메뉴 건너뛰기




Volumn 23, Issue 4, 1998, Pages 313-329

Heat stress response and heat stress transcription factors

Author keywords

Heat stress; Reporter assays; Transcription factors

Indexed keywords

DNA BINDING PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

EID: 0031729007     PISSN: 02505991     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02936124     Document Type: Conference Paper
Times cited : (51)

References (171)
  • 1
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts wild HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya K, Myers M P, Murphy S P and Mon moto R I 1992 The human heat shock protein hsp70 interacts wild 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    Mon Moto, R.I.4
  • 2
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • Ananthan J, Goldberg A L and Vocllmy R 1986 Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes; Science 232 522-524
    • (1986) Science , vol.232 , pp. 522-524
    • Ananthan, J.1    Goldberg, A.L.2    Vocllmy, R.3
  • 3
    • 0018382014 scopus 로고
    • The induction of gene activity in Drosophila by heat shock
    • Ashburnre M and Bonner J J 1979 The induction of gene activity in Drosophila by heat shock; Cell 17 241-254
    • (1979) Cell , vol.17 , pp. 241-254
    • Ashburnre, M.1    Bonner, J.J.2
  • 4
    • 0027474909 scopus 로고
    • Activation of human heat shock-genes is accompanied by oligomerisation, modification and rapid translocation of heat shock transcription factor
    • Baler R, Dahl G and Vocllmy R 1993 Activation of human heat shock-genes is accompanied by oligomerisation, modification and rapid translocation of heat shock transcription factor; Mol. Cell. Biol. 13 2486-2496
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2486-2496
    • Baler, R.1    Dahl, G.2    Vocllmy, R.3
  • 5
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins -Hsp70 as a potential autoregulatory factor
    • Baler R, Welch W J and 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
  • 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 and Voellmy R 1996 Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells; Cell Stress Chap. 1 33-39
    • (1996) Cell Stress Chap. , vol.1 , pp. 33-39
    • Baler, R.1    Zou, J.2    Voellmy, R.3
  • 7
    • 0026623463 scopus 로고
    • Examining the function and regulation of hsp70 in cells subjected to metabolic stress
    • Beckmann R P, Lovett M and Welch W J 1992 Examining the function and regulation of hsp70 in cells subjected to metabolic stress; J. Cell Biol. 117 1137-1150
    • (1992) J. Cell Biol. , vol.117 , pp. 1137-1150
    • Beckmann, R.P.1    Lovett, M.2    Welch, W.J.3
  • 8
    • 0343195960 scopus 로고
    • Protein denaturation during heat shock and related stress
    • (eds) M J Schlesinecr, G Santoro and E Garaci (Berlin: Springer) Chapter 8
    • Bensaude O, Pinto M, Dubois M-F, Trung N V and Morange M 1990 Protein denaturation during heat shock and related stress; in Stress proteins (eds) M J Schlesinecr, G Santoro and E Garaci (Berlin: Springer) Chapter 8, pp 89-99
    • (1990) Stress Proteins , pp. 89-99
    • Bensaude, O.1    Pinto, M.2    Dubois, M.-F.3    Trung, N.V.4    Morange, M.5
  • 9
    • 0032510285 scopus 로고    scopus 로고
    • Induction of the DNA-binding and transcriptional activities of heat shock factor 1 is uncoupled in Xenopus oocytes
    • Bharadwaj S, Hnatov A, Ali A and Ovsenek N 1998 Induction of the DNA-binding and transcriptional activities of heat shock factor 1 is uncoupled in Xenopus oocytes; BBA Mol Cell Res. 1402 79-85
    • (1998) BBA Mol Cell Res. , vol.1402 , pp. 79-85
    • Bharadwaj, S.1    Hnatov, A.2    Ali, A.3    Ovsenek, N.4
  • 10
    • 0023515282 scopus 로고
    • Mechanisms of heat-shock gene activation in higher eukaryotcs
    • Bienz M and Pelham H R B 1987 Mechanisms of heat-shock gene activation in higher eukaryotcs; Adv. Genet. 24 31-72
    • (1987) Adv. Genet. , vol.24 , pp. 31-72
    • Bienz, M.1    Pelham, H.R.B.2
  • 11
    • 0025351346 scopus 로고
    • Transcriptional regulation of SSA3, an HSP70 gene from Saccharomyces cerevisiae
    • Boorstien W R and Craig E A 1990 Transcriptional regulation of SSA3, an HSP70 gene from Saccharomyces cerevisiae; Mol. Cell. Biol. 10 3262-3267
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3262-3267
    • Boorstien, W.R.1    Craig, E.A.2
  • 12
    • 0030877053 scopus 로고    scopus 로고
    • Heat stress transcription factors from tomato can functionally replace HSF1 in the yeast Saccharomyces cerevisiae
    • Boscheinen O, Lyck R, Queitsch C, Treuter E, Zimarino V and Scharf K-D 1997 Heat stress transcription factors from tomato can functionally replace HSF1 in the yeast Saccharomyces cerevisiae; Mol. Gen. Genet. 255 322-331
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 322-331
    • Boscheinen, O.1    Lyck, R.2    Queitsch, C.3    Treuter, E.4    Zimarino, V.5    Scharf, K.-D.6
  • 13
    • 0027501822 scopus 로고
    • SKN7, a yeast multicopy suppressor of a mutation affecting cell wall beta-glucan assembly, encodes a product with domains homologous to prokaryotic 2-component regulators and to heat shock transcription factors
    • Brown J L, North S and Bussey H 1993 SKN7, a yeast multicopy suppressor of a mutation affecting cell wall beta-glucan assembly, encodes a product with domains homologous to prokaryotic 2-component regulators and to heat shock transcription factors; J. Bacteriol. 175 6908-6915
    • (1993) J. Bacteriol. , vol.175 , pp. 6908-6915
    • Brown, J.L.1    North, S.2    Bussey, H.3
  • 14
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat-shock response
    • Bukau B 1993 Regulation of the Escherichia coli heat-shock response; Mol. Microbiol. 9 671-680
    • (1993) Mol. Microbiol. , vol.9 , pp. 671-680
    • Bukau, B.1
  • 15
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones and thermotolerance
    • Bush K T, Goldberg A L and Nigam S K 1997 Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones and thermotolerance; J. Biol. Chem. 272 9086-9092
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 16
    • 0027491654 scopus 로고
    • Identification of the C-terminal activator domain in yeast heat shock factor - Independent control of transient and sustained transcriptional activity
    • Chen Y Q, Barlev N A. Westergaard O and Jakobsen B K 1993 Identification of the C-terminal activator domain in yeast heat shock factor - Independent control of transient and sustained transcriptional activity; EMBO J. 12 5007-5018
    • (1993) EMBO J. , vol.12 , pp. 5007-5018
    • Chen, Y.Q.1    Barlev, N.A.2    Westergaard, O.3    Jakobsen, B.K.4
  • 17
    • 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 and Calderwood S K 1996 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) 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
  • 18
    • 0025606431 scopus 로고
    • Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation
    • Clos J, Westwood J T, Becker P B, Wilson S, Lambert U and Wu C 1990 Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation; Cell 63 1085-1097
    • (1990) Cell , vol.63 , pp. 1085-1097
    • Clos, J.1    Westwood, J.T.2    Becker, P.B.3    Wilson, S.4    Lambert, U.5    Wu, C.6
  • 19
    • 0030043401 scopus 로고    scopus 로고
