메뉴 건너뛰기




Volumn 6, Issue 7, 1992, Pages 1153-1164

The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression

Author keywords

Heat shock protein; Heat shock transcription factor; Human hsp70 gene

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL EXTRACT; HEAT SHOCK PROTEIN; MONOCLONAL ANTIBODY; PROTEIN ANTIBODY; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR;

EID: 0026665975     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.6.7.1153     Document Type: Article
Times cited : (428)

References (78)
  • 1
    • 0026033076 scopus 로고
    • Heat shock-induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting
    • Abravaya, K., B. Phillips, and R.I. Morimoto. 1991a. Heat shock-induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting. Mol Cell. Biol. 11: 586-592.
    • (1991) Mol Cell. Biol. , vol.11 , pp. 586-592
    • Abravaya, K.1    Phillips, B.2    Morimoto, R.I.3
  • 2
    • 0025935407 scopus 로고
    • Attenuation of the heat response in HeLa cells is mediated by the release of bound heat shock transcription factor and is modulated by changes in growth and heat shock temperatures
    • _. 1991b. Attenuation of the heat response in HeLa cells is mediated by the release of bound heat shock transcription factor and is modulated by changes in growth and heat shock temperatures. Genes & Dev. 5: 2117-2127.
    • (1991) Genes & Dev. , vol.5 , pp. 2117-2127
  • 3
    • 0023694311 scopus 로고
    • Key features of heat shock regulatory elements
    • Amin, J., J. Ananthan, and R. Voellmy. 1988. Key features of heat shock regulatory elements. Mol Cell. Biol. 8: 3761-3769.
    • (1988) Mol Cell. Biol. , vol.8 , pp. 3761-3769
    • Amin, J.1    Ananthan, J.2    Voellmy, R.3
  • 4
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • Ananthan, J., A.L. Goldberg, and R. Voellmy. 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    Voellmy, R.3
  • 5
    • 0026033385 scopus 로고
    • IP-I: A dominant inhibitor of fos/jun whose activity is modulated by phosphorylation
    • Auwerx, J. and P. Sassone-Corsi. 1991. IP-I: A dominant inhibitor of fos/jun whose activity is modulated by phosphorylation. Cell 64: 983-993.
    • (1991) Cell , vol.64 , pp. 983-993
    • Auwerx, J.1    Sassone-Corsi, P.2
  • 6
    • 0024294357 scopus 로고
    • Activation of DNA-binding is an apparently cytoplasmic precursor of the NF-kB transcription factor
    • Baeuerle, P.A. and D. Baltimore. 1988. Activation of DNA-binding is an apparently cytoplasmic precursor of the NF-kB transcription factor. Cell 53: 211-217.
    • (1988) Cell , vol.53 , pp. 211-217
    • Baeuerle, P.A.1    Baltimore, D.2
  • 7
    • 0025303147 scopus 로고
    • Interaction of hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann, R.P., L.A. Mizzen, and W.J. Welch. 1990. Interaction of hsp70 with newly synthesized proteins: Implications for protein folding and assembly. Science 248: 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 8
    • 0025238437 scopus 로고
    • The protein Id: A negative regulator of helix-loop-helix DNA binding proteins
    • Benezra, R., R.L. Davis, D. Lockshon, D.L. Turner, and H. Weintraub. 1990. The protein Id: A negative regulator of helix-loop-helix DNA binding proteins. Cell 61: 49-59.
    • (1990) Cell , vol.61 , pp. 49-59
    • Benezra, R.1    Davis, R.L.2    Lockshon, D.3    Turner, D.L.4    Weintraub, H.5
  • 9
    • 0025351346 scopus 로고
    • Transcriptional regulation of ssa3, an hsp70 gene from Saccharomyces cerevisae
    • Boorstein, W.R. and E.A. Craig. 1990. Transcriptional regulation of ssa3, an hsp70 gene from Saccharomyces cerevisae. Mol Cell Biol. 10: 3262-3267.
