메뉴 건너뛰기




Volumn 7, Issue 4-6, 1999, Pages 271-282

Heat shock factor function and regulation in response to cellular stress, growth, and differentiation signals

Author keywords

Cell cycle; Growth signals; Heat shock; HSF; Hsp; Stress

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90;

EID: 0032780311     PISSN: 10522166     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (117)

References (92)
  • 1
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya, K.; Myers, M. P.; Murphy, S. P.; Morimoto, R. I. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev. 6:1153-1164; 1992.
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 2
    • 0031866191 scopus 로고    scopus 로고
    • HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes
    • Ali, A.; Bharadwaj, S.; O'Carroll, R.; Ovsenek, N. HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes. Mol. Cell. Biol. 18: 4949-4960; 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4949-4960
    • Ali, A.1    Bharadwaj, S.2    O'Carroll, R.3    Ovsenek, N.4
  • 3
    • 0028589101 scopus 로고
    • A role for Hsp90 in cell cycle control: Weel tyrosine kinase activity requires interaction with Hsp90
    • Aligue, R.; Akhavan-Niak, H.; Russell, P. A role for Hsp90 in cell cycle control: Weel tyrosine kinase activity requires interaction with Hsp90. EMBO J. 13: 6099-6106; 1994.
    • (1994) EMBO J. , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-Niak, H.2    Russell, P.3
  • 5
    • 0023959196 scopus 로고
    • A novel hsp70-like protein (P70) is present in mouse spermatogenic cells
    • Allen, R. L.; O'Brien, D. A.; Eddy, E. M. A novel hsp70-like protein (P70) is present in mouse spermatogenic cells. Mol. Cell. Biol. 8:828-832; 1988.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 828-832
    • Allen, R.L.1    O'Brien, D.A.2    Eddy, E.M.3
  • 6
    • 0030112452 scopus 로고    scopus 로고
    • Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells
    • Baler, R.; Zou, J.; Voellmy, R. Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1:33-39; 1996.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 33-39
    • Baler, R.1    Zou, J.2    Voellmy, R.3
  • 7
    • 0026688162 scopus 로고
    • Apoptotic cell death induced by c-myc is inhibited by bcl-2
    • Bissonnette, R. P.; Echeverri, F.; Mahboubi, A.; Green, D. R. Apoptotic cell death induced by c-myc is inhibited by bcl-2. Nature 359:552-554; 1992.
    • (1992) Nature , vol.359 , pp. 552-554
    • Bissonnette, R.P.1    Echeverri, F.2    Mahboubi, A.3    Green, D.R.4
  • 8
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny, M. V.; Toretsky, J.; Bohen, S.; Neckers, L. Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc. Natl. Acad. Sci. USA 93:8379-8383; 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 9
    • 0031868061 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins
    • Bohen, S. P. Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins. Mol. Cell. Biol. 18: 3330-3339; 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3330-3339
    • Bohen, S.P.1
  • 10
    • 0031427558 scopus 로고    scopus 로고
    • Potential role of heat shock transcription factor in the expression of inflammatory cytokines
    • Cahill, C. M.; Lin, H. S.; Price, B. D.; Brace, J. L.; Calderwood, S. K. Potential role of heat shock transcription factor in the expression of inflammatory cytokines. Adv. Exp. Med. Biol. 4008:625-630; 1997.