    • Activation of heat shock factor 1 DNA-binding precedes stress-induced serine phosphorylation
    • Cotto J J, Kline M and Morimoto R I 1996 Activation of heat shock factor 1 DNA-binding precedes stress-induced serine phosphorylation; J. Biol, Chem. 271 3335-3358
    • (1996) J. Biol, Chem. , vol.271 , pp. 3335-3358
    • Cotto, J.J.1    Kline, M.2    Morimoto, R.I.3
  • 20
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor thai controls the unfolded protein response
    • Cox J S and Walter P 1996 A novel mechanism for regulating activity of a transcription factor thai controls the unfolded protein response; Cell 87 391-404
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 21
    • 0000920828 scopus 로고
    • The packaging of α-helices: Simple coiled-coils
    • Crick FHC 1953 The packaging of α-helices: simple coiled-coils; Acta Crystallogr. 6 689-697
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 22
    • 0029379806 scopus 로고
    • Isolation and characterization of six heat shock transcription factor cDNA clones from soybean
    • Czarnecka-Verner E, Yuan C-X, Fox P C and Gurley W B 1995 Isolation and characterization of six heat shock transcription factor cDNA clones from soybean; Plant Mol. Biol. 29 37-51
    • (1995) Plant Mol. Biol. , vol.29 , pp. 37-51
    • Czarnecka-Verner, E.1    Yuan, C.-X.2    Fox, P.C.3    Gurley, W.B.4
  • 24
    • 0028113437 scopus 로고
    • Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy
    • Dambergcr F F, Pelton J G, Harrison C J, Nelson H C M and Wemmre D E 1994 Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy; Protein Sci. 3 1806-1821
    • (1994) Protein Sci. , vol.3 , pp. 1806-1821
    • Dambergcr, F.F.1    Pelton, J.G.2    Harrison, C.J.3    Nelson, H.C.M.4    Wemmre, D.E.5
  • 25
    • 0030998321 scopus 로고    scopus 로고
    • The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • Danese P N and Silhavy T J 1997 The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli; Genes Dev. 11 1183-1193
    • (1997) Genes Dev. , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 26
    • 0030611303 scopus 로고    scopus 로고
    • The sigma(E)-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigma(E)
    • DeLasPenas A, Connolly L and Gross C A 1997 The sigma(E)-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigma(E); Mol Microbiol. 24 373-385
    • (1997) Mol Microbiol. , vol.24 , pp. 373-385
    • DeLasPenas, A.1    Connolly, L.2    Gross, C.A.3
  • 27
    • 0020409205 scopus 로고
    • The heat shock response is self-regulated at both the transcriptional and posttranscriplional levels
    • DiDomenico B J, Bugaisky G E and Lindquist S 1982 The heat shock response is self-regulated at both the transcriptional and posttranscriplional levels; Cell 31 593-603
    • (1982) Cell , vol.31 , pp. 593-603
    • DiDomenico, B.J.1    Bugaisky, G.E.2    Lindquist, S.3
  • 28
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - a consensus?
    • Dingwall C and Laskey R A 1991 Nuclear targeting sequences - a consensus?; Trends Biochem. Sci. 16 478-481
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 30
    • 0025883203 scopus 로고
    • Heat-shock-induced denaturation of proteins - characterization of the insolubilization of the interferon-induccd p68 kinase
    • Dubois M F, Hovanessian A G and Bensaude O 1991 Heat-shock-induced denaturation of proteins - characterization of the insolubilization of the interferon-induccd p68 kinase; J. Biol. Chem. 266 9707-9711
    • (1991) J. Biol. Chem. , vol.266 , pp. 9707-9711
    • Dubois, M.F.1    Hovanessian, A.G.2    Bensaude, O.3
  • 31
    • 0031931412 scopus 로고    scopus 로고
    • Intramolecular repression of mouse heat shock factor 1
    • Farkas T, Kutskova Y A and Zimarino V 1998 Intramolecular repression of mouse heat shock factor 1; Mol. Cell. Biol. 18 906-918
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 906-918
    • Farkas, T.1    Kutskova, Y.A.2    Zimarino, V.3
  • 33
    • 0031760058 scopus 로고    scopus 로고
    • Heat induced stress proteins and the concept of molecular chaparones
    • Forreiter C and Nover L 1998 Heat induced stress proteins and the concept of molecular chaparones; J. Biosci. 23 287-302
    • (1998) J. Biosci. , vol.23 , pp. 287-302
    • Forreiter, C.1    Nover, L.2
  • 34
    • 0025825895 scopus 로고
    • Modular structure of transcription factors: Implications for gene regulation
    • Frankel A D and Kim PS 1991 Modular structure of transcription factors: Implications for gene regulation; Cell 65 717-719
    • (1991) Cell , vol.65 , pp. 717-719
    • Frankel, A.D.1    Kim, P.S.2
  • 35
    • 0029411225 scopus 로고
    • Expression of heat shock factor and heat shock protein 70 genes during maize pollen development
    • Gagliardi D, Breton C, Chaboud A, Vergne P and Dumas C 1995 Expression of heat shock factor and heat shock protein 70 genes during maize pollen development; Plant Mol. Biol. 29 841-856
    • (1995) Plant Mol. Biol. , vol.29 , pp. 841-856
    • Gagliardi, D.1    Breton, C.2    Chaboud, A.3    Vergne, P.4    Dumas, C.5
  • 36
    • 0027439593 scopus 로고
    • Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe
    • Gallo G J, Prentice H and Kingston R E 1993 Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe; Mol Cell. Biol. 13 749-761
    • (1993) Mol Cell. Biol. , vol.13 , pp. 749-761
    • Gallo, G.J.1    Prentice, H.2    Kingston, R.E.3
  • 37
    • 0030044799 scopus 로고    scopus 로고
    • A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates the activity of the Escherichia coli heat shock transcription factor sigma 32
    • Gamer J, Multhaup G, Tomoyasu T, McCarthy J S, Rüdiger S, Schönfeld H J, Schirra C, Bujard H and Bukau B 1996 A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates the activity of the Escherichia coli heat shock transcription factor sigma 32; EMBO J. 15 607-617
    • (1996) EMBO J. , vol.15 , pp. 607-617
    • Gamer, J.1    Multhaup, G.2    Tomoyasu, T.3    McCarthy, J.S.4    Rüdiger, S.5    Schönfeld, H.J.6    Schirra, C.7    Bujard, H.8    Bukau, B.9
  • 38
    • 0023216021 scopus 로고
    • An increased content of protease La, the Ion gene product, increases protein degradation and blocks growth in Escherichia coli
    • Goff S A and Goldberg A L 1987 An increased content of protease La, the Ion gene product, increases protein degradation and blocks growth in Escherichia coli; J. Biol. Chem. 262 4508-4515
    • (1987) J. Biol. Chem. , vol.262 , pp. 4508-4515
    • Goff, S.A.1    Goldberg, A.L.2
  • 39
    • 0029037406 scopus 로고
    • Regulated expression of heat shock factor 1 isoforms with distinct leucine zipper arrays via tissue-dependent alternative splicing
    • Goodson M L and Sarge K D 1995 Regulated expression of heat shock factor 1 isoforms with distinct leucine zipper arrays via tissue-dependent alternative splicing; Biochem. Biophys. Res. Commun. 211 943-949
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 943-949
    • Goodson, M.L.1    Sarge, K.D.2
  • 40
    • 0029087566 scopus 로고
    • Tissue-dependent expression of heat shock factor 2 isoforms with distinct transcriptional activities
    • Goodson M L, Park-Sarge O K and Sarge K D 1995 Tissue-dependent expression of heat shock factor 2 isoforms with distinct transcriptional activities; Mol. Cell. Biol. 15 5288-5293
