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Volumn 19, Issue 2, 1999, Pages 1025-1037

Discrimination between NL1- and NL2-mediated nuclear localization of the glucocorticoid receptor

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN; KARYOPHERIN; LEPTOMYCIN B;

EID: 0032929622     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.2.1025     Document Type: Article
Times cited : (192)

References (109)
  • 1
    • 0026726806 scopus 로고
    • Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation
    • Allan, G. F., X. Leng, S. Y. Tsai, N. L. Weigel, D. P. Edwards, M. J. Tsai, and B. W. O'Malley. 1992. Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. J. Biol. Chem. 267:19513-19520.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19513-19520
    • Allan, G.F.1    Leng, X.2    Tsai, S.Y.3    Weigel, N.L.4    Edwards, D.P.5    Tsai, M.J.6    O'Malley, B.W.7
  • 2
    • 0019851061 scopus 로고
    • Cell cycle-specific glucocorticoid growth regulation of a human cell line (NHIK 3025)
    • Bakke, O., and K. B. Eik-Nes. 1981. Cell cycle-specific glucocorticoid growth regulation of a human cell line (NHIK 3025). J. Cell Physiol. 109:489-496.
    • (1981) J. Cell Physiol. , vol.109 , pp. 489-496
    • Bakke, O.1    Eik-Nes, K.B.2
  • 3
    • 0026783210 scopus 로고
    • I kappa B interacts with the nuclear localization sequences of the subunits of NF-kappa B: A mechanism for cytoplasmic retention
    • Beg, A. A., S. M. Ruben, R. I. Scheinman, S. Haskill, C. A. Rosen, and A. S. Baldwin, Jr. 1992. I kappa B interacts with the nuclear localization sequences of the subunits of NF-kappa B: a mechanism for cytoplasmic retention. Genes Dev. 6:1899-1913.
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1    Ruben, S.M.2    Scheinman, R.I.3    Haskill, S.4    Rosen, C.A.5    Baldwin A.S., Jr.6
  • 4
    • 0028987379 scopus 로고
    • Hormone-induced hyperphosphorylation of specific phosphorylated sites in the mouse glucocorticoid receptor
    • Bodwell, J. E., J. M. Hu, E. Orti, and A. Munck. 1995. Hormone-induced hyperphosphorylation of specific phosphorylated sites in the mouse glucocorticoid receptor. J. Steroid Biochem. Mol. Biol. 52:135-140.
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.52 , pp. 135-140
    • Bodwell, J.E.1    Hu, J.M.2    Orti, E.3    Munck, A.4
  • 5
    • 0024567048 scopus 로고
    • Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor
    • Bresnick, E. H., F. C. Dalman, E. R. Sanchez, and W. B. Pratt. 1989. Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J. Biol. Chem. 264:4992-4997.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4992-4997
    • Bresnick, E.H.1    Dalman, F.C.2    Sanchez, E.R.3    Pratt, W.B.4
  • 7
    • 0028607388 scopus 로고
    • Intragenic sequences of the human glucocorticoid receptor complementary DNA mediate hormone-inducible receptor messenger RNA down-regulation through multiple mechanisms
    • Burnstein, K. L., C. M. Jewell, M. Sar, and J. A. Cidlowski. 1994. Intragenic sequences of the human glucocorticoid receptor complementary DNA mediate hormone-inducible receptor messenger RNA down-regulation through multiple mechanisms. Mol. Endocrinol. 8:1764-1773.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 1764-1773
    • Burnstein, K.L.1    Jewell, C.M.2    Sar, M.3    Cidlowski, J.A.4
  • 10
    • 0022776986 scopus 로고
    • The hormone regulatory element of mouse mammary tumor virus mediates progesterone induction
    • Cato, A. C. B., R. Miksicek, G. Schütz, J. Arnemann, and M. Beato. 1986. The hormone regulatory element of mouse mammary tumor virus mediates progesterone induction. EMBO J. 5:2237-2240.
    • (1986) EMBO J. , vol.5 , pp. 2237-2240
    • Cato, A.C.B.1    Miksicek, R.2    Schütz, G.3    Arnemann, J.4    Beato, M.5
  • 11
    • 0027985148 scopus 로고
    • Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae
    • Chang, H. C., and S. Lindquist. 1994. Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae. J. Biol. Chem. 269:24983-24988.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24983-24988
    • Chang, H.C.1    Lindquist, S.2
  • 12
    • 0019816203 scopus 로고
    • Regulation of glucocorticoid receptors by glucocorticoids in cultured HeLa S3 cells
    • Cidlowski, J. A., and N. B. Cidlowski. 1981. Regulation of glucocorticoid receptors by glucocorticoids in cultured HeLa S3 cells. Endocrinology 109: 1975-1982.
    • (1981) Endocrinology , vol.109 , pp. 1975-1982
    • Cidlowski, J.A.1    Cidlowski, N.B.2
  • 14
    • 0025260972 scopus 로고
    • In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90
    • Dalman, F. C., R. J. Koenig, G. H. Perdew, E. Massa, and W. B. Pratt. 1990. In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90. J. Biol. Chem. 265:3615-3618.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3615-3618
    • Dalman, F.C.1    Koenig, R.J.2    Perdew, G.H.3    Massa, E.4    Pratt, W.B.5
  • 15
    • 0026600841 scopus 로고
    • Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
    • Danielian, P. S., R. White, J. A. Lees, and M. G. Parker. 1992. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. EMBO J. 11:1025-1033.
