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Volumn 9, Issue 1, 2014, Pages

Transcription regulation of HYPK by heat shock factor 1

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK TRANSCRIPTION FACTOR 1; HISTONE H4; RNA POLYMERASE II;

EID: 84908083066     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0085552     Document Type: Article
Times cited : (15)

References (60)
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 3
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • Akerfelt M, Morimoto RI, Sistonen L (2010) Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 11: 545-555.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 4
    • 79251582523 scopus 로고    scopus 로고
    • Whole-genome analysis reveals that active heat shock factor binding sites are mostly associated with non-heat shock genes in Drosophila melanogaster
    • Gonsalves SE, Moses AM, Razak Z, Robert F, Westwood JT (2011) Whole-genome analysis reveals that active heat shock factor binding sites are mostly associated with non-heat shock genes in Drosophila melanogaster. PLoS One 6: e15934.
    • (2011) PLoS One , vol.6
    • Gonsalves, S.E.1    Moses, A.M.2    Razak, Z.3    Robert, F.4    Westwood, J.T.5
  • 5
    • 1542373742 scopus 로고    scopus 로고
    • The Role of Heat Shock Transcription Factor 1 in the Genome-wide Regulation of the Mammalian Heat Shock Response
    • DOI 10.1091/mbc.E03-10-0738
    • Trinklein ND, Murray JI, Hartman SJ, Botstein D, Myers RM (2004) The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol Biol Cell 15: 1254-1261. (Pubitemid 38316232)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 6
    • 2942598422 scopus 로고    scopus 로고
    • Genome-wide analysis of the biology of stress responses through heat shock transcription factor
    • DOI 10.1128/MCB.24.12.5249-5256.2004
    • Hahn JS, Hu Z, Thiele DJ, Iyer VR (2004) Genome-wide analysis of the biology of stress responses through heat shock transcription factor. Mol Cell Biol 24: 5249-5256. (Pubitemid 38738160)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.12 , pp. 5249-5256
    • Hahn, J.-S.1    Hu, Z.2    Thiele, D.J.3    Iyer, V.R.4
  • 7
    • 33751092252 scopus 로고    scopus 로고
    • Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival
    • DOI 10.1039/b606129j
    • Page TJ, Sikder D, Yang L, Pluta L, Wolfinger RD, et al. (2006) Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival. Mol Biosyst 2: 627-639. (Pubitemid 44772306)
    • (2006) Molecular BioSystems , vol.2 , Issue.12 , pp. 627-639
    • Page, T.J.1    Sikder, D.2    Yang, L.3    Pluta, L.4    Wolfinger, R.D.5    Kodadek, T.6    Thomas, R.S.7
  • 8
    • 84864585171 scopus 로고    scopus 로고
    • HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers
    • Mendillo ML, Santagata S, Koeva M, Bell GW, Hu R, et al. (2012) HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers. Cell 150: 549-562.
    • (2012) Cell , vol.150 , pp. 549-562
    • Mendillo, M.L.1    Santagata, S.2    Koeva, M.3    Bell, G.W.4    Hu, R.5
  • 9
    • 84934443868 scopus 로고    scopus 로고
    • Heat shock factor 1 as a coordinator of stress and developmental pathways
    • Anckar J, Sistonen L (2007) Heat shock factor 1 as a coordinator of stress and developmental pathways. Adv Exp Med Biol 594: 78-88.
    • (2007) Adv Exp Med Biol , vol.594 , pp. 78-88
    • Anckar, J.1    Sistonen, L.2
  • 10
    • 0027960541 scopus 로고
    • Selection of new HSF1 and HSF2 DNA-binding sites reveals differences in trimer cooperativity
    • Kroeger PE, Morimoto RI (1994) Selection of new HSF1 and HSF2 DNA-binding sites reveals difference in trimer cooperativity. Mol Cell Biol 14: 7592-7603. (Pubitemid 24326425)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.11 , pp. 7592-7603
    • Kroeger, P.E.1    Morimoto, R.I.2
  • 11
    • 0028137261 scopus 로고
    • Cooperative interaction of human HSF1 heat shock transcription factor with promoter DNA
    • Wang Y, Morgan WD (1994) Cooperative interaction of human HSF1 heat shock transcription factor with promoter DNA. Nucleic Acids Res 22: 3113-3118. (Pubitemid 24260643)
    • (1994) Nucleic Acids Research , vol.22 , Issue.15 , pp. 3113-3118
    • Wang, Y.1    Morgan, W.D.2
  • 12
    • 0020827719 scopus 로고
    • The dnaK protein modulates the heat-shock response of Escherichia coli
    • Tilly K, McKittrick N, Zylicz M, Georgopoulos C (1983) The dnaK protein modulates the heat-shock response of Escherichia coli. Cell 34: 641-646.