    • (1990) Mol Cell Biol. , vol.10 , pp. 3262-3267
    • Boorstein, W.R.1    Craig, E.A.2
  • 10
  • 12
    • 0023968426 scopus 로고
    • Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: In vitro dissociation of hsc70 and dnaK from murine p53 by ATP
    • Clarke, C.F., K. Cheng, A.B. Frey, R. Stein, P.H. Hinds, and A.J. Levine. 1988. Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: In vitro dissociation of hsc70 and dnaK from murine p53 by ATP. Mol. Cell. Biol. 8: 1206-1215.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1206-1215
    • Clarke, C.F.1    Cheng, K.2    Frey, A.B.3    Stein, R.4    Hinds, P.H.5    Levine, A.J.6
  • 13
    • 0025606431 scopus 로고
    • Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation
    • Clos, J., J.T. Westwood, P.B. Becker, S. Wilson, K. Lambert, and C. Wu. 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, K.5    Wu, C.6
  • 14
    • 0025967766 scopus 로고
    • Is hsp70 the cellular thermometer?
    • Craig, E. and C.A. Gross. 1991. Is hsp70 the cellular thermometer? Trends Biochem. Sci. 16: 135-140.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 135-140
    • Craig, E.1    Gross, C.A.2
  • 15
    • 0021685896 scopus 로고
    • Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth
    • Craig, E.A. and K. Jakobsen. 1984. Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth. Cell 38: 841-849.
    • (1984) Cell , vol.38 , pp. 841-849
    • Craig, E.A.1    Jakobsen, K.2
  • 16
    • 0020409205 scopus 로고
    • The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels
    • DiDomenico, B.T., G.E. Bugaisky, and S. Lindquist. 1982. The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels. Cell 31: 593-603.
    • (1982) Cell , vol.31 , pp. 593-603
    • DiDomenico, B.T.1    Bugaisky, G.E.2    Lindquist, S.3
  • 17
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of protein assembly
    • Flynn, G.C., T.G. Chappell, and J.E. Rothman. 1989. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245: 385-390.
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 18
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BIP
    • Flynn, G.G., J. Pohl, M.T. Flocco, and J.E. Rothman. 1991. Peptide-binding specificity of the molecular chaperone BIP. Na-tute 353: 726-730.
    • (1991) Na-tute , vol.353 , pp. 726-730
    • Flynn, G.G.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 19
    • 0025825895 scopus 로고
    • Modular structure of transcription factors: Implications for gene regulation
    • Frankel, A.D. and P.S. Kim. 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
  • 20
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J. and J. Sambrook. 1992. Protein folding in the cell. Nature 355: 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 21
    • 0022344755 scopus 로고
    • Production of abnormal proteins in E. coli stimulates transcription of Ion and other heat shock genes
    • Goff, S.A. and A.L. Goldberg. 1985. Production of abnormal proteins in E. coli stimulates transcription of Ion and other heat shock genes. Cell 41: 587-595.
    • (1985) Cell , vol.41 , pp. 587-595
    • Goff, S.A.1    Goldberg, A.L.2
  • 22
    • 0017710978 scopus 로고
    • Characteristics of a human cell line transformed by DNA from human adenovirus type 5
    • Graham, F.L. and J. Smiley. 1977. Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J. Gen. Virol 36: 59-72.
    • (1977) J. Gen. Virol , vol.36 , pp. 59-72
    • Graham, F.L.1    Smiley, J.2
  • 23
    • 0021225289 scopus 로고
    • The htpR gene product of E. coli is a sigma factor for heat shock promoters
    • Grossman, A.D., J.W. Erikson, and C.A. Gross. 1984. The htpR gene product of E. coli is a sigma factor for heat shock promoters. Cell 38: 383-390.
    • (1984) Cell , vol.38 , pp. 383-390
    • Grossman, A.D.1    Erikson, J.W.2    Gross, C.A.3
  • 25
    • 0023394825 scopus 로고
    • Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p53-plus-ras-transformed cell lines
    • Hinds, P.W., C.A. Finlay, A.B. Frey, and A.J. Levine. 1987. Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p53-plus-ras-transformed cell lines. Mol Cell. Biol. 7: 2863-2869.
