메뉴 건너뛰기




Volumn 54, Issue C, 1998, Pages 167-205

Steroid Hormone Receptors and Heat Shock Proteins

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; STEROID RECEPTOR;

EID: 0031612706     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0083-6729(08)60925-5     Document Type: Article
Times cited : (23)

References (198)
  • 1
    • 0026511544 scopus 로고
    • Subunit composition of the untransformed glucocorticoid receptor in the cytosol and in the cell
    • Alexis M.N., Mavridou I., and Mitsiou D.J. Subunit composition of the untransformed glucocorticoid receptor in the cytosol and in the cell. Eur. J. Biochem. 204 (1992) 75-84
    • (1992) Eur. J. Biochem. , vol.204 , pp. 75-84
    • Alexis, M.N.1    Mavridou, I.2    Mitsiou, D.J.3
  • 2
    • 0027288627 scopus 로고
    • The steroid binding domain influences intracellular solubility of the Baculovirus overexpressed glucocorticoid and mineralocorticoid receptors
    • Alnemri E.S., and Litwack G. The steroid binding domain influences intracellular solubility of the Baculovirus overexpressed glucocorticoid and mineralocorticoid receptors. Biochemistry 32 (1993) 5387-5393
    • (1993) Biochemistry , vol.32 , pp. 5387-5393
    • Alnemri, E.S.1    Litwack, G.2
  • 3
    • 0024295007 scopus 로고
    • Covalent stabilization of the nontransformed chick oviduct cytosol progesterone receptor by chemical cross-linking
    • Aranyi P., Radanyi C., Renoir M., Devin J., and Baulieu E.-E. Covalent stabilization of the nontransformed chick oviduct cytosol progesterone receptor by chemical cross-linking. Biochemistry 27 (1988) 1330-1336
    • (1988) Biochemistry , vol.27 , pp. 1330-1336
    • Aranyi, P.1    Radanyi, C.2    Renoir, M.3    Devin, J.4    Baulieu, E.-E.5
  • 4
    • 0026722491 scopus 로고
    • Immunosuppressants FK506 and rapamycin function as reversal agents of the multidrug resistance phenotype
    • Arceci R.J., Stieglitz K., and Bierer B.E. Immunosuppressants FK506 and rapamycin function as reversal agents of the multidrug resistance phenotype. Blood 80 (1992) 1528-1536
    • (1992) Blood , vol.80 , pp. 1528-1536
    • Arceci, R.J.1    Stieglitz, K.2    Bierer, B.E.3
  • 7
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker J., and Craig E.A. Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219 (1994) 11-23
    • (1994) Eur. J. Biochem. , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 8
    • 0028786089 scopus 로고
    • Distinct functions of the 90 kDa heat-shock protein (Hsp90) in oestrogen and mineralocorticoid receptor activity: Effects of hsp90 deletion mutants
    • Binard N., Lombes M., and Baulieu E.-E. Distinct functions of the 90 kDa heat-shock protein (Hsp90) in oestrogen and mineralocorticoid receptor activity: Effects of hsp90 deletion mutants. Biochem. J. 311 (1995) 797-804
    • (1995) Biochem. J. , vol.311 , pp. 797-804
    • Binard, N.1    Lombes, M.2    Baulieu, E.-E.3
  • 9
    • 0027742105 scopus 로고
    • Glucocorticoid receptors: ATP-dependent cycling and hormone-dependent hyperphosphorylation
    • Bodwell J.E., Hu L.-M., Hu J.-M., Orti E., and Munck A. Glucocorticoid receptors: ATP-dependent cycling and hormone-dependent hyperphosphorylation. J. Steroid Biochem. Mol. Biol. 47 (1993) 31-38
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.47 , pp. 31-38
    • Bodwell, J.E.1    Hu, L.-M.2    Hu, J.-M.3    Orti, E.4    Munck, A.5
  • 10
    • 0028858102 scopus 로고
    • Hsp90 mutants disrupt glucocorticoid receptor ligand binding and destabilize aporeceptor complexes
    • Bohen S.P. Hsp90 mutants disrupt glucocorticoid receptor ligand binding and destabilize aporeceptor complexes. J. Biol. Chem. 270 (1995) 29433-29438
    • (1995) J. Biol. Chem. , vol.270 , pp. 29433-29438
    • Bohen, S.P.1
  • 11
    • 0027359404 scopus 로고
    • Isolation of hsp90 mutants by screening for decreased steroid receptor function
    • Bohen S.P., and Yamamoto K.R. Isolation of hsp90 mutants by screening for decreased steroid receptor function. Proc. Natl. Acad. Sci. USA 90 (1993) 11424-11428
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11424-11428
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 12
    • 0002830140 scopus 로고
    • Modulation of steroid receptor signal transduction by heat shock proteins
    • Morimoto R.I., Tissieres A., and Georgopoulos C. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • Bohen S.P., and Yamamoto K.R. Modulation of steroid receptor signal transduction by heat shock proteins. In: Morimoto R.I., Tissieres A., and Georgopoulos C. (Eds). The Biology of Heat Shock Proteins and Molecular Chaperones (1994), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 313-334
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 313-334
    • Bohen, S.P.1    Yamamoto, K.R.2
  • 13
    • 0024421221 scopus 로고
    • Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich K.A., Farrelly F.W., Finkelstein D.B., Taulien J., and Lindquist S. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9 (1989) 3919-3930
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 14
    • 0027214172 scopus 로고
    • Expression of an mdr gene is associated with a new form of resistance to dexamethasone-induced apoptosis