    • (1992) EMBO J. , vol.11 , pp. 1025-1033
    • Danielian, P.S.1    White, R.2    Lees, J.A.3    Parker, M.G.4
  • 16
    • 0027768899 scopus 로고
    • The antiestrogen ICI182780 disrupts estrogen receptor nucleocytoplasmic shuttling
    • Dauvois, S., R. White, and M. G. Parker. 1993. The antiestrogen ICI182780 disrupts estrogen receptor nucleocytoplasmic shuttling. J. Cell Sci. 106: 1377-1388.
    • (1993) J. Cell Sci. , vol.106 , pp. 1377-1388
    • Dauvois, S.1    White, R.2    Parker, M.G.3
  • 17
    • 0029060051 scopus 로고
    • The nuclear pore complex
    • Davis, L. I. 1995. The nuclear pore complex. Annu. Rev. Biochem. 64:865-896.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 865-896
    • Davis, L.I.1
  • 18
    • 0023896114 scopus 로고
    • Requirement of hormone for thermal conversion of the glucocorticoid receptor to the DNA-binding state
    • Denis, M., L. Poellinger, A.-C. Wilstom, and J.-A. Gustafsson. 1988. Requirement of hormone for thermal conversion of the glucocorticoid receptor to the DNA-binding state. Nature 333:686-688.
    • (1988) Nature , vol.333 , pp. 686-688
    • Denis, M.1    Poellinger, L.2    Wilstom, A.-C.3    Gustafsson, J.-A.4
  • 19
    • 0025293580 scopus 로고
    • Evidence from pulse-chase labelling studies that the antiglucocorticoid hormone RU486 stabilizes the nonactivated form of the glucocorticoid receptor in mouse lymphoma cells
    • Distelhorst, C. W., and K. J. Howard. 1990. Evidence from pulse-chase labelling studies that the antiglucocorticoid hormone RU486 stabilizes the nonactivated form of the glucocorticoid receptor in mouse lymphoma cells. J. Steroid Biochem. Mol. Biol. 36:25-31.
    • (1990) J. Steroid Biochem. Mol. Biol. , vol.36 , pp. 25-31
    • Distelhorst, C.W.1    Howard, K.J.2
  • 20
    • 0032571320 scopus 로고    scopus 로고
    • The role of DnaJ-like proteins in glucocorticoid receptor-hsp90 heterocomplex assembly by the reconstituted hsp90-p60-hsp70 foldosome complex
    • Dittmar, K. D., M. Banach, M. D. Galigniana, and W. B. Pratt. 1998. The role of DnaJ-like proteins in glucocorticoid receptor-hsp90 heterocomplex assembly by the reconstituted hsp90-p60-hsp70 foldosome complex. J. Biol. Chem. 273:7358-7366.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7358-7366
    • Dittmar, K.D.1    Banach, M.2    Galigniana, M.D.3    Pratt, W.B.4
  • 21
    • 17544384391 scopus 로고    scopus 로고
    • Reconstitution of the steroid receptor-hsp90 heterocomplex assembly system of rabbit reticulocyte lysate
    • Dittmar, K. D., K. A. Hutchison, J. K. Owens-Grillo, and W. B. Pratt. 1996. Reconstitution of the steroid receptor-hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. J. Biol. Chem. 271:12833-12839.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12833-12839
    • Dittmar, K.D.1    Hutchison, K.A.2    Owens-Grillo, J.K.3    Pratt, W.B.4
  • 22
    • 0030989277 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the reconstituted hsp90 based chaperone machinery. The initial hsp90/p60/hsp70-dependent step is sufficient for creating the steroid binding conformation
    • Dittmar, K. D., and W. B. Pratt. 1997. Folding of the glucocorticoid receptor by the reconstituted hsp90 based chaperone machinery. The initial hsp90/p60/hsp70-dependent step is sufficient for creating the steroid binding conformation. J. Biol. Chem. 272:13047-13054.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13047-13054
    • Dittmar, K.D.1    Pratt, W.B.2
  • 23
    • 0024204439 scopus 로고
    • Regulation of glucocorticoid receptor expression: Evidence for transcriptional and post-translational mechanisms
    • Dong, Y., L. Poellinger, J. A. Gustafsson, and S. Okret. 1988. Regulation of glucocorticoid receptor expression: evidence for transcriptional and post-translational mechanisms. Mol. Endocrinol. 2:1256-1264.
    • (1988) Mol. Endocrinol. , vol.2 , pp. 1256-1264
    • Dong, Y.1    Poellinger, L.2    Gustafsson, J.A.3    Okret, S.4
  • 24
    • 0028124463 scopus 로고
    • The two-hybrid system: An assay for protein-protein interactions
    • Fields, S., and R. Sternglanz. 1994. The two-hybrid system: an assay for protein-protein interactions. Trends Genet. 10:286-292.
