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Volumn 72, Issue 1-2, 2000, Pages 1-12

Alteration of the glucocorticoid receptor subcellular localization by non steroidal compounds

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL NUCLEUS RECEPTOR; CHAPERONE; CORTICOSTERONE; CYCLOSPORIN A; DEOXYCORTICOSTERONE; DEXAMETHASONE; GELDANAMYCIN; GLUCOCORTICOID; GLUCOCORTICOID ANTAGONIST; GLUCOCORTICOID RECEPTOR; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HYBRID PROTEIN; IMMUNOPHILIN; IMMUNOSUPPRESSIVE AGENT; MIFEPRISTONE; PROGESTERONE; RECEPTOR PROTEIN; RIFAMPICIN; TACROLIMUS; TRIAMCINOLONE ACETONIDE;

EID: 0034019417     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(99)00146-6     Document Type: Article
Times cited : (46)

References (52)
  • 1
    • 0031848850 scopus 로고    scopus 로고
    • Recent advances in the study of hsp90 structure and mechanism of action
    • Toft D.O. Recent advances in the study of hsp90 structure and mechanism of action. Trends. Endocrinol. Metab. 9:1998;238-243.
    • (1998) Trends. Endocrinol. Metab. , vol.9 , pp. 238-243
    • Toft, D.O.1
  • 2
    • 0031871101 scopus 로고    scopus 로고
    • Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly
    • Pratt W.B., Dittmar K.D. Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly. Trends. Endocrinol. Metab. 9:1998;244-252.
    • (1998) Trends. Endocrinol. Metab. , vol.9 , pp. 244-252
    • Pratt, W.B.1    Dittmar, K.D.2
  • 3
    • 0028999582 scopus 로고
    • Hold'em and fold'em: Chaperones and signal transduction
    • Bohen S.P., Kralli A., Yamamoto K.R. Hold'em and fold'em: Chaperones and signal transduction. Science. 268:1995;1303-1304.
    • (1995) Science , vol.268 , pp. 1303-1304
    • Bohen, S.P.1    Kralli, A.2    Yamamoto, K.R.3
  • 4
    • 0029026540 scopus 로고
    • Role of the protein chaperone YDJ1 in establishing Hsp90- mediated signal transduction pathways
    • Kimura Y., Yahara I., Lindquist S. Role of the protein chaperone YDJ1 in establishing Hsp90- mediated signal transduction pathways. Science. 268:1995;1362-1365.
    • (1995) Science , vol.268 , pp. 1362-1365
    • Kimura, Y.1    Yahara, I.2    Lindquist, S.3
  • 5
    • 0025778706 scopus 로고
    • Cytoplasmic 8S glucocorticoid receptor binds to actin filaments through the 90 kDa heat shock protein moiety
    • Miyata Y., Yahara I. Cytoplasmic 8S glucocorticoid receptor binds to actin filaments through the 90 kDa heat shock protein moiety. J. Biol. Chem. 266:1991;8779-8783.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8779-8783
    • Miyata, Y.1    Yahara, I.2
  • 6
    • 0342651927 scopus 로고
    • Two mammalian heat shock proteins, hsp90 and hsp100, are actin-binding proteins
    • Koyasu S., Nishida E., Kodanaki T., Yahara I. Two mammalian heat shock proteins, hsp90 and hsp100, are actin-binding proteins. Proc. Natl. Acad. Sci. USA. 83:1986;8054-8061.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8054-8061
    • Koyasu, S.1    Nishida, E.2    Kodanaki, T.3    Yahara, I.4
  • 7
    • 0023766565 scopus 로고
    • Evidence that the 90 kda heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells
    • Sanchez E.R., Bresnick E.H., Redmond T., Scherrer L.C., Welsh M.J., Pratt W.B. Evidence that the 90 kda heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells. Mol Endocrinol. 2:1988;756-760.
    • (1988) Mol Endocrinol. , vol.2 , pp. 756-760
    • Sanchez, E.R.1    Bresnick, E.H.2    Redmond, T.3    Scherrer, L.C.4    Welsh, M.J.5    Pratt, W.B.6
  • 8
    • 0027106265 scopus 로고
    • Control of steroid receptor function and cytoplasmic-nuclear transport by heat-shock proteins
    • Pratt W.B. Control of steroid receptor function and cytoplasmic-nuclear transport by heat-shock proteins. BioEssays. 14:1992;841-847.