    • (1997) Adv. Exp. Med. Biol. , vol.4008 , pp. 625-630
    • Cahill, C.M.1    Lin, H.S.2    Price, B.D.3    Brace, J.L.4    Calderwood, S.K.5
  • 11
    • 0029763452 scopus 로고    scopus 로고
    • Transcriptional repression of the prointerleukin 1β gene by heat shock factor 1
    • Cahill, C. M; Waterman, W. R.; Xie, Y.; Auron, P. E.; Calderwood, S. K. Transcriptional repression of the prointerleukin 1β gene by heat shock factor 1. J. Biol. Chem. 271:24874-24879; 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24874-24879
    • Cahill, C.M.1    Waterman, W.R.2    Xie, Y.3    Auron, P.E.4    Calderwood, S.K.5
  • 12
    • 0027985148 scopus 로고
    • Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae
    • Chang, H. C.; Lindquist, S. Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae. J. Biol. Chem. 269:24983-24988; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24983-24988
    • Chang, H.C.1    Lindquist, S.2
  • 13
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the Hsp90 cochaperone Stil (p60)
    • Chang, H. C.; Nathan, D. F.; Lindquist, S. In vivo analysis of the Hsp90 cochaperone Stil (p60). Mol. Cell. Biol. 17:318-325; 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 318-325
    • Chang, H.C.1    Nathan, D.F.2    Lindquist, S.3
  • 14
    • 0030777357 scopus 로고    scopus 로고
    • Heat shock factor 1 represses Rasinduced transcriptional activation of the c-fos gene
    • Chen, C.; Xie, Y.; Stevenson, M. A.; Auron, P. E.; Calderwood, S. K. Heat shock factor 1 represses Rasinduced transcriptional activation of the c-fos gene. J. Biol. Chem. 272:26803-26806; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26803-26806
    • Chen, C.1    Xie, Y.2    Stevenson, M.A.3    Auron, P.E.4    Calderwood, S.K.5
  • 15
    • 0029846433 scopus 로고    scopus 로고
    • Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1
    • Chu, B.; Soncin, F.; Price, B. D.; Stevenson, M. A.; Calderwood, S. K. Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1. J. Biol. Chem. 271:30847-30857; 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30847-30857
    • Chu, B.1    Soncin, F.2    Price, B.D.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 16
    • 0032541032 scopus 로고    scopus 로고
    • Transcriptional activity of heat shock factor 1 at 37 degrees C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases Cα and Cζ
    • Chu, B.; Zhong, R.; Soncin, F.; Stevenson, M. A.; Calderwood, S. K. Transcriptional activity of heat shock factor 1 at 37 degrees C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases Cα and Cζ. J. Biol. Chem. 273:18640-18646; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18640-18646
    • Chu, B.1    Zhong, R.2    Soncin, F.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 17
    • 0031750178 scopus 로고    scopus 로고
    • Antibodies to heat-shock protein 27 are associated with improved survival in patients with breast cancer
    • Conroy, S. E.; Sasieni, P. D.; Amin, V.; Wang, D. Y.; Smith, P.; Fentiman, I. S.; Latchman, D. S. Antibodies to heat-shock protein 27 are associated with improved survival in patients with breast cancer. Br. J. Cancer 77:1875-1879; 1998.
    • (1998) Br. J. Cancer , vol.77 , pp. 1875-1879
    • Conroy, S.E.1    Sasieni, P.D.2    Amin, V.3    Wang, D.Y.4    Smith, P.5    Fentiman, I.S.6    Latchman, D.S.7
  • 18
    • 0032058966 scopus 로고    scopus 로고
    • Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients
    • Conroy, S. E.; Sasieni, P. D.; Fentiman, I.; Latchman, D. S. Autoantibodies to the 90kDa heat shock protein and poor survival in breast cancer patients. Eur. J. Cancer 34:942-943; 1998.
    • (1998) Eur. J. Cancer , vol.34 , pp. 942-943
    • Conroy, S.E.1    Sasieni, P.D.2    Fentiman, I.3    Latchman, D.S.4
  • 19
    • 0025967766 scopus 로고
    • Is hsp70 the cellular thermometer? Trends Biochem
    • Craig, E. A.; Gross, C. A. Is hsp70 the cellular thermometer? Trends Biochem. Sci. 16:135-140; 1991.
    • (1991) Sci. , vol.16 , pp. 135-140
    • Craig, E.A.1    Gross, C.A.2
  • 22
    • 0029879539 scopus 로고    scopus 로고
    • Developmentally regulated expression of Hsp70-2 and a Hsp70-2/lacZ transgene during spermatogenesis
    • Dix, D. J.; Rosario-Herrle, M.; Gotoh, H.; Mori, C.; Goulding, E. H.; Barren, C. V.; Eddy, E. M. Developmentally regulated expression of Hsp70-2 and a Hsp70-2/lacZ transgene during spermatogenesis. Dev. Biol. 174:310-321; 1996.