    • (1994) Trends Genet. , vol.10 , pp. 286-292
    • Fields, S.1    Sternglanz, R.2
  • 25
    • 0029130169 scopus 로고
    • The HIV-1 rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer, U., J. Huber, W. C. Boelens, I. W. Mattaj, and R. Lurhmann. 1995. The HIV-1 rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82:475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lurhmann, R.5
  • 26
    • 0030924190 scopus 로고    scopus 로고
    • CRM is an export receptor leucine-rich nuclear export signal
    • Fornerod, M., O. Mutsuhito, M. Yoshida, and I. W. Mattaj. 1997. CRM is an export receptor leucine-rich nuclear export signal. Cell 90:1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Mutsuhito, O.2    Yoshida, M.3    Mattaj, I.W.4
  • 27
    • 0027078835 scopus 로고
    • I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding
    • Ganchi, P. A., S. C. Sun, W. C. Greene, and D. W. Ballard. 1992. I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding. Mol. Biol. Cell 3:1339-1352.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1339-1352
    • Ganchi, P.A.1    Sun, S.C.2    Greene, W.C.3    Ballard, D.W.4
  • 28
    • 0027073107 scopus 로고
    • Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast
    • Garabedian, M. J., and K. R. Yamamoto. 1992 Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast. Mol. Biol. Cell 3:1245-1257.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1245-1257
    • Garabedian, M.J.1    Yamamoto, K.R.2
  • 29
    • 0031054252 scopus 로고    scopus 로고
    • Sequence-specific DNA binding and transcription factor phosphorylation by Ku autoantigen/DNA-dependent protein kinase. Phosphorylation of Ser-527 of the rat glucocorticoid receptor
    • Giffin, W., J. Kwast-Welfeld, U. J. Rodda, G. G. Prefontainé, M. Traykova-Andonova, Y. Zhang, N. L. Weigel, Y. A. Lefebvre, and R. J. Haché 1997. Sequence-specific DNA binding and transcription factor phosphorylation by Ku autoantigen/DNA-dependent protein kinase. Phosphorylation of Ser-527 of the rat glucocorticoid receptor. J. Biol. Chem. 272:5647-5658.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5647-5658
    • Giffin, W.1    Kwast-Welfeld, J.2    Rodda, U.J.3    Prefontainé, G.G.4    Traykova-Andonova, M.5    Zhang, Y.6    Weigel, N.L.7    Lefebvre, Y.A.8    Haché, R.J.9
  • 30
    • 0023150589 scopus 로고
    • Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement
    • Godowski, P. J., S. Rusconi, R. Miesfeld, and K. R. Yamamoto. 1987. Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement. Nature 325:365-368.
    • (1987) Nature , vol.325 , pp. 365-368
    • Godowski, P.J.1    Rusconi, S.2    Miesfeld, R.3    Yamamoto, K.R.4
  • 31
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich, D., and I. W. Mattaj. 1996. Nucleocytoplasmic transport. Science 271:1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.W.2
  • 32
    • 0024283936 scopus 로고
    • A versatile in vivo and in vitro eukaryotic expression vector for protein engineering
    • Green, S., I. Issemann, and E. Sheer, 1988. A versatile in vivo and in vitro eukaryotic expression vector for protein engineering. Nucleic Acids Res. 16:369.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 369
    • Green, S.1    Issemann, I.2    Sheer, E.3
  • 33
    • 0028233394 scopus 로고
    • Nuclear localization signals also mediate the outward movement of proteins from the nucleus
    • Guiochon-Mantel, A., K. Delabre, P. Lescop, and E. Milgrom. 1994 Nuclear localization signals also mediate the outward movement of proteins from the nucleus. Proc. Natl Acad. Sci. USA 91:7179-7183.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 7179-7183
    • Guiochon-Mantel, A.1    Delabre, K.2    Lescop, P.3    Milgrom, E.4
  • 35
    • 0024372113 scopus 로고
    • Mechanisms of nuclear localization of the progesterone receptor: Evidence for interaction between monomers
    • Guiochon-Mantel, A., H. Lossfelt, P. Lescop, S. Sar, M. Atger, M. Perrot-Applanant, and E. Milgrom. 1989. Mechanisms of nuclear localization of the progesterone receptor: evidence for interaction between monomers. Cell 57:1147-1154.
    • (1989) Cell , vol.57 , pp. 1147-1154
    • Guiochon-Mantel, A.1    Lossfelt, H.2    Lescop, P.3    Sar, S.4    Atger, M.5    Perrot-Applanant, M.6    Milgrom, E.7
  • 37
    • 0026523562 scopus 로고
    • Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit
    • Henkel, T., Z. Ulrike, K. van Zee, and P. Baeuerle. 1992. Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit. Cell 68:1121-1133.
    • (1992) Cell , vol.68 , pp. 1121-1133
    • Henkel, T.1    Ulrike, Z.2    Van Zee, K.3    Baeuerle, P.4
  • 38
    • 0024365831 scopus 로고
    • Down-regulation and phosphorylation of glucocorticoid receptors in cultured cells
    • Hoeck, W., S. Rusconi, and B. Groner. 1989. Down-regulation and phosphorylation of glucocorticoid receptors in cultured cells. J. Biol. Chem. 264:14396-14402.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14396-14402
    • Hoeck, W.1    Rusconi, S.2    Groner, B.3
  • 41
    • 0028890810 scopus 로고
    • Selectivity of cell cycle regulation of glucocorticoid receptor function
    • Hsu, S. C., and D. B. DeFranco. 1995. Selectivity of cell cycle regulation of glucocorticoid receptor function. J. Biol. Chem. 270:3359-3364.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3359-3364
    • Hsu, S.C.1    DeFranco, D.B.2
  • 42
    • 0026658220 scopus 로고
    • Cell cycle regulation of glucocorticoid receptor function
    • Hsu, S. C., M. Qi, and D. B. DeFranco. 1992. Cell cycle regulation of glucocorticoid receptor function. EMBO J. 11:3457-3468.