    • (1987) Mol Cell. Biol. , vol.7 , pp. 2863-2869
    • Hinds, P.W.1    Finlay, C.A.2    Frey, A.B.3    Levine, A.J.4
  • 26
    • 0000097632 scopus 로고
    • Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70
    • Hunt, C.R. and R.I. Morimoto. 1985. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl. Acad. Sci. 82: 6455-6459.
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , pp. 6455-6459
    • Hunt, C.R.1    Morimoto, R.I.2
  • 27
    • 0023701108 scopus 로고
    • Constitutive binding of yeast heat-shock factor to DNA in vivo
    • Jakobsen, B.K. and H.R.B. Pelham. 1988. Constitutive binding of yeast heat-shock factor to DNA in vivo. Mol. Cell. Biol. 8: 5040-5042.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5040-5042
    • Jakobsen, B.K.1    Pelham, H.R.B.2
  • 28
    • 0025965063 scopus 로고
    • A conserved heptapeptide restrains the activity of the yeast heat shock transcription factor
    • _. 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
  • 29
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich, D.A., L. Sistonen, R.A. Kroes, and R.I. Morimoto. 1992. Effect of sodium salicylate on the human heat shock response. Science 255: 1243-1245.
    • (1992) Science , vol.255 , pp. 1243-1245
    • Jurivich, D.A.1    Sistonen, L.2    Kroes, R.A.3    Morimoto, R.I.4
  • 30
    • 0020857523 scopus 로고
    • Transcriptional activation and subsequent control of the human heat shock gene during adenovirus infection
    • Kao, H.T. and J.R. Nevins. 1983. Transcriptional activation and subsequent control of the human heat shock gene during adenovirus infection. Mol. Cell. Biol. 3: 2058-2065.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 2058-2065
    • Kao, H.T.1    Nevins, J.R.2
  • 32
    • 0023735270 scopus 로고
    • Activation in vitro of a sequence specific DNA binding by a human regulatory factor
    • Larson, J.S., T.J. Schuetz, and R.E. Kingston. 1988. Activation in vitro of a sequence specific DNA binding by a human regulatory factor. Nature 335: 372-375.
    • (1988) Nature , vol.335 , pp. 372-375
    • Larson, J.S.1    Schuetz, T.J.2    Kingston, R.E.3
  • 33
    • 0024430704 scopus 로고
    • Mutational analysis of the human hsp70 protein: Distinct domains for nucleolar localization and adenosine triphosphate binding
    • Milarski, K.L. and R.I. Morimoto. 1989. Mutational analysis of the human hsp70 protein: Distinct domains for nucleolar localization and adenosine triphosphate binding. J. Cell. Biol. 109: 1947-1962.
    • (1989) J. Cell. Biol. , vol.109 , pp. 1947-1962
    • Milarski, K.L.1    Morimoto, R.I.2
  • 34
    • 0024396320 scopus 로고
    • Transcriptional regulation in mammalian cells by sequence specific DNA binding proteins
    • Mitchell, P.J. and R. Tjian. 1989. Transcriptional regulation in mammalian cells by sequence specific DNA binding proteins. Science 245: 371-378.
    • (1989) Science , vol.245 , pp. 371-378
    • Mitchell, P.J.1    Tjian, R.2
  • 35
    • 0001806571 scopus 로고
    • The stress response, functions of the proteins, and perspectives
    • ed. R.I. Morimoto, A. Tissières, and C. Georgopoulus, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Morimoto, R.I., A. Tissières, and C. Georgopoulos. 1990. The stress response, functions of the proteins, and perspectives. In Stress proteins in biology and medicine (ed. R.I. Morimoto, A. Tissières, and C. Georgopoulus), pp. 1-36. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1990) Stress Proteins in Biology and Medicine , pp. 1-36
    • Morimoto, R.I.1    Tissières, A.2    Georgopoulos, C.3
  • 36
    • 0023815651 scopus 로고
    • Coordinate changes in heat shock element binding activity and hsp70 gene transcription rates in human cells
    • Mosser, D.D., N.G. Theodorakis, and R.I. Morimoto. 1988. Coordinate changes in heat shock element binding activity and hsp70 gene transcription rates in human cells. Mol. Cell. Biol. 8: 4736-4744.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4736-4744
    • Mosser, D.D.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 37
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • Mosser, D.D., P.T. Kotzbauer, K.D. Sarge, and R.I. Morimoto. 1990. In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc. Natl. Acad. Sci. 87: 3748-3752.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 38
    • 0026016404 scopus 로고
    • A naturally occuring truncated form of FosB that inhibits fos/jun transcriptional activity
    • Nakabeppu, Y. and D. Nathans. 1991. A naturally occuring truncated form of FosB that inhibits fos/jun transcriptional activity. Cell 64: 751-759.