    • Bourgeois S., Gruol D.J., Newby R.F., and Rajah F.M. Expression of an mdr gene is associated with a new form of resistance to dexamethasone-induced apoptosis. Mol. Endocrinol. 7 (1993) 840-851
    • (1993) Mol. Endocrinol. , vol.7 , pp. 840-851
    • Bourgeois, S.1    Gruol, D.J.2    Newby, R.F.3    Rajah, F.M.4
  • 15
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet W., Ruff M., Chambon P., Gronemeyer H., and Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α. Nature 375 (1995) 377-382
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 16
    • 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., Dalman F.C., Sanchez E.R., and Pratt W.B. 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 (1989) 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
  • 17
    • 0025128697 scopus 로고
    • r 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex
    • r 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex. Biochemistry 29 (1990) 520-527
    • (1990) Biochemistry , vol.29 , pp. 520-527
    • Bresnick, E.H.1    Dalman, F.C.2    Pratt, W.B.3
  • 19
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • Buchner J. Supervising the fold: Functional principles of molecular chaperones. FASEB J. 10 (1996) 10-19
    • (1996) FASEB J. , vol.10 , pp. 10-19
    • Buchner, J.1
  • 20
    • 0025992101 scopus 로고
    • Estrogen-dependent alterations in differentiation state of myeloid cells caused by a v-myb/estrogen receptor fusion protein
    • Burk O., and Klempnauer K.-H. Estrogen-dependent alterations in differentiation state of myeloid cells caused by a v-myb/estrogen receptor fusion protein. EMBO J. 10 (1991) 3713-3719
    • (1991) EMBO J. , vol.10 , pp. 3713-3719
    • Burk, O.1    Klempnauer, K.-H.2
  • 21
    • 0027305758 scopus 로고
    • A bacterially expressed mineralocorticoid receptor is associated in vitro with the 90-kilodalton heat shock protein and shows typical hormone- and DNA-binding characteristics
    • Caamano C.A., Morano M.I., Patel P.D., Watson S.J., and Akil H. A bacterially expressed mineralocorticoid receptor is associated in vitro with the 90-kilodalton heat shock protein and shows typical hormone- and DNA-binding characteristics. Biochemistry 32 (1993) 8589-8595
    • (1993) Biochemistry , vol.32 , pp. 8589-8595
    • Caamano, C.A.1    Morano, M.I.2    Patel, P.D.3    Watson, S.J.4    Akil, H.5
  • 22
    • 0027429134 scopus 로고
    • Interaction of glucocorticosteroid receptor and wildtype or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells
    • Cadepond F., Binart N., Chambraud B., Jibard N., Schweizer-Groyer G., Segard-Maurel I., and Baulieu E.E. Interaction of glucocorticosteroid receptor and wildtype or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells. Proc. Natl. Acad. Sci. USA 90 (1993) 10434-10438
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10434-10438
    • Cadepond, F.1    Binart, N.2    Chambraud, B.3    Jibard, N.4    Schweizer-Groyer, G.5    Segard-Maurel, I.6    Baulieu, E.E.7
  • 24
    • 0028898217 scopus 로고
    • Hormone-dependent trans-activation by the human androgen receptor is regulated by a dnaj protein
    • Caplan A.J., Langley E., Wilson E.M., and Vidal J. Hormone-dependent trans-activation by the human androgen receptor is regulated by a dnaj protein. J. Biol. Chem. 270 (1995) 5251-5257
    • (1995) J. Biol. Chem. , vol.270 , pp. 5251-5257
    • Caplan, A.J.1    Langley, E.2    Wilson, E.M.3    Vidal, J.4
  • 26
    • 0027985148 scopus 로고
    • Conservation of hsp90 macromolecular complexes in Saccharomyces cerevisiae
    • Chang H.-C.J., and Lindquist S. Conservation of hsp90 macromolecular complexes in Saccharomyces cerevisiae. J. Biol. Chem. 269 (1994) 24983-24988
    • (1994) J. Biol. Chem. , vol.269 , pp. 24983-24988
    • Chang, H.-C.J.1    Lindquist, S.2
  • 27
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the hsp90 cochaperone Stil (p60
    • Chang H.-C.J., Nathan D.F., and Lindquist S. In vivo analysis of the hsp90 cochaperone Stil (p60. Mol. Cell. Biol. 17 (1997) 318-325
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 318-325
    • Chang, H.-C.J.1    Nathan, D.F.2    Lindquist, S.3
  • 28
    • 0029760873 scopus 로고    scopus 로고
    • A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock
    • Chen C.-F., Chen Y., Dai K., Chen P.-L., Riley D.J., and Lee W.-H. A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock. Mol. Cell. Biol. 16 (1996) 4691-4699
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4691-4699
    • Chen, C.-F.1    Chen, Y.2    Dai, K.3    Chen, P.-L.4    Riley, D.J.5    Lee, W.-H.6
  • 29
    • 0029751136 scopus 로고    scopus 로고
    • The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant
    • Chen M.-S., Silverstein A.M., Pratt W.B., and Chinkers M. The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant. J. Biol. Chem. 271 (1996) 32315-32320
    • (1996) J. Biol. Chem. , vol.271 , pp. 32315-32320
    • Chen, M.-S.1    Silverstein, A.M.2    Pratt, W.B.3    Chinkers, M.4
  • 30
    • 0029885423 scopus 로고    scopus 로고
    • Interaction of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70
    • Chen S., Prapapanich V., Rimerman R.A., Honore B., and Smith D.F. Interaction of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70. Mol. Endocrinol. 10 (1996) 682-693