    • (1992) EMBO J. , vol.11 , pp. 3457-3468
    • Hsu, S.C.1    Qi, M.2    DeFranco, D.B.3
  • 43
    • 0029943273 scopus 로고    scopus 로고
    • Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera
    • Htun, H., J. Barsony, I. Renyi, D. L. Gould, and G. U Hager. 1996. Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera. Proc. Natl. Acad. Sci. USA 93:4845-4850.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4845-4850
    • Htun, H.1    Barsony, J.2    Renyi, I.3    Gould, D.L.4    Hager, G.U.5
  • 44
    • 0028356962 scopus 로고
    • Glucocorticoid receptors in ATP-depleted cells. Dephosphorylation, loss of hormone binding, hsp90 dissociation, and ATP-dependent cycling
    • Hu, L. M., J. Bodwell, J. M. Hu, E. Orti, and A. Munck. 1994. Glucocorticoid receptors in ATP-depleted cells. Dephosphorylation, loss of hormone binding, hsp90 dissociation, and ATP-dependent cycling. J. Biol. Chem. 269:6571-6577.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6571-6577
    • Hu, L.M.1    Bodwell, J.2    Hu, J.M.3    Orti, E.4    Munck, A.5
  • 45
    • 0026629289 scopus 로고
    • Monovalent cation selectivity for ATP-dependent association of the glucocorticoid receptor with hsp70 and hsp90
    • Hutchison, K. A., M. J. Czar, L. C. Scherrer, and W. B. Pratt. 1992. Monovalent cation selectivity for ATP-dependent association of the glucocorticoid receptor with hsp70 and hsp90. J. Biol. Chem. 267:14047-14053.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14047-14053
    • Hutchison, K.A.1    Czar, M.J.2    Scherrer, L.C.3    Pratt, W.B.4
  • 46
    • 0027985678 scopus 로고
    • All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome"
    • Hutchison, K. A., K. D. Dittmar, and W. B. Pratt. 1994. All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome". J. Biol. Chem. 269:27894-27899.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27894-27899
    • Hutchison, K.A.1    Dittmar, K.D.2    Pratt, W.B.3
  • 48
    • 0029161506 scopus 로고
    • The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90
    • Hutchison, K. A., L. F. Stancato, J. K. Owens-Grillo, J. L. Johnson, P. Krishna, D. O. Toft, and W. B. Pratt. 1995. The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90. J. Biol. Chem. 270:18841-18847.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18841-18847
    • Hutchison, K.A.1    Stancato, L.F.2    Owens-Grillo, J.K.3    Johnson, J.L.4    Krishna, P.5    Toft, D.O.6    Pratt, W.B.7
  • 50
    • 0029146850 scopus 로고
    • Cyclin-dependent kinase site-regulated signal-dependent nuclear localization of the SW15 yeast transcription factor in mammalian cells
    • Jans, D. A., T. Moll, K. Nasmyth, and P. Jans. 1995. Cyclin-dependent kinase site-regulated signal-dependent nuclear localization of the SW15 yeast transcription factor in mammalian cells. J. Biol. Chem. 270:17064-17067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17064-17067
    • Jans, D.A.1    Moll, T.2    Nasmyth, K.3    Jans, P.4
  • 51
    • 0028863337 scopus 로고
    • Immunocytochemical analysis of hormone mediated nuclear translocation of wild type and mutant glucocorticoid receptors
    • Jewell, C. M., J. C. Webster, K. L. Burnstein, M. Sar, J. E. Bodwell, and J. A. Cidlowski. 1995. Immunocytochemical analysis of hormone mediated nuclear translocation of wild type and mutant glucocorticoid receptors. J. Steroid Biochem. Mol. Biol. 55:135-146.
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.55 , pp. 135-146
    • Jewell, C.M.1    Webster, J.C.2    Burnstein, K.L.3    Sar, M.4    Bodwell, J.E.5    Cidlowski, J.A.6
  • 52
    • 0029029232 scopus 로고
    • Nuclear localization signals overlap DNA-or RNA-binding domains in nucleic acid-binding proteins
    • LaCasse, E. C., and Y. A. Lefebvre. 1995. Nuclear localization signals overlap DNA-or RNA-binding domains in nucleic acid-binding proteins. Nucleic Acids Res. 23:1647-1656.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1647-1656
    • LaCasse, E.C.1    Lefebvre, Y.A.2
  • 54
    • 0017887199 scopus 로고
    • Physical measurements of the liver glucocorticoid receptor
    • Litwack, G., M. H. Cake, R. Filler, and K. Taylor, 1978. Physical measurements of the liver glucocorticoid receptor. Biochem. J. 169:445-448.
    • (1978) Biochem. J. , vol.169 , pp. 445-448
    • Litwack, G.1    Cake, M.H.2    Filler, R.3    Taylor, K.4
  • 55
    • 0027416853 scopus 로고
    • Bidirectional transport of glucocorticoid receptors across the nuclear envelope
    • Madan, A. P., and D. B. DeFranco. 1993. Bidirectional transport of glucocorticoid receptors across the nuclear envelope. Proc. Natl. Acad. Sci. USA 90:3588-3592.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3588-3592
    • Madan, A.P.1    DeFranco, D.B.2
  • 56
    • 0026585315 scopus 로고
    • Molecular mechanism of RU-486 action - A review
    • Mao, J., W. Regelson, and M. Kalimi. 1992. Molecular mechanism of RU-486 action - a review. Mol. Cell. Biochem. 109:1-8.