    • (1992) BioEssays , vol.14 , pp. 841-847
    • Pratt, W.B.1
  • 9
    • 0000949265 scopus 로고    scopus 로고
    • Structural and functional determinants of DNA binding and dimerization by the vitamin D receptor
    • L.P. Freedman, B.D. Lemon, Structural and functional determinants of DNA binding and dimerization by the vitamin D receptor. Vitamin D (1997) 127-148.
    • (1997) Vitamin D , pp. 127-148
    • Freedman, L.P.1    Lemon, B.D.2
  • 10
    • 0031421439 scopus 로고    scopus 로고
    • Chromatin modulation of glucocorticoid and progesterone receptor activity
    • Archer T.K., Deroo B.J., Fryer C.J. Chromatin modulation of glucocorticoid and progesterone receptor activity. Trends. Endocrinol. Metab. 8:1997;384-390.
    • (1997) Trends. Endocrinol. Metab. , vol.8 , pp. 384-390
    • Archer, T.K.1    Deroo, B.J.2    Fryer, C.J.3
  • 11
    • 0023186939 scopus 로고
    • Antiglucocorticoid effect suggest why steroid hormone is required for receptors to bind DNA in-vivo but not in-vitro
    • Groyer A., Scheiwzer-Groyer G., Cadepond F., Marrillier M., Baulieu E.E. Antiglucocorticoid effect suggest why steroid hormone is required for receptors to bind DNA in-vivo but not in-vitro. Nature. 328:1987;624-626.
    • (1987) Nature , vol.328 , pp. 624-626
    • Groyer, A.1    Scheiwzer-Groyer, G.2    Cadepond, F.3    Marrillier, M.4    Baulieu, E.E.5
  • 12
    • 0024246492 scopus 로고
    • Association of the glucocorticoid receptor binding subunit with the 90K nonsteroid-binding component is stabilized by both steroidal and nonsteroidal antiglucocorticoids in intact cells
    • Lefebvre P., Danze P.M., Sablonniére B., Formstecher P., Richard C., Dautrevaux M. Association of the glucocorticoid receptor binding subunit with the 90K nonsteroid-binding component is stabilized by both steroidal and nonsteroidal antiglucocorticoids in intact cells. Biochemistry. 27:1988;9186-9194.
    • (1988) Biochemistry , vol.27 , pp. 9186-9194
    • Lefebvre, P.1    Danze, P.M.2    Sablonniére, B.3    Formstecher, P.4    Richard, C.5    Dautrevaux, M.6
  • 13
    • 0030987768 scopus 로고    scopus 로고
    • Disruption of the glucocorticoid receptor assembly with heat shock protein 90 by a peptidic antiglucocorticoid
    • Dao-Phan H.-P., Formstecher P., Lefebvre P. Disruption of the glucocorticoid receptor assembly with heat shock protein 90 by a peptidic antiglucocorticoid. Molec. Endocrinol. 11:1997;962-972.
    • (1997) Molec. Endocrinol. , vol.11 , pp. 962-972
    • Dao-Phan, H.-P.1    Formstecher, P.2    Lefebvre, P.3
  • 14
    • 0030808079 scopus 로고    scopus 로고
    • Geldanamycin, a heat shock protein 90-binding steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus
    • Czar M.J., Galigniana M.D., Silverstein A.M., Pratt W.B. Geldanamycin, a heat shock protein 90-binding steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus. Biochemistry. 36:1997;7776-7785.
    • (1997) Biochemistry , vol.36 , pp. 7776-7785
    • Czar, M.J.1    Galigniana, M.D.2    Silverstein, A.M.3    Pratt, W.B.4
  • 15
    • 0030930051 scopus 로고    scopus 로고
    • Inhibition of mineralocorticoid and glucocorticoid receptor function by the heat shock protein 90-binding agent geldanamycin
    • Bamberger C.M., Wald M., Bamberger A.M., Schulte H.M. Inhibition of mineralocorticoid and glucocorticoid receptor function by the heat shock protein 90-binding agent geldanamycin. Mol. Cell Endocrinol. 131:1997;233-240.