    • (1991) Cell , vol.64 , pp. 751-759
    • Nakabeppu, Y.1    Nathans, D.2
  • 39
    • 0024465765 scopus 로고
    • The cellular proteins which can associate specifically with polyomavirus middle-T antigen in human 293 cells include the major human 70-kilodalton heat shock proteins
    • Pallas, D.C., W. Morgan, and T.M. Roberts. 1989. The cellular proteins which can associate specifically with polyomavirus middle-T antigen in human 293 cells include the major human 70-kilodalton heat shock proteins. J. Viral. 63: 4533-4539.
    • (1989) J. Viral. , vol.63 , pp. 4533-4539
    • Pallas, D.C.1    Morgan, W.2    Roberts, T.M.3
  • 40
    • 0026063035 scopus 로고
    • Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding
    • Palleros, D.R., W.J. Welch, and A.L. Fink. 1991. Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding. Proc. Natl. Acad. Sci. 88: 5719-5723.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 5719-5723
    • Palleros, D.R.1    Welch, W.J.2    Fink, A.L.3
  • 41
    • 0024709959 scopus 로고
    • Induction of a heat shock-like response by unfolded protein in Escherichia coli: Dependence on protein level not protein degradation
    • Parsell, D.A. and R.T. Sauer. 1989. Induction of a heat shock-like response by unfolded protein in Escherichia coli: Dependence on protein level not protein degradation. Genes & Dev. 3: 1226-1232.
    • (1989) Genes & Dev. , vol.3 , pp. 1226-1232
    • Parsell, D.A.1    Sauer, R.T.2
  • 42
    • 0020184673 scopus 로고
    • A regulatory upstream promoter element in the Drosophila hsp70 heat-shock gene
    • Pelham, H.R.B. 1982. A regulatory upstream promoter element in the Drosophila hsp70 heat-shock gene. Cell 30: 517-528.
    • (1982) Cell , vol.30 , pp. 517-528
    • Pelham, H.R.B.1
  • 43
    • 0022969885 scopus 로고
    • Speculations on the functions of the major heat shock and glucose regulated proteins
    • _. 1986. Speculations on the functions of the major heat shock and glucose regulated proteins. Cell 46: 959-961.
    • (1986) Cell , vol.46 , pp. 959-961
  • 44
    • 0002193920 scopus 로고
    • Functions of the hsp70 protein family: An overview
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • _. 1990. Functions of the hsp70 protein family: An overview. In Stress proteins in biology and medicine (ed. R.I. Morimoto, A. Tissières, and C. Georgopoulus), pp. 287-299. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1990) Stress Proteins in Biology and Medicine , pp. 287-299
    • Morimoto, R.I.1    Tissières, A.2    Georgopoulus, C.3
  • 46
    • 0022637380 scopus 로고
    • Specific interaction between the p53 cellular tumor antigen and major heat shock proteins
    • Pinhasi-Kimhi, O., D. Michalovitz, A. Ben-Zeev, and M. Oren. 1986. Specific interaction between the p53 cellular tumor antigen and major heat shock proteins. Nature 320: 182-185.