    • (1996) Mol. Endocrinol. , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honore, B.4    Smith, D.F.5
  • 31
    • 0030071724 scopus 로고    scopus 로고
    • Effects of tyrosine kinase inhibitors on the proliferation of human breast cancer cell lines and proteins important in the Ras signaling pathway
    • Clark J.W., Santos-Moore A., Stevenson L.E., and Frackelton Jr. A.R. Effects of tyrosine kinase inhibitors on the proliferation of human breast cancer cell lines and proteins important in the Ras signaling pathway. Int. J. Cancer 65 (1996) 186-191
    • (1996) Int. J. Cancer , vol.65 , pp. 186-191
    • Clark, J.W.1    Santos-Moore, A.2    Stevenson, L.E.3    Frackelton Jr., A.R.4
  • 32
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of hsp70
    • Cyr D.M., Langer T., and Douglas M.G. DnaJ-like proteins: Molecular chaperones and specific regulators of hsp70. Trends Biochem. Sci. 19 (1994) 176-181
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 34
    • 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., and 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
  • 35
    • 0030808079 scopus 로고    scopus 로고
    • Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus
    • Czar M.J., Galigniana M.D., Silverstein A.M., and Pratt W.B. Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits 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
  • 36
    • 0021288960 scopus 로고
    • Effects of molybdate and endogenous inhibitors on steroid-receptor inactivation, transformation, and translocation
    • Dahmer M.K., Housley P.R., and Pratt W.B. Effects of molybdate and endogenous inhibitors on steroid-receptor inactivation, transformation, and translocation. Annu. Rev. Physiol. 46 (1984) 67-81
    • (1984) Annu. Rev. Physiol. , vol.46 , pp. 67-81
    • Dahmer, M.K.1    Housley, P.R.2    Pratt, W.B.3
  • 37
    • 0024332067 scopus 로고
    • Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation
    • Dalman F.C., Bresnick E.H., Patel P.D., Perdew G.H., Watson S.J., and Pratt W.B. Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation. J. Biol. Chem. 264 (1989) 19815-19821
    • (1989) J. Biol. Chem. , vol.264 , pp. 19815-19821
    • Dalman, F.C.1    Bresnick, E.H.2    Patel, P.D.3    Perdew, G.H.4    Watson, S.J.5    Pratt, W.B.6
  • 38
    • 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., Koenig R.J., Perdew G.H., Massa E., and Pratt W.B. 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 (1990) 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
  • 40
    • 0026077942 scopus 로고
    • Cell-free synthesis of rat glucocorticoid receptor in rabbit reticulocyte lysate
    • Daniel V., Maksymowych A.B., Alnemri E.S., and Litwack G. Cell-free synthesis of rat glucocorticoid receptor in rabbit reticulocyte lysate. J. Biol. Chem. 266 (1991) 1320-1325
    • (1991) J. Biol. Chem. , vol.266 , pp. 1320-1325
    • Daniel, V.1    Maksymowych, A.B.2    Alnemri, E.S.3    Litwack, G.4
  • 41
    • 0029186560 scopus 로고
    • Nucleocytoplasmic shuttling of steroid receptors
    • Litwack G. (Ed), Academic Press, San Diego
    • DeFranco D.B., Madan A.P., Tang Y., Chandran U.R., Xiao N., and Yang J. Nucleocytoplasmic shuttling of steroid receptors. In: Litwack G. (Ed). Vitamins and Hormones 51 (1995), Academic Press, San Diego 315-338
    • (1995) Vitamins and Hormones , vol.51 , pp. 315-338
    • DeFranco, D.B.1    Madan, A.P.2    Tang, Y.3    Chandran, U.R.4    Xiao, N.5    Yang, J.6
  • 43
    • 0024596723 scopus 로고
    • Translation of glucocorticoid receptor mRNA in vitro yields a nonactivated protein
    • Denis M., and Gustafsson J.-A. Translation of glucocorticoid receptor mRNA in vitro yields a nonactivated protein. J. Biol. Chem. 264 (1989) 6005-6008
    • (1989) J. Biol. Chem. , vol.264 , pp. 6005-6008
    • Denis, M.1    Gustafsson, J.-A.2
  • 44
    • 0027743317 scopus 로고
    • Heat shock protein 70 is associated in substoichiometric amounts with the rat hepatic glucocorticoid receptor
    • Diehl E.E., and Schmidt T.J. Heat shock protein 70 is associated in substoichiometric amounts with the rat hepatic glucocorticoid receptor. Biochemistry 32 (1993) 13510-13515
    • (1993) Biochemistry , vol.32 , pp. 13510-13515
    • Diehl, E.E.1    Schmidt, T.J.2
  • 45
    • 17544384391 scopus 로고    scopus 로고
    • Reconstitution of the steroid receptor-hsp90 heterocomplex assembly system of rabbit reticulocyte lysate
    • Dittmar K.D., Hutchison K.A., Owens-Grillo J.K., and Pratt W.B. Reconstitution of the steroid receptor-hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. J. Biol. Chem. 271 (1996) 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
  • 46
    • 0021235161 scopus 로고
    • Polypeptide components of two 8 S forms of chicken oviduct progesterone receptors
    • Dougherty J.J., Puri R.K., and Toft D.O. Polypeptide components of two 8 S forms of chicken oviduct progesterone receptors. J. Biol. Chem. 259 (1984) 8004-8009
    • (1984) J. Biol. Chem. , vol.259 , pp. 8004-8009
    • Dougherty, J.J.1    Puri, R.K.2    Toft, D.O.3
  • 47
    • 0026524142 scopus 로고
    • Heat shock alters the composition of heteromeric steroid receptor complexes and enhances receptor activity in vivo