    • (1997) Mol. Cell Endocrinol. , vol.131 , pp. 233-240
    • Bamberger, C.M.1    Wald, M.2    Bamberger, A.M.3    Schulte, H.M.4
  • 16
    • 0030046766 scopus 로고    scopus 로고
    • Assessment of glucocorticoid receptor heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking
    • Yang J., DeFranco D.B. Assessment of glucocorticoid receptor heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking. Mol. Endocrinol. 10:1996;3-13.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 3-13
    • Yang, J.1    Defranco, D.B.2
  • 17
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell L., Cook P. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol. Endocrinol. 10:1996;705-712.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 18
    • 0029067084 scopus 로고
    • Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyltransferase activity in LMCAT cells: A possible role for different heat shock protein-binding immunophilins in glucocorticosteroid receptor-mediated gene expression
    • Renoir J.M., Mercier-Bodard C., Hoffmann K., Lebihan S., Ning Y.M., Sanchez E.R., Handschumacher R.E., Baulieu E.E. Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyltransferase activity in LMCAT cells: A possible role for different heat shock protein-binding immunophilins in glucocorticosteroid receptor-mediated gene expression. Proc. Natl. Acad. Sci. USA. 92:1995;4977-4981.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4977-4981
    • Renoir, J.M.1    Mercier-Bodard, C.2    Hoffmann, K.3    Lebihan, S.4    Ning, Y.M.5    Sanchez, E.R.6    Handschumacher, R.E.7    Baulieu, E.E.8
  • 19
    • 0029943273 scopus 로고    scopus 로고
    • Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera
    • Htun H., Barsony J., Renyi I., Gould D.L., Hager G.L. Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera. Proc. Natl. Acad. Sci. USA. 93:1996;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.L.5
  • 20
    • 0023829691 scopus 로고
    • RU 486 stabilizes a high molecular weight form of the glucocorticoid receptor containing the 90K non-steroid binding protein in intact thymus cells
    • Lefebvre P., Formstecher P., Richard C., Dautrevaux M. RU 486 stabilizes a high molecular weight form of the glucocorticoid receptor containing the 90K non-steroid binding protein in intact thymus cells. Biochem. Biophys. Res. Commun. 150:1988;1221-1229.
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , pp. 1221-1229
    • Lefebvre, P.1    Formstecher, P.2    Richard, C.3    Dautrevaux, M.4
  • 21
    • 0022981876 scopus 로고
    • In vivo protein-DNA interactions in a glucocorticoid response element require the presence of the hormone
    • Becker P.B., Gloss B., Schmid W., Strähle U., Schütz G. In vivo protein-DNA interactions in a glucocorticoid response element require the presence of the hormone. Nature. 324:1986;686-688.
    • (1986) Nature , vol.324 , pp. 686-688
    • Becker, P.B.1    Gloss, B.2    Schmid, W.3    Strähle, U.4    Schütz, G.5
  • 22
    • 0027157804 scopus 로고
    • FK506 binding to the 56 kda immunophilin (Hsp56) in the glucocorticoid receptor heterocomplex has no effect on receptor folding or function
    • Hutchison K.A., Scherrer L.C., Czar M.J., Ning Y.M., Sanchez E.R., Leach K.L., Deibel M.R., Pratt W.B. FK506 binding to the 56 kda immunophilin (Hsp56) in the glucocorticoid receptor heterocomplex has no effect on receptor folding or function. Biochemistry. 32:1993;3953-3957.