    • (1996) Dev. Biol. , vol.174 , pp. 310-321
    • Dix, D.J.1    Rosario-Herrle, M.2    Gotoh, H.3    Mori, C.4    Goulding, E.H.5    Barren, C.V.6    Eddy, E.M.7
  • 23
    • 0029807530 scopus 로고    scopus 로고
    • A cyclophilin function in Hsp90-dependent signal transduction
    • Duina, A. A.; Chang, H. C.; Marsh, J. A.; Lindquist, S.; Gaber, R. F. A cyclophilin function in Hsp90-dependent signal transduction. Science 274:1713-1715; 1996.
    • (1996) Science , vol.274 , pp. 1713-1715
    • Duina, A.A.1    Chang, H.C.2    Marsh, J.A.3    Lindquist, S.4    Gaber, R.F.5
  • 24
    • 0032563195 scopus 로고    scopus 로고
    • Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response
    • Duina, A. A.; Kalton, H. M.; Gaber, R. F. Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J. Biol. Chem. 273:18974-18978; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18974-18978
    • Duina, A.A.1    Kalton, H.M.2    Gaber, R.F.3
  • 26
    • 0028813131 scopus 로고
    • An efficient method to isolate yeast genes causing overexpression-mediated growth arrest
    • Espinet, C.; de la Torre, M. A.; Aldea, M.; Herrero, E. An efficient method to isolate yeast genes causing overexpression-mediated growth arrest. Yeast 11:25-32; 1995.
    • (1995) Yeast , vol.11 , pp. 25-32
    • Espinet, C.1    De La Torre, M.A.2    Aldea, M.3    Herrero, E.4
  • 27
    • 0031832233 scopus 로고    scopus 로고
    • SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins
    • Fang, Y.; Fliss, A. E.; Rao, J.; Caplan, A. J. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol. Cell. Biol. 18:3727-3734; 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3727-3734
    • Fang, Y.1    Fliss, A.E.2    Rao, J.3    Caplan, A.J.4
  • 28
    • 0026645957 scopus 로고
    • The consequences of expressing hsp70 in Drosophila cells at normal temperatures
    • Feder, J. H.; Rossi, J. M.; Solomon, J.; Solomon, N.; Lindquist, S. The consequences of expressing hsp70 in Drosophila cells at normal temperatures. Genes Dev. 6:1402-1413; 1992.
    • (1992) Genes Dev. , vol.6 , pp. 1402-1413
    • Feder, J.H.1    Rossi, J.M.2    Solomon, J.3    Solomon, N.4    Lindquist, S.5
  • 30
    • 0027439593 scopus 로고
    • Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe
    • Gallo, G. J.; Prentice, H.; Kingston, R. E. Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe. Mol. Cell. Biol. 13:749-761; 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 749-761
    • Gallo, G.J.1    Prentice, H.2    Kingston, R.E.3
  • 32
    • 0026844368 scopus 로고
    • Myb: A transcriptional activator linking proliferation and differentiation in hematopoietic cells
    • Graf, T. Myb: A transcriptional activator linking proliferation and differentiation in hematopoietic cells. Curr. Opin. Genet. Dev. 2:249-255; 1992.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 249-255
    • Graf, T.1
  • 33
    • 0031742046 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3β and extracellular signal-regulated kinase inactivate heat shock transcription factor 1 by facilitating the disappearance of transcriptionally active granules after heat shock
    • He, B.; Meng, Y. H.; Mivechi, N. F. Glycogen synthase kinase 3β and extracellular signal-regulated kinase inactivate heat shock transcription factor 1 by facilitating the disappearance of transcriptionally active granules after heat shock. Mol. Cell. Biol. 18:6624-6633; 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6624-6633
    • He, B.1    Meng, Y.H.2    Mivechi, N.F.3
  • 34
    • 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. 51:5245-5252; 1991.
    • (1991) Cancer Res. , vol.51 , pp. 5245-5252
    • Huot, J.1    Roy, G.2    Lambert, H.3    Chretien, P.4    Landry, J.5
  • 36
    • 0030985251 scopus 로고    scopus 로고
    • Multiple functions of Drosophila heat shock transcription factor in vivo
    • Jedlicka, P.; Mortin, M. A.; Wu, C. Multiple functions of Drosophila heat shock transcription factor in vivo. EMBO J. 16:2452-2462; 1997.