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5288-5293
    • Goodson, M.L.1    Park-Sarge, O.K.2    Sarge, K.D.3
  • 41
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Görlich D and Mattaj I W 1996 Nucleocytoplasmic transport; Science 2271 1513-1518
    • (1996) Science , vol.2271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.W.2
  • 42
    • 0024610090 scopus 로고
    • Mistranslation induces the heat-shock response in the yeast Saccharomyces cerevisiae
    • Grant C M, Firoozan M and Tuite M F 1989 Mistranslation induces the heat-shock response in the yeast Saccharomyces cerevisiae; Mol. Microbiol. 3 215-220
    • (1989) Mol. Microbiol. , vol.3 , pp. 215-220
    • Grant, C.M.1    Firoozan, M.2    Tuite, M.F.3
  • 43
    • 0029039963 scopus 로고
    • The heat shock-responsive domain of human HSF1 that regulates transcription activation domain function
    • Green M, Schuetz T J, Sullivan E K and Kingston R E 1995 The heat shock-responsive domain of human HSF1 that regulates transcription activation domain function; Mol Cell. Biol. 15 3354-3362
    • (1995) Mol Cell. Biol. , vol.15 , pp. 3354-3362
    • Green, M.1    Schuetz, T.J.2    Sullivan, E.K.3    Kingston, R.E.4
  • 44
    • 0027958045 scopus 로고
    • Crystal structure of the DNA binding domain of the heat shock transcription factor
    • Harrison C J, Bohm A A and Nelson HCM 1994 Crystal structure of the DNA binding domain of the heat shock transcription factor; Science 263 224-227
    • (1994) Science , vol.263 , pp. 224-227
    • Harrison, C.J.1    Bohm, A.A.2    Nelson, H.C.M.3
  • 45
    • 0028847062 scopus 로고
    • Short circuiting stress protein expression via a tyrosine kinase inhibitor, herbimycin
    • Hegde R S, Zuo J, Vocllmy R and Welch W J 1995 Short circuiting stress protein expression via a tyrosine kinase inhibitor, herbimycin; Am. J. Cell Physiol. 165 186-200
    • (1995) Am. J. Cell Physiol. , vol.165 , pp. 186-200
    • Hegde, R.S.1    Zuo, J.2    Vocllmy, R.3    Welch, W.J.4
  • 46
    • 0027425585 scopus 로고
    • Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
    • Hendrick J P, Langer T, Davis T A, Hartl F U and Wiedmann M 1993 Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides; Proc. Natl. Acad. Sci. USA 90 10216-10220
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10216-10220
    • Hendrick, J.P.1    Langer, T.2    Davis, T.A.3    Hartl, F.U.4    Wiedmann, M.5
  • 47
    • 0019494188 scopus 로고
    • Cellular response to stress: Comparison of a family of 71-73 kilodalton proteins rapidly synthesized in rat tissue slices and canavanine-treated cells in culture
    • Hightower L E and While F P 1981 Cellular response to stress: Comparison of a family of 71-73 kilodalton proteins rapidly synthesized in rat tissue slices and canavanine-treated cells in culture; J. Cell. Physiol. 108 261-275
    • (1981) J. Cell. Physiol. , vol.108 , pp. 261-275
    • Hightower, L.E.1    While, F.P.2
  • 48
    • 0001089240 scopus 로고
    • Actin gene mutations in Drosophila; Heat shock activation in the direct flight muscles
    • Hiromi Y and Hotta Y 1985 Actin gene mutations in Drosophila; Heat shock activation in the direct flight muscles; EMBO J. 4 1681-1687
    • (1985) EMBO J. , vol.4 , pp. 1681-1687
    • Hiromi, Y.1    Hotta, Y.2
  • 49
    • 0028321786 scopus 로고
    • A short element required for turning off heat shock transcription factor: Evidence that phosphorylation enhances deactivation
    • HoJ A and Jakobsen B K 1994 A short element required for turning off heat shock transcription factor: Evidence that phosphorylation enhances deactivation; EMBO J. 13 2617-2624
    • (1994) EMBO J. , vol.13 , pp. 2617-2624
    • Hoj, A.1    Jakobsen, B.K.2
  • 50
    • 0028518911 scopus 로고
    • Arabidopsis heat shock factor: Isolation and characterization of the gene and the recombinant protein
    • Hübel A and Schöffl F 1994 Arabidopsis heat shock factor: Isolation and characterization of the gene and the recombinant protein; Plant Mol. Biol. 26 353-362
    • (1994) Plant Mol. Biol. , vol.26 , pp. 353-362
    • Hübel, A.1    Schöffl, F.2
  • 51
    • 0029048272 scopus 로고
    • Arabidopsis heat shock factor is constitutively active in Drosophila and human cells
    • Hübel A, Lee J H, Wu C and Schöffl F 1995 Arabidopsis heat shock factor is constitutively active in Drosophila and human cells; Mol Gen. Genet. 248 136-141
    • (1995) Mol Gen. Genet. , vol.248 , pp. 136-141
    • Hübel, A.1    Lee, J.H.2    Wu, C.3    Schöffl, F.4
  • 52
    • 0030030578 scopus 로고    scopus 로고
    • Importins/karyopherins meet nucleoporins
    • Hurt E C 1996 Importins/karyopherins meet nucleoporins ;Cell 84 509-515
    • (1996) Cell , vol.84 , pp. 509-515
    • Hurt, E.C.1
  • 54
    • 0025965063 scopus 로고
    • A conserved heptapeptide restrains the activity of the yeast heat shock transcription factor
    • Jakobsen B K and Pelham H R B 1991 A conserved heptapeptide restrains the activity of the yeast heat shock transcription factor; EMBO J. 10 369-375
    • (1991) EMBO J. , vol.10 , pp. 369-375
    • Jakobsen, B.K.1    Pelham, H.R.B.2
  • 55
    • 0030985251 scopus 로고    scopus 로고
    • Multiple functions of Drosophila heat shock transcription factor in vivo
    • Jedlicka P, Mortin M A and Wu C 1997 Multiple functions of Drosophila heat shock transcription factor in vivo; EMBO J. 16 2452-2462
    • (1997) EMBO J. , vol.16 , pp. 2452-2462
    • Jedlicka, P.1    Mortin, M.A.2    Wu, C.3
  • 56
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich D H, Sistonen L, Kroes R A and Morimoto R I 1992 Effect of sodium salicylate on the human heat shock response; Science 255 1243-1245
    • (1992) Science , vol.255 , pp. 1243-1245
    • Jurivich, D.H.1    Sistonen, L.2    Kroes, R.A.3    Morimoto, R.I.4
  • 57
    • 0032488855 scopus 로고    scopus 로고
    • Eukaryotic transcription; An interlaced network of transcription factors and chromatin-modifying machines
    • Kadonaga J T 1998 Eukaryotic transcription; An interlaced network of transcription factors and chromatin-modifying machines; Cell 92 307-313
    • (1998) Cell , vol.92 , pp. 307-313
    • Kadonaga, J.T.1
  • 58
    • 0030933962 scopus 로고    scopus 로고
    • c-Myb and cyclin d1 mediate heat shock element dependent activation of the human hsp70 promoter
    • Kamano H and Klempnauer K H 1997 c-Myb and cyclin d1 mediate heat shock element dependent activation of the human hsp70 promoter; Oncogene 14 1223-1229
    • (1997) Oncogene , vol.14 , pp. 1223-1229
    • Kamano, H.1    Klempnauer, K.H.2
  • 59
    • 0027457953 scopus 로고
    • Thermotolerance in mammalian cells -Protein denaturation and aggregation and stress proteins
    • Kampinga H H 1993 Thermotolerance in mammalian cells -Protein denaturation and aggregation and stress proteins; J. Cell Sci. 104 11-17
    • (1993) J. Cell Sci. , vol.104 , pp. 11-17
    • Kampinga, H.H.1
  • 60
    • 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 and Ishii S 1997 Activation of heat shock transcription factor 3 by c-Myb in the absence of cellular stress; Science 277 246-248
    • (1997) Science , vol.277 , pp. 246-248
    • Kanei-Ishii, C.1    Tanikawa, J.2    Nakai, A.3    Morimoto, R.I.4    Ishii, S.5
  • 61
    • 0030613795 scopus 로고    scopus 로고
    • Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma 32 and abnormal proteins in Escherichia coli
    • Kanemori M, Nishihara K, Yanagi H and Yura T 1997 Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma 32 and abnormal proteins in Escherichia coli; J. Bacteriol. 179 7219-7225
    • (1997) J. Bacteriol. , vol.179 , pp. 7219-7225
    • Kanemori, M.1    Nishihara, K.2    Yanagi, H.3    Yura, T.4
  • 62
    • 0030808558 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response
    • Kawahara T, Yanagi H, Yura T and Mori K 1997 Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response; Mol. Cell. Biol. 8 1845-1862
    • (1997) Mol. Cell. Biol. , vol.8 , pp. 1845-1862
    • Kawahara, T.1    Yanagi, H.2    Yura, T.3    Mori, K.4
  • 63
    • 0018257409 scopus 로고
    • The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblasts
    • Kelley P M and Schlesinger M J 1978 The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblasts; Cell 15 1277-1286
    • (1978) Cell , vol.15 , pp. 1277-1286
    • Kelley, P.M.1    Schlesinger, M.J.2
  • 64
    • 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 and Li G C 1995 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) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2126-2130
    • Kim, D.1    Ouyang, H.2    Li, G.C.3
  • 65
    • 0030988941 scopus 로고    scopus 로고
    • Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
    • Kline M P and Morimoto R I 1997 Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation; Mol. Cell. Biol. 17 2107-2115
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2107-2115
    • Kline, M.P.1    Morimoto, R.I.2
  • 66
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor1 activity at control temperature by phosphorylation
    • Knauf U, Newton E M, Kyriakis J and Kingston R E 1996 Repression of human heat shock factor1 activity at control temperature by phosphorylation; Genes Dev. 10 2782-2793
    • (1996) Genes Dev. , vol.10 , pp. 2782-2793
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 67
    • 0028906080 scopus 로고
    • Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress
    • Krems B, Charizanis C and Entian K-D 1995 Mutants of Saccharomyces cerevisiae sensitive to oxidative and osmotic stress; Curr. Genet. 27 427-434
    • (1995) Curr. Genet. , vol.27 , pp. 427-434
    • Krems, B.1    Charizanis, C.2    Entian, K.-D.3
  • 68
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echols H, Flanagan J, Haycr M K and Hartl F-U 1992 Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding; Nature (London) 356 683-689
    • (1992) Nature (London) , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Haycr, M.K.5    Hartl, F.-U.6
  • 69
    • 0002858113 scopus 로고    scopus 로고
    • Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae
    • Lee D H and Goldberg A L 1998 Proteasome inhibitors cause induction of heat shock proteins and trehalose, which together confer thermotolerance in Saccharomyces cerevisiae; Mol. Cell. Biol. 18 30-38
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 30-38
    • Lee, D.H.1    Goldberg, A.L.2
  • 70
    • 0029379547 scopus 로고
    • Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis
    • Lee J H, Hubel A and Schöffl F 1995 Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis; Plant J. 8 603-612
    • (1995) Plant J. , vol.8 , pp. 603-612
    • Lee, J.H.1    Hubel, A.2    Schöffl, F.3
  • 71
    • 0023805040 scopus 로고
    • Abnormal protein as the trigger for the induction of stress responses: Heat, diamide and sodium arsenite
    • Lee K-J and Hahn G M 1988 Abnormal protein as the trigger for the induction of stress responses: Heat, diamide and sodium arsenite; J. Cell. Physiol. 136 411-420
    • (1988) J. Cell. Physiol. , vol.136 , pp. 411-420
    • Lee, K.-J.1    Hahn, G.M.2
  • 72
    • 0032523882 scopus 로고    scopus 로고
    • Regulation of gene expression by TBP-associated proteins
    • Lee T I and Young R A 1998 Regulation of gene expression by TBP-associated proteins; Genes Dev. 12 1398-1408
    • (1998) Genes Dev. , vol.12 , pp. 1398-1408
    • Lee, T.I.1    Young, R.A.2
  • 73
    • 0023191088 scopus 로고
    • Effect of cycloheximide or puromycin on induction of thermotolerance by sodium arsenite in Chinese hamster ovary cells: Involvement of heat shock proteins
    • Lee Y L and Dewey WC 1987 Effect of cycloheximide or puromycin on induction of thermotolerance by sodium arsenite in Chinese hamster ovary cells: Involvement of heat shock proteins; J Cell. Physiol. 132 41-48
    • (1987) J Cell. Physiol. , vol.132 , pp. 41-48
    • Lee, Y.L.1    Dewey, W.C.2
  • 74
    • 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 and Sistonen L 1997 Overexpression of HSF2-beta inhibits hemin-induced heat shock gene expression and erythroid differentiation in K562 cells; J. Biol. Chem. 272 15293-15298
    • (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
  • 76
    • 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 and Thiele D J 1997 Conservation of a stress response: human heat shock transcription factors functionally substitute for yeast Hsf; EMBO J. 16 6466-6477
    • (1997) EMBO J. , vol.16 , pp. 6466-6477
    • Liu, X.D.1    Liu, P.C.C.2    Santoro, N.3    Thiele, D.J.4
  • 78
    • 0030910075 scopus 로고    scopus 로고
    • Intracellular distribution and identification of the nuclear localization signals of two plant heat-stress transcription factors
    • Lyck R, Harmening U, Höhfeld I, Treuter E, Scharf K-D and Nover L 1997 Intracellular distribution and identification of the nuclear localization signals of two plant heat-stress transcription factors; Planta 202 117-125
    • (1997) Planta , vol.202 , pp. 117-125
    • Lyck, R.1    Harmening, U.2    Höhfeld, I.3    Treuter, E.4    Scharf, K.-D.5    Nover, L.6
  • 80
    • 0017783206 scopus 로고
    • Translation in vitro of Drosophila heat shock messages
    • McKenzie S L and Meselson M 1977 Translation in vitro of Drosophila heat shock messages; J. Mol. Biol. 117 279-283
    • (1977) J. Mol. Biol. , vol.117 , pp. 279-283
    • McKenzie, S.L.1    Meselson, M.2
  • 81
    • 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 Z, Shao L, Graves K and Benjamin I J 1998 Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis; J. Biol. Chem. 273 7523-7528
    • (1998) J. Biol. Chem. , vol.273 , pp. 7523-7528
    • McMillan, D.R.1    Xiao, X.Z.2    Shao, L.3    Graves, K.4    Benjamin, I.J.5
  • 82
    • 0031006855 scopus 로고    scopus 로고
    • Xenopus heat shock factor 1 is a nuclear protein before heat stress
    • Mercier P A, Foksa J, Ovsenek N and Westwood J T 1997 Xenopus heat shock factor 1 is a nuclear protein before heat stress; J. Biol. Chem. 272 14147-14151
    • (1997) J. Biol. Chem. , vol.272 , pp. 14147-14151
    • Mercier, P.A.1    Foksa, J.2    Ovsenek, N.3    Westwood, J.T.4
  • 83
    • 0028260658 scopus 로고
    • Characterization of denatured protein inducers of the heat shock (stress) response in Xenopsu laevis oocytes
    • Mifflin L C and Cohen R E 1994a Characterization of denatured protein inducers of the heat shock (stress) response in Xenopsu laevis oocytes; J. Biol. Chem. 269 15710-15717
    • (1994) J. Biol. Chem. , vol.269 , pp. 15710-15717
    • Mifflin, L.C.1    Cohen, R.E.2
  • 84
    • 0028199083 scopus 로고