    • Edwards D.P., Estes P.A., Fadok V.A., Bona B.J., Onate S., Nordeen S.K., and Welch W.J. Heat shock alters the composition of heteromeric steroid receptor complexes and enhances receptor activity in vivo. Biochemistry 31 (1992) 2482-2491
    • (1992) Biochemistry , vol.31 , pp. 2482-2491
    • Edwards, D.P.1    Estes, P.A.2    Fadok, V.A.3    Bona, B.J.4    Onate, S.5    Nordeen, S.K.6    Welch, W.J.7
  • 48
    • 0024396222 scopus 로고
    • Chimaeras of Myc on-coprotein and steroid receptors cause hormone-dependent transformation of cells
    • Eilers M., Picard D., Yamamoto K.R., and Bishop J.M. Chimaeras of Myc on-coprotein and steroid receptors cause hormone-dependent transformation of cells. Nature 340 (1989) 66-68
    • (1989) Nature , vol.340 , pp. 66-68
    • Eilers, M.1    Picard, D.2    Yamamoto, K.R.3    Bishop, J.M.4
  • 49
    • 0029670092 scopus 로고    scopus 로고
    • The estrogen-dependent c-JunER protein causes a reversible loss of mammary epithelial cell polarity involving a destabilization of adherens junctions
    • Fialka I., Schwarz H., Reichmann E., Oft M., Busslinger M., and Beug H. The estrogen-dependent c-JunER protein causes a reversible loss of mammary epithelial cell polarity involving a destabilization of adherens junctions. J. Cell Biol. 132 (1996) 1115-1132
    • (1996) J. Cell Biol. , vol.132 , pp. 1115-1132
    • Fialka, I.1    Schwarz, H.2    Reichmann, E.3    Oft, M.4    Busslinger, M.5    Beug, H.6
  • 50
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman B.C., Toft D.O., and Morimoto R.I. Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274 (1996) 1718-1720
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 51
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman J., and Höhfeld J. Chaperones get in touch: The Hip-Hop connection. Trends Biochem. Sci. 22 (1997) 87-92
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Höhfeld, J.2
  • 52
    • 0001779561 scopus 로고
    • Intracellular and plasma membrane-resident glucocorticoid receptors in rodent leukemia models
    • Gametchu B. (Ed), Molecular Biology Intelligence Unit, R. G. Landes Company, Austin, TX.
    • Gametchu B., Chen F., and Watson C.S. Intracellular and plasma membrane-resident glucocorticoid receptors in rodent leukemia models. In: Gametchu B. (Ed). Glucocorticoid Receptor Structure and Leukemic Cell Responses (1995), Molecular Biology Intelligence Unit, R. G. Landes Company, Austin, TX. 75-103
    • (1995) Glucocorticoid Receptor Structure and Leukemic Cell Responses , pp. 75-103
    • Gametchu, B.1    Chen, F.2    Watson, C.S.3
  • 53
    • 0002502630 scopus 로고
    • Stucture of the nonactivated glucocorticoid receptor and activation to DNA binding
    • Gametchu B. (Ed), Molecular Biology Intellegence Unit, R. G. Landes Company, Austin, TX.
    • Gehring U. Stucture of the nonactivated glucocorticoid receptor and activation to DNA binding. In: Gametchu B. (Ed). Glucocorticoid Receptor Structure and Leukemic Cell Responses (1995), Molecular Biology Intellegence Unit, R. G. Landes Company, Austin, TX. 33-56
    • (1995) Glucocorticoid Receptor Structure and Leukemic Cell Responses , pp. 33-56
    • Gehring, U.1
  • 54
    • 0021991462 scopus 로고
    • Heteromeric nature of glucocorticoid hormone receptors
    • Gehring U., and Arndt H. Heteromeric nature of glucocorticoid hormone receptors. FEBS Lett. 179 (1985) 138-142
    • (1985) FEBS Lett. , vol.179 , pp. 138-142
    • Gehring, U.1    Arndt, H.2
  • 56
    • 0023199059 scopus 로고
    • Subunit dissociation and activation of wild-type and mutant glucocorticoid receptors
    • Gehring U., Mugele K., Arndt H., and Busch W. Subunit dissociation and activation of wild-type and mutant glucocorticoid receptors. Mol. Cell. Endocrinol. 53 (1987) 33-44
    • (1987) Mol. Cell. Endocrinol. , vol.53 , pp. 33-44
    • Gehring, U.1    Mugele, K.2    Arndt, H.3    Busch, W.4
  • 58
    • 0023254634 scopus 로고
    • Oestradiol induction of a glucocorticoid-responsive gene by a chimaeric receptor
    • Green S., and Chambon P. Oestradiol induction of a glucocorticoid-responsive gene by a chimaeric receptor. Nature 325 (1987) 75-78
    • (1987) Nature , vol.325 , pp. 75-78
    • Green, S.1    Chambon, P.2
  • 59
    • 0029440036 scopus 로고
    • Transcription factors 3: Nuclear receptors
    • Gronemeyer H., and Laudet V. Transcription factors 3: Nuclear receptors. Protein Profile 2 (1995) 1173-1308
    • (1995) Protein Profile , vol.2 , pp. 1173-1308
    • Gronemeyer, H.1    Laudet, V.2
  • 61
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.-U. Molecular chaperones in cellular protein folding. Nature 381 (1996) 571-580
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.-U.1
  • 62
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • Hartl F.-U., Hlodan R., and Langer T. Molecular chaperones in protein folding: The art of avoiding sticky situations. Trends Biochem. Sci. 19 (1994) 20-25
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 20-25
    • Hartl, F.-U.1    Hlodan, R.2    Langer, T.3
  • 63
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle
    • Höhfeld J., Minami Y., and Hartl F.-U. Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle. Cell 83 (1995) 589-598
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    Hartl, F.-U.3
