.1    Bai, F.2    McGaha, R.3    Andley, U.P.4
  • 129
    • 0030724879 scopus 로고    scopus 로고
    • AlphaB-crystallin interacts with intermediate filaments in response to stress
    • Djabali, K.; de Nechaud, B.; Landon, F.; Portier, M.M. AlphaB-crystallin interacts with intermediate filaments in response to stress. J. Cell Sci. 1997, 110, 2759-2769.
    • (1997) J. Cell Sci , vol.110 , pp. 2759-2769
    • Djabali, K.1    de Nechaud, B.2    Landon, F.3    Portier, M.M.4
  • 130
    • 0033571984 scopus 로고    scopus 로고
    • alphaB-crystallin interacts with cytoplasmic intermediate filament bundles during mitosis
    • Djabali, K.; Piron, G.; de Nechaud, B.; Portier, M.M. alphaB-crystallin interacts with cytoplasmic intermediate filament bundles during mitosis. Exp. Cell Res. 1999, 253, 649-662.
    • (1999) Exp. Cell Res , vol.253 , pp. 649-662
    • Djabali, K.1    Piron, G.2    de Nechaud, B.3    Portier, M.M.4
  • 132
    • 41149138739 scopus 로고    scopus 로고
    • alpha B-crystallin is a cytoplasmic interaction partner of the kidney-specific cadherin-16
    • Thedieck, C.; Kalbacher, H.; Kratzer, U.; Lammers, R.; Stevanovic, S.; Klein, G. alpha B-crystallin is a cytoplasmic interaction partner of the kidney-specific cadherin-16. J. Mol. Biol. 2008, 378, 145-153.
    • (2008) J. Mol. Biol , vol.378 , pp. 145-153
    • Thedieck, C.1    Kalbacher, H.2    Kratzer, U.3    Lammers, R.4    Stevanovic, S.5    Klein, G.6
  • 133
    • 0032587169 scopus 로고    scopus 로고
    • AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress
    • Muchowski, P.J.; Valdez, M.M.; Clark, J.I. AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress. Invest. Ophthalmol. Vis. Sci. 1999, 40, 951-958.
    • (1999) Invest. Ophthalmol. Vis. Sci , vol.40 , pp. 951-958
    • Muchowski, P.J.1    Valdez, M.M.2    Clark, J.I.3
  • 134
    • 66149126023 scopus 로고    scopus 로고
    • Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens
    • Barton, K.A.; Hsu, C.D.; Petrash, J.M. Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens. Biochemistry 2009, 48, 3956-3966.
    • (2009) Biochemistry , vol.48 , pp. 3956-3966
    • Barton, K.A.1    Hsu, C.D.2    Petrash, J.M.3
  • 135
    • 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.; Fazli, L.; Vessella, R.L.; Nelson, C.; Gleave, M. 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, 11083-11093.
    • (2005) Cancer Res , vol.65 , pp. 11083-11093
    • Rocchi, P.1    Beraldi, E.2    Ettinger, S.3    Fazli, L.4    Vessella, R.L.5    Nelson, C.6    Gleave, M.7
  • 136
    • 70349287559 scopus 로고    scopus 로고
    • Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity
    • Brunet Simioni, M.; de Thonel, A.; Hammann, A.; Joly, A.L.; Bossis, G.; Fourmaux, E.; Bouchot, A.; Landry, J.; Piechaczyk, M.; Garrido, C. Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity. Oncogene 2009, 28, 3332-3344.
    • (2009) Oncogene , vol.28 , pp. 3332-3344
    • Brunet, S.M.1    de Thonel, A.2    Hammann, A.3    Joly, A.L.4    Bossis, G.5    Fourmaux, E.6    Bouchot, A.7    Landry, J.8    Piechaczyk, M.9    Garrido, C.10
  • 138
    • 0034659505 scopus 로고    scopus 로고
    • Chaperone Hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes
    • Cuesta, R.; Laroia, G.; Schneider, R.J. Chaperone Hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev. 2000, 14, 1460-1470.
    • (2000) Genes Dev , vol.14 , pp. 1460-1470
    • Cuesta, R.1    Laroia, G.2    Schneider, R.J.3
  • 139
    • 77950518207 scopus 로고    scopus 로고
    • Heat shock protein 27 confers resistance to androgen ablation and chemotherapy in prostate cancer cells through eIF4E
    • Andrieu, C.; Taieb, D.; Baylot, V.; Ettinger, S.; Soubeyran, P.; De-Thonel, A.; Nelson, C.; Garrido, C.; So, A.; Fazli, L.; et al. Heat shock protein 27 confers resistance to androgen ablation and chemotherapy in prostate cancer cells through eIF4E. Oncogene 2010, 29, 1883-1896.
    • (2010) Oncogene , vol.29 , pp. 1883-1896
    • Andrieu, C.1    Taieb, D.2    Baylot, V.3    Ettinger, S.4    Soubeyran, P.5    De-Thonel, A.6    Nelson, C.7    Garrido, C.8    So, A.9    Fazli, L.10
  • 142
    • 80054864989 scopus 로고    scopus 로고
    • Ubiquitination of heat shock protein 27 is mediated by its interaction with Smad ubiquitination regulatory factor 2 in A549 cells
    • Sun, Y.; Zhou, M.; Fu, D.; Xu, B.; Fang, T.; Ma, Y.; Chen, J.; Zhang, J. Ubiquitination of heat shock protein 27 is mediated by its interaction with Smad ubiquitination regulatory factor 2 in A549 cells. Exp. Lung Res. 2011, 37, 568-573.