    • Hsc70 moderates the heat shock (stress) response in Xenopus laevis oocytes and binds to denatured protein inducers
    • Mifflin L C and Cohen R E 1994b Hsc70 moderates the heat shock (stress) response in Xenopus laevis oocytes and binds to denatured protein inducers; J. Biol. Chem. 269 15718-15723
    • (1994) J. Biol. Chem. , vol.269 , pp. 15718-15723
    • Mifflin, L.C.1    Cohen, R.E.2
  • 85
    • 0006849332 scopus 로고
    • Expression of human HSP70 during the synthetic phase of the cell cycle
    • Milarski K L and Morimoto R I 1986 Expression of human HSP70 during the synthetic phase of the cell cycle; Proc. Natl. Acad. Sci. USA 83 9517-9522
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9517-9522
    • Milarski, K.L.1    Morimoto, R.I.2
  • 86
    • 0030907038 scopus 로고    scopus 로고
    • Modulation of the Escherichia coli sigma(E) (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins
    • Missiakas D, Maycr M P, Lemaire M, Georgopoulos C and Raina S 1997 Modulation of the Escherichia coli sigma(E) (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins; Mol. Microbiol. 24 355-371
    • (1997) Mol. Microbiol. , vol.24 , pp. 355-371
    • Missiakas, D.1    Maycr, M.P.2    Lemaire, M.3    Georgopoulos, C.4    Raina, S.5
  • 87
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas D and Raina S 1997a Protein folding in the bacterial periplasm; J. Bacteriol. 179 2465-2471
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 88
    • 0030976053 scopus 로고    scopus 로고
    • Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: Role of two new phsophoprotein phosphatases PrpA and PrpB
    • Missiakas D and Raina S 1997b Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phsophoprotein phosphatases PrpA and PrpB; EMBO J. 16 1670-1685
    • (1997) EMBO J. , vol.16 , pp. 1670-1685
    • Missiakas, D.1    Raina, S.2
  • 89
    • 0031048280 scopus 로고    scopus 로고
    • The Skn7 response regulator controls gene expression in the oxidative stress response of the budding yeast Saccharomyces cerevisiae
    • Morgan B A, Banks G R, Toone W M, Raitt D, Kuge S and Johnston L H 1997 The Skn7 response regulator controls gene expression in the oxidative stress response of the budding yeast Saccharomyces cerevisiae; EMBO J. 16 1035-1044
    • (1997) EMBO J. , vol.16 , pp. 1035-1044
    • Morgan, B.A.1    Banks, G.R.2    Toone, W.M.3    Raitt, D.4    Kuge, S.5    Johnston, L.H.6
  • 90
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori K, Sant A, Kohno K, Normington K, Gething M J and Sambrook J F 1992 A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins; EMBO J. 11 2583-2593
    • (1992) EMBO J. , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.J.5    Sambrook, J.F.6
  • 91
    • 0027522356 scopus 로고
    • Cells in stress - transcriptional activation of heat shock genes
    • Morimoto R I 1993 Cells in stress - transcriptional activation of heat shock genes; Science 259 1409-1410
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.I.1
  • 92
    • 0027202273 scopus 로고
    • The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70
    • Mosser D D, Duchaine J and Massie B 1993 The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70; Mol. Cell. Biol. 13 5427-5438
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5427-5438
    • Mosser, D.D.1    Duchaine, J.2    Massie, B.3
  • 93
    • 0028040816 scopus 로고
    • Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells
    • Murphy S P, Gorzowski J J, Sarge K D and Phillips B 1994 Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells; Mol. Cell. Biol. 14 5309-5317
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5309-5317
    • Murphy, S.P.1    Gorzowski, J.J.2    Sarge, K.D.3    Phillips, B.4
  • 94
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: Estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf 1 and the aryl hydrocarbon receptor
    • Nair S C, Toran E J, Rimerman R A, Hyermstad S, Smithgall T E and Smith D F 1996 A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf 1 and the aryl hydrocarbon receptor; Cell Stress Chap. 1 237-250
    • (1996) Cell Stress Chap. , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hyermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 96
    • 0029121347 scopus 로고
    • The DNA-binding properties of two heat shock factors, Hsf1 and Hsf3, are induced in the avian erythroblast cell line HD6
    • Nakai A, Kawazoe Y, Tanabe M, Nagata K and Morimoto R I 1995 The DNA-binding properties of two heat shock factors, Hsf1 and Hsf3, are induced in the avian erythroblast cell line HD6; Mol. Cell. Biol. 15 5268-5278
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5268-5278
    • Nakai, A.1    Kawazoe, Y.2    Tanabe, M.3    Nagata, K.4    Morimoto, R.I.5
  • 97
    • 0027406535 scopus 로고
    • Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggest a new regulatory pathway
    • Nakai A and Morimoto R I 1993 Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggest a new regulatory pathway; Mol. Cell. Biol. 13 1983-1997
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1983-1997
    • Nakai, A.1    Morimoto, R.I.2
  • 98
    • 0031032550 scopus 로고    scopus 로고
    • HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator
    • Nakai A, Tanabe M, Kawazoe Y, Inazawa J, Morimoto R I and Nagata K 1997 HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator; Mot. Cell. Biol. 17 469-481
    • (1997) Mot. Cell. Biol. , vol.17 , pp. 469-481
    • Nakai, A.1    Tanabe, M.2    Kawazoe, Y.3    Inazawa, J.4    Morimoto, R.I.5    Nagata, K.6
  • 99
    • 0030049318 scopus 로고    scopus 로고
    • The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress
    • Newton E M, Knauf U, Green M and Kingston R E 1996 The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress; Mol. Cell. Biol. 16 839-846
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 839-846
    • Newton, E.M.1    Knauf, U.2    Green, M.3    Kingston, R.E.4
  • 100
    • 0028156829 scopus 로고
    • Increased thermal aggregation of proteins in ATP-depleted mammalian cells
    • Nguyen V T and Bensaude O 1994 Increased thermal aggregation of proteins in ATP-depleted mammalian cells; Eur. J. Biochem. 220 239-246
    • (1994) Eur. J. Biochem. , vol.220 , pp. 239-246
    • Nguyen, V.T.1    Bensaude, O.2
  • 101
    • 0025122831 scopus 로고
    • The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions
    • Nieto-Sotelo J, Wiederrecht G, Okuda A and Parker CS 1990 The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions; Cell 62 807-817
    • (1990) Cell , vol.62 , pp. 807-817
    • Nieto-Sotelo, J.1    Wiederrecht, G.2    Okuda, A.3    Parker, C.S.4
  • 102
    • 0030834398 scopus 로고    scopus 로고
    • Suppression of the Saccharomyces cerevisiae hac1/ire 15 mutation by yeast genes and human cDNAs
    • Nikawa J, Sugiyama M, Hayashi K and Nakashima A 1997 Suppression of the Saccharomyces cerevisiae hac1/ire 15 mutation by yeast genes and human cDNAs; Gene 201 5-10
    • (1997) Gene , vol.201 , pp. 5-10
    • Nikawa, J.1    Sugiyama, M.2    Hayashi, K.3    Nakashima, A.4
  • 103
    • 0023306058 scopus 로고
    • Expression of heat shock genes in homologous and heterologous systems
    • Nover L 1987 Expression of heat shock genes in homologous and heterologous systems; Enzyme Microb. Technol. 9 130-144