  • 64
    • 0023794190 scopus 로고
    • Multiple and cooperative trans-activation domains of the human glucocorticoid receptor
    • Hollenberg S.M., and Evans R.M. Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell 55 (1988) 899-906
    • (1988) Cell , vol.55 , pp. 899-906
    • Hollenberg, S.M.1    Evans, R.M.2
  • 65
    • 0028892084 scopus 로고
    • A role for hsp90 in retinoid receptor signal transduction
    • Holley S.J., and 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
  • 66
    • 0026640657 scopus 로고
    • Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1
    • Honoré B., Leffers H., Madsen P., Rasmussen H.H., Vandekerckhove J., and Celis J.E. Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1. J. Biol. Chem. 267 (1992) 8485-8491
    • (1992) J. Biol. Chem. , vol.267 , pp. 8485-8491
    • Honoré, B.1    Leffers, H.2    Madsen, P.3    Rasmussen, H.H.4    Vandekerckhove, J.5    Celis, J.E.6
  • 67
    • 0022407992 scopus 로고
    • The molybdate-stabilized L-cell glucocorticoid receptor isolated by affinity chromatography or with a monoclonal antibody is associated with a 90-92-kDa nonsteroid-binding phosphoprotein
    • Housley P.R., Sanchez E.R., Westphal H.M., Beato M., and Pratt W.B. The molybdate-stabilized L-cell glucocorticoid receptor isolated by affinity chromatography or with a monoclonal antibody is associated with a 90-92-kDa nonsteroid-binding phosphoprotein. J. Biol. Chem. 260 (1985) 13810-13817
    • (1985) J. Biol. Chem. , vol.260 , pp. 13810-13817
    • Housley, P.R.1    Sanchez, E.R.2    Westphal, H.M.3    Beato, M.4    Pratt, W.B.5
  • 68
    • 0023828728 scopus 로고
    • Evidence for intracellular association of the glucocorticoid receptor with the 90-kDa heat shock protein
    • Howard K.J., and Distelhorst C.W. Evidence for intracellular association of the glucocorticoid receptor with the 90-kDa heat shock protein. J. Biol. Chem. 263 (1988) 3474-3481
    • (1988) J. Biol. Chem. , vol.263 , pp. 3474-3481
    • Howard, K.J.1    Distelhorst, C.W.2
  • 69
    • 0030035038 scopus 로고    scopus 로고
    • Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase
    • Hu J., and Seeger C. Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc. Natl. Acad. Sci. USA 93 (1996) 1060-1064
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1060-1064
    • Hu, J.1    Seeger, C.2
  • 71
    • 0026629289 scopus 로고
    • Monovalent cation selectivity for ATP-dependent association of the glucocorticoid receptor with hsp70 and hsp90
    • Hutchison K.A., Czar M.J., Scherrer L.C., and Pratt W.B. Monovalent cation selectivity for ATP-dependent association of the glucocorticoid receptor with hsp70 and hsp90. J. Biol. Chem. 267 (1992) 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
  • 72
    • 0027157804 scopus 로고
    • FK506 binding to the 56-kilodalton 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., Sanchez E.R., Leach K.L., Deibel M.R., and Pratt W.B. FK506 binding to the 56-kilodalton 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.4    Sanchez, E.R.5    Leach, K.L.6    Deibel, M.R.7    Pratt, W.B.8
  • 73
    • 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., Dittmar K.D., and Pratt W.B. 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 (1994) 27894-27899
    • (1994) J. Biol. Chem. , vol.269 , pp. 27894-27899
    • Hutchison, K.A.1    Dittmar, K.D.2    Pratt, W.B.3
  • 74
    • 0027969323 scopus 로고
    • Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90
    • Hutchison K.A., Dittmar K.D., Czar M.J., and Pratt W.B. Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90. J. Biol. Chem. 269 (1994) 5043-5049
    • (1994) J. Biol. Chem. , vol.269 , pp. 5043-5049
    • Hutchison, K.A.1    Dittmar, K.D.2    Czar, M.J.3    Pratt, W.B.4
  • 75
    • 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., Stancato L.F., Owens-Grillo J.K., Johnson J.L., Krishna P., Toft D.O., and Pratt W.B. 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 (1995) 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
  • 76
    • 0028181755 scopus 로고
    • Association of the βγ subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein, hsp90
    • Inanobe A., Takahashi K., and Katada T. Association of the βγ subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein, hsp90. J. Biochem. 115 (1994) 486-492
    • (1994) J. Biochem. , vol.115 , pp. 486-492
    • Inanobe, A.1    Takahashi, K.2    Katada, T.3
  • 78
    • 0021261383 scopus 로고
    • Common non-hormone binding component in non-transformed chick oviduct receptors for four steroid hormones
    • Joab I., Radanyi C., Renoir M., Buchou T., Catelli M.-G., Binart N., Mester J., and Baulieu E.-E. Common non-hormone binding component in non-transformed chick oviduct receptors for four steroid hormones. Nature 308 (1984) 850-853
    • (1984) Nature , vol.308 , pp. 850-853
    • Joab, I.1    Radanyi, C.2    Renoir, M.3    Buchou, T.4    Catelli, M.-G.5    Binart, N.6    Mester, J.7    Baulieu, E.-E.8
  • 79
    • 0028027504 scopus 로고
    • A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23
    • Johnson J.L., and Toft D.O. A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. J. Biol. Chem. 269 (1994) 24989-24993
    • (1994) J. Biol. Chem. , vol.269 , pp. 24989-24993