    • (1983) Cell , vol.34 , pp. 641-646
    • Tilly, K.1    McKittrick, N.2    Zylicz, M.3    Georgopoulos, C.4
  • 13
    • 0025632973 scopus 로고
    • DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma32
    • Straus D, Walter W, Gross CA (1990) DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32. Genes Dev 4: 2202-2209. (Pubitemid 120034525)
    • (1990) Genes and Development , vol.4 , Issue.12 , pp. 2202-2209
    • Straus, D.1    Walter, W.2    Gross, C.A.3
  • 14
    • 0029095916 scopus 로고
    • A heat shock transcription factor with reduced activity suppresses a yeast HSP70 mutant
    • Halladay JT, Craig EA (1995) A heat shock transcription factor with reduced activity suppresses a yeast HSP70 mutant. Mol Cell Biol 15: 4890-4897.
    • (1995) Mol Cell Biol , vol.15 , pp. 4890-4897
    • Halladay, J.T.1    Craig, E.A.2
  • 15
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi Y, Mosser DD, Morimoto RI (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev 12: 654-666. (Pubitemid 28134298)
    • (1998) Genes and Development , vol.12 , Issue.5 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 16
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor
    • Baler R, Welch WJ, Voellmy R (1992) Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor. J Cell Biol 117: 1151-1159.
    • (1992) J Cell Biol , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.J.2    Voellmy, R.3
  • 17
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94: 471-480. (Pubitemid 28391863)
    • (1998) Cell , vol.94 , Issue.4 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 18
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya K, Myers MP, Murphy SP, Morimoto RI (1992) The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev 6: 1153-1164.
    • (1992) Genes Dev , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 19
    • 3542991477 scopus 로고    scopus 로고
    • On mechanisms that control heat shock transcription factor activity in metazoan cells
    • Voellmy R (2004) On mechanisms that control heat shock transcription factor activity in metazoan cells. Cell Stress Chaperones 9: 122-133.
    • (2004) Cell Stress Chaperones , vol.9 , pp. 122-133
    • Voellmy, R.1
  • 21
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • Jana NR, Tanaka M, Wang G, Nukina N (2000) Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum Mol Genet 9: 2009-2018. (Pubitemid 30642666)
    • (2000) Human Molecular Genetics , vol.9 , Issue.13 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.-H.3    Nukina, N.4
  • 22
    • 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 AP, et al. (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 11: 1137-1151. (Pubitemid 34521094)
    • (2002) Human Molecular Genetics , vol.11 , Issue.9 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.-P.5    Rubinsztein, D.C.6
  • 23
    • 77949884097 scopus 로고    scopus 로고
    • Induction of molecular chaperones as a therapeutic strategy for the polyglutamine diseases
    • Nagai Y, Fujikake N, Popiel HA, Wada K (2010) Induction of molecular chaperones as a therapeutic strategy for the polyglutamine diseases. Curr Pharm Biotechnol 11: 188-197.
    • (2010) Curr Pharm Biotechnol , vol.11 , pp. 188-197
    • Nagai, Y.1    Fujikake, N.2    Popiel, H.A.3    Wada, K.4
  • 24
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake N, Nagai Y, Popiel HA, Okamoto Y, Yamaguchi M, et al. (2008) Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J Biol Chem 283: 26188-26197.
    • (2008) J Biol Chem , vol.283 , pp. 26188-26197
    • Fujikake, N.1    Nagai, Y.2    Popiel, H.A.3    Okamoto, Y.4    Yamaguchi, M.5
  • 27
    • 37849012236 scopus 로고    scopus 로고
    • HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity
    • Raychaudhuri S, Sinha M, Mukhopadhyay D, Bhattacharyya NP (2008) HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity. Hum Mol Genet 17: 240-255.
    • (2008) Hum Mol Genet , vol.17 , pp. 240-255
    • Raychaudhuri, S.1    Sinha, M.2    Mukhopadhyay, D.3    Bhattacharyya, N.P.4
  • 29
    • 77950667600 scopus 로고    scopus 로고
    • The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation
    • Arnesen T, Starheim KK, Van Damme P, Evjenth R, Dinh H, et al. (2010) The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation. Mol Cell Biol 30: 1898-1909.