    • (1992) Mol. Cell. Biochem. , vol.109 , pp. 1-8
    • Mao, J.1    Regelson, W.2    Kalimi, M.3
  • 57
    • 0026028847 scopus 로고
    • Demonstration by confocal microscopy that unliganded overexpressed glucocorticoid receptors are distributed in a nonrandom manner throughout all planes of the nucleus
    • Martins, V. R., W. B. Pratt, L. Terracio, M. A. Hirst, G. M. Ringold, and P. R. Housley. 1991. Demonstration by confocal microscopy that unliganded overexpressed glucocorticoid receptors are distributed in a nonrandom manner throughout all planes of the nucleus. Mol. Endocrinol. 5:217-225.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 217-225
    • Martins, V.R.1    Pratt, W.B.2    Terracio, L.3    Hirst, M.A.4    Ringold, G.M.5    Housley, P.R.6
  • 58
    • 0021213190 scopus 로고
    • RU38486: Potent anti-glucocorticoid activity correlated with strong binding to the cytosolic glucocorticoid receptor followed by an impaired activation
    • Moguilewsky, M., and D. Philbert. 1984. RU38486: potent anti-glucocorticoid activity correlated with strong binding to the cytosolic glucocorticoid receptor followed by an impaired activation. J. Steroid Biochem. 20:271-276.
    • (1984) J. Steroid Biochem. , vol.20 , pp. 271-276
    • Moguilewsky, M.1    Philbert, D.2
  • 59
    • 0025764782 scopus 로고
    • The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5
    • Moll, T., G. Tebb, U. Surana, H. Robitsch, and K. Nasmyth. 1991. The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell 66:743-758.
    • (1991) Cell , vol.66 , pp. 743-758
    • Moll, T.1    Tebb, G.2    Surana, U.3    Robitsch, H.4    Nasmyth, K.5
  • 60
    • 0017038708 scopus 로고
    • Kinetics of glucocorticoid-receptor complexes in rat thymus cells
    • Munck, A., and R. Foley. 1976. Kinetics of glucocorticoid-receptor complexes in rat thymus cells. J. Steroid Biochem. 7:1117-1122.
    • (1976) J. Steroid Biochem. , vol.7 , pp. 1117-1122
    • Munck, A.1    Foley, R.2
  • 61
    • 0021365332 scopus 로고
    • Glucocorticoid-receptor complexes in rat thymus cells. Rapid kinetic behaviour and a cyclic model
    • Munck, A., and N. J. Holbrook. 1984. Glucocorticoid-receptor complexes in rat thymus cells. Rapid kinetic behaviour and a cyclic model. J. Biol. Chem. 259:820-831.
    • (1984) J. Biol. Chem. , vol.259 , pp. 820-831
    • Munck, A.1    Holbrook, N.J.2
  • 62
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport - Signals, mechanisms and regulation
    • Nigg, E. A. 1997. Nucleocytoplasmic transport - signals, mechanisms and regulation. Nature 386:779-787.
    • (1997) Nature , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 63
    • 0029586689 scopus 로고
    • Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells
    • Ogawa, H., S. Inouye, F. I. Tsuji, K. Yasuda, and K. Umesono. 1995. Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells. Proc. Natl. Acad. Sci. USA 92:11899-11903.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11899-11903
    • Ogawa, H.1    Inouye, S.2    Tsuji, F.I.3    Yasuda, K.4    Umesono, K.5
  • 64
    • 0032489013 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The last 200 nanometers
    • Ohno, M., M, Fornerod, and I. W. Mattaj. 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
  • 65
    • 0027516721 scopus 로고
    • Kinetics of glucocorticoid receptor phosphorylation in intact cells. Evidence for hormone-induced hyperphosphorylation after activation and recycling of hyperphosphorylated receptors
    • Orti, E., L. M. Hu, and A. Munck. 1993. Kinetics of glucocorticoid receptor phosphorylation in intact cells. Evidence for hormone-induced hyperphosphorylation after activation and recycling of hyperphosphorylated receptors. J. Biol. Chem. 268:7779-7784.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7779-7784
    • Orti, E.1    Hu, L.M.2    Munck, A.3
  • 66
    • 0028819808 scopus 로고
    • Exploring nuclear pore complex structure and function in molecular detail
    • Panté, N., and V. Aebi. 1995. Exploring nuclear pore complex structure and function in molecular detail. J. Cell Sci. 19:1-11.
    • (1995) J. Cell Sci. , vol.19 , pp. 1-11
    • Panté, N.1    Aebi, V.2
  • 67
    • 0027394555 scopus 로고
    • Mineralocorticoid and glucocorticoid receptor activities distinguished by nonreceptor factors at a composite response element
    • Pearce, D., and K. R. Yamamoto. 1993. Mineralocorticoid and glucocorticoid receptor activities distinguished by nonreceptor factors at a composite response element. Science 259:1161-1165.
    • (1993) Science , vol.259 , pp. 1161-1165
    • Pearce, D.1    Yamamoto, K.R.2
  • 68
    • 0025382801 scopus 로고
    • Signal transduction by steroid hormones: Nuclear localization is differentially regulated in estrogen and glucocorticoid receptors
    • Picard, D., V. Kumar, P. Chambon, and K. R. Yamamoto. 1990. Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors. Cell. Regul. 1:291-299.
    • (1990) Cell. Regul. , vol.1 , pp. 291-299
    • Picard, D.1    Kumar, V.2    Chambon, P.3    Yamamoto, K.R.4
  • 69
    • 0023441954 scopus 로고
    • Two signals mediate hormone-dependent nuclear localization of the giucocorticoid receptor
    • Picard, D., and K. R. Yamamoto. 1987. Two signals mediate hormone-dependent nuclear localization of the giucocorticoid receptor. EMBO J. 6:3333-3340.
    • (1987) EMBO J. , vol.6 , pp. 3333-3340
    • Picard, D.1    Yamamoto, K.R.2
  • 70
    • 0027933911 scopus 로고
    • The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B
    • Pines, J., and T. Hunter. 1994. The differential localization of human cyclins A and B is due to a cytoplasmic retention signal in cyclin B. EMBO J. 13:3772-3781.