    • Johnson, J.L.1    Toft, D.O.2
  • 80
    • 0029075280 scopus 로고
    • Binding of p23 and hsp90 during assembly with the progesterone receptor
    • Johnson J.L., and Toft D.O. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol. Endocrinol. 9 (1995) 670-678
    • (1995) Mol. Endocrinol. , vol.9 , pp. 670-678
    • Johnson, J.L.1    Toft, D.O.2
  • 81
    • 0028266874 scopus 로고
    • Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes
    • Johnson J.L., Beito T.G., Kreo C.J., and Toft D.O. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol. Cell. Biol. 14 (1994) 1956-1963
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1956-1963
    • Johnson, J.L.1    Beito, T.G.2    Kreo, C.J.3    Toft, D.O.4
  • 82
    • 0029872081 scopus 로고    scopus 로고
    • The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes
    • Johnson J., Corbisier R., Stensgard B., and Toft D.O. The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes. J. Steroid Biochem. Mol. Biol. 56 (1996) 31-37
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.56 , pp. 31-37
    • Johnson, J.1    Corbisier, R.2    Stensgard, B.3    Toft, D.O.4
  • 85
    • 0029026540 scopus 로고
    • Role of protein chaperone YDJ1 in establishing hsp90-mediated signal transduction pathways
    • Kimura Y., Yahara I., and Lindquist S. Role of 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
  • 89
    • 0030035694 scopus 로고    scopus 로고
    • An FK506-sensitive transporter selectively decreases intracellular levels and potency of steroid hormones
    • Kralli A., and Yamamoto K.R. An FK506-sensitive transporter selectively decreases intracellular levels and potency of steroid hormones. J. Biol. Chem. 271 (1996) 17152-17156
    • (1996) J. Biol. Chem. , vol.271 , pp. 17152-17156
    • Kralli, A.1    Yamamoto, K.R.2
  • 90
    • 0029013333 scopus 로고
    • LEM1, an ATP-binding-cassette transporter, selectively modulates the biological potency of steroid hormones
    • Kralli A., Bohen S.P., and 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
  • 91
    • 0028331871 scopus 로고
    • Steroid hormone receptor phosphorylation: Is there a physiological role?
    • Kuiper G.G.J.M., and Brinkmann A.O. Steroid hormone receptor phosphorylation: Is there a physiological role?. Mol. Cell. Endocrinol. 100 (1994) 103-107
    • (1994) Mol. Cell. Endocrinol. , vol.100 , pp. 103-107
    • Kuiper, G.G.J.M.1    Brinkmann, A.O.2
  • 92
    • 0021708673 scopus 로고
    • Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies
    • Lai B.-T., Chin N.W., Stanek A.E., Keh W., and Lanks K.W. Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies. Mol. Cell. Biol. 4 (1984) 2802-2810
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2802-2810
    • Lai, B.-T.1    Chin, N.W.2    Stanek, A.E.3    Keh, W.4    Lanks, K.W.5
  • 95
    • 0023896947 scopus 로고
    • The glucocorticoid receptor at the protein level
    • Litwack G. The glucocorticoid receptor at the protein level. Cancer Res. 48 (1988) 2636-2640
    • (1988) Cancer Res. , vol.48 , pp. 2636-2640
    • Litwack, G.1
  • 96
    • 0030462612 scopus 로고    scopus 로고
    • Two eukaryote-specific regions of hsp82 are dispensable for its viability and signal transduction functions in yeast
    • Louvion J.-F., Warth R., and Picard D. Two eukaryote-specific regions of hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc. Natl. Acad. Sci. USA 93 (1996) 13937-13942
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13937-13942
    • Louvion, J.-F.1    Warth, R.2    Picard, D.3
  • 98
    • 0026731621 scopus 로고
    • Interaction of the 90-kDa heat shock protein with native and in vitro translated androgen receptor and receptor fragments
    • Marivoet S., Van Dijck P., Verhoeven G., and Heyns W. Interaction of the 90-kDa heat shock protein with native and in vitro translated androgen receptor and receptor fragments. Mol. Cell. Endocrinol. 88 (1992) 165-174
    • (1992) Mol. Cell. Endocrinol. , vol.88 , pp. 165-174
    • Marivoet, S.1    Van Dijck, P.2    Verhoeven, G.3    Heyns, W.4
  • 99
    • 0023006215 scopus 로고
    • Glucocorticoid receptors lacking hormone-binding activity are bound in nuclei of ATP-depleted cells
    • Mendel D.B., Bodwell J.E., and Munck A. Glucocorticoid receptors lacking hormone-binding activity are bound in nuclei of ATP-depleted cells. Nature 324 (1986) 478-480
    • (1986) Nature , vol.324 , pp. 478-480
    • Mendel, D.B.1    Bodwell, J.E.2    Munck, A.3
  • 100
    • 0029922568 scopus 로고    scopus 로고
    • Mutational analysis of hsp90α dimerization and subcellular localization: Dimer disruption does not impede "in vivo" interaction with estrogen receptor
    • Meng X., Devin J., Sullivan W.P., Toft D., Baulieu E.-E., and Catelli M.-G. Mutational analysis of hsp90α dimerization and subcellular localization: Dimer disruption does not impede "in vivo" interaction with estrogen receptor. J. Cell Sci. 109 (1996) 1677-1687
    • (1996) J. Cell Sci. , vol.109 , pp. 1677-1687
    • Meng, X.1    Devin, J.2    Sullivan, W.P.3    Toft, D.4    Baulieu, E.-E.5    Catelli, M.-G.6
  • 102
    • 0029812759 scopus 로고    scopus 로고
    • c-erbB-2 receptor protein-tyrosine kinase induced by gel-danamycin