    • (1987) Enzyme Microb. Technol. , vol.9 , pp. 130-144
    • Nover, L.1
  • 106
    • 0030818414 scopus 로고    scopus 로고
    • Heat stress proteins and transcription factors
    • Nover L and Scharf K-D 1997 Heat stress proteins and transcription factors; Cell. Mol. Life Sci. 53 80-103
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 80-103
    • Nover, L.1    Scharf, K.-D.2
  • 108
    • 0024639409 scopus 로고
    • Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs
    • Nover L, Scharf K-D and Neumann D 1989 Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs; Mol. Cell. Biol. 9 1298-1308
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1298-1308
    • Nover, L.1    Scharf, K.-D.2    Neumann, D.3
  • 109
    • 0029112851 scopus 로고
    • Heat shock factor-1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells
    • Nunes S L and Calderwood S K 1995 Heat shock factor-1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells; Biochem. Biophys. Res. Commun. 213 1-6
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 1-6
    • Nunes, S.L.1    Calderwood, S.K.2
  • 110
    • 0032489013 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The last 200 nanometers
    • Ohno M, Fornerod M and Mattaj I W 1998 Nucleocytoplasmic transport: The last 200 nanometers; Cell 92 327-336
    • (1998) Cell , vol.92 , pp. 327-336
    • Ohno, M.1    Fornerod, M.2    Mattaj, I.W.3
  • 111
    • 0029860750 scopus 로고    scopus 로고
    • Regulation of Drosophila heat shock factor trimerization: Global sequence requirements and independence of nuclear localization
    • Orosz A, Wisniewski J and Wu C 1996 Regulation of Drosophila heat shock factor trimerization: Global sequence requirements and independence of nuclear localization; Mol. Cell. Biol. 16 7018-7030
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7018-7030
    • Orosz, A.1    Wisniewski, J.2    Wu, C.3
  • 112
    • 0026063035 scopus 로고
    • Interactions of Hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros D R, Welch W J and Fink A L 1991 Interactions of Hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding; Proc. Natl. Acad. Sci. USA 88 5719-5723
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 113
    • 0020184673 scopus 로고
    • A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene
    • Pelham H R B 1982 A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene; Cell 30 517-528
    • (1982) Cell , vol.30 , pp. 517-528
    • Pelham, H.R.B.1
  • 114
    • 0020341083 scopus 로고
    • A synthetic heat-shock promoter element confers heat-inducibility on the Herpes simplex virus thymidine kinase gene
    • Pelham H R B and Bienz M 1982 A synthetic heat-shock promoter element confers heat-inducibility on the Herpes simplex virus thymidine kinase gene; EMBO J. 1 1473-1477
    • (1982) EMBO J. , vol.1 , pp. 1473-1477
    • Pelham, H.R.B.1    Bienz, M.2
  • 115
    • 0026621935 scopus 로고
    • Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil
    • Peteranderl R and Nelson H C M 1992 Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil; Biochemistry 31 12272-12276
    • (1992) Biochemistry , vol.31 , pp. 12272-12276
    • Peteranderl, R.1    Nelson, H.C.M.2
  • 116
    • 0025740514 scopus 로고
    • Denaturation of proteins during heat shock - In vivo recovery of solubility and activity of reporter enzymes
    • Pinto M, Morange M and Bensaude O 1991 Denaturation of proteins during heat shock - In vivo recovery of solubility and activity of reporter enzymes; J. Biol. Chem. 266 13941-13946
    • (1991) J. Biol. Chem. , vol.266 , pp. 13941-13946
    • Pinto, M.1    Morange, M.2    Bensaude, O.3
  • 117
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • Pogliano J, Lynch A S, Belin D, Lin E C C and Beckwith J 1997 Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system; Genes Dev. 11 1169-1182
    • (1997) Genes Dev. , vol.11 , pp. 1169-1182
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lin, E.C.C.4    Beckwith, J.5
  • 119
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimerization: Role of a conserved leucine zipper
    • Rabindran S K, Haroun R I, Clos J, Wisniewski J and Wu C 1993 Regulation of heat shock factor trimerization: Role of a conserved leucine zipper; Science 259 230-234
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 120
    • 0028025643 scopus 로고
    • Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNBA-binding activity in vivo
    • Rabindran S K, Wisniewski J, Li L, Li G C and Wu C 1994 Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNBA-binding activity in vivo; Mol. Cell. Biol. 14 6552-6560
    • (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
  • 122
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa F 1962 A new puffing pattern induced by temperature shock and DNP in Drosophila; Experientia 18 571-573
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 123
    • 0031972647 scopus 로고    scopus 로고
    • Heat shock factor increases the reinitiation rate from potentiated chromatin templates
    • Sandaltzopoulos R and Becker P B 1998 Heat shock factor increases the reinitiation rate from potentiated chromatin templates; Mol. Cell. Biol. 18 361-367
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 361-367
    • Sandaltzopoulos, R.1    Becker, P.B.2
  • 124
    • 0027461364 scopus 로고
    • Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity and nuclear localization and can occur in the absence of stress
    • Sarge K D, Murphy S P and Morimoto R I 1993 Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity and nuclear localization and can occur in the absence of stress; Mo. Clell. Biol. 13 1392-1407
    • (1993) Mo. Clell. Biol. , vol.13 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 125
    • 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 and Morimoto R I 1994 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) 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
  • 126
    • 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 and Morimoto R I 1991 Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA binding ability; Genes Dev. 5 1902-1911
    • (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
  • 127
    • 0031948387 scopus 로고    scopus 로고
    • The tomato Hsf system: HsfA2 needs interaction with HsAf1 for efficient nuclear import and may be localized in cytoplasmic heat stress granules
    • Scharf K-D, Heider H, Höhfeld I, Lyck R, Schmidt E and Nover L 1998 The tomato Hsf system: HsfA2 needs interaction with HsAf1 for efficient nuclear import and may be localized in cytoplasmic heat stress granules; Mol. Cell. Biol. 18 2240-2251
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2240-2251
    • Scharf, K.-D.1    Heider, H.2    Höhfeld, I.3    Lyck, R.4    Schmidt, E.5    Nover, L.6
  • 129
  • 130
    • 0025686194 scopus 로고
    • Three tomato genes code for heat stress transcription factors with a region of remarkable homology to the DNA-binding domain of the yeast HSF
    • Scharf K-D, Rose S, Zott W, Schoeffl F and Nover L 1990 Three tomato genes code for heat stress transcription factors with a region of remarkable homology to the DNA-binding domain of the yeast HSF; EMBO J. 9 4495-4501
    • (1990) EMBO J. , vol.9 , pp. 4495-4501