    • (2011) Exp. Lung Res , vol.37 , pp. 568-573
    • Sun, Y.1    Zhou, M.2    Fu, D.3    Xu, B.4    Fang, T.5    Ma, Y.6    Chen, J.7    Zhang, J.8
  • 146
    • 0035847115 scopus 로고    scopus 로고
    • Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7
    • Boelens, W.C.; Croes, Y.; de Jong, W.W. Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7. Biochim. Biophys. Acta 2001, 1544, 311-319.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 311-319
    • Boelens, W.C.1    Croes, Y.2    De Jong, W.W.3
  • 147
    • 0031454881 scopus 로고    scopus 로고
    • Hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells
    • Mehlen, P.; Mehlen, A.; Godet, J.; Arrigo, A.-P. Hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells. J. Biol. Chem. 1997, 272, 31657-31665.
    • (1997) J. Biol. Chem , vol.272 , pp. 31657-31665
    • Mehlen, P.1    Mehlen, A.2    Godet, J.3    Arrigo, A.-P.4
  • 148
    • 84867815944 scopus 로고    scopus 로고
    • Editorial: Heat shock proteins in cancer
    • Arrigo, A.P. Editorial: Heat shock proteins in cancer. Curr. Mol. Med. 2012, 12, 1099-1101.
    • (2012) Curr. Mol. Med , vol.12 , pp. 1099-1101
    • Arrigo, A.P.1
  • 152
    • 0028817419 scopus 로고
    • Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts
    • Mehlen, P.; Préville, X.; Chareyron, P.; Briolay, J.; Klemenz, R.; Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts. J. Immunol. 1995, 154, 363-374.
    • (1995) J. Immunol , vol.154 , pp. 363-374
    • Mehlen, P.1    Préville, X.2    Chareyron, P.3    Briolay, J.4    Klemenz, R.5
  • 153
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of daxx-mediated apoptosis by heat shock protein 27
    • Charette, S.J.; Lavoie, J.N.; Lambert, H.; Landry, J. Inhibition of daxx-mediated apoptosis by heat shock protein 27. Mol. Cell. Biol. 2000, 20, 7602-7612.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3    Landry, J.4
  • 156
    • 84856573441 scopus 로고    scopus 로고
    • Deletion of the SPARC acidic domain or EGF-like module reduces SPARC-induced migration and signaling through p38 MAPK/HSP27 in glioma
    • McClung, H.M.; Golembieski, W.A.; Schultz, C.R.; Jankowski, M.; Schultz, L.R.; Rempel, S.A. Deletion of the SPARC acidic domain or EGF-like module reduces SPARC-induced migration and signaling through p38 MAPK/HSP27 in glioma. Carcinogenesis 2012, 33, 275-284.
    • (2012) Carcinogenesis , vol.33 , pp. 275-284
    • McClung, H.M.1    Golembieski, W.A.2    Schultz, C.R.3    Jankowski, M.4    Schultz, L.R.5    Rempel, S.A.6
  • 157
    • 0034711260 scopus 로고    scopus 로고
    • Differential protective activity of {alpha}A- and {alpha}B-crystallin in lens epithelial cells
    • Andley, U.P.; Song, Z.; Wawrousek, E.F.; Fleming, T.P.; Bassnett, S. Differential protective activity of {alpha}A- and {alpha}B-crystallin in lens epithelial cells. J. Biol. Chem. 2000, 275, 36823-36831.
    • (2000) J. Biol. Chem , vol.275 , pp. 36823-36831
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3    Fleming, T.P.4    Bassnett, S.5
  • 158
    • 78549288555 scopus 로고    scopus 로고
    • Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells
    • Launay, N.; Tarze, A.; Vicart, P.; Lilienbaum, A. Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells. J. Biol. Chem. 2010, 285, 37324-37332.
    • (2010) J. Biol. Chem , vol.285 , pp. 37324-37332
    • Launay, N.1    Tarze, A.2    Vicart, P.3    Lilienbaum, A.4
  • 160
    • 84870858502 scopus 로고    scopus 로고
    • HSP27 expression in primary colorectal cancers is dependent on mutation of KRAS and PI3K/AKT activation status and is independent of TP53
    • Ghosh, A.; Lai, C.; McDonald, S.; Suraweera, N.; Sengupta, N.; Propper, D.; Dorudi, S.; Silver, A. HSP27 expression in primary colorectal cancers is dependent on mutation of KRAS and PI3K/AKT activation status and is independent of TP53. Exp. Mol. Pathol. 2013, 94, 103-108.
    • (2013) Exp. Mol. Pathol , vol.94 , pp. 103-108
    • Ghosh, A.1    Lai, C.2    McDonald, S.3    Suraweera, N.4    Sengupta, N.5    Propper, D.6    Dorudi, S.7    Silver, A.8
  • 163
    • 78149249046 scopus 로고    scopus 로고
    • Heat shock proteins in prostate cancer: From tumorigenesis to the clinic
    • Ciocca, D.R.; Fanelli, M.A.; Cuello-Carrion, F.D.; Castro, G.N. Heat shock proteins in prostate cancer: From tumorigenesis to the clinic. Int. J. Hyperth. 2010, 26, 737-747.
    • (2010) Int. J. Hyperth , vol.26 , pp. 737-747
    • Ciocca, D.R.1    Fanelli, M.A.2    Cuello-Carrion, F.D.3    Castro, G.N.4
  • 164
    • 0027482463 scopus 로고
    • Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of Heat Shock Protein 27
    • Lavoie, J.N.; Hickey, E.; Weber, L.A.; Landry, J. Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of Heat Shock Protein 27. J. Biol. Chem. 1993, 268, 24210-24214.