    • c-erbB-2 receptor protein-tyrosine kinase induced by gel-danamycin. J. Biol. Chem. 271 (1996) 22796-22801
    • (1996) J. Biol. Chem. , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 103
    • 0020635972 scopus 로고
    • In vivo activation and nuclear binding of the AtT-20 mouse pituitary tumor cell glucocorticoid receptor
    • Miyabe S., and Harrison R.W. In vivo activation and nuclear binding of the AtT-20 mouse pituitary tumor cell glucocorticoid receptor. Endocrinology 112 (1983) 2174-2180
    • (1983) Endocrinology , vol.112 , pp. 2174-2180
    • Miyabe, S.1    Harrison, R.W.2
  • 104
    • 0018417911 scopus 로고
    • Activation of steroid hormone-receptor complexes in intact target cells in physiological conditions
    • Munck A., and Foley R. Activation of steroid hormone-receptor complexes in intact target cells in physiological conditions. Nature 278 (1979) 752-754
    • (1979) Nature , vol.278 , pp. 752-754
    • Munck, A.1    Foley, R.2
  • 105
    • 0021988845 scopus 로고
    • Development of a monoclonal antibody to the rabbit 8.5S uterine progestin receptor
    • Nakao K., Myers J.E., and Faber L.E. Development of a monoclonal antibody to the rabbit 8.5S uterine progestin receptor. Can. J. Biochem. Cell. Biol. 63 (1985) 33-40
    • (1985) Can. J. Biochem. Cell. Biol. , vol.63 , pp. 33-40
    • Nakao, K.1    Myers, J.E.2    Faber, L.E.3
  • 106
    • 0029037110 scopus 로고
    • Mutational analysis of hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan D.F., and Lindquist S. Mutational analysis of hsp90 function: Interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15 (1995) 3917-3925
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 107
    • 0025161860 scopus 로고
    • The transformed glucocorticoid receptor has a lower steroid-binding affinity than the nontransformed receptor
    • Nemoto T., Ohara-Nemoto Y., and Gustafsson J.-A. The transformed glucocorticoid receptor has a lower steroid-binding affinity than the nontransformed receptor. Biochemistry 29 (1990) 1880-1886
    • (1990) Biochemistry , vol.29 , pp. 1880-1886
    • Nemoto, T.1    Ohara-Nemoto, Y.2    Gustafsson, J.-A.3
  • 108
    • 0026640216 scopus 로고
    • Association of the 90-kDa heat shock protein does not affect the ligand-binding ability of androgen receptor
    • Nemoto T., Ohara-Nemoto Y., and Ota M. Association of the 90-kDa heat shock protein does not affect the ligand-binding ability of androgen receptor. J. Steroid Biochem. Mol. Biol. 42 (1992) 803-812
    • (1992) J. Steroid Biochem. Mol. Biol. , vol.42 , pp. 803-812
    • Nemoto, T.1    Ohara-Nemoto, Y.2    Ota, M.3
  • 109
    • 0024462407 scopus 로고
    • Identification and characterization of nuclear retinoic acid-binding activity in human myeloblastic leukemia HL-60 cells
    • Nervi C., Grippo J.F., Sherman M.I., George M.D., and Jetten A.M. Identification and characterization of nuclear retinoic acid-binding activity in human myeloblastic leukemia HL-60 cells. Proc. Natl. Acad. Sci. USA 86 (1989) 5854-5858
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5854-5858
    • Nervi, C.1    Grippo, J.F.2    Sherman, M.I.3    George, M.D.4    Jetten, A.M.5
  • 110
    • 0024469206 scopus 로고
    • Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae
    • Nicolet C.M., and Craig E.A. Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9 (1989) 3638-3646
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3638-3646
    • Nicolet, C.M.1    Craig, E.A.2
  • 111
    • 0027480072 scopus 로고
    • Potentiation of glucocorticoid receptor-mediated gene expression by the immunophilin ligands FK506 and rapamycin
    • Ning Y.-M., and 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
  • 112
    • 0028922055 scopus 로고
    • Stabilization in vitro of the untransformed glucocorticoid receptor complex of S49 lymphocytes by the immunophilin ligand FK506
    • Ning Y.-M., and Sanchez E.R. Stabilization in vitro of the untransformed glucocorticoid receptor complex of S49 lymphocytes by the immunophilin ligand FK506. J. Steroid Biochem. Mol. Biol. 52 (1995) 187-194
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.52 , pp. 187-194
    • Ning, Y.-M.1    Sanchez, E.R.2
  • 113
    • 0030818414 scopus 로고    scopus 로고
    • Heat stress proteins and transcription factors
    • Nover L., and Scharf K.-D. Heat stress proteins and transcription factors. CMLS Cell. Mol. Life Sci. 53 (1997) 80-103
    • (1997) CMLS Cell. Mol. Life Sci. , vol.53 , pp. 80-103
    • Nover, L.1    Scharf, K.-D.2
  • 115
    • 0028152845 scopus 로고
    • In vivo antitumor activity of herbimycin A, a tyrosine kinase inhibitor, targeted against BCR/ABL oncoprotein in mice bearing BCR/ABL-transfected cells
    • Okabe M., Uehara Y., Noshima T., Itaya T., Kunieda Y., and Kurosawa M. In vivo antitumor activity of herbimycin A, a tyrosine kinase inhibitor, targeted against BCR/ABL oncoprotein in mice bearing BCR/ABL-transfected cells. Leuk. Res. 18 (1994) 867-873
    • (1994) Leuk. Res. , vol.18 , pp. 867-873
    • Okabe, M.1    Uehara, Y.2    Noshima, T.3    Itaya, T.4    Kunieda, Y.5    Kurosawa, M.6
  • 116
    • 0022412623 scopus 로고
    • Molybdate-stabilized glucocorticoid receptor: Evidence for a receptor heteromer