    • (1997) EMBO J. , vol.16 , pp. 2452-2462
    • Jedlicka, P.1    Mortin, M.A.2    Wu, C.3
  • 37
    • 0030827157 scopus 로고    scopus 로고
    • Activation of heat shock transcription factor 3 by c-Myb in the absence of cellular stress
    • Kanei-Ishii, C.; Tanikawa, J.; Nakai, A.; Morimoto, R. I.; Ishii, S. Activation of heat shock transcription factor 3 by c-Myb in the absence of cellular stress. Science 277:246-248; 1997.
    • (1997) Science , vol.277 , pp. 246-248
    • Kanei-Ishii, C.1    Tanikawa, J.2    Nakai, A.3    Morimoto, R.I.4    Ishii, S.5
  • 38
    • 0028216771 scopus 로고
    • c-Myb-induced trans-activation mediated by heat shock elements without sequence-specific DNA binding of c-Myb
    • Kanei-Ishii, C.; Yasukawa, T.; Morimoto, R. I.; Ishii, S. c-Myb-induced trans-activation mediated by heat shock elements without sequence-specific DNA binding of c-Myb. J. Biol. Chem. 269:15768-15775; 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15768-15775
    • Kanei-Ishii, C.1    Yasukawa, T.2    Morimoto, R.I.3    Ishii, S.4
  • 39
    • 0021916394 scopus 로고
    • Cell cycle control of the human HSP70 gene: Implications for the role of a cellular E1A-like function
    • Kao, H. T.; Capasso, O.; Heintz, N.; Nevins, J. R. Cell cycle control of the human HSP70 gene: Implications for the role of a cellular E1A-like function. Mol. Cell. Biol. 5:628-633; 1985.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 628-633
    • Kao, H.T.1    Capasso, O.2    Heintz, N.3    Nevins, J.R.4
  • 40
    • 0028960212 scopus 로고
    • Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1
    • Kim, D.; Ouyang, H.; Li, G. C. Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1. Proc. Natl. Acad. Sci. USA 92: 2126-2130; 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2126-2130
    • Kim, D.1    Ouyang, H.2    Li, G.C.3
  • 42
    • 0029026540 scopus 로고
    • Role of the protein chaperone YDJI in establishing Hsp90-mediated signal transduction pathways
    • Kimura, Y.; Yahara, I.; Lindquist, S. Role of the protein chaperone YDJI in establishing Hsp90-mediated signal transduction pathways. Science 268:1362-1365; 1995.
    • (1995) Science , vol.268 , pp. 1362-1365
    • Kimura, Y.1    Yahara, I.2    Lindquist, S.3
  • 43
    • 0030988941 scopus 로고    scopus 로고
    • Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
    • Kline, M. P.; Morimoto, R. I. Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation. Mol. Cell. Biol. 17:2107-2115; 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2107-2115
    • Kline, M.P.1    Morimoto, R.I.2
  • 44
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor 1 activity at control temperature by phosphorylation
    • Knauf, U.; Newton, E. M.; Kyriakis, J.; Kingston, R. E. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev. 10:2782-2793; 1996.
    • (1996) Genes Dev. , vol.10 , pp. 2782-2793
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 45
    • 0030966628 scopus 로고    scopus 로고
    • Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells
    • Leppa, S.; Pirkkala, L.; Saarento, H.; Sarge, K. D.; Sistonen, L. Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells. J. Biol. Chem. 272:15293-15298; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15293-15298
    • Leppa, S.1    Pirkkala, L.2    Saarento, H.3    Sarge, K.D.4    Sistonen, L.5
  • 46
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine, A. J. p53, the cellular gatekeeper for growth and division. Cell 88:323-331; 1997.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 47
    • 0029886404 scopus 로고    scopus 로고
    • Apoptosis in heat-induced cell killing: The protective role of hsp-70 and the sensitization effect of the c-myc gene
    • Li, W. X.; Chen, C. H.; Ling, C. C.; Li, G. C. Apoptosis in heat-induced cell killing: The protective role of hsp-70 and the sensitization effect of the c-myc gene. Radiat. Res. 145:324-330; 1996.