    • (1993) Biochemistry , vol.32 , pp. 3953-3957
    • Hutchison, K.A.1    Scherrer, L.C.2    Czar, M.J.3    Ning, Y.M.4    Sanchez, E.R.5    Leach, K.L.6    Deibel, M.R.7    Pratt, W.B.8
  • 23
    • 0027480072 scopus 로고
    • Potentiation of glucocorticoid receptor-mediated gene expression by the immunophilin ligands FK506 and rapamycin
    • Ning Y.M., Sanchez E.R. Potentiation of glucocorticoid receptor-mediated gene expression by the immunophilin ligands FK506 and rapamycin. J. Biol. Chem. 268:1993;6073-6076.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6073-6076
    • Ning, Y.M.1    Sanchez, E.R.2
  • 24
    • 0029101382 scopus 로고
    • The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor
    • Owens-Grillo J., Hoffmann K., Hutchison K.A., Yem A.W., Deibel M.R., Handschumacher R.E., Pratt W.B. The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin hsp56 bind to a common site on hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor. J. Biol. Chem. 270:1995;20479-20484.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20479-20484
    • Owens-Grillo, J.1    Hoffmann, K.2    Hutchison, K.A.3    Yem, A.W.4    Deibel, M.R.5    Handschumacher, R.E.6    Pratt, W.B.7
  • 26
    • 0029015872 scopus 로고
    • ATP induces dissociation of the 90 kDa heat shock protein (hsp90) from F-actin: Interference with the binding of heavy meromyosin
    • Kellermayer M.S.Z., Csermely P. ATP induces dissociation of the 90 kDa heat shock protein (hsp90) from F-actin: Interference with the binding of heavy meromyosin. Biochem. Biophys. Res. Commun. 211:1995;166-174.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 166-174
    • Kellermayer, M.S.Z.1    Csermely, P.2
  • 27
    • 0030869037 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery - The role of p23 is to stabilize receptor-hsp90 heterocomplexes formed by hsp90-p60-hsp70
    • Dittmar K.D., Demady D.R., Stancato L.F., Krishna P., Pratt W.B. Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery - The role of p23 is to stabilize receptor-hsp90 heterocomplexes formed by hsp90-p60-hsp70. J. Biol. Chem. 272:1997;21213-21220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21213-21220
    • Dittmar, K.D.1    Demady, D.R.2    Stancato, L.F.3    Krishna, P.4    Pratt, W.B.5
  • 28
    • 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., Pratt W.B. 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. 272:1997;13047-13054.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13047-13054
    • Dittmar, K.D.1    Pratt, W.B.2
  • 29
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • Whitesell L., Cook P. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol. Endocrinol. 10:1996;705-712.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 31
    • 0023340611 scopus 로고
    • Functional dissection of the hormone and DNA binding activities on the glucocorticoid receptor
    • Rusconi S., Yamamoto K.R. Functional dissection of the hormone and DNA binding activities on the glucocorticoid receptor. EMBO J. 6:1987;1309-1315.
    • (1987) EMBO J. , vol.6 , pp. 1309-1315
    • Rusconi, S.1    Yamamoto, K.R.2
  • 32
    • 0026345830 scopus 로고
    • Two regions of the Mouse Mammary Tumor Long Terminal Repeat regulate the activity of its promoter in mammary cell lines
    • Lefebvre P., Berard D.S., Cordingley M.G., Hager G.L. Two regions of the Mouse Mammary Tumor Long Terminal Repeat regulate the activity of its promoter in mammary cell lines. Mol. Cell. Biol. 11:1991;2529-2537.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2529-2537
    • Lefebvre, P.1    Berard, D.S.2    Cordingley, M.G.3    Hager, G.L.4
  • 33
    • 0031587928 scopus 로고    scopus 로고
    • MRNA expression of HNF-4 isoforms and of HNF-1 alpha/HNF-1 beta variants and differentiation of human cell lines that mimic highly specialized phenotypes of intestinal epithelium
    • Suaud L., Joseph B., Formstecher P., Laine B. mRNA expression of HNF-4 isoforms and of HNF-1 alpha/HNF-1 beta variants and differentiation of human cell lines that mimic highly specialized phenotypes of intestinal epithelium. Biochem. Biophys. Res. Commun. 235:1997;820-825.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 820-825
    • Suaud, L.1    Joseph, B.2    Formstecher, P.3    Laine, B.4
  • 34
    • 0032581032 scopus 로고    scopus 로고
    • H11-H12 loop retinoic acid receptor mutants exhibit distinct trans-activating and trans-repressing activities in the presence of natural or synthetic retinoids
    • Lefebvre B., Mouchon A., Formstecher P., Lefebvre P. H11-H12 loop retinoic acid receptor mutants exhibit distinct trans-activating and trans-repressing activities in the presence of natural or synthetic retinoids. Biochemistry. 37:1998;9240-9249.