    • (1993) J. Biol. Chem , vol.268 , pp. 24210-24214
    • Lavoie, J.N.1    Hickey, E.2    Weber, L.A.3    Landry, J.4
  • 165
    • 0030069517 scopus 로고    scopus 로고
    • HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot, J.; Houle, F.; Spitz, D.R.; Landry, J. HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res. 1996, 56, 273-279.
    • (1996) Cancer Res , vol.56 , pp. 273-279
    • Huot, J.1    Houle, F.2    Spitz, D.R.3    Landry, J.4
  • 166
    • 0035893961 scopus 로고    scopus 로고
    • The actin cytoskeleton response to oxidants: From small heat shock protein phosphorylation to changes in the redox state of actin itself
    • Dalle-Donne, I.; Rossi, R.; Milzani, A.; di Simplicio, P.; Colombo, R. The actin cytoskeleton response to oxidants: From small heat shock protein phosphorylation to changes in the redox state of actin itself. Free Radic. Biol. Med. 2001, 31, 1624-1632.
    • (2001) Free Radic. Biol. Med , vol.31 , pp. 1624-1632
    • Dalle-Donne, I.1    Rossi, R.2    Milzani, A.3    di Simplicio, P.4    Colombo, R.5
  • 167
    • 84864488251 scopus 로고    scopus 로고
    • Small heat shock proteins and the cytoskeleton: An essential interplay for cell integrity
    • Wettstein, G.; Bellaye, P.S.; Micheau, O.; Bonniaud, P. Small heat shock proteins and the cytoskeleton: An essential interplay for cell integrity? Int. J. Biochem. Cell Biol. 2012, 44, 1680-1686.
    • (2012) Int. J. Biochem. Cell Biol , vol.44 , pp. 1680-1686
    • Wettstein, G.1    Bellaye, P.S.2    Micheau, O.3    Bonniaud, P.4
  • 168
    • 33646859435 scopus 로고    scopus 로고
    • MAPKAPK2 and HSP27 are downstream effectors of p38 MAP kinase-mediated matrix metalloproteinase type 2 activation and cell invasion in human prostate cancer
    • Xu, L.; Chen, S.; Bergan, R.C. MAPKAPK2 and HSP27 are downstream effectors of p38 MAP kinase-mediated matrix metalloproteinase type 2 activation and cell invasion in human prostate cancer. Oncogene 2006, 25, 2987-2998.
    • (2006) Oncogene , vol.25 , pp. 2987-2998
    • Xu, L.1    Chen, S.2    Bergan, R.C.3
  • 169
    • 79961225122 scopus 로고    scopus 로고
    • Lymphovascular invasion of colorectal cancer is correlated to SPARC expression in the tumor stromal microenvironment
    • Yoshimura, T.; Nagahara, M.; Kuo, C.; Turner, R.R.; Soon-Shiong, P.; Hoon, D.S. Lymphovascular invasion of colorectal cancer is correlated to SPARC expression in the tumor stromal microenvironment. Epigenetics 2011, 6, 1001-1011.
    • (2011) Epigenetics , vol.6 , pp. 1001-1011
    • Yoshimura, T.1    Nagahara, M.2    Kuo, C.3    Turner, R.R.4    Soon-Shiong, P.5    Hoon, D.S.6
  • 170
    • 84859331722 scopus 로고    scopus 로고
    • Inhibition of HSP27 alone or in combination with pAKT inhibition as therapeutic approaches to target SPARC-induced glioma cell survival
    • Schultz, C.R.; Golembieski, W.A.; King, D.A.; Brown, S.L.; Brodie, C.; Rempel, S.A. Inhibition of HSP27 alone or in combination with pAKT inhibition as therapeutic approaches to target SPARC-induced glioma cell survival. Mol. Cancer 2012, 11, 20.
    • (2012) Mol. Cancer , vol.11 , pp. 20
    • Schultz, C.R.1    Golembieski, W.A.2    King, D.A.3    Brown, S.L.4    Brodie, C.5    Rempel, S.A.6
  • 171
    • 84855546696 scopus 로고    scopus 로고
    • Silencing Hsp25/Hsp27 gene expression augments proteasome activity and increases CD8+T-cell-mediated tumor killing and memory responses
    • Nagaraja, G.M.; Kaur, P.; Neumann, W.; Asea, E.E.; Bausero, M.A.; Multhoff, G.; Asea, A. Silencing Hsp25/Hsp27 gene expression augments proteasome activity and increases CD8+T-cell-mediated tumor killing and memory responses. Cancer Prev. Res. Phila 2012, 5, 122-137.
    • (2012) Cancer Prev. Res. Phila , vol.5 , pp. 122-137
    • Nagaraja, G.M.1    Kaur, P.2    Neumann, W.3    Asea, E.E.4    Bausero, M.A.5    Multhoff, G.6    Asea, A.7
  • 172
    • 31044436397 scopus 로고    scopus 로고
    • Is the small heat shock protein alphaB-crystallin an oncogene
    • Gruvberger-Saal, S.K.; Parsons, R. Is the small heat shock protein alphaB-crystallin an oncogene? J. Clin. Invest. 2006, 116, 30-32.