    • (1996) Radiat. Res. , vol.145 , pp. 324-330
    • Li, W.X.1    Chen, C.H.2    Ling, C.C.3    Li, G.C.4
  • 48
    • 0030728446 scopus 로고    scopus 로고
    • Conservation of a stress response: Human heat shock transcription factors functionally substitute for yeast HSF
    • Liu, X.-D.; Liu, P. C. C.; Santoro, N.; Thiele, D. J. Conservation of a stress response: Human heat shock transcription factors functionally substitute for yeast HSF. EMBO J 16:6466-6477; 1997.
    • (1997) EMBO J , vol.16 , pp. 6466-6477
    • Liu, X.-D.1    Liu, P.C.C.2    Santoro, N.3    Thiele, D.J.4
  • 49
    • 0029664413 scopus 로고    scopus 로고
    • Oxidative stress induces heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription
    • Liu, X.-D.; Thiele, D. J. Oxidative stress induces heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription. Genes Dev. 10:592-603; 1996.
    • (1996) Genes Dev. , vol.10 , pp. 592-603
    • Liu, X.-D.1    Thiele, D.J.2
  • 50
    • 0031795189 scopus 로고    scopus 로고
    • Hsp90 is required for pheromone signaling in yeast
    • Louvion, J. F.; Abbas-Terki, T.; Picard, D. Hsp90 is required for pheromone signaling in yeast. Mol. Biol. Cell 9:3071-3083; 1998.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3071-3083
    • Louvion, J.F.1    Abbas-Terki, T.2    Picard, D.3
  • 51
    • 0024652576 scopus 로고
    • Heat-shock cognate protein (hsc71) and related. proteins in mouse spermatogenic cells
    • Maekawa, M.; O'Brien, D. A.; Allen, R. L.; Eddy, E. M. Heat-shock cognate protein (hsc71) and related . proteins in mouse spermatogenic cells. Biol. Reprod. 40:843-852; 1989.
    • (1989) Biol. Reprod. , vol.40 , pp. 843-852
    • Maekawa, M.1    O'Brien, D.A.2    Allen, R.L.3    Eddy, E.M.4
  • 53
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis
    • McMillan, D. R.; Xiao, X.; Shao, L.; Graves, K.; Benjamin, I. J. Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis. J. Biol. Chem. 273: 7523-7528; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7523-7528
    • McMillan, D.R.1    Xiao, X.2    Shao, L.3    Graves, K.4    Benjamin, I.J.5
  • 55
    • 0031469912 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells
    • Michels, A. A.; Kanon, B.; Konings, A. W.; Ohtsuka, K.; Bensaude, O.; Kampinga, H. H. Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J. Biol. Chem. 272:33283-33289; 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33283-33289
    • Michels, A.A.1    Kanon, B.2    Konings, A.W.3    Ohtsuka, K.4    Bensaude, O.5    Kampinga, H.H.6
  • 56
    • 0006849332 scopus 로고
    • Expression of human HSP70 during the synthetic phase of the cell cycle
    • Milarski, K. L.; Morimoto, R. I. Expression of human HSP70 during the synthetic phase of the cell cycle. Proc. Natl. Acad. Sci. USA 83:9517-9521; 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9517-9521
    • Milarski, K.L.1    Morimoto, R.I.2
  • 57
    • 0028881937 scopus 로고
    • Mitogen-activated protein kinase acts as a negative regulator of the heat shock response in NIH3T3 cells
    • Mivechi, N. F.; Giaccia, A. J. Mitogen-activated protein kinase acts as a negative regulator of the heat shock response in NIH3T3 cells. Cancer Res. 55:5512-5519; 1995.
    • (1995) Cancer Res. , vol.55 , pp. 5512-5519
    • Mivechi, N.F.1    Giaccia, A.J.2
  • 58
    • 0032931842 scopus 로고    scopus 로고
    • A trans-activation domain in yeast heat shock tran-scription factor is essential for cell cycle progression during stress
    • Morano, K. A.; Santoro, N.; Kock, K. A.; Thiele, D. J. A trans-activation domain in yeast heat shock tran-scription factor is essential for cell cycle progression during stress. Mol. Cell. Biol. 19(1):402-411; 1999.
