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Volumn 4, Issue 2, 1999, Pages 219-228

A human nuclear-localized chaperone that regulates dimerization, DNA binding, and transcriptional activity of bZIP proteins

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BZIP ENHANCING FACTOR; CHAPERONE; CHAPERONIN; DIMER; DNA; DNA BINDING PROTEIN; GLUCOCORTICOID RECEPTOR; LEUCINE ZIPPER PROTEIN; MONOMER; PEPTIDE; POLYPEPTIDE; RECOMBINANT PROTEIN; STEROID; TAX PROTEIN; THIOSULFATE SULFURTRANSFERASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1; UNCLASSIFIED DRUG;

EID: 0033179986     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80369-X     Document Type: Article
Times cited : (67)

References (68)
  • 1
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya, K., Myers, M.P., Murphy, S.P., and Morimoto, R.I. (1992). The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev. 6, 1153-1164.
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 2
    • 0028102598 scopus 로고
    • Quantitative studies of the effect of HTLV-I tax protein on CREB protein-DNA binding
    • Anderson, M.G., and Dynan, W.S. (1994). Quantitative studies of the effect of HTLV-I tax protein on CREB protein-DNA binding. Nucleic Acid Res. 22, 3194-3201.
    • (1994) Nucleic Acid Res. , vol.22 , pp. 3194-3201
    • Anderson, M.G.1    Dynan, W.S.2
  • 3
    • 0025720735 scopus 로고
    • The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation
    • Angel, P., and Karin, M. (1991). The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation. Biochim. Biophys. Acta 10, 129-157.
    • (1991) Biochim. Biophys. Acta , vol.10 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 4
    • 0031994436 scopus 로고    scopus 로고
    • Accessory factor-bZIP-DNA interactions
    • Baranger, A.M. (1998). Accessory factor-bZIP-DNA interactions. Curr. Opin. Chem. Biol. 2, 18-23.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 18-23
    • Baranger, A.M.1
  • 6
    • 0030878836 scopus 로고    scopus 로고
    • The hepatitis B virus X protein enhances the DNA binding potential and transcription efficacy of bZIP transcription factors
    • Barnabas, S., Hai, T., and Andrisani, O.M. (1997). The hepatitis B virus X protein enhances the DNA binding potential and transcription efficacy of bZIP transcription factors. J. Biol. Chem. 272, 20684-20690.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20684-20690
    • Barnabas, S.1    Hai, T.2    Andrisani, O.M.3
  • 7
    • 0030896455 scopus 로고    scopus 로고
    • ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRα enhancer function
    • Bruhn, L, Munnerlyn, A., and Grosschedl, R. (1997). ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for TCRα enhancer function. Genes Dev. 11, 640-653.
    • (1997) Genes Dev. , vol.11 , pp. 640-653
    • Bruhn, L.1    Munnerlyn, A.2    Grosschedl, R.3
  • 8
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaper-one machines
    • Bukau, B., and Horwich, A.L. (1998). The Hsp70 and Hsp60 chaper-one machines. Cell 92, 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 9
    • 0027772890 scopus 로고
    • Eukaryotic activators function during multiple steps of preinitiation complex assembly
    • Choy, B., and Green, M.R. (1993). Eukaryotic activators function during multiple steps of preinitiation complex assembly. Nature 366, 531-536.
    • (1993) Nature , vol.366 , pp. 531-536
    • Choy, B.1    Green, M.R.2
  • 10
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalain nuclei
    • Dignam, J.D., Lebovitz, R.M., and Roeder, R.G. (1983). Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalain nuclei. Nucleic Acids Res. 11, 1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 11
    • 0027296741 scopus 로고
    • Mechanism of transcriptional synergism between distinct virus-inducible enhancer elements
    • Du, W., Thanos, D., and Maniatis, T. (1993). Mechanism of transcriptional synergism between distinct virus-inducible enhancer elements. Cell 74, 887-898.