    • (2006) J. Clin. Invest , vol.116 , pp. 30-32
    • Gruvberger-Saal, S.K.1    Parsons, R.2
  • 173
    • 79958748545 scopus 로고    scopus 로고
    • Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: A form of communication during injury, infection, and cell damage It is never known how far a controversial finding will go! Dedicated to Ferruccio Ritossa
    • De Maio, A. Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: A form of communication during injury, infection, and cell damage. It is never known how far a controversial finding will go! Dedicated to Ferruccio Ritossa. Cell Stress Chaperones 2011, 16, 235-249.
    • (2011) Cell Stress Chaperones , vol.16 , pp. 235-249
    • De Maio, A.1
  • 176
    • 48849088564 scopus 로고    scopus 로고
    • Extracellular release of the atheroprotective heat shock protein 27 is mediated by estrogen and competitively inhibits acLDL binding to scavenger receptor-A
    • Rayner, K.; Chen, Y.X.; McNulty, M.; Simard, T.; Zhao, X.; Wells, D.J.; de Belleroche, J.; O'Brien, E.R. Extracellular release of the atheroprotective heat shock protein 27 is mediated by estrogen and competitively inhibits acLDL binding to scavenger receptor-A. Circ. Res. 2008, 103, 133-141
    • (2008) Circ. Res , vol.103 , pp. 133-141
    • Rayner, K.1    Chen, Y.X.2    McNulty, M.3    Simard, T.4    Zhao, X.5    Wells, D.J.6    de Belleroche, J.7    O'Brien, E.R.8
  • 178
    • 76649097628 scopus 로고    scopus 로고
    • Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells
    • Chalmin, F.; Ladoire, S.; Mignot, G.; Vincent, J.; Bruchard, M.; Remy-Martin, J.P.; Boireau, W.; Rouleau, A.; Simon, B.; Lanneau, D.; et al. Membrane-associated Hsp72 from tumor-derived exosomes mediates STAT3-dependent immunosuppressive function of mouse and human myeloid-derived suppressor cells. J. Clin. Invest. 2010, 120, 457-471.
    • (2010) J. Clin. Invest , vol.120 , pp. 457-471
    • Chalmin, F.1    Ladoire, S.2    Mignot, G.3    Vincent, J.4    Bruchard, M.5    Remy-Martin, J.P.6    Boireau, W.7    Rouleau, A.8    Simon, B.9    Lanneau, D.10
  • 181
    • 34447118860 scopus 로고    scopus 로고
    • Antibodies to alpha B-crystallin, vimentin, and heat shock protein 70 in aqueous humor of patients with normal tension glaucoma and IgG antibody patterns against retinal antigen in aqueous humor
    • Joachim, S.C.; Bruns, K.; Lackner, K.J.; Pfeiffer, N.; Grus, F.H. Antibodies to alpha B-crystallin, vimentin, and heat shock protein 70 in aqueous humor of patients with normal tension glaucoma and IgG antibody patterns against retinal antigen in aqueous humor. Curr. Eye Res. 2007, 32, 501-509.
    • (2007) Curr. Eye Res , vol.32 , pp. 501-509
    • Joachim, S.C.1    Bruns, K.2    Lackner, K.J.3    Pfeiffer, N.4    Grus, F.H.5
  • 182
    • 0034657707 scopus 로고    scopus 로고
    • The mechanisms of hsp27 antibody-mediated apoptosis in retinal neuronal cells
    • Tezel, G.; Wax, M.B. The mechanisms of hsp27 antibody-mediated apoptosis in retinal neuronal cells. J. Neurosci. 2000, 20, 3552-3562.
    • (2000) J. Neurosci , vol.20 , pp. 3552-3562
    • Tezel, G.1    Wax, M.B.2
  • 183
    • 33646160623 scopus 로고    scopus 로고
    • Inflammation, a key event in cancer development
    • Lu, H.; Ouyang, W.; Huang, C. Inflammation, a key event in cancer development. Mol. Cancer Res. 2006, 4, 221-233.
    • (2006) Mol. Cancer Res , vol.4 , pp. 221-233
    • Lu, H.1    Ouyang, W.2    Huang, C.3
  • 186
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these protein against TNFα-induced cell death
    • Mehlen, P.; Préville, X.; Kretz-Remy, C.; Arrigo, A.-P. Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these protein against TNFα-induced cell death. EMBO J. 1996, 15, 2695-2706.
    • (1996) EMBO J , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Préville, X.2    Kretz-Remy, C.3    Arrigo, A.-P.4
  • 187
    • 0031962486 scopus 로고    scopus 로고
    • Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death
    • Arrigo, A.P. Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death. Biol. Chem. 1998, 379, 19-26.
    • (1998) Biol. Chem , vol.379 , pp. 19-26
    • Arrigo, A.P.1
  • 188
    • 0031961844 scopus 로고    scopus 로고
    • Overexpression of HSP25 reduces the level of TNF alpha-induced oxidative DNA damage biomarker, 8-hydroxy-2'-deoxyguanosine, in L929 cells
    • Park, Y.M.; Han, M.Y.; Blackburn, R.V.; Lee, Y.J. Overexpression of HSP25 reduces the level of TNF alpha-induced oxidative DNA damage biomarker, 8-hydroxy-2'-deoxyguanosine, in L929 cells. J. Cell. Physiol. 1998, 174, 27-34.
    • (1998) J. Cell. Physiol , vol.174 , pp. 27-34
    • Park, Y.M.1    Han, M.Y.2    Blackburn, R.V.3    Lee, Y.J.4
  • 189
    • 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.; Kotlyarov, A.; Lutsch, G.; Ducasse, C.; Paul, C.; Wieske, M.; Arrigo, A.P.; Buchner, J.; 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, 18947-18956.