    • (1998) Biochemistry , vol.37 , pp. 9240-9249
    • Lefebvre, B.1    Mouchon, A.2    Formstecher, P.3    Lefebvre, P.4
  • 35
    • 0032230285 scopus 로고    scopus 로고
    • Positive and negative discrimination of estrogen receptor agonists and antagonists using site-specific DNA recombinase fusion proteins
    • Logie C., Nichols M., Myles K., Funder J.W., Stewart A.F. Positive and negative discrimination of estrogen receptor agonists and antagonists using site-specific DNA recombinase fusion proteins. Mol. Endocrinol. 12:1998;1120-1132.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1120-1132
    • Logie, C.1    Nichols, M.2    Myles, K.3    Funder, J.W.4    Stewart, A.F.5
  • 36
    • 0028200018 scopus 로고
    • The hormone binding domain of the mineralocorticoid receptor can regulate heterologous activities in cis
    • Fankhauser C.P., Briand P.A., Picard D. The hormone binding domain of the mineralocorticoid receptor can regulate heterologous activities in cis. Biochem. Biophys. Res. Commun. 200:1994;195-201.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 195-201
    • Fankhauser, C.P.1    Briand, P.A.2    Picard, D.3
  • 37
    • 0027941792 scopus 로고
    • Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: Presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity
    • Durand B., Saunders M., Gaudon C., Roy B., Losson R., Chambon P. Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: Presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity. EMBO J. 13:1994;5370-5382.
    • (1994) EMBO J. , vol.13 , pp. 5370-5382
    • Durand, B.1    Saunders, M.2    Gaudon, C.3    Roy, B.4    Losson, R.5    Chambon, P.6
  • 38
    • 0028233763 scopus 로고
    • Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor
    • Barettino D., Ruiz M.D.M.V., Stunnenberg H.G. Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor. EMBO J. 13:1994;3039-3049.
    • (1994) EMBO J. , vol.13 , pp. 3039-3049
    • Barettino, D.1    Ruiz, M.D.M.V.2    Stunnenberg, H.G.3
  • 39
    • 0027403603 scopus 로고
    • Reconstitution of ligand-mediated glucocorticoid receptor activity by trans-acting functional domains
    • Spanjaard R.A., Chin W.W. Reconstitution of ligand-mediated glucocorticoid receptor activity by trans-acting functional domains. Mol. Endocrinol. 7:1993;12-16.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 12-16
    • Spanjaard, R.A.1    Chin, W.W.2
  • 40
    • 0031914323 scopus 로고    scopus 로고
    • The antibiotic rifampicin is a nonsteroidal ligand and activator of the human glucocorticoid receptor
    • Calleja C., Pascussi J.M., Mani J.C., Maurel P., Vilarem M.J. The antibiotic rifampicin is a nonsteroidal ligand and activator of the human glucocorticoid receptor. Nat. Med. 4:1998;92-96.
    • (1998) Nat. Med. , vol.4 , pp. 92-96
    • Calleja, C.1    Pascussi, J.M.2    Mani, J.C.3    Maurel, P.4    Vilarem, M.J.5
  • 41
    • 0028862366 scopus 로고
    • Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus
    • Czar M.J., Lyons R.H., Welsh M.J., Renoir J.M., Pratt W.B. Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus. Mol. Endocrinol. 9:1995;1549-1560.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 1549-1560
    • Czar, M.J.1    Lyons, R.H.2    Welsh, M.J.3    Renoir, J.M.4    Pratt, W.B.5
  • 42
    • 0029013333 scopus 로고
    • LEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones
    • Kralli A., Bohen S.P., Yamamoto K.R. LEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones. Proc. Natl. Acad. Sci. USA. 92:1995;4701-4705.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4701-4705
    • Kralli, A.1    Bohen, S.P.2    Yamamoto, K.R.3
  • 43
    • 0029100883 scopus 로고
    • Cyclosporin A promotes nuclear transfer of a cytoplasmic progesterone receptor mutant
    • Jung-Testas, Lebeau M.C., Catelli M.G., Baulieu E.E. Cyclosporin A promotes nuclear transfer of a cytoplasmic progesterone receptor mutant. C. R. Acad. Sci. [III]. 318:1995;873-878.