    • (1986) Nature , vol.320 , pp. 182-185
    • Pinhasi-Kimhi, O.1    Michalovitz, D.2    Ben-Zeev, A.3    Oren, M.4
  • 47
    • 0025864313 scopus 로고
    • Molecular cloning and expression of a human heat shock factor, HSF1
    • Rabindran, S.K., G. Giorgi, J. Clos, and C. Wu. 1991. Molecular cloning and expression of a human heat shock factor, HSF1. Proc. Natl. Acad. Sci. 88: 6906-6910.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 6906-6910
    • Rabindran, S.K.1    Giorgi, G.2    Clos, J.3    Wu, C.4
  • 48
    • 0022342203 scopus 로고
    • Evidence that the 90 kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
    • Sanchez, E.R., D.O. Toft, M.J. Schlesinger, and W.B. Pratt. 1985. Evidence that the 90 kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem. 260: 12358-12403.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12358-12403
    • Sanchez, E.R.1    Toft, D.O.2    Schlesinger, M.J.3    Pratt, W.B.4
  • 49
    • 0025989349 scopus 로고
    • Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability
    • Sarge, K.D., V. Zimarino, K. Holm, C. Wu, and R.I. Morimoto. 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
  • 50
    • 0024354855 scopus 로고
    • Association of a cellular heat shock protein with simian virus 40 large T antigen in transformed cells
    • Sawai, E.T. and J.S. Butel. 1989. Association of a cellular heat shock protein with simian virus 40 large T antigen in transformed cells. J. Viral 63: 3961-3973.
    • (1989) J. Viral , vol.63 , pp. 3961-3973
    • Sawai, E.T.1    Butel, J.S.2
  • 51
    • 0025686194 scopus 로고
    • Three tomato genes code for heat stress transcription factors with a remarkable degree of homology to the DNA-binding domain of the yeast HSF
    • Scharf, K.D., S. Rose, W. Zott, F. Schoff, and L. Nover. 1990. Three tomato genes code for heat stress transcription factors with a remarkable degree of 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    Schoff, F.4    Nover, L.5
  • 52
  • 53
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B. and K.A. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67: 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.A.2
  • 54
    • 0025787706 scopus 로고
    • Changes in hsp70 alter thermotolerance and heat-shock regulation in Drosophila
    • Solomon, J.M., J.M. Rossi, K. Golic, T. McGarry, and S. Lindquist. 1991. Changes in hsp70 alter thermotolerance and heat-shock regulation in Drosophila. New Biol. 3: 1106-1120.
    • (1991) New Biol. , vol.3 , pp. 1106-1120
    • Solomon, J.M.1    Rossi, J.M.2    Golic, K.3    McGarry, T.4    Lindquist, S.5
  • 55
    • 0025755922 scopus 로고
    • Heat shock factor and heat shock response
    • Sorger, P.K. 1991. Heat shock factor and heat shock response. Cell 65: 363-366.
    • (1991) Cell , vol.65 , pp. 363-366
    • Sorger, P.K.1
  • 56
    • 0023427519 scopus 로고
    • Purification and characterization of a heat-shock element binding protein from yeast
    • Sorger, P.K. and H.R.B. Pelham. 1987. Purification and characterization of a heat-shock element binding protein from yeast. EMBO J. 6: 3035-3041.
    • (1987) EMBO J. , vol.6 , pp. 3035-3041
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 57
    • 0024852809 scopus 로고
    • Trimerization of a yeast transcriptional activator via coiled-coil motif
    • Sorger, P.K. and H.C.M. Nelson 1989. Trimerization of a yeast transcriptional activator via coiled-coil motif. Cell 59: 807-813.
    • (1989) Cell , vol.59 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.M.2
  • 58
    • 0023643235 scopus 로고
    • Heat shock factor is regulated differently in yeast and HeLa cells
    • Sorger, P.K., M.J. Lewis, and M.H.B. Pelham. 1987. Heat shock factor is regulated differently in yeast and HeLa cells. Nature 329: 81-84.
    • (1987) Nature , vol.329 , pp. 81-84
    • Sorger, P.K.1    Lewis, M.J.2    Pelham, M.H.B.3
  • 59
    • 0023240043 scopus 로고
    • The heat shock response of E. coli is regulated by changes in the concentration of sigma 32
    • Straus, D.B., W.A. Walter, and C.A. Gross. 1987. The heat shock response of E. coli is regulated by changes in the concentration of sigma 32. Nature 329: 348-351.