    • (1999) Mol. Cell. Biol. , vol.19 , Issue.1 , pp. 402-411
    • Morano, K.A.1    Santoro, N.2    Kock, K.A.3    Thiele, D.J.4
  • 59
    • 0028040816 scopus 로고
    • Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells
    • Murphy, S. P.; Gorzowski, J. J.; Sarge, K. D.; Phillips, B. Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells. Mol. Cell. Biol. 14:5309-5317; 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5309-5317
    • Murphy, S.P.1    Gorzowski, J.J.2    Sarge, K.D.3    Phillips, B.4
  • 60
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
    • Nadeau, K.; Das, A.; Walsh, C. T. Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J. Biol. Chem. 268:1479-1487; 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 61
    • 0026645052 scopus 로고
    • Isolation and characterization of extragenic suppressors of mutations in the SSA hsp70 genes of Saccharomyces cerevisiae
    • Nelson, R. J.; Heschl, M. F.; Craig, E. A. Isolation and characterization of extragenic suppressors of mutations in the SSA hsp70 genes of Saccharomyces cerevisiae. Genetics 131:277-285; 1992.
    • (1992) Genetics , vol.131 , pp. 277-285
    • Nelson, R.J.1    Heschl, M.F.2    Craig, E.A.3
  • 62
    • 0027366354 scopus 로고
    • The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines
    • Oesterreich, S.; Weng, C. N.; Qiu, M.; Hilsenbeck, S. G.; Osborne, C. K.; Fuqua, S. A. The small heat shock protein hsp27 is correlated with growth and drug resistance in human breast cancer cell lines. Cancer Res. 53:4443-4448; 1993.
    • (1993) Cancer Res. , vol.53 , pp. 4443-4448
    • Oesterreich, S.1    Weng, C.N.2    Qiu, M.3    Hilsenbeck, S.G.4    Osborne, C.K.5    Fuqua, S.A.6
  • 64
    • 0031895351 scopus 로고    scopus 로고
    • The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt, W. B. The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors. Proc. Soc. Exp. Biol. Med. 217:420-434; 1998.
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 65
    • 0028025643 scopus 로고
    • Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo
    • Rabindran, S. K.; Wisniewski, J.; Li, L.; Li, G. C.; Wu, C. Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo. Mol. Cell. Biol. 14:6552-6560; 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6552-6560
    • Rabindran, S.K.1    Wisniewski, J.2    Li, L.3    Li, G.C.4    Wu, C.5
  • 67
    • 0031224919 scopus 로고    scopus 로고
    • Phosphorylation by a cyclin-dependent kinase modulates DNA binding of the Arabidopsis heat-shock transcription factor HSF1 in vitro
    • Reindl, A.; Schoffl, F.; Schell, J.; Koncz, C.; Bako, L. Phosphorylation by a cyclin-dependent kinase modulates DNA binding of the Arabidopsis heat-shock transcription factor HSF1 in vitro. Plant Physiol. 115:93-100; 1997.
    • (1997) Plant Physiol. , vol.115 , pp. 93-100
    • Reindl, A.1    Schoffl, F.2    Schell, J.3    Koncz, C.4    Bako, L.5
  • 68
    • 0028241317 scopus 로고
    • Expression of heat shock factor 2 in mouse testis: Potential role as a regulator of heat-shock protein gene expression during spermatogenesis
    • Sarge, K. D.; Park-Sarge, O. K.; Kirby, J. D.; Mayo, K. E.; Morimoto, R. I. Expression of heat shock factor 2 in mouse testis: Potential role as a regulator of heat-shock protein gene expression during spermatogenesis. Biol. Reprod. 50:1334-1343; 1994.
    • (1994) Biol. Reprod. , vol.50 , pp. 1334-1343
    • Sarge, K.D.1    Park-Sarge, O.K.2    Kirby, J.D.3    Mayo, K.E.4    Morimoto, R.I.5
  • 69
    • 0025989349 scopus 로고
    • Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability
    • Sarge, K. D.; Zimarino, V.; Holm, K.; Wu, C.; Morimoto, R. I. Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability. Genes Dev. 5:1902-1911; 1991.