    • (1993) Cell , vol.74 , pp. 887-898
    • Du, W.1    Thanos, D.2    Maniatis, T.3
  • 12
    • 0031239894 scopus 로고    scopus 로고
    • Molecular chaperones: Avoiding the crowd
    • Ellis, R.J. (1997). Molecular chaperones: avoiding the crowd. Curr. Biol. 7, R531-R533.
    • (1997) Curr. Biol. , vol.7
    • Ellis, R.J.1
  • 13
    • 0033602228 scopus 로고    scopus 로고
    • Molecular chaperones: Pathways and networks
    • Ellis, R.J. (1999). Molecular chaperones: pathways and networks. Curr. Biol. 9, R137-R139.
    • (1999) Curr. Biol. , vol.9
    • Ellis, R.J.1
  • 14
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • Ellis, R.J., and Hartl, F.U. (1999). Principles of protein folding in the cellular environment. Curr. Opin. Struct. Biol. 9, 102-110.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 16
    • 0023500809 scopus 로고
    • Transcription in yeast activated by a putative amphipathic alpha helix linked to a DNA binding unit
    • Giniger, E., and Ptashne, M. (1987). Transcription in yeast activated by a putative amphipathic alpha helix linked to a DNA binding unit. Nature 330, 670-672.
    • (1987) Nature , vol.330 , pp. 670-672
    • Giniger, E.1    Ptashne, M.2
  • 17
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman, S., Wickner, S., and Maurizi, M.R. (1997) Protein quality control: Triage by chaperones and proteases. Genes Dev. 11, 815-823.
    • (1997) Genes Dev. , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 18
    • 0032485415 scopus 로고    scopus 로고
    • Mmip1 : A novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc
    • Gupta, K., Anand, G., Yin, X., Grove, L., and Prochownik, E.V. (1998). Mmip1 : A novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc. Oncogene 16, 1149-1159.
    • (1998) Oncogene , vol.16 , pp. 1149-1159
    • Gupta, K.1    Anand, G.2    Yin, X.3    Grove, L.4    Prochownik, E.V.5
  • 19
    • 0026055806 scopus 로고
    • Purification of his-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies
    • Hoffmann, A., and Roeder, R.G. (1991). Purification of his-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies. Nucleic Acids Res. 19, 6337-6338.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6337-6338
    • Hoffmann, A.1    Roeder, R.G.2
  • 20
    • 0025598302 scopus 로고
    • Sequence requirements for coiled-coils: Analysis with lambda repressor-GCN4 leucine zipper fusions
    • Hu, J.C., O'Shea, E.K., Kim, P.S., and Sauer, R.T. (1990). Sequence requirements for coiled-coils: Analysis with lambda repressor-GCN4 leucine zipper fusions. Science 250, 1400-1403.
    • (1990) Science , vol.250 , pp. 1400-1403
    • Hu, J.C.1    O'Shea, E.K.2    Kim, P.S.3    Sauer, R.T.4
  • 21
    • 0029174419 scopus 로고
    • Transcription factors 1: bZIP proteins
    • Hurst, H.C. (1995). Transcription factors 1: bZip proteins. Protein Profile 2, 101-168.
    • (1995) Protein Profile , vol.2 , pp. 101-168
    • Hurst, H.C.1
  • 22
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • Jakob, U., and Buchner, J. (1994). Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci. 19, 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 23
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob, U., Gaestel, M., Engel, K., and Buchner, J. (1993). Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 24
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson, J.L., and Craig, E.A. (1997). Protein folding in vivo: Unraveling complex pathways. Cell 90, 201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 25
    • 0030753648 scopus 로고    scopus 로고
    • Muscle LIM protein promotes myogenesis by enhancng the activity of MyoD
    • Kong, Y., Flick, M.J., Kudla, A.J., and Konieczny, S.F. (1997). Muscle LIM protein promotes myogenesis by enhancng the activity of MyoD. Mol. Cell. Biol. 17, 4750-4760.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4750-4760
    • Kong, Y.1    Flick, M.J.2    Kudla, A.J.3    Konieczny, S.F.4
  • 26
    • 0024205841 scopus 로고
    • The role of the leucine zipper in the fos-jun interaction
    • Kouzarides, T., and Ziff, E. (1988). The role of the leucine zipper in the fos-jun interaction. Nature 336, 646-651.