    • (1999) J. Biol. Chem , vol.274 , pp. 18947-18956
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3    Kotlyarov, A.4    Lutsch, G.5    Ducasse, C.6    Paul, C.7    Wieske, M.8    Arrigo, A.P.9    Buchner, J.10
  • 190
    • 0036186869 scopus 로고    scopus 로고
    • Hsp27: Novel regulator of intracellular redox state
    • Arrigo, A.P. Hsp27: Novel regulator of intracellular redox state. IUBMB Life 2001, 52, 303-307.
    • (2001) IUBMB Life , vol.52 , pp. 303-307
    • Arrigo, A.P.1
  • 192
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach, A.; Sauvageot, O.; Carmichael, J.; Diaz-Latoud, C.; Arrigo, A.P.; Rubinsztein, D.C. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Mol. Genet. 2002, 11, 1137-1151.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 193
    • 0036790590 scopus 로고    scopus 로고
    • Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage
    • Yan, L.J.; Christians, E.S.; Liu, L.; Xiao, X.; Sohal, R.S.; Benjamin, I.J. Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage. EMBO J. 2002, 21, 5164-5172.
    • (2002) EMBO J , vol.21 , pp. 5164-5172
    • Yan, L.J.1    Christians, E.S.2    Liu, L.3    Xiao, X.4    Sohal, R.S.5    Benjamin, I.J.6
  • 194
    • 14044250859 scopus 로고    scopus 로고
    • Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels
    • Arrigo, A.P.; 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, 414-422.
    • (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
  • 195
    • 33745221655 scopus 로고    scopus 로고
    • Analysis of oxidative events induced by expanded polyglutamine huntingtin exon 1 that are differentially restored by expression of heat shock proteins or treatment with an antioxidant
    • Firdaus, W.J.; Wyttenbach, A.; Diaz-Latoud, C.; Currie, R.W.; Arrigo, A.P. Analysis of oxidative events induced by expanded polyglutamine huntingtin exon 1 that are differentially restored by expression of heat shock proteins or treatment with an antioxidant. FEBS J. 2006, 273, 3076-3093.
    • (2006) FEBS J , vol.273 , pp. 3076-3093
    • Firdaus, W.J.1    Wyttenbach, A.2    Diaz-Latoud, C.3    Currie, R.W.4    Arrigo, A.P.5
  • 196
    • 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
    • Aloy, M.T.; Hadchity, E.; Bionda, C.; Diaz-Latoud, C.; Claude, L.; Rousson, R.; Arrigo, A.P.; Rodriguez-Lafrasse, C. 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, 543-553.
    • (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    Arrigo, A.P.7    Rodriguez-Lafrasse, C.8
  • 197
    • 84864437102 scopus 로고    scopus 로고
    • Small heat shock proteins in redox metabolism: Implications for cardiovascular diseases
    • Christians, E.S.; Ishiwata, T.; Benjamin, I.J. Small heat shock proteins in redox metabolism: Implications for cardiovascular diseases. Int. J. Biochem. Cell Biol. 2012, 44, 1632-1645.
    • (2012) Int. J. Biochem. Cell Biol , vol.44 , pp. 1632-1645
    • Christians, E.S.1    Ishiwata, T.2    Benjamin, I.J.3
  • 198
    • 33646192717 scopus 로고    scopus 로고
    • Heat shock protein 27 downregulates the transferrin receptor 1-mediated iron uptake
    • Chen, H.; Zheng, C.; Zhang, Y.; Chang, Y.Z.; Qian, Z.M.; Shen, X. Heat shock protein 27 downregulates the transferrin receptor 1-mediated iron uptake. Int. J. Biochem. Cell Biol. 2006, 38, 1402-1416.
    • (2006) Int. J. Biochem. Cell Biol , vol.38 , pp. 1402-1416
    • Chen, H.1    Zheng, C.2    Zhang, Y.3    Chang, Y.Z.4    Qian, Z.M.5    Shen, X.6
  • 199
    • 0031715855 scopus 로고    scopus 로고
    • Phosphorylation is not essential for protection of L929 cells by Hsp25 against H2O2-mediated disruption actin cytoskeleton, a protection which appears related to the redox change mediated by Hsp25
    • Preville, X.; Gaestel, M.; Arrigo, A.P. Phosphorylation is not essential for protection of L929 cells by Hsp25 against H2O2-mediated disruption actin cytoskeleton, a protection which appears related to the redox change mediated by Hsp25. Cell Stress Chaperones 1998, 3, 177-187.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 177-187
    • Preville, X.1    Gaestel, M.2    Arrigo, A.P.3
  • 200
    • 34447135482 scopus 로고    scopus 로고
    • Inhibition of heat shock protein 27-mediated resistance to DNA damaging agents by a novel PKC delta-V5 heptapeptide
    • Kim, E.H.; Lee, H.J.; Lee, D.H.; Bae, S.; Soh, J.W.; Jeoung, D.; Kim, J.; Cho, C.K.; Lee, Y.J.; Lee, Y.S. Inhibition of heat shock protein 27-mediated resistance to DNA damaging agents by a novel PKC delta-V5 heptapeptide. Cancer Res. 2007, 67, 6333-6341.
    • (2007) Cancer Res , vol.67 , pp. 6333-6341
    • Kim, E.H.1    Lee, H.J.2    Lee, D.H.3    Bae, S.4    Soh, J.W.5    Jeoung, D.6    Kim, J.7    Cho, C.K.8    Lee, Y.J.9    Lee, Y.S.10
  • 201
    • 0032077942 scopus 로고    scopus 로고
    • Effects of G6PD overexpression in NIH3T3 cells treated with tert-butyl hydroperoxide or paraquat
    • Kuo, W.Y.; Tang, T.K. Effects of G6PD overexpression in NIH3T3 cells treated with tert-butyl hydroperoxide or paraquat. Free Radic. Biol. Med. 1998, 24, 1130-1138.