    • Scharf, K.-D.1    Rose, S.2    Zott, W.3    Schoeffl, F.4    Nover, L.5
  • 132
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder H, Langer T, Hartl F-U and Bukau B 1993 DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage; EMBO J. 12 4137-4144
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.-U.3    Bukau, B.4
  • 134
    • 0029943714 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of the tomato heat stress transcription factor HSF24
    • Schultheiss J, Kunert O, Gase U, Scharf K-D, Nover L and Rüterjans H 1996 Solution structure of the DNA-binding domain of the tomato heat stress transcription factor HSF24; Eur. J. Biochem. 236 911-921
    • (1996) Eur. J. Biochem. , vol.236 , pp. 911-921
    • Schultheiss, J.1    Kunert, O.2    Gase, U.3    Scharf, K.-D.4    Nover, L.5    Rüterjans, H.6
  • 135
    • 0027177579 scopus 로고
    • Hydrophobic coiled-coil domains regulate the subcellular localization of human heat shock factor-2
    • Sheldon L A and Kingston R E 1993 Hydrophobic coiled-coil domains regulate the subcellular localization of human heat shock factor-2; Genes Dev. 7 1549-1558
    • (1993) Genes Dev. , vol.7 , pp. 1549-1558
    • Sheldon, L.A.1    Kingston, R.E.2
  • 136
    • 0029025078 scopus 로고
    • The carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive
    • Shi Y, Kroeger P E and Morimoto R I 1995 The carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive; Mol. Cell. Biol. 15 4309-4318
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4309-4318
    • Shi, Y.1    Kroeger, P.E.2    Morimoto, R.I.3
  • 137
    • 0026643651 scopus 로고
    • The transport of proteins into the nucleus requires the 70 kilodalton heat shock protein or its cytosolic cognate
    • Shi Y G and Thomas J O 1992 The transport of proteins into the nucleus requires the 70 kilodalton heat shock protein or its cytosolic cognate; Mol. Cell. Biol. 12 2186-2192
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2186-2192
    • Shi, Y.G.1    Thomas, J.O.2
  • 138
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi Y H, Mosser D D and Morimoto R I 1998 Molecular chaperones as HSF1-specific transcriptional repressors; Genes Dev. 12 654-666
    • (1998) Genes Dev. , vol.12 , pp. 654-666
    • Shi, Y.H.1    Mosser, D.D.2    Morimoto, R.I.3
  • 139
    • 0029960517 scopus 로고    scopus 로고
    • In vivo nuclear transport kinetics in Saccharomyces cerevisiae - a role for heat shock protein 70 during targeting and translocation
    • Shulga N, Roberts P, Gu Z Y, Spitx L, Tabb M M, Nomura M and Goldfarb D S 1996 In vivo nuclear transport kinetics in Saccharomyces cerevisiae - a role for heat shock protein 70 during targeting and translocation; J. Cell Biol. 135 329-339
    • (1996) J. Cell Biol. , vol.135 , pp. 329-339
    • Shulga, N.1    Roberts, P.2    Gu, Z.Y.3    Spitx, L.4    Tabb, M.M.5    Nomura, M.6    Goldfarb, D.S.7
  • 140
    • 0030297538 scopus 로고    scopus 로고
    • tRNA ligase is required for regulated tRNA splicing in the unfolded protein response
    • Sidrauski C, Cox J S and Walter P 1996 tRNA ligase is required for regulated tRNA splicing in the unfolded protein response; Cell 87 405-413
    • (1996) Cell , vol.87 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 141
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • Sidrauski C and Walter P 1997 The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response; Cell 90 1031-1039
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 142
    • 0028314945 scopus 로고
    • Human heat shock factors 1 and 2 are differentially activated and can synergistically induce Hsp70 gene transcription
    • Sistonen L, Sarge K D and Morimoto R I 1994 Human heat shock factors 1 and 2 are differentially activated and can synergistically induce Hsp70 gene transcription; Mol. Cell. Biol. 14 2087-2099
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2087-2099
    • Sistonen, L.1    Sarge, K.D.2    Morimoto, R.I.3
  • 143
    • 0026746491 scopus 로고
    • Activation of heat shock factor 2 during hmien-induccd differentiation of human erythreoleukemia cells
    • Sistonen L, Sarge K D, Phillips B, Abravaya K and Morimoto R I 1992 Activation of heat shock factor 2 during hmien-induccd differentiation of human erythreoleukemia cells; Mo.l Cell. Biol. 12 4104-4111
    • (1992) Mo.l Cell. Biol. , vol.12 , pp. 4104-4111
    • Sistonen, L.1    Sarge, K.D.2    Phillips, B.3    Abravaya, K.4    Morimoto, R.I.5
  • 144
    • 0024852809 scopus 로고
    • Trimerization of a yeast transcriptional activator via a coiled-coil motif
    • Sorger P K and Nelson H C M 1989 Trimerization of a yeast transcriptional activator via a coiled-coil motif; Cell 59 807-813
    • (1989) Cell , vol.59 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.M.2
  • 145
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger P K and Pelham H R B 1988 Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation; Cell 54 855-864
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 147
    • 0025218811 scopus 로고
    • Self-regulation of 70-kilodalton heat shock proteins in Saccharomyces cerevisiae
    • Stone D E and Craig E A 1990 Self-regulation of 70-kilodalton heat shock proteins in Saccharomyces cerevisiae; Mol. Cell. Biol. 10 1622-1632
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1622-1632
    • Stone, D.E.1    Craig, E.A.2
  • 148
    • 0030054054 scopus 로고    scopus 로고
    • Chromatin structure and RNA polymerase II connection - Implications for transcription
    • Struhl K 1996 Chromatin structure and RNA polymerase II connection - Implications for transcription; Cell 84 179-182
    • (1996) Cell , vol.84 , pp. 179-182
    • Struhl, K.1
  • 149
    • 0032503940 scopus 로고    scopus 로고
    • The TAFs in the HAT
    • Struhl K and Moqtaderi Z 1998 The TAFs in the HAT; Cell 94 1-4
    • (1998) Cell , vol.94 , pp. 1-4
    • Struhl, K.1    Moqtaderi, Z.2
  • 150
    • 0029100782 scopus 로고
    • The cDNA encoding Xenopus laevis heat-shock factor 1(XHsf1)-nucleotidc and deduced amino-acid sequences and properties of the encoded protein
    • Stump D G, Landsberger N and Wolffe A P 1995 The cDNA encoding Xenopus laevis heat-shock factor 1(XHsf1)-nucleotidc and deduced amino-acid sequences and properties of the encoded protein; Gene 160 207-211
    • (1995) Gene , vol.160 , pp. 207-211
    • Stump, D.G.1    Landsberger, N.2    Wolffe, A.P.3
  • 151
    • 0032536772 scopus 로고    scopus 로고
    • Disruption of the HSF3 gene results in the severe reduction of heat shock gene expression and loss of thermotolerance
    • Tanabe M, Kawazoe Y, Takeda S, Morimoto R I, Nagata K and Nakai A 1998 Disruption of the HSF3 gene results in the severe reduction of heat shock gene expression and loss of thermotolerance; EMBO J. 17 1750-1758
    • (1998) EMBO J. , vol.17 , pp. 1750-1758
    • Tanabe, M.1    Kawazoe, Y.2    Takeda, S.3    Morimoto, R.I.4    Nagata, K.5    Nakai, A.6
  • 152
    • 0030920718 scopus 로고    scopus 로고
    • Different thresholds in the responses of two heat shock transcription factors, HSF1 and HSF3
    • Tanabe M, Nakai A, Kawazoe Y and Nagata K 1997 Different thresholds in the responses of two heat shock transcription factors, HSF1 and HSF3; J. Biol. Chem. 272 15389-15395