    • (1988) Nature , vol.336 , pp. 646-651
    • Kouzarides, T.1    Ziff, E.2
  • 27
    • 0025291463 scopus 로고
    • The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor
    • Laminet, A.A., Ziegelhoffer, T., Georgopoulos, C., and Pluckthun, A. (1990). The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor. EMBO J. 9, 2317-2319.
    • (1990) EMBO J. , vol.9 , pp. 2317-2319
    • Laminet, A.A.1    Ziegelhoffer, T.2    Georgopoulos, C.3    Pluckthun, A.4
  • 28
    • 0028949832 scopus 로고
    • Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea
    • Lee, G.J., Pokala, N., and Vierling, E. (1995). Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea. J. Biol. Chem. 270, 10432-10438.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10432-10438
    • Lee, G.J.1    Pokala, N.2    Vierling, E.3
  • 29
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin, J.A., and Yamamoto, K.R. (1998). Allosteric effects of DNA on transcriptional regulators. Nature 392, 885-888.
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 30
    • 0027171075 scopus 로고
    • The cAMP response element binding protein, CREB, is a potent inhibitor of diverse transcriptional activators
    • Lemaigre, F.P., Ace, C.I., and Green, M.R. (1993). The cAMP response element binding protein, CREB, is a potent inhibitor of diverse transcriptional activators. Nucleic Acid Res. 21, 2907-2911.
    • (1993) Nucleic Acid Res. , vol.21 , pp. 2907-2911
    • Lemaigre, F.P.1    Ace, C.I.2    Green, M.R.3
  • 31
  • 32
    • 0025284903 scopus 로고
    • A specific member of the ATF transcription factor family can mediate transcription activation by the adenovirus E1a protein
    • Liu, F., and Green, M.R. (1990). A specific member of the ATF transcription factor family can mediate transcription activation by the adenovirus E1a protein. Cell 61, 1217-1224.
    • (1990) Cell , vol.61 , pp. 1217-1224
    • Liu, F.1    Green, M.R.2
  • 33
    • 0028223147 scopus 로고
    • Promoter targeting by adenovirus E1a through interaction with different cellular DNA-binding domains
    • Liu, F., and Green, M.R. (1994). Promoter targeting by adenovirus E1a through interaction with different cellular DNA-binding domains. Nature 368, 520-525.
    • (1994) Nature , vol.368 , pp. 520-525
    • Liu, F.1    Green, M.R.2
  • 34
    • 0028346021 scopus 로고
    • Targeted nuclear antisense RNA mimics natural antisense-induced degradation of polyoma virus early RNA
    • Liu, Z., Batt, B., and Carmichael, G.G. (1994). Targeted nuclear antisense RNA mimics natural antisense-induced degradation of polyoma virus early RNA. Proc. Natl. Acad. Sci. USA 91, 4258-4262.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4258-4262
    • Liu, Z.1    Batt, B.2    Carmichael, G.G.3
  • 35
    • 0029965491 scopus 로고    scopus 로고
    • Transcription revisited: A commentary on the 1995 Cold Spring Harbour Laboratory meeting, "mechanisms of eukaryotic transcription."
    • McKnight, S.L. (1996). Transcription revisited: A commentary on the 1995 Cold Spring Harbour Laboratory meeting, "mechanisms of eukaryotic transcription." Genes Dev. 10, 367-381.