    • (1998) Free Radic. Biol. Med , vol.24 , pp. 1130-1138
    • Kuo, W.Y.1    Tang, T.K.2
  • 202
    • 0033613855 scopus 로고    scopus 로고
    • Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression
    • Salvemini, F.; Franze, A.; Iervolino, A.; Filosa, S.; Salzano, S.; Ursini, M.V. Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression. J. Biol. Chem. 1999, 274, 2750-2757.
    • (1999) J. Biol. Chem , vol.274 , pp. 2750-2757
    • Salvemini, F.1    Franze, A.2    Iervolino, A.3    Filosa, S.4    Salzano, S.5    Ursini, M.V.6
  • 203
    • 33845301225 scopus 로고    scopus 로고
    • Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism
    • McCollum, A.K.; Teneyck, C.J.; Sauer, B.M.; Toft, D.O.; Erlichman, C. Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism. Cancer Res. 2006, 66, 10967-10975.
    • (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
  • 204
    • 0037441888 scopus 로고    scopus 로고
    • Inhibition of STAT3 signaling induces apoptosis and decreases survivin expression in primary effusion lymphoma
    • Aoki, Y.; Feldman, G.M.; Tosato, G. Inhibition of STAT3 signaling induces apoptosis and decreases survivin expression in primary effusion lymphoma. Blood 2003, 101, 1535-1542
    • (2003) Blood , vol.101 , pp. 1535-1542
    • Aoki, Y.1    Feldman, G.M.2    Tosato, G.3
  • 205
    • 30444458235 scopus 로고    scopus 로고
    • Stats: Multifaceted regulators of transcription
    • Brierley, M.M.; Fish, E.N. Stats: Multifaceted regulators of transcription. J. Interferon Cytokine Res. 2005, 25, 733-744.
    • (2005) J. Interferon Cytokine Res , vol.25 , pp. 733-744
    • Brierley, M.M.1    Fish, E.N.2
  • 206
    • 31544458469 scopus 로고    scopus 로고
    • Persistent activation of stat3 signaling induces survivin gene expression and confers resistance to apoptosis in human breast cancer cells
    • Gritsko, T.; Williams, A.; Turkson, J.; Kaneko, S.; Bowman, T.; Huang, M.; Nam, S.; Eweis, I.; Diaz, N.; Sullivan, D.; et al. Persistent activation of stat3 signaling induces survivin gene expression and confers resistance to apoptosis in human breast cancer cells. Clin. Cancer Res. 2006, 12, 11-19.
    • (2006) Clin. Cancer Res , vol.12 , pp. 11-19
    • Gritsko, T.1    Williams, A.2    Turkson, J.3    Kaneko, S.4    Bowman, T.5    Huang, M.6    Nam, S.7    Eweis, I.8    Diaz, N.9    Sullivan, D.10
  • 207
    • 31544460437 scopus 로고    scopus 로고
    • Activation of stat3 in primary tumors from high-risk breast cancer patients is associated with elevated levels of activated SRC and survivin expression
    • Diaz, N.; Minton, S.; Cox, C.; Bowman, T.; Gritsko, T.; Garcia, R.; Eweis, I.; Wloch, M.; Livingston, S.; Seijo, E.; et al. Activation of stat3 in primary tumors from high-risk breast cancer patients is associated with elevated levels of activated SRC and survivin expression. Clin. Cancer Res. 2006, 12, 20-28.
    • (2006) Clin. Cancer Res , vol.12 , pp. 20-28
    • Diaz, N.1    Minton, S.2    Cox, C.3    Bowman, T.4    Gritsko, T.5    Garcia, R.6    Eweis, I.7    Wloch, M.8    Livingston, S.9    Seijo, E.10
  • 208
    • 0347986522 scopus 로고    scopus 로고
    • Stat3 modulates heat shock 27 kDa protein expression in breast epithelial cells
    • Song, H.; Ethier, S.P.; Dziubinski, M.L.; Lin, J. Stat3 modulates heat shock 27 kDa protein expression in breast epithelial cells. Biochem. Biophys. Res. Commun. 2004, 314, 143-150.
    • (2004) Biochem. Biophys. Res. Commun , vol.314 , pp. 143-150
    • Song, H.1    Ethier, S.P.2    Dziubinski, M.L.3    Lin, J.4
  • 209
    • 7944233465 scopus 로고    scopus 로고
    • Role of STATs as downstream signal transducers in Src family kinase-mediated tumorigenesis
    • Silva, C.M. Role of STATs as downstream signal transducers in Src family kinase-mediated tumorigenesis. Oncogene 2004, 23, 8017-8023.
    • (2004) Oncogene , vol.23 , pp. 8017-8023
    • Silva, C.M.1
  • 210
    • 6344276574 scopus 로고    scopus 로고
    • Central role of the threonine residue within the p+1 loop of receptor tyrosine kinase in STAT3 constitutive phosphorylation in metastatic cancer cells
    • Yuan, Z.L.; Guan, Y.J.; Wang, L.; Wei, W.; Kane, A.B.; Chin, Y.E. Central role of the threonine residue within the p+1 loop of receptor tyrosine kinase in STAT3 constitutive phosphorylation in metastatic cancer cells. Mol. Cell Biol. 2004, 24, 9390-9400.