    • (2010) Mol Cell Biol , vol.30 , pp. 1898-1909
    • Arnesen, T.1    Starheim, K.K.2    Van Damme, P.3    Evjenth, R.4    Dinh, H.5
  • 30
    • 84870862685 scopus 로고    scopus 로고
    • Identification of HYPK-interacting proteins reveals involvement of HYPK in regulating cell growth, cell cycle, unfolded protein response and cell death
    • Choudhury KR, Raychaudhuri S, Bhattacharyya NP (2012) Identification of HYPK-interacting proteins reveals involvement of HYPK in regulating cell growth, cell cycle, unfolded protein response and cell death. PLoS One 7: e51415.
    • (2012) PLoS One , vol.7
    • Choudhury, K.R.1    Raychaudhuri, S.2    Bhattacharyya, N.P.3
  • 31
    • 78751505781 scopus 로고    scopus 로고
    • KRIBB11 inhibits HSP70 synthesis through inhibition of heat shock factor 1 function by impairing the recruitment of positive transcription elongation factor b to the hsp70 promoter
    • Yoon YJ, Kim JA, Shin KD, Shin DS, Han YM, et al. (2011) KRIBB11 inhibits HSP70 synthesis through inhibition of heat shock factor 1 function by impairing the recruitment of positive transcription elongation factor b to the hsp70 promoter. J Biol Chem 286: 1737-1747.
    • (2011) J Biol Chem , vol.286 , pp. 1737-1747
    • Yoon, Y.J.1    Kim, J.A.2    Shin, K.D.3    Shin, D.S.4    Han, Y.M.5
  • 32
    • 80053188620 scopus 로고    scopus 로고
    • Regulation of RE1 protein silencing transcription factor (REST) expression by HIP1 protein interactor (HIPPI)
    • Datta M, Bhattacharyya NP (2011) Regulation of RE1 protein silencing transcription factor (REST) expression by HIP1 protein interactor (HIPPI). J Biol Chem 286: 33759-33769.
    • (2011) J Biol Chem , vol.286 , pp. 33759-33769
    • Datta, M.1    Bhattacharyya, N.P.2
  • 33
    • 34147149523 scopus 로고    scopus 로고
    • Heat Shock Factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1
    • DOI 10.1074/jbc.M607556200
    • Ostling P, Bjork JK, Roos-Mattjus P, Mezger V, Sistonen L (2007) Heat shock factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1. J Biol Chem 282: 7077-7086. (Pubitemid 47093630)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7077-7086
    • Ostling, P.1    Bjork, J.K.2    Roos-Mattjus, P.3    Mezger, V.4    Sistonen, L.5
  • 34
    • 84856722935 scopus 로고    scopus 로고
    • Regulation of cyclooxygenase-2 expression by heat: A novel aspect of heat shock factor 1 function in human cells
    • Rossi A, Coccia M, Trotta E, Angelini M, Santoro MG (2012) Regulation of cyclooxygenase-2 expression by heat: a novel aspect of heat shock factor 1 function in human cells. PLoS One 7: e31304.
    • (2012) PLoS One , vol.7
    • Rossi, A.1    Coccia, M.2    Trotta, E.3    Angelini, M.4    Santoro, M.G.5
  • 35
    • 78049440475 scopus 로고    scopus 로고
    • Chromatin landscape dictates HSF binding to target DNA elements
    • Guertin MJ, Lis JT (2010) Chromatin landscape dictates HSF binding to target DNA elements. PLoS Genet 6.
    • (2010) PLoS Genet , vol.6
    • Guertin, M.J.1    Lis, J.T.2
  • 36
    • 11844298901 scopus 로고    scopus 로고
    • Transcriptional regulation of the metazoan stress protein response
    • Voellmy R (2004) Transcriptional regulation of the metazoan stress protein response. Prog Nucleic Acid Res Mol Biol 78: 143-185.
    • (2004) Prog Nucleic Acid Res Mol Biol , vol.78 , pp. 143-185
    • Voellmy, R.1
  • 37
    • 0028150986 scopus 로고
    • Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure
    • Zuo J, Baler R, Dahl G, Voellmy R (1994) Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Mol Cell Biol 14: 7557-7568.