    • (1996) Genes Dev. , vol.10 , pp. 367-381
    • McKnight, S.L.1
  • 36
    • 0003915447 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • McKnight, S., and Yamamoto, K.R., eds. (1992). Transcriptional Regulation (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
    • (1992) Transcriptional Regulation
    • McKnight, S.1    Yamamoto, K.R.2
  • 38
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate
    • Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A.L., and Hartl, F.U. (1991). Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate. Nature 352, 36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.U.6
  • 39
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan, D.F., and Lindquist, S. (1995). Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15, 3917-3925.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 40
    • 0025991706 scopus 로고
    • DNA-induced increase in the alpha-helical content of C/EBP and GCN4
    • O'Neil, K.T., Shuman, J.D., Ampe, C., and DeGrado, W.F. (1991). DNA-induced increase in the alpha-helical content of C/EBP and GCN4. Biochemistry 30, 9030-9034.
    • (1991) Biochemistry , vol.30 , pp. 9030-9034
    • O'Neil, K.T.1    Shuman, J.D.2    Ampe, C.3    DeGrado, W.F.4
  • 41
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E.K., Rutkowski, R., and Kim, P.S. (1989a). Evidence that the leucine zipper is a coiled coil. Science 243, 538-542.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 42
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zippers from fos and jun
    • O'Shea, E.K., Rutkowski, R., Stafford, W.F., 3rd, and Kim, P.S. (1989b). Preferential heterodimer formation by isolated leucine zippers from fos and jun. Science 245, 646-648.
    • (1989) Science , vol.245 , pp. 646-648
    • O'Shea, E.K.1    Rutkowski, R.2    Stafford W.F. III3    Kim, P.S.4
  • 43
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E.K., Klemm, J.D., Kim, P.S., and Alber, T. (1991). X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254, 539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 44
    • 0028964648 scopus 로고
    • The Rhizobium meliloti groELc locus is required for regulation of early nod genes by the transcription activator NodD
    • Ogawa, J., and Long, S.R. (1995). The Rhizobium meliloti groELc locus is required for regulation of early nod genes by the transcription activator NodD. Genes Dev. 9, 714-729.
    • (1995) Genes Dev. , vol.9 , pp. 714-729
    • Ogawa, J.1    Long, S.R.2
  • 45
    • 0343811676 scopus 로고    scopus 로고
    • Mechanism of DNA binding enhancement by hepatitis B virus protein pX
    • Palmer, C.R., Gegnas, L.D., and Schepartz, A. (1997). Mechanism of DNA binding enhancement by hepatitis B virus protein pX. Biochemistry 36, 15349-15355.
    • (1997) Biochemistry , vol.36 , pp. 15349-15355
    • Palmer, C.R.1    Gegnas, L.D.2    Schepartz, A.3
  • 46
    • 0028364259 scopus 로고
    • Energy transfer analysis of Fos-Jun dimerization and DNA binding
    • Patel, L.R., Curran, T., and Kerppola, T.K. (1994). Energy transfer analysis of Fos-Jun dimerization and DNA binding. Proc. Natl. Acad. Sci. USA 91, 7360-7364.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7360-7364
    • Patel, L.R.1    Curran, T.2    Kerppola, T.K.3
  • 47
    • 0029153112 scopus 로고
    • Recognition of bZIP proteins by the human T-cell leukaemia virus transactivator tax
    • Perini, G., Wagner, S., and Green, M.R. (1995). Recognition of bZIP proteins by the human T-cell leukaemia virus transactivator tax. Nature 376, 602-605.