    • (1991) Genes Dev. , vol.5 , pp. 1902-1911
    • Sarge, K.D.1    Zimarino, V.2    Holm, K.3    Wu, C.4    Morimoto, R.I.5
  • 70
    • 0030946332 scopus 로고    scopus 로고
    • The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication
    • Schutz, A. R.; Giddings, T., Jr.; Steiner, E.; Winey, M. The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication. J. Cell Biol. 136:969-982; 1997.
    • (1997) J. Cell Biol. , vol.136 , pp. 969-982
    • Schutz, A.R.1    Giddings Jr., T.2    Steiner, E.3    Winey, M.4
  • 71
    • 15844363948 scopus 로고    scopus 로고
    • Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell
    • Sepehrnia, B.; Paz, I. B.; Dasgupta, G.; Momand, J. Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell. J. Biol. Chem. 271:15084-15090; 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15084-15090
    • Sepehrnia, B.1    Paz, I.B.2    Dasgupta, G.3    Momand, J.4
  • 72
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressers
    • Shi, Y.; Mosser, D. D.; Morimoto, R. I. Molecular chaperones as HSF1-specific transcriptional repressers. Genes Dev. 12:654-666; 1998.
    • (1998) Genes Dev. , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 73
    • 0026746491 scopus 로고
    • Activation of heat shock factor 2 during hemin-induced differentiation of human erythroleukemia cells
    • Sistonen, L.; Sarge, K. D.; Phillips, B.; Abravaya, K.; Morimoto, R. I. Activation of heat shock factor 2 during hemin-induced differentiation of human erythroleukemia cells. Mol. Cell. Biol. 12:4104-1111; 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4104-11111
    • Sistonen, L.1    Sarge, K.D.2    Phillips, B.3    Abravaya, K.4    Morimoto, R.I.5
  • 74
    • 0026342691 scopus 로고
    • A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle
    • Smith, B. J.; Yaffe, M. P. A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle. Mol. Cell. Biol. 11:2647-2655; 1991.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2647-2655
    • Smith, B.J.1    Yaffe, M.P.2
  • 75
    • 0024989583 scopus 로고
    • Yeast heat shock factor contains separable transient and sustained response transcriptional activators
    • Sorger, P. K. Yeast heat shock factor contains separable transient and sustained response transcriptional activators. Cell 62:793-805; 1990.
    • (1990) Cell , vol.62 , pp. 793-805
    • Sorger, P.K.1
  • 76
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger, P. K.; Pelham, H. R. B. Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54:855-864; 1988.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 77
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova, L.; Leng, X.; Parker, S. B.; Harper, J. W. Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev. 10:1491-1502; 1996.
    • (1996) Genes Dev. , vol.10 , pp. 1491-1502
    • Stepanova, L.1    Leng, X.2    Parker, S.B.3    Harper, J.W.4
  • 78
    • 0029060160 scopus 로고
    • Bcl-2 and thermotolerance cooperate in cell survival
    • Strasser, A.; Anderson, R. L. Bcl-2 and thermotolerance cooperate in cell survival. Cell Growth Differ. 6: 799-805; 1995.
    • (1995) Cell Growth Differ. , vol.6 , pp. 799-805
    • Strasser, A.1    Anderson, R.L.2
  • 79
    • 0027940568 scopus 로고
    • Heat shock transcription factor activates yeast metallothionein gene expression in response to heat and glucose starvation via distinct signalling pathways
    • Tamai, K. T.; Liu, X.; Silar, P.; Sosinowski, T.; Thiele, D. J. Heat shock transcription factor activates yeast metallothionein gene expression in response to heat and glucose starvation via distinct signalling pathways. Mol. Cell. Biol. 14:8155-8165; 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8155-8165
    • Tamai, K.T.1    Liu, X.2    Silar, P.3    Sosinowski, T.4    Thiele, D.J.5
  • 81
    • 0032500690 scopus 로고    scopus 로고
    • Transcriptional factor mutations reveal regulatory complexities of heat shock and newly identified stress genes in Saccharomyccs cerevisiae
    • Treger, J. M.; Schmitt, A. P.; Simon, J. R.; McEntee, K. Transcriptional factor mutations reveal regulatory complexities of heat shock and newly identified stress genes in Saccharomyccs cerevisiae. J. Biol. Chem. 273:26875-26879; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26875-26879
    • Treger, J.M.1    Schmitt, A.P.2    Simon, J.R.3    McEntee, K.4
  • 82
    • 0030896688 scopus 로고    scopus 로고
    • The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila
    • van der Straten, A.; Rommel, C.; Dickson, B.; Hafen, E. The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila. EMBO J. 16: 1961-1969; 1997.