    • (1994) Mol Cell Biol , vol.14 , pp. 7557-7568
    • Zuo, J.1    Baler, R.2    Dahl, G.3    Voellmy, R.4
  • 39
    • 0029055176 scopus 로고
    • Multiple layers of regulation of human heat shock transcription factor 1
    • Zuo J, Rungger D, Voellmy R (1995) Multiple layers of regulation of human heat shock transcription factor 1. Mol Cell Biol 15: 4319-4330.
    • (1995) Mol Cell Biol , vol.15 , pp. 4319-4330
    • Zuo, J.1    Rungger, D.2    Voellmy, R.3
  • 40
    • 0024999067 scopus 로고
    • Activation of the heat shock transcription factor by hypoxia in mammalian cells
    • Benjamin IJ, Kroger B, Williams RS (1990) Activation of the heat shock transcription factor by hypoxia in mammalian cells. Proc Natl Acad Sci U S A 87: 6263-6267.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 6263-6267
    • Benjamin, I.J.1    Kroger, B.2    Williams, R.S.3
  • 41
    • 33845972658 scopus 로고    scopus 로고
    • Induction of the heat shock pathway during hypoxia requires regulation of heat shock factor by hypoxia-inducible factor-1
    • DOI 10.1074/jbc.M608013200
    • Baird NA, Turnbull DW, Johnson EA (2006) Induction of the heat shock pathway during hypoxia requires regulation of heat shock factor by hypoxia-inducible factor-1. J Biol Chem 281: 38675-38681. (Pubitemid 46041993)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.50 , pp. 38675-38681
    • Baird, N.A.1    Turnbull, D.W.2    Johnson, E.A.3
  • 42
    • 0029103274 scopus 로고
    • Hypoxia regulates vascular endothelial growth factor gene expression in endothelial cells. Identification of a 59 enhancer
    • Liu Y, Cox SR, Morita T, Kourembanas S (1995) Hypoxia regulates vascular endothelial growth factor gene expression in endothelial cells. Identification of a 59 enhancer. Circ Res 77: 638-643.
    • (1995) Circ Res , vol.77 , pp. 638-643
    • Liu, Y.1    Cox, S.R.2    Morita, T.3    Kourembanas, S.4
  • 43
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • DOI 10.1074/jbc.272.14.9086
    • Bush KT, Goldberg AL, Nigam SK (1997) Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J Biol Chem 272: 9086-9092. (Pubitemid 27154911)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 44
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • DOI 10.1016/S0092-8674(94)90462-6
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, et al. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78: 761-771. (Pubitemid 24294452)
    • (1994) Cell , vol.78 , Issue.5 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 45
    • 0020130877 scopus 로고
    • Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts
    • Li GC, Werb Z (1982) Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts. Proc Natl Acad Sci U S A 79: 3218-3222.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 3218-3222
    • Li, G.C.1    Werb, Z.2
  • 46
    • 0030724378 scopus 로고    scopus 로고
    • Heat shock proteins and heat adaptation of the whole organism
    • Moseley PL (1997) Heat shock proteins and heat adaptation of the whole organism. J Appl Physiol 83: 1413-1417.
    • (1997) J Appl Physiol , vol.83 , pp. 1413-1417
    • Moseley, P.L.1
  • 47
    • 79954572267 scopus 로고    scopus 로고
    • Heat perception and signalling in plants: A tortuous path to thermotolerance
    • Saidi Y, Finka A, Goloubinoff P (2011) Heat perception and signalling in plants: a tortuous path to thermotolerance. New Phytol 190: 556-565.
    • (2011) New Phytol , vol.190 , pp. 556-565
    • Saidi, Y.1    Finka, A.2    Goloubinoff, P.3
  • 48
    • 84866083679 scopus 로고    scopus 로고
    • Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions
    • Reidy M, Miot M, Masison DC (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192: 185-193.
    • (2012) Genetics , vol.192 , pp. 185-193
    • Reidy, M.1    Miot, M.2    Masison, D.C.3
  • 50
    • 0022327491 scopus 로고
    • Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein
    • Lewis MJ, Pelham HR (1985) Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein. EMBO J 4: 3137-3143.