    • (2004) Mol. Cell Biol , vol.24 , pp. 9390-9400
    • Yuan, Z.L.1    Guan, Y.J.2    Wang, L.3    Wei, W.4    Kane, A.B.5    Chin, Y.E.6
  • 212
    • 84861567294 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription 3 (STAT3) protein suppresses adenoma-to-carcinoma transition in Apcmin/+ mice via regulation of Snail-1 (SNAI) protein stability
    • Lee, J.; Kim, J.C.; Lee, S.E.; Quinley, C.; Kim, H.; Herdman, S.; Corr, M.; Raz, E. Signal transducer and activator of transcription 3 (STAT3) protein suppresses adenoma-to-carcinoma transition in Apcmin/+ mice via regulation of Snail-1 (SNAI) protein stability. J. Biol. Chem. 2012, 287, 18182-18189.
    • (2012) J. Biol. Chem , vol.287 , pp. 18182-18189
    • Lee, J.1    Kim, J.C.2    Lee, S.E.3    Quinley, C.4    Kim, H.5    Herdman, S.6    Corr, M.7    Raz, E.8
  • 213
    • 79960036820 scopus 로고    scopus 로고
    • GATA transcription factors and cancer
    • Zheng, R.; Blobel, G.A. GATA transcription factors and cancer. Genes Cancer 2010, 1, 1178-1188.
    • (2010) Genes Cancer , vol.1 , pp. 1178-1188
    • Zheng, R.1    Blobel, G.A.2
  • 214
    • 14044259324 scopus 로고    scopus 로고
    • Substitution of the unique cysteine residue of murine hsp25 interferes with the protective activity of this stress protein through inhibition of dimer formation
    • Diaz-Latoud, C.; Buache, E.; Javouhey, E.; Arrigo, A.P. Substitution of the unique cysteine residue of murine hsp25 interferes with the protective activity of this stress protein through inhibition of dimer formation. Antioxid. Redox. Signal 2005, 7, 436-445.
    • (2005) Antioxid. Redox. Signal , vol.7 , pp. 436-445
    • Diaz-Latoud, C.1    Buache, E.2    Javouhey, E.3    Arrigo, A.P.4
  • 215
    • 40149107721 scopus 로고    scopus 로고
    • Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins
    • Ghosh, J.G.; Houck, S.A.; Clark, J.I. Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins. Int. J. Biochem. Cell Biol. 2008, 40, 954-967.
    • (2008) Int. J. Biochem. Cell Biol , vol.40 , pp. 954-967
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 216
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2
    • Colas, P.; Cohen, B.; Jessen, T.; Grishina, I.; McCoy, J.; Brent, R. Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2. Nature 1996, 380, 548-550.
    • (1996) Nature , vol.380 , pp. 548-550
    • Colas, P.1    Cohen, B.2    Jessen, T.3    Grishina, I.4    McCoy, J.5    Brent, R.6
  • 218
    • 34147125167 scopus 로고    scopus 로고
    • Selection and characterization of large collections of peptide aptamers through optimized yeast two-hybrid procedures
    • Bickle, M.B.; Dusserre, E.; Moncorge, O.; Bottin, H.; Colas, P. Selection and characterization of large collections of peptide aptamers through optimized yeast two-hybrid procedures. Nat. Protoc. 2006, 1, 1066-1091.
    • (2006) Nat. Protoc , vol.1 , pp. 1066-1091
    • Bickle, M.B.1    Dusserre, E.2    Moncorge, O.3    Bottin, H.4    Colas, P.5
  • 222
    • 34447621200 scopus 로고    scopus 로고
    • Small interference RNA targeting heat-shock protein 27 inhibits the growth of prostatic cell lines and induces apoptosis via caspase-3 activation in vitro
    • Rocchi, P.; Jugpal, P.; So, A.; Sinneman, S.; Ettinger, S.; Fazli, L.; Nelson, C.; Gleave, M. Small interference RNA targeting heat-shock protein 27 inhibits the growth of prostatic cell lines and induces apoptosis via caspase-3 activation in vitro. BJU Int. 2006, 28, 28.
    • (2006) BJU Int , vol.28 , pp. 28
    • Rocchi, P.1    Jugpal, P.2    So, A.3    Sinneman, S.4    Ettinger, S.5    Fazli, L.6    Nelson, C.7    Gleave, M.8
  • 224
    • 4043145061 scopus 로고    scopus 로고
    • Paclitaxel inhibits expression of heat shock protein 27 in ovarian and uterine cancer cells
    • Tanaka, Y.; Fujiwara, K.; Tanaka, H.; Maehata, K.; Kohno, I. Paclitaxel inhibits expression of heat shock protein 27 in ovarian and uterine cancer cells. Int. J. Gynecol. Cancer 2004, 14, 616-620.
    • (2004) Int. J. Gynecol. Cancer , vol.14 , pp. 616-620
    • Tanaka, Y.1    Fujiwara, K.2    Tanaka, H.3    Maehata, K.4    Kohno, I.5
  • 226
    • 48149108436 scopus 로고    scopus 로고
    • IFN-gamma down-regulates Hsp27 and enhances hyperthermia-induced tumor cell death in vitro and tumor suppression in vivo
    • Oba, M.; Yano, S.; Shuto, T.; Suico, M.A.; Eguma, A.; Kai, H. IFN-gamma down-regulates Hsp27 and enhances hyperthermia-induced tumor cell death in vitro and tumor suppression in vivo. Int. J. Oncol. 2008, 32, 1317-1324.