    • (1994) EMBO J. , vol.13 , pp. 3772-3781
    • Pines, J.1    Hunter, T.2
  • 71
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt, W. B. 1993. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268: 21455-21458.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 72
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heal shock protein and immunophilin chaperones
    • Pratt, W. B., and D. O. Toft. 1997. Steroid receptor interactions with heal shock protein and immunophilin chaperones. Endocrinol. Rev. 18:306-360.
    • (1997) Endocrinol. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 74
    • 0023882307 scopus 로고
    • Localization of progesterone receptor with monoclonal antibodies to the human progestin receptor
    • Press, M. F., and G. L. Greene. 1988. Localization of progesterone receptor with monoclonal antibodies to the human progestin receptor. Endocrinology 122:1165-75.
    • (1988) Endocrinology , vol.122 , pp. 1165-1175
    • Press, M.F.1    Greene, G.L.2
  • 75
    • 0031876317 scopus 로고    scopus 로고
    • Differential importin-alpha recognition and nuclear transport by nuclear localization signals within the high-mobility-group DNA binding domains of lymphoid enhancer factor 1 and T-cell factor 1
    • Prieve, M. G., K. L. Guttridge, J. Munguia, and M. L. Waterman. 1998. Differential importin-alpha recognition and nuclear transport by nuclear localization signals within the high-mobility-group DNA binding domains of lymphoid enhancer factor 1 and T-cell factor 1. Mol. Cell. Biol. 18:4819-4832.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4819-4832
    • Prieve, M.G.1    Guttridge, K.L.2    Munguia, J.3    Waterman, M.L.4
  • 76
    • 0029887635 scopus 로고    scopus 로고
    • The nuclear localization signal of lymphoid enhancer factor-1 is recognized by two differentially expressed Srp1-nuclear localization sequence receptor proteins
    • Prieve, M. G., K. L. Guttridge, J. E. Munguia, and M. L. Waterman. 1996. The nuclear localization signal of lymphoid enhancer factor-1 is recognized by two differentially expressed Srp1-nuclear localization sequence receptor proteins. J. Biol. Chem. 271:7654-7658.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7654-7658
    • Prieve, M.G.1    Guttridge, K.L.2    Munguia, J.E.3    Waterman, M.L.4
  • 77
    • 0022930322 scopus 로고
    • Interaction between estrogen receptor and subcellular structures of target cells: Nuclear localization of unoccupied receptor and its modification induced by estradiol
    • Puca, G. A., N. Medici, I. Armetta, V. Nigro, B. Moncharmont, and A. M. Molinari. 1986. Interaction between estrogen receptor and subcellular structures of target cells: nuclear localization of unoccupied receptor and its modification induced by estradiol. Ann. N.Y. Acad. Sci. 464:168-189.
    • (1986) Ann. N.Y. Acad. Sci. , vol.464 , pp. 168-189
    • Puca, G.A.1    Medici, N.2    Armetta, I.3    Nigro, V.4    Moncharmont, B.5    Molinari, A.M.6
  • 78
    • 0024360979 scopus 로고
    • v-mos oncoproteins affect the nuclear retention and reutilization of glucocorticoid receptors
    • Qi, M., B. J. Hamilton, and D. DeFranco. 1989. v-mos oncoproteins affect the nuclear retention and reutilization of glucocorticoid receptors. Mol. Endocrinol. 3:1279-1288.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1279-1288
    • Qi, M.1    Hamilton, B.J.2    DeFranco, D.3
  • 79
    • 0026026630 scopus 로고
    • The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen
    • Rihs, H. P., D. A. Jans, H. Fan, and R. Peters. 1991. The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J 10:633-639.
    • (1991) EMBO J , vol.10 , pp. 633-639
    • Rihs, H.P.1    Jans, D.A.2    Fan, H.3    Peters, R.4
  • 80
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins, J., S. M. Dilworth, R. A. Laskey, and C. Dingwall. 1991. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell 64:615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 81
    • 0030964828 scopus 로고    scopus 로고
    • Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors
    • Roderick, H. L., A. K. Campbell, and D. H. Llewellyn. 1997. Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors. FEBS Lett. 405:181-185.
    • (1997) FEBS Lett. , vol.405 , pp. 181-185
    • Roderick, H.L.1    Campbell, A.K.2    Llewellyn, D.H.3
  • 82
    • 0023340611 scopus 로고
    • Functional dissection of the hormone and DNA binding activities of the glucocorticoid receptor
    • Rusconi, S., and K. R. Yamamoto. 1987. Functional dissection of the hormone and DNA binding activities of the glucocorticoid receptor. EMBO J. 6:1309-1315.
    • (1987) EMBO J. , vol.6 , pp. 1309-1315
    • Rusconi, S.1    Yamamoto, K.R.2
  • 84
    • 0025221344 scopus 로고
    • Hormone-free mouse glucocorticoid receptors overexpressed in Chinese hamster ovary cells are localized to the nucleus and are associated with both hsp70 and hsp90
    • Sanchez, E. R., M. Hirst, L. C. Scherrer, H. Y. Tang, M. J. Welsh, J. M. Harmon, S. S. Simons, Jr., G. M. Ringold, and W. B. Pratt. 1990. Hormone-free mouse glucocorticoid receptors overexpressed in Chinese hamster ovary cells are localized to the nucleus and are associated with both hsp70 and hsp90. J. Biol. Chem. 265:20123-20130.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20123-20130
    • Sanchez, E.R.1    Hirst, M.2    Scherrer, L.C.3    Tang, H.Y.4    Welsh, M.J.5    Harmon, J.M.6    Simons S.S., Jr.7    Ringold, G.M.8    Pratt, W.B.9
  • 86
    • 0023792645 scopus 로고
    • Mammalian glucocorticoid receptor derivatives enhance transcription in yeast
    • Schena, M., and K. R. Yamamoto. 1988. Mammalian glucocorticoid receptor derivatives enhance transcription in yeast. Science 241:965-967.