    • (1985) EMBO J , vol.4 , pp. 3137-3143
    • Lewis, M.J.1    Pelham, H.R.2
  • 51
    • 0024345716 scopus 로고
    • Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells
    • Landry J, Chretien P, Lambert H, Hickey E, Weber LA (1989) Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells. J Cell Biol 109: 7-15. (Pubitemid 19180115)
    • (1989) Journal of Cell Biology , vol.109 , Issue.1 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, H.3    Hickey, E.4    Weber, L.A.5
  • 52
    • 0034653824 scopus 로고    scopus 로고
    • Overexpression of the 27 KDa heat shock protein is associated with thermoresistance and chemoresistance but not with radioresistance
    • DOI 10.1016/S0360-3016(99)00410-1, PII S0360301699004101
    • Fortin A, Raybaud-Diogene H, Tetu B, Deschenes R, Huot J, et al. (2000) Overexpression of the 27 KDa heat shock protein is associated with thermoresistance and chemoresistance but not with radioresistance. Int J Radiat Oncol Biol Phys 46: 1259-1266. (Pubitemid 30139438)
    • (2000) International Journal of Radiation Oncology Biology Physics , vol.46 , Issue.5 , pp. 1259-1266
    • Fortin, A.1    Raybaud-Diogene, H.2    Tetu, B.3    Huot, J.4    Landry, J.5    Deschenes, M.R.6
  • 53
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis
    • DOI 10.1074/jbc.273.13.7523
    • McMillan DR, Xiao X, Shao L, Graves K, Benjamin IJ (1998) Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis. J Biol Chem 273: 7523-7528. (Pubitemid 28152777)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.13 , pp. 7523-7528
    • McMillan, D.R.1    Xiao, X.2    Shao, L.3    Graves, K.4    Benjamin, I.J.5
  • 54
    • 4444257379 scopus 로고    scopus 로고
    • The biology of hypoxia: The role of oxygen sensing in development, normal function, and disease
    • DOI 10.1101/gad.1243304
    • Giaccia AJ, Simon MC, Johnson R (2004) The biology of hypoxia: the role of oxygen sensing in development, normal function, and disease. Genes Dev 18: 2183-2194. (Pubitemid 39209567)
    • (2004) Genes and Development , vol.18 , Issue.18 , pp. 2183-2194
    • Giaccia, A.J.1    Simon, M.C.2    Johnson, R.3
  • 55
    • 20144362749 scopus 로고    scopus 로고
    • Roles of the HIF-1 hypoxia-inducible factor during hypoxia response in Caenorhabditis elegans
    • DOI 10.1074/jbc.M501894200
    • Shen C, Nettleton D, Jiang M, Kim SK, Powell-Coffman JA (2005) Roles of the HIF-1 hypoxia-inducible factor during hypoxia response in Caenorhabditis elegans. J Biol Chem 280: 20580-20588. (Pubitemid 40776760)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20580-20588
    • Shen, C.1    Nettleton, D.2    Jiang, M.3    Kim, S.K.4    Powell-Coffman, J.A.5
  • 56
    • 84872693386 scopus 로고    scopus 로고
    • Hypoxia-inducible Factor-1 (HIF-1)-independent hypoxia response of the small heat shock protein hsp-16.1 gene regulated by chromatin-remodeling factors in the nematode Caenorhabditis elegans
    • Lee J, Lee J (2013) Hypoxia-inducible Factor-1 (HIF-1)-independent hypoxia response of the small heat shock protein hsp-16.1 gene regulated by chromatin-remodeling factors in the nematode Caenorhabditis elegans. J Biol Chem 288: 1582-1589.
    • (2013) J Biol Chem , vol.288 , pp. 1582-1589
    • Lee, J.1    Lee, J.2
  • 57
    • 28244466794 scopus 로고    scopus 로고
    • Induction of the hypoxia-inducible factor system by low levels of heat shock protein 90 inhibitors
    • DOI 10.1158/0008-5472.CAN-05-1877
    • Ibrahim NO, Hahn T, Franke C, Stiehl DP, Wirthner R, et al. (2005) Induction of the hypoxia-inducible factor system by low levels of heat shock protein 90 inhibitors. Cancer Res 65: 11094-11100. (Pubitemid 41713380)
    • (2005) Cancer Research , vol.65 , Issue.23 , pp. 11094-11100
    • Ibrahim, N.O.1    Hahn, T.2    Franke, C.3    Stiehl, D.P.4    Wirthner, R.5    Wenger, R.H.6    Katschinski, D.M.7
  • 58
    • 0035824621 scopus 로고    scopus 로고
    • Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
    • Guo Y, Guettouche T, Fenna M, Boellmann F, Pratt WB, et al. (2001) Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J Biol Chem 276: 45791-45799.
    • (2001) J Biol Chem , vol.276 , pp. 45791-45799
    • Guo, Y.1    Guettouche, T.2    Fenna, M.3    Boellmann, F.4    Pratt, W.B.5
  • 59
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI (1998) Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 12: 3788-3796.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1


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