    • (2008) Int. J. Oncol , vol.32 , pp. 1317-1324
    • Oba, M.1    Yano, S.2    Shuto, T.3    Suico, M.A.4    Eguma, A.5    Kai, H.6
  • 228
    • 29244479188 scopus 로고    scopus 로고
    • Blocking tumor cell migration and invasion with biphenyl isoxazole derivative KRIBB3, a synthetic molecule that inhibits Hsp27 phosphorylation
    • Shin, K.D.; Lee, M.Y.; Shin, D.S.; Lee, S.; Son, K.H.; Koh, S.; Paik, Y.K.; Kwon, B.M.; Han, D.C. Blocking tumor cell migration and invasion with biphenyl isoxazole derivative KRIBB3, a synthetic molecule that inhibits Hsp27 phosphorylation. J. Biol. Chem. 2005, 280, 41439-41448.
    • (2005) J. Biol. Chem , vol.280 , pp. 41439-41448
    • Shin, K.D.1    Lee, M.Y.2    Shin, D.S.3    Lee, S.4    Son, K.H.5    Koh, S.6    Paik, Y.K.7    Kwon, B.M.8    Han, D.C.9
  • 229
    • 80054720155 scopus 로고    scopus 로고
    • RP101 (brivudine) binds to heat shock protein HSP27 (HSPB1) and enhances survival in animals and pancreatic cancer patients
    • Heinrich, J.C.; 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, 1349-1361.
    • (2011) J. Cancer Res. Clin. Oncol , vol.137 , pp. 1349-1361
    • Heinrich, J.C.1    Tuukkanen, A.2    Schroeder, M.3    Fahrig, T.4    Fahrig, R.5
  • 230
    • 84893962067 scopus 로고    scopus 로고
    • Available online, Accessed on 16 November
    • Resprotect-Prevention of Chemoresistance. Available online: http://www.resprotect.de/Pipeline-Summary/Pipeline-Summary.html/ (Accessed on 16 November 2013).
    • (2013) Resprotect-Prevention of Chemoresistance
  • 231
    • 84865745518 scopus 로고    scopus 로고
    • A chemical proteomics approach reveals Hsp27 as a target for proapoptotic clerodane diterpenes
    • Faiella, L.; Piaz, F.D.; Bisio, A.; Tosco, A.; de Tommasi, N. A chemical proteomics approach reveals Hsp27 as a target for proapoptotic clerodane diterpenes. Mol. Biosyst. 2012, 8, 2637-2644.
    • (2012) Mol. Biosyst , vol.8 , pp. 2637-2644
    • Faiella, L.1    Piaz, F.D.2    Bisio, A.3    Tosco, A.4    de Tommasi, N.5
  • 232
    • 34548067977 scopus 로고    scopus 로고
    • Residue R120 is essential for the quaternary structure and functional integrity of human alphaB-crystallin
    • Simon, S.; Michiel, M.; Skouri-Panet, F.; Lechaire, J.P.; Vicart, P.; Tardieu, A. Residue R120 is essential for the quaternary structure and functional integrity of human alphaB-crystallin. Biochemistry 2007, 46, 9605-9614
    • (2007) Biochemistry , vol.46 , pp. 9605-9614
    • Simon, S.1    Michiel, M.2    Skouri-Panet, F.3    Lechaire, J.P.4    Vicart, P.5    Tardieu, A.6
  • 234
    • 80054747192 scopus 로고    scopus 로고
    • Large potentials of small heat shock proteins
    • Mymrikov, E.V.; Seit-Nebi, A.S.; Gusev, N.B. Large potentials of small heat shock proteins. Physiol. Rev. 2011, 91, 1123-1159.
    • (2011) Physiol. Rev , vol.91 , pp. 1123-1159
    • Mymrikov, E.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 235
    • 84867138177 scopus 로고    scopus 로고
    • The Wnt/beta-catenin pathway cross-talks with STAT3 signaling to regulate survival of retinal pigment epithelium cells
    • Fragoso, M.A.; Patel, A.K.; Nakamura, R.E.; Yi, H.; Surapaneni, K.; Hackam, A.S. The Wnt/beta-catenin pathway cross-talks with STAT3 signaling to regulate survival of retinal pigment epithelium cells. PLoS One 2012, 7, e46892.
    • (2012) PLoS One , vol.7
    • Fragoso, M.A.1    Patel, A.K.2    Nakamura, R.E.3    Yi, H.4    Surapaneni, K.5    Hackam, A.S.6
  • 236
    • 0026632361 scopus 로고
    • Heat shock protein 27 and αB-cristallin can form a complex, which dissociates by heat shock
    • Zantema, A.; Vries, M.V.-D.; Maasdam, D.; Bol, S.; Eb, A.V.D. Heat shock protein 27 and αB-cristallin can form a complex, which dissociates by heat shock. J. Biol. Chem. 1992, 267, 12936-12941.
    • (1992) J. Biol. Chem , vol.267 , pp. 12936-12941
    • Zantema, A.1    Vries, M.V.-D.2    Maasdam, D.3    Bol, S.4    Eb, A.V.D.5
  • 237
    • 84862848512 scopus 로고    scopus 로고
    • Heterooligomeric complexes of human small heat shock proteins
    • Mymrikov, E.V.; Seit-Nebi, A.S.; Gusev, N.B. Heterooligomeric complexes of human small heat shock proteins. Cell Stress Chaperones 2012, 17, 157-169.
    • (2012) Cell Stress Chaperones , vol.17 , pp. 157-169
    • Mymrikov, E.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3


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