    • (1995) Nature , vol.376 , pp. 602-605
    • Perini, G.1    Wagner, S.2    Green, M.R.3
  • 48
    • 0033553572 scopus 로고    scopus 로고
    • The hepatitis B pX protein promotes dimerization and DNA binding of cellular basic region/leucine zipper proteins by targeting the conserved basic region
    • Perini, G., Oetjen, E., and Green, M.R. (1999). The hepatitis B pX protein promotes dimerization and DNA binding of cellular basic region/leucine zipper proteins by targeting the conserved basic region. J. Biol. Chem. 274, 13970-13977.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13970-13977
    • Perini, G.1    Oetjen, E.2    Green, M.R.3
  • 49
    • 0024687774 scopus 로고
    • Fos-Jun interaction: Mutational analysis of the leucine zipper domain of both proteins
    • Ransone, L.J., Visvader, J., Sassone-Corsi, P., and Verma, I.M. (1989). Fos-Jun interaction: Mutational analysis of the leucine zipper domain of both proteins. Genes Dev. 3, 770-781.
    • (1989) Genes Dev. , vol.3 , pp. 770-781
    • Ransone, L.J.1    Visvader, J.2    Sassone-Corsi, P.3    Verma, I.M.4
  • 50
    • 0030041098 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of carbonic anhydrase B
    • Rozema, D., and Gellman, S.H. (1996). Artificial chaperone-assisted refolding of carbonic anhydrase B. J. Biol. Chem. 271, 3478-3487.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3478-3487
    • Rozema, D.1    Gellman, S.H.2
  • 51
    • 0031030579 scopus 로고    scopus 로고
    • Assisted protein folding
    • Ruddon, R.W., and Bedows, E. (1997). Assisted protein folding. J. Biol. Chem. 272, 3125-3128.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3125-3128
    • Ruddon, R.W.1    Bedows, E.2
  • 52
  • 53
    • 0027980828 scopus 로고
    • Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90
    • Shue, G., and Kohtz, D.S. (1994). Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90. J. Biol. Chem. 269, 2707-2711.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2707-2711
    • Shue, G.1    Kohtz, D.S.2
  • 54
    • 0030922704 scopus 로고    scopus 로고
    • ATF-2 and c/EBPalpha can form a heterodimeric DNA binding complex in vitro. Functional implications for transcriptional regulation
    • Shuman, J.D., Cheong, J., and Coligan, J.E. (1997). ATF-2 and c/EBPalpha can form a heterodimeric DNA binding complex in vitro. Functional implications for transcriptional regulation. J. Biol. Chem. 272, 12793-12800.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12793-12800
    • Shuman, J.D.1    Cheong, J.2    Coligan, J.E.3
  • 55
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B., and Johnson, K.S. (1988). Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Genes 67, 31-40.
    • (1988) Genes , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 56
    • 0027172822 scopus 로고
    • Different TRE-related elements are distinguished by sets of DNA-binding proteins with overlapping sequence specificity
    • Smith, S.E., Papavassiliou, A.G., and Bohmann, D. (1993). Different TRE-related elements are distinguished by sets of DNA-binding proteins with overlapping sequence specificity. Nucleic Acid Res. 21, 1581-1585.
    • (1993) Nucleic Acid Res. , vol.21 , pp. 1581-1585
    • Smith, S.E.1    Papavassiliou, A.G.2    Bohmann, D.3
  • 58
    • 0027184480 scopus 로고
    • A cellular factor stimulates the DNA-binding activity of MyoD and E47
    • Thayer, M.J., and Weintraub, H. (1993). A cellular factor stimulates the DNA-binding activity of MyoD and E47. Proc. Natl. Acad. Sci. USA 90, 6483-6487.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6483-6487
    • Thayer, M.J.1    Weintraub, H.2
  • 59
    • 0027245801 scopus 로고
    • Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
    • Thompson, K.S., Vinson, C.R., and Freire, E. (1993). Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry 32, 5491-5496.
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.S.1    Vinson, C.R.2    Freire, E.3
  • 60
    • 0024535960 scopus 로고
    • Leucine repeats and an adjacent DNA binding domain mediate the formation of functional cFos-cJun heterodimers
    • Turner, R., and Tjian, R. (1989). Leucine repeats and an adjacent DNA binding domain mediate the formation of functional cFos-cJun heterodimers. Science 243, 1689-1694.