    • (1987) Nature , vol.329 , pp. 348-351
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 60
    • 0024854864 scopus 로고
    • 32 is reduced under conditions of excess heat shock protein production in Escherichia coli
    • 32 is reduced under conditions of excess heat shock protein production in Escherichia coli. Genes & Dev. 3: 2003-2010.
    • (1989) Genes & Dev. , vol.3 , pp. 2003-2010
  • 61
    • 0025632973 scopus 로고
    • 32
    • 32. Genes & Dev. 4: 2202-2209.
    • (1990) Genes & Dev. , vol.4 , pp. 2202-2209
  • 63
    • 0020827719 scopus 로고
    • The dnaK protein modulates the heat shock response of Escherichia coli
    • Tilly, K., N. McKittrick, M. Zylicz, and C. Georgopoulos. 1983. The dnaK protein modulates the heat shock response of Escherichia coli. Cell 34: 641-646.
    • (1983) Cell , vol.34 , pp. 641-646
    • Tilly, K.1    McKittrick, N.2    Zylicz, M.3    Georgopoulos, C.4
  • 64
    • 0024584414 scopus 로고
    • Modulation of stability of the Escherichia coli heat shock regulatory factor sigma 32
    • Tilly, K., J. Spence, and C. Georgopoulos. 1989. Modulation of stability of the Escherichia coli heat shock regulatory factor sigma 32. J. Bacteriol. 171: 1585-1589.
    • (1989) J. Bacteriol. , vol.171 , pp. 1585-1589
    • Tilly, K.1    Spence, J.2    Georgopoulos, C.3
  • 65
    • 0026427246 scopus 로고
    • I-POU: A POU-domain protein that inhibits neuron specific gene activation
    • Treacy, M.N., X. He, and M.G. Rosenfeld. 1991. I-POU: A POU-domain protein that inhibits neuron specific gene activation. Nature 350: 577-584.
    • (1991) Nature , vol.350 , pp. 577-584
    • Treacy, M.N.1    He, X.2    Rosenfeld, M.G.3
  • 66
    • 0025200592 scopus 로고
    • The 65-kD subunit of NF-κB is a receptor for IκB and a modulator of DNA-binding specificity
    • Urban, M.B. and P.A. Baeuerle. 1990. The 65-kD subunit of NF-κB is a receptor for IκB and a modulator of DNA-binding specificity. Genes & Dev. 4: 1974-1984.
    • (1990) Genes & Dev. , vol.4 , pp. 1974-1984
    • Urban, M.B.1    Baeuerle, P.A.2
  • 67
    • 0023155617 scopus 로고
    • Medium tumor antigen of polyomavirus transformation defective mutant NG59 is associated with 73-kilodalton heat shock protein
    • Walter, G., A. Carbone, and W.J. Welch. 1987. Medium tumor antigen of polyomavirus transformation defective mutant NG59 is associated with 73-kilodalton heat shock protein. J. Virol. 61: 405-410.
    • (1987) J. Virol. , vol.61 , pp. 405-410
    • Walter, G.1    Carbone, A.2    Welch, W.J.3
  • 68
    • 0021922919 scopus 로고
    • Rapid purification of mammalian 70,000 dalton stress protein: Affinity of proteins for nucleotides
    • Welch, W.J. and J.R. Feramisco. 1985. Rapid purification of mammalian 70,000 dalton stress protein: Affinity of proteins for nucleotides. Mol Cell Biol. 5: 1229-1236.
    • (1985) Mol Cell Biol. , vol.5 , pp. 1229-1236
    • Welch, W.J.1    Feramisco, J.R.2
  • 69
    • 0023924167 scopus 로고
    • Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat shock protein 70, intermediate filaments and small nuclear ribonuclear complexes
    • Welch, W.J. and L.A. Mizzen. 1988. Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat shock protein 70, intermediate filaments and small nuclear ribonuclear complexes. J. Cell. Biol. 106: 1117-1130.