    • (1997) EMBO J. , vol.16 , pp. 1961-1969
    • Van Der Straten, A.1    Rommel, C.2    Dickson, B.3    Hafen, E.4
  • 83
    • 0025955517 scopus 로고
    • Stress-induced oligomerization and chromosomal relocalization of heat-shock factor
    • Westwood, J. T.; Clos, J.; Wu, C. Stress-induced oligomerization and chromosomal relocalization of heat-shock factor. Nature 353:822-827; 1991.
    • (1991) Nature , vol.353 , pp. 822-827
    • Westwood, J.T.1    Clos, J.2    Wu, C.3
  • 84
    • 0031909866 scopus 로고    scopus 로고
    • The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
    • Whitesell, L.; Sutphin, P. D.; Pulcini, E. J.; Martinez, J. D.; Cook, P. H. The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol. 18:1517-1524; 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1517-1524
    • Whitesell, L.1    Sutphin, P.D.2    Pulcini, E.J.3    Martinez, J.D.4    Cook, P.H.5
  • 85
    • 0024282788 scopus 로고
    • Isolation of the gene encoding the S. cerevisiae heat shock transcription factor
    • Wiederrecht, G.; Seto, D.; Parker, C. S. Isolation of the gene encoding the S. cerevisiae heat shock transcription factor. Cell 54:841-853; 1988.
    • (1988) Cell , vol.54 , pp. 841-853
    • Wiederrecht, G.1    Seto, D.2    Parker, C.S.3
  • 86
    • 0029564954 scopus 로고
    • Heat shock transcription factors: Structure and regulation
    • Wu, C. Heat shock transcription factors: Structure and regulation. Annu. Rev. Cell. Dev. Biol. 11:441-469; 1995.
    • (1995) Annu. Rev. Cell. Dev. Biol. , vol.11 , pp. 441-469
    • Wu, C.1
  • 87
    • 0032502705 scopus 로고    scopus 로고
    • Transcriptional activation of heat shock factor HSF1 probed by phosphopeptide analysis of factor 32P-labeled in vivo
    • Xia, W.; Guo, Y.; Vilaboa, N.; Zuo, J.; Voellmy, R. Transcriptional activation of heat shock factor HSF1 probed by phosphopeptide analysis of factor 32P-labeled in vivo. J. Biol. Chem. 273:8749-8755; 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8749-8755
    • Xia, W.1    Guo, Y.2    Vilaboa, N.3    Zuo, J.4    Voellmy, R.5
  • 89
    • 0023921692 scopus 로고
    • Identification and sequence analysis of a new member of the mouse HSP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line
    • Zakeri, Z. F.; Wolgemuth, D. J.; Hunt, C. R. Identification and sequence analysis of a new member of the mouse HSP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line. Mol. Cell. Biol. 8:2925-2932; 1988.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2925-2932
    • Zakeri, Z.F.1    Wolgemuth, D.J.2    Hunt, C.R.3
  • 90
    • 0030779154 scopus 로고    scopus 로고
    • A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication
    • Zarzov, P.; Boucherie, H.; Mann, C. A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication. J. Cell Sci. 110:1879-1891; 1997.
    • (1997) J. Cell Sci. , vol.110 , pp. 1879-1891
    • Zarzov, P.1    Boucherie, H.2    Mann, C.3
  • 91
    • 0031806619 scopus 로고    scopus 로고
    • Molecular mechanism governing heme signaling in yeast: A higher-order complex mediates heme regulation of the transcriptional activator HAP1
    • Zhang, L.; Hach, A.; Wang, C. Molecular mechanism governing heme signaling in yeast: A higher-order complex mediates heme regulation of the transcriptional activator HAP1. Mol. Cell. Biol. 18:3819-3828; 1998.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3819-3828
    • Zhang, L.1    Hach, A.2    Wang, C.3
  • 92
    • 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, D. F.; Voellmy, R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94: 471-480; 1998.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.