    • (1989) Science , vol.243 , pp. 1689-1694
    • Turner, R.1    Tjian, R.2
  • 61
    • 0027422749 scopus 로고
    • HTLV-1 tax protein stimulation of DNA binding of bZIP proteins by enhancing dimerization
    • Wagner, S., and Green, M.R. (1993). HTLV-1 tax protein stimulation of DNA binding of bZIP proteins by enhancing dimerization. Science 262, 395-399.
    • (1993) Science , vol.262 , pp. 395-399
    • Wagner, S.1    Green, M.R.2
  • 62
    • 0028362695 scopus 로고
    • DNA-binding domains: Targets for viral and cellular regulators
    • Wagner, S., and Green, M.R. (1994). DNA-binding domains: Targets for viral and cellular regulators. Curr. Opin. Cell Biol. 6, 410-414.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 410-414
    • Wagner, S.1    Green, M.R.2
  • 63
    • 0025155512 scopus 로고
    • Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA
    • Weiss, M.A., Ellenberger, T., Wobbe, C.R., Lee, J.P., Harrison, S.C., and Struhl, K. (1990). Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA. Nature 347, 575-578.
    • (1990) Nature , vol.347 , pp. 575-578
    • Weiss, M.A.1    Ellenberger, T.2    Wobbe, C.R.3    Lee, J.P.4    Harrison, S.C.5    Struhl, K.6
  • 64
    • 0026778032 scopus 로고
    • Hsp90 chaperones protein folding in vitro
    • Wiech, H., Buchner, J., Zimmermann, R., and Jakob, U. (1992). Hsp90 chaperones protein folding in vitro. Nature 358, 169-170.
    • (1992) Nature , vol.358 , pp. 169-170
    • Wiech, H.1    Buchner, J.2    Zimmermann, R.3    Jakob, U.4
  • 65
    • 0031849099 scopus 로고    scopus 로고
    • Small heat-shock protein family: Function in health and disease
    • Welsh, M.J., and Gaestel, M. (1998). Small heat-shock protein family: function in health and disease. Ann. NY Acad. Sci. 851, 28-35.
    • (1998) Ann. NY Acad. Sci. , vol.851 , pp. 28-35
    • Welsh, M.J.1    Gaestel, M.2
  • 66
    • 0029135176 scopus 로고
    • Chimeric proteins composed of jun and creb define domains required for interaction with the human T-cell leukemia virus type 1 tax protein
    • Yin, M.J., Paulssen, E., Seeler, J., and Gaynor, R.B. (1995). Chimeric proteins composed of jun and creb define domains required for interaction with the human T-cell leukemia virus type 1 tax protein. J. Virol. 69, 6209-6218.
    • (1995) J. Virol. , vol.69 , pp. 6209-6218
    • Yin, M.J.1    Paulssen, E.2    Seeler, J.3    Gaynor, R.B.4
  • 67
    • 0028600629 scopus 로고
    • Localization of pre-mRNA splicing in mammalian nuclei
    • Zhang, G., Taneja, K., Singer, R.H., and Green, M.R. (1994). Localization of pre-mRNA splicing in mammalian nuclei. Nature 372, 809-812.
    • (1994) Nature , vol.372 , pp. 809-812
    • Zhang, G.1    Taneja, K.2    Singer, R.H.3    Green, M.R.4
  • 68
    • 0026338755 scopus 로고
    • Interaction of the human T-cell lymphotrophic virus type I (HTLV-I) transcriptional activator tax with cellular factors that bind specifically to the 21-base pair repeats in the HTLV-I enhancer
    • Zhao, L.J., and Giam, C.Z. (1991). Interaction of the human T-cell lymphotrophic virus type I (HTLV-I) transcriptional activator tax with cellular factors that bind specifically to the 21-base pair repeats in the HTLV-I enhancer. Proc. Natl. Acad. Sci. USA 88, 11445-11449.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11445-11449
    • Zhao, L.J.1    Giam, C.Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.