    • (1997) J. Biol. Chem. , vol.272 , pp. 15389-15395
    • Tanabe, M.1    Nakai, A.2    Kawazoe, Y.3    Nagata, K.4
  • 153
    • 0021171377 scopus 로고
    • Alterations of transcription and translation in HeLa cells exposed to amino acid analogs
    • Thomas G P and Mathews M B 1984 Alterations of transcription and translation in HeLa cells exposed to amino acid analogs; Mol Cell. Biol. 4 1063-1072
    • (1984) Mol Cell. Biol. , vol.4 , pp. 1063-1072
    • Thomas, G.P.1    Mathews, M.B.2
  • 154
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of D melanogaster Relation to chromosome puffs
    • Tissieres A, Mitchell H K and Tracy U M 1974 Protein synthesis in salivary glands of D melanogaster Relation to chromosome puffs; J. Mol Biol. 84 389-398
    • (1974) J. Mol Biol. , vol.84 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 155
    • 0027163642 scopus 로고
    • Promoter specificity and deletion analysis.of three heat stress transcription factors of tomato
    • Treuter E, Nover L, Ohme K and Scharf K-D 1993 Promoter specificity and deletion analysis.of three heat stress transcription factors of tomato; Mol. Gen. Genet. 240 113-125
    • (1993) Mol. Gen. Genet. , vol.240 , pp. 113-125
    • Treuter, E.1    Nover, L.2    Ohme, K.3    Scharf, K.-D.4
  • 156
    • 0030756675 scopus 로고    scopus 로고
    • Induced alpha helix in the VP16 activation domain upon binding to a humanTAF
    • Uesugi M, Nyanguile O, Lu H, Levine A J and Verdine G L 1997 Induced alpha helix in the VP16 activation domain upon binding to a humanTAF; Science 277 1310-1313
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 157
    • 0028500990 scopus 로고
    • Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor
    • Vuister G W, Kim S-J, Orosz A, Marquardt J, Wu C and Bax A 1994 Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor; Nature Struct Biol 1 605-614
    • (1994) Nature Struct Biol , vol.1 , pp. 605-614
    • Vuister, G.W.1    Kim, S.-J.2    Orosz, A.3    Marquardt, J.4    Wu, C.5    Bax, A.6
  • 158
    • 0024670024 scopus 로고
    • Yeast Hsp70 RNA levels vary in response to the physiological status of the cell
    • Werner-Washburne M, Becker J, Kosic-Smithers J and Craig E A 1989 Yeast Hsp70 RNA levels vary in response to the physiological status of the cell; J. Bacterial. 171 2680-2688
    • (1989) J. Bacterial. , vol.171 , pp. 2680-2688
    • Werner-Washburne, M.1    Becker, J.2    Kosic-Smithers, J.3    Craig, E.A.4
  • 159
    • 0027159173 scopus 로고
    • Activation of Drosophila heat shock factor - Conformational change associated with a monomer-to-trimer transition
    • Westwood J T and Wu C 1993 Activation of Drosophila heat shock factor - Conformational change associated with a monomer-to-trimer transition; Mol. Cell. Biol. 13 3481-3486
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3481-3486
    • Westwood, J.T.1    Wu, C.2
  • 160
    • 0024282788 scopus 로고
    • Isolation of the gene encoding the S. cerevisiae heat shock transcription factor
    • Wiederrecht G, Seto D and Parker CS 1988 Isolation of the gene encoding the S. cerevisiae heat shock transcription factor; Cell 54 841-853
    • (1988) Cell , vol.54 , pp. 841-853
    • Wiederrecht, G.1    Seto, D.2    Parker, C.S.3
  • 161
    • 0029670087 scopus 로고    scopus 로고
    • The C-terminal region of Drosophila heat shock factor (Hsf) contains a constitutively functional transactivation domain
    • Wisniewski J, Orosz A, Allada R and Wu C 1996 The C-terminal region of Drosophila heat shock factor (Hsf) contains a constitutively functional transactivation domain; Nucleic Acids Res. 24 367-374
    • (1996) Nucleic Acids Res. , vol.24 , pp. 367-374
    • Wisniewski, J.1    Orosz, A.2    Allada, R.3    Wu, C.4
  • 162
    • 0029564954 scopus 로고
    • Heat stress transcription factors
    • Wu C 1995 Heat stress transcription factors; Annu. Rev. Cell Biol, 11, 441-469
    • (1995) Annu. Rev. Cell Biol , vol.11 , pp. 441-469
    • Wu, C.1
  • 163
    • 0031055277 scopus 로고    scopus 로고
    • Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers
    • Xia W L and Voellmy R 1997 Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers; J. Biol. Chem. 272 4094-4102
    • (1997) J. Biol. Chem. , vol.272 , pp. 4094-4102
    • Xia, W.L.1    Voellmy, R.2
  • 164
    • 0027960539 scopus 로고
    • A highly conserved domain of RNA polymerase II shares a functional element with acidic activation domains of upstream transcription factors
    • Xiao H, Friesen J D and Lis J T 1994 A highly conserved domain of RNA polymerase II shares a functional element with acidic activation domains of upstream transcription factors; Mol. Cell. Biol. 14 7507-7516
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7507-7516
    • Xiao, H.1    Friesen, J.D.2    Lis, J.T.3
  • 165
    • 0031447219 scopus 로고    scopus 로고
    • Overexpression of unliganded steroid receptors activates endogenous heat shock factor
    • Xiao N Q and DeFranco D B 1997 Overexpression of unliganded steroid receptors activates endogenous heat shock factor; Mol. Endocrinol. 11 1365-1374
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1365-1374
    • Xiao, N.Q.1    DeFranco, D.B.2
  • 166
    • 0028136156 scopus 로고
    • Differential roles of heat shock protein 70 in the in vitro nuclear import of glucocorticoid receptor and simian virus 40 large tumor antigen
    • Yang J and Defranco D B 1994 Differential roles of heat shock protein 70 in the in vitro nuclear import of glucocorticoid receptor and simian virus 40 large tumor antigen; Mol. Cell. Biol. 14 5088-5098
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5088-5098
    • Yang, J.1    Defranco, D.B.2
  • 167
    • 0031473993 scopus 로고    scopus 로고
    • Expression of human heat shock transcription factors 1 and 2 in HeLa cells and yeast
    • Yuan C-X, Czarnecka-Verner E and Gurley WB 1997 Expression of human heat shock transcription factors 1 and 2 in HeLa cells and yeast; Cell Stress Chap. 2 263-275
    • (1997) Cell Stress Chap. , vol.2 , pp. 263-275
    • Yuan, C.-X.1    Czarnecka-Verner, E.2    Gurley, W.B.3
  • 168
    • 0030089685 scopus 로고    scopus 로고
    • Regulation and conservation of the heat-shock transcription factor sigma 32
    • Yura T 1996 Regulation and conservation of the heat-shock transcription factor sigma 32; Genes Cells 1 277-284
    • (1996) Genes Cells , vol.1 , pp. 277-284
    • Yura, T.1
  • 169
    • 0030911696 scopus 로고    scopus 로고
    • Nuclear entry, oligomerization and DNA binding of the Drosophila heat shock transcription factor are regulated by a unique nuclear localization sequence
    • Zandi E, Tran T N T, Chamberlain W and Parker C S 1997 Nuclear entry, oligomerization and DNA binding of the Drosophila heat shock transcription factor are regulated by a unique nuclear localization sequence; Genes Dev. 11 1299-1314
    • (1997) Genes Dev. , vol.11 , pp. 1299-1314
    • Zandi, E.1    Tran, T.N.T.2    Chamberlain, W.3    Parker, C.S.4
  • 170
    • 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 and 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
  • 171
    • 0029055176 scopus 로고
    • Multiple layers of regulation of human heat shock transcription factor 1
    • Zuo J, Rungger D and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.