    • (1988) Science , vol.241 , pp. 965-967
    • Schena, M.1    Yamamoto, K.R.2
  • 87
    • 0025644194 scopus 로고
    • Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex
    • Scherrer, L. C., F. C. Dalman, E. Massa, S. Meshinchi, and W. B. Pratt. 1990. Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex. J. Biol. Chem. 265:21397-21400.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21397-21400
    • Scherrer, L.C.1    Dalman, F.C.2    Massa, E.3    Meshinchi, S.4    Pratt, W.B.5
  • 88
    • 0026784554 scopus 로고
    • A heat shock protein complex isolated from rabbit reticulocyte lysate can reconstitute a functional glucocorticoid receptor-Hsp90 complex
    • Scherrer, L. C., K. A. Hutchison, E. R. Sanchez, S. K. Randall, and W. B. Pratt. 1992. A heat shock protein complex isolated from rabbit reticulocyte lysate can reconstitute a functional glucocorticoid receptor-Hsp90 complex. Biochemistry 31:7325-7329.
    • (1992) Biochemistry , vol.31 , pp. 7325-7329
    • Scherrer, L.C.1    Hutchison, K.A.2    Sanchez, E.R.3    Randall, S.K.4    Pratt, W.B.5
  • 89
    • 0025201181 scopus 로고
    • Nuclear accumulation of p53 protein is mediated by several nuclear localization signals and plays a role in tumorigenesis
    • Shaulsky, G., N. Goldfinger, A. Ben-Ze'ev, and V. Rotter. 1990. Nuclear accumulation of p53 protein is mediated by several nuclear localization signals and plays a role in tumorigenesis. Mol. Cell. Biol. 10:6565-6577.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6565-6577
    • Shaulsky, G.1    Goldfinger, N.2    Ben-Ze'ev, A.3    Rotter, V.4
  • 90
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade, K., C. S. Ford, C. Guthrie, and K. Weis. 1997. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90:1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 91
    • 0030054166 scopus 로고    scopus 로고
    • Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90
    • Stancato, L. F., K. A. Hutchison, P. Krishna, and W. B. Pratt. 1996. Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90. Biochemistry 35:554-561.
    • (1996) Biochemistry , vol.35 , pp. 554-561
    • Stancato, L.F.1    Hutchison, K.A.2    Krishna, P.3    Pratt, W.B.4
  • 92
    • 0026664729 scopus 로고
    • Analysis of a developmentally regulated nuclear localization signal in Xenopus
    • Standiford, D. M., and J. D. Richter. 1992. Analysis of a developmentally regulated nuclear localization signal in Xenopus. J. Cell Biol. 118:991-1002.
    • (1992) J. Cell Biol. , vol.118 , pp. 991-1002
    • Standiford, D.M.1    Richter, J.D.2
  • 93
    • 0031008364 scopus 로고    scopus 로고
    • A role of HDJ-2/HSDJ in correcting subnuclear trafficking, transactivation, and transrepression defects of a glucocoricoid receptor zinc finger mutant
    • Tang, Y., C. Ramakrishnan, J. Thomas, and D. B. DeFranco. 1997. A role of HDJ-2/HSDJ in correcting subnuclear trafficking, transactivation, and transrepression defects of a glucocoricoid receptor zinc finger mutant. Mol. Biol. Cell 8:795-809.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 795-809
    • Tang, Y.1    Ramakrishnan, C.2    Thomas, J.3    DeFranco, D.B.4
  • 94
    • 0024542030 scopus 로고
    • Region-specific antiglucocorticoid receptor antibodies selectively recognize the activated form of the ligand-occupied receptor and inhibit the binding of activated complexes to deoxyribonucleic acid
    • Urda, L. A., P. M. Yen, S. S. Simons, Jr., and J. M. Harmon. 1989. Region-specific antiglucocorticoid receptor antibodies selectively recognize the activated form of the ligand-occupied receptor and inhibit the binding of activated complexes to deoxyribonucleic acid. Mol. Endocrinol. 3:251-260.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 251-260
    • Urda, L.A.1    Yen, P.M.2    Simons S.S., Jr.3    Harmon, J.M.4
  • 95
    • 0029052413 scopus 로고
    • Two nuclear localization signals present in the basic-helix 1 domains of MyoD promote its active nuclear translocation and can function independently
    • Vandromme, M., J. C. Cavadore, A. Bonnieu, A. Froeschle, N. Lamb, and A. Fernandez. 1995. Two nuclear localization signals present in the basic-helix 1 domains of MyoD promote its active nuclear translocation and can function independently. Proc. Natl. Acad. Sci. USA 92:4646-4650.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4646-4650
    • Vandromme, M.1    Cavadore, J.C.2    Bonnieu, A.3    Froeschle, A.4    Lamb, N.5    Fernandez, A.6
  • 96
    • 85047673784 scopus 로고    scopus 로고
    • Regulation of transcription factor localization: Fine-tuning of gene expression
    • Vandromme, M., C. Gauthier-Rouviere, N. Lamb, and A. Fernandez. 1996. Regulation of transcription factor localization: fine-tuning of gene expression. Trends Biochem. Sci. 21:59-64.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 59-64
    • Vandromme, M.1    Gauthier-Rouviere, C.2    Lamb, N.3    Fernandez, A.4
  • 97
    • 0024353722 scopus 로고
    • The mouse type IV c-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localization
    • Van Etten, R. A., P. Jackson, and D. Baltimore. 1989. The mouse type IV c-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localization. Cell 58:669-678.