    • (1988) J. Cell. Biol. , vol.106 , pp. 1117-1130
    • Welch, W.J.1    Mizzen, L.A.2
  • 70
    • 0025955517 scopus 로고
    • Stress induced oligomerization and chromosomal relocalization of heat-shock factor
    • Westwood, J.T., J. Clos, and C. Wu. 1991. Stress induced oligomerization and chromosomal relocalization of heat-shock factor. Nature 353: 822-827.
    • (1991) Nature , vol.353 , pp. 822-827
    • Westwood, J.T.1    Clos, J.2    Wu, C.3
  • 71
    • 0025788990 scopus 로고
    • Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin
    • Wickner, S., J. Hoskins, and K. McKenney. 1991. Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin. Proc. Natl. Acad. Sci. 88: 7903-7907.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 7903-7907
    • Wickner, S.1    Hoskins, J.2    McKenney, K.3
  • 72
    • 0023652307 scopus 로고
    • The Saccharomyces and Drosophila heat shock transcription factors are identical in size and DNA binding properties
    • Wiederrecht, G., D.J. Shuey, W.A. Kibbe, and C. Parker. 1987. The Saccharomyces and Drosophila heat shock transcription factors are identical in size and DNA binding properties. Cell 48: 507-515.
    • (1987) Cell , vol.48 , pp. 507-515
    • Wiederrecht, G.1    Shuey, D.J.2    Kibbe, W.A.3    Parker, C.4
  • 73
    • 0024282788 scopus 로고
    • Isolation of the gene encoding the S. cerevisiae heat shock transcription factor
    • Wiederrecht, G., D. Seto, and C.S. Parker. 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
  • 74
    • 0024411246 scopus 로고
    • E1a transactivation of the human HSP70 promoter is mediated through the basal transcriptional complex
    • Williams, G.T., T.K. McClanahan, and R.I. Morimoto. 1989. E1a transactivation of the human HSP70 promoter is mediated through the basal transcriptional complex. Mol. Cell. Biol. 9: 2574-2587.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2574-2587
    • Williams, G.T.1    McClanahan, T.K.2    Morimoto, R.I.3
  • 75
    • 0022768857 scopus 로고
    • The E1A 13S product of adenovirus 5 activates transcription of the cellular human hsp70 gene
    • Wu, B., H.C. Hurst, N.C. Jones and R.I. Morimoto. 1986. The E1A 13S product of adenovirus 5 activates transcription of the cellular human hsp70 gene. Mol. Cell. Biol. 6: 2994-2999.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2994-2999
    • Wu, B.1    Hurst, H.C.2    Jones, N.C.3    Morimoto, R.I.4
  • 76
    • 0011439458 scopus 로고
    • Transcriptional regulation of heat shock genes
    • ed. R.I. Morimoto, G. Tissières, and C. Georgopoulus, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Wu, C., V. Zimarino, B. Tsai, B. Walker, and S. Wilson. 1990. Transcriptional regulation of heat shock genes. In Stress proteins in biology and medicine (ed. R.I. Morimoto, G. Tissières, and C. Georgopoulus), pp. 429-442. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1990) Stress Proteins in Biology and Medicine , pp. 429-442
    • Wu, C.1    Zimarino, V.2    Tsai, B.3    Walker, B.4    Wilson, S.5
  • 77
    • 0023863121 scopus 로고
    • Germline transformation used to define key features of the heat shock response element
    • Xiao, H. and J.T. Lis. 1988. Germline transformation used to define key features of the heat shock response element. Science 239: 1139-1142.
    • (1988) Science , vol.239 , pp. 1139-1142
    • Xiao, H.1    Lis, J.T.2
  • 78
    • 0043104253 scopus 로고
    • The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system
    • Zylicz, M., J.H. LeBowitz, R. McMacken, and C. Georgopoulos. 1983. The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system. Proc. Natl. Acad. Sci. 80: 6431-6435.
    • (1983) Proc. Natl. Acad. Sci. , vol.80 , pp. 6431-6435
    • Zylicz, M.1    LeBowitz, J.H.2    McMacken, R.3    Georgopoulos, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.