    • (1995) C. R. Acad. Sci. [III] , vol.318 , pp. 873-878
    • Jung-Testas1    Lebeau, M.C.2    Catelli, M.G.3    Baulieu, E.E.4
  • 44
    • 0023024149 scopus 로고
    • Calmodulin-regulated binding of the 90 kDa heat shock protein to actin filaments
    • Nishida E., Koyasu S., Sakai H., Yahara I. Calmodulin-regulated binding of the 90 kDa heat shock protein to actin filaments. J. Biol. Chem. 261:1986;16033-16036.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16033-16036
    • Nishida, E.1    Koyasu, S.2    Sakai, H.3    Yahara, I.4
  • 47
    • 0031757167 scopus 로고    scopus 로고
    • Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton
    • Galigniana M.D., Scruggs J.L., Herrington J., Welsh M.J., Cartersu C., Housley P.R., Pratt W.B. Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton. Mol. Endocrinol. 12:1998;1903-1913.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1903-1913
    • Galigniana, M.D.1    Scruggs, J.L.2    Herrington, J.3    Welsh, M.J.4    Cartersu, C.5    Housley, P.R.6    Pratt, W.B.7
  • 48
    • 0026731880 scopus 로고
    • Evidence for reversible, non-microtubule and non-microfilament-dependent nuclear translocation of hsp90 after heat shock in human fibroblasts
    • Akner G., Mossberg K., Sundqvist K.G., Gustafsson J.A., Wikstrom A.C. Evidence for reversible, non-microtubule and non-microfilament-dependent nuclear translocation of hsp90 after heat shock in human fibroblasts. Eur. J. Cell Biol. 58:1992;356-364.
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 356-364
    • Akner, G.1    Mossberg, K.2    Sundqvist, K.G.3    Gustafsson, J.A.4    Wikstrom, A.C.5
  • 49
    • 0033052229 scopus 로고    scopus 로고
    • The cytoskeletal network controls c-Jun expression and glucocorticoid receptor transcriptional activity in an antagonistic and cell-type-specific manner
    • Oren A., Herschkovitz I., Bendror V., Holdengreber Y., BenShaul R., Seger R., Vardimon L. The cytoskeletal network controls c-Jun expression and glucocorticoid receptor transcriptional activity in an antagonistic and cell-type-specific manner. Mol. Cell Biol. 19:1999;1742-1750.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1742-1750
    • Oren, A.1    Herschkovitz, I.2    Bendror, V.3    Holdengreber, Y.4    Benshaul, R.5    Seger, R.6    Vardimon, L.7
  • 50
    • 0028892084 scopus 로고
    • A role for hsp90 in retinoid receptor signal transduction
    • Holley S.J., Yamamoto K.R. A role for hsp90 in retinoid receptor signal transduction. Mol. Biol. Cell. 6:1995;1833-1842.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1833-1842
    • Holley, S.J.1    Yamamoto, K.R.2
  • 51
    • 0028979080 scopus 로고
    • Subcellular distribution of the glucocorticoid receptor and evidence for its association with microtubules
    • Akner G., Wikström A.C., Gustafsson J.Å. Subcellular distribution of the glucocorticoid receptor and evidence for its association with microtubules. J. Ster. Biochem. Molec. Biol. 52:1995;1-16.
    • (1995) J. Ster. Biochem. Molec. Biol. , vol.52 , pp. 1-16
    • Akner, G.1    Wikström, A.C.2    Gustafsson, J.Å.3
  • 52
    • 0032846619 scopus 로고    scopus 로고
    • Immunocytochemical analysis of the glucocorticoid receptor alpha isoform (GRalpha) using GRalpha-specific antibody
    • Oakley R.H., Webster J.C., Jewell C.M., Sar M., Cidlowski J.A. Immunocytochemical analysis of the glucocorticoid receptor alpha isoform (GRalpha) using GRalpha-specific antibody. Steroids. 64:1999;742-751.
    • (1999) Steroids , vol.64 , pp. 742-751
    • Oakley, R.H.1    Webster, J.C.2    Jewell, C.M.3    Sar, M.4    Cidlowski, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.