    • (1989) Cell , vol.58 , pp. 669-678
    • Van Etten, R.A.1    Jackson, P.2    Baltimore, D.3
  • 98
    • 0028988731 scopus 로고
    • Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences
    • Weis, K., I. W. Mattaj, and A. I. Lamond. 1995. Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences. Science 268:1049-1053.
    • (1995) Science , vol.268 , pp. 1049-1053
    • Weis, K.1    Mattaj, I.W.2    Lamond, A.I.3
  • 99
    • 0029879676 scopus 로고    scopus 로고
    • The cytostatic function of c-Ab1 is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene products
    • Wen, S. T., P. K. Jackson, and R. A. Van Etten. 1996. The cytostatic function of c-Ab1 is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene products. EMBO J. 15: 1583-1595.
    • (1996) EMBO J. , vol.15 , pp. 1583-1595
    • Wen, S.T.1    Jackson, P.K.2    Van Etten, R.A.3
  • 100
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., J. L. Meinkoth, Y. Y. Tsien, and S. S. Taylor. 1995. Identification of a signal for rapid export of proteins from the nucleus. Cell 82:463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, Y.Y.3    Taylor, S.S.4
  • 101
    • 0023146969 scopus 로고
    • Intracellular localization of the glucocorticoid receptor: Evidence for cytoplasmic and nuclear localization
    • Wikstrom, A. C., O. Bakke, S. Okret, M. Bronnegard, and J. A. Gustafsson. 1987. Intracellular localization of the glucocorticoid receptor: evidence for cytoplasmic and nuclear localization. Endocrinology 120:1232-1242.
    • (1987) Endocrinology , vol.120 , pp. 1232-1242
    • Wikstrom, A.C.1    Bakke, O.2    Okret, S.3    Bronnegard, M.4    Gustafsson, J.A.5
  • 102
    • 0031079648 scopus 로고    scopus 로고
    • Leptomycin B is an inhibitor of nuclear export: Inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA
    • Wolff, B., J. J. Sanglier, and Y. Wang. 1997. Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem. Biol. 4:139-147.
    • (1997) Chem. Biol. , vol.4 , pp. 139-147
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 104
    • 0029829893 scopus 로고    scopus 로고
    • Modular structure of glucocorticoid receptor domains is not equivalent to functional independence. Stability and activity of the steroid binding domain are controlled by sequences in separate domains
    • Xu, M., P. K. Chakraborti, M. J. Garabedian, K. R. Yamamoto, and S. S. Simons. 1996. Modular structure of glucocorticoid receptor domains is not equivalent to functional independence. Stability and activity of the steroid binding domain are controlled by sequences in separate domains. J. Biol. Chem. 271:21430-21438.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21430-21438
    • Xu, M.1    Chakraborti, P.K.2    Garabedian, M.J.3    Yamamoto, K.R.4    Simons, S.S.5
  • 105
    • 0032528001 scopus 로고    scopus 로고
    • Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1
    • Yang, J., E. S. G. Bardes, J. D. Moore, J. Brennan, M. A. Powers, and S. Kornbluth. 1998. Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1. Genes Dev. 12:2131-2143.
    • (1998) Genes Dev. , vol.12 , pp. 2131-2143
    • Yang, J.1    Bardes, E.S.G.2    Moore, J.D.3    Brennan, J.4    Powers, M.A.5    Kornbluth, S.6
  • 106
    • 0030046766 scopus 로고    scopus 로고
    • Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking
    • Yang, J., and D. B. DeFranco. 1996. Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking. Mol. Endocrinol. 10:3-13.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 3-13
    • Yang, J.1    DeFranco, D.B.2
  • 107
    • 0030907634 scopus 로고    scopus 로고
    • Subnuclear trafficking of glucocorticoid receptors in vitro: Chromatin recycling and nuclear export
    • Yang, J., J. Liu, and D. B. DeFranco. 1997. Subnuclear trafficking of glucocorticoid receptors in vitro: chromatin recycling and nuclear export. J. Cell Biol. 137:523-538.
    • (1997) J. Cell Biol. , vol.137 , pp. 523-538
    • Yang, J.1    Liu, J.2    DeFranco, D.B.3
  • 108
    • 0026713869 scopus 로고
    • Cooperation of protosignals for nuclear accumulation of estrogen and progesterone receptors
    • Ylikomi, T., M. T. Bocquel, M. Berry, H. Gronemeyer, and P. Chambon. 1992. Cooperation of protosignals for nuclear accumulation of estrogen and progesterone receptors. EMBO J. 11:3681-3694.
    • (1992) EMBO J. , vol.11 , pp. 3681-3694
    • Ylikomi, T.1    Bocquel, M.T.2    Berry, M.3    Gronemeyer, H.4    Chambon, P.5
  • 109
    • 0030024586 scopus 로고    scopus 로고
    • Role of the C terminus of the glucocorticoid receptor in hormone binding and agonist/antagonist discrimination
    • Zhang, S., X. Liang, and M. Danielsen. 1996. Role of the C terminus of the glucocorticoid receptor in hormone binding and agonist/antagonist discrimination. Mol. Endocrinol. 10:24-34.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 24-34
    • Zhang, S.1    Liang, X.2    Danielsen, M.3


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