    • Okret S., Wikström A.-C., and Gustafsson J.-A. Molybdate-stabilized glucocorticoid receptor: Evidence for a receptor heteromer. Biochemistry 24 (1985) 6581-6586
    • (1985) Biochemistry , vol.24 , pp. 6581-6586
    • Okret, S.1    Wikström, A.-C.2    Gustafsson, J.-A.3
  • 117
    • 0024579336 scopus 로고
    • Phosphorylation of glucocorticoid receptor-associated and free forms of the ~90-kDa heat shock protein before and after receptor activation
    • Orti E., Mendel D.B., and Munck A. Phosphorylation of glucocorticoid receptor-associated and free forms of the ~90-kDa heat shock protein before and after receptor activation. J. Biol. Chem. 264 (1989) 231-237
    • (1989) J. Biol. Chem. , vol.264 , pp. 231-237
    • Orti, E.1    Mendel, D.B.2    Munck, A.3
  • 118
    • 0026597699 scopus 로고
    • Phosphorylation of steroid hormone receptors
    • Orti E., Bodwell J.E., and Munck A. Phosphorylation of steroid hormone receptors. Endocr. Rev. 13 (1992) 105-128
    • (1992) Endocr. Rev. , vol.13 , pp. 105-128
    • Orti, E.1    Bodwell, J.E.2    Munck, A.3
  • 119
    • 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
    • 20384
    • Owens-Grillo J.K., Hoffmann K., Hutchison K.A., Yem A.W., Deibel Jr. M.R., Handschumacher R.E., and 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 20384
    • (1995) J. Biol. Chem. , vol.270 , pp. 20479
    • Owens-Grillo, J.K.1    Hoffmann, K.2    Hutchison, K.A.3    Yem, A.W.4    Deibel Jr., M.R.5    Handschumacher, R.E.6    Pratt, W.B.7
  • 120
    • 0029889955 scopus 로고    scopus 로고
    • A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains
    • Owens-Grillo J.K., Czar M.J., Hutchison K.A., Hoffmann K., Perdew G.H., and Pratt W.B. A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains. J. Biol. Chem. 271 (1996) 13468-13475
    • (1996) J. Biol. Chem. , vol.271 , pp. 13468-13475
    • Owens-Grillo, J.K.1    Czar, M.J.2    Hutchison, K.A.3    Hoffmann, K.4    Perdew, G.H.5    Pratt, W.B.6
  • 121
    • 0028925081 scopus 로고
    • Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding
    • Pappas T.C., Gametchu B., and Watson C.S. Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding. FASEB J. 9 (1995) 404-410
    • (1995) FASEB J. , vol.9 , pp. 404-410
    • Pappas, T.C.1    Gametchu, B.2    Watson, C.S.3
  • 122
    • 0026495863 scopus 로고
    • Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes
    • Peattie D.A., Harding M.W., Fleming M.A., DeCenzo M.T., Lippke J.A., Livingston D.J., and Benasutti M. Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. Proc. Natl. Acad. Sci. USA 89 (1992) 10974-10978
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10974-10978
    • Peattie, D.A.1    Harding, M.W.2    Fleming, M.A.3    DeCenzo, M.T.4    Lippke, J.A.5    Livingston, D.J.6    Benasutti, M.7
  • 123
    • 0025815731 scopus 로고
    • Evidence that the 90kDa heat shock protein (hsp90) exists in cytosol in heteromeric complexes containing hsp70 and three other proteins with Mr of 63,000, 56,000, and 50,000
    • Perdew G.H., and Whitelaw M.L. Evidence that the 90kDa heat shock protein (hsp90) exists in cytosol in heteromeric complexes containing hsp70 and three other proteins with Mr of 63,000, 56,000, and 50,000. J. Biol. Chem. 266 (1991) 6708-6713
    • (1991) J. Biol. Chem. , vol.266 , pp. 6708-6713
    • Perdew, G.H.1    Whitelaw, M.L.2
  • 124
    • 0023789310 scopus 로고
    • A movable and regulable inactivating function within the steroid binding domain of the glucocorticoid receptor
    • Picard D., Salser S.J., and Yamamoto K.R. A movable and regulable inactivating function within the steroid binding domain of the glucocorticoid receptor. Cell 54 (1988) 1073-1080
    • (1988) Cell , vol.54 , pp. 1073-1080
    • Picard, D.1    Salser, S.J.2    Yamamoto, K.R.3
  • 126
    • 0029964506 scopus 로고    scopus 로고
    • Molecular cloning of human p48, a transient component of progesterone receptor complexes and an hsp70-binding protein
    • Prapapanich V., Chen S., Nair S.C., Rimerman R.A., and Smith D.F. Molecular cloning of human p48, a transient component of progesterone receptor complexes and an hsp70-binding protein. Mol. Endocrinol. 10 (1996) 420-431
    • (1996) Mol. Endocrinol. , vol.10 , pp. 420-431
    • Prapapanich, V.1    Chen, S.2    Nair, S.C.3    Rimerman, R.A.4    Smith, D.F.5
  • 127
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt W.B. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268 (1993) 21455-21458
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 128
    • 0028418758 scopus 로고
    • Chaperone functions of the heat shock proteins associated with steroid receptors
    • Pratt W.B., and Welsh M.J. Chaperone functions of the heat shock proteins associated with steroid receptors. Sem. Cell Biol. 5 (1994) 83-93
    • (1994) Sem. Cell Biol. , vol.5 , pp. 83-93
    • Pratt, W.B.1    Welsh, M.J.2
  • 129
    • 0027366385 scopus 로고
    • The hsp56 immunophilin component of steroid receptor heterocomplexes: Could this be the elusive nuclear localization signal-binding protein?
    • Pratt W.B., Czar M.J., Stancato L.F., and Owens J.K. The hsp56 immunophilin component of steroid receptor heterocomplexes: Could this be the elusive nuclear localization signal-binding protein?. J. Steroid. Biochem. Mol. Biol. 46 (1993) 269-279
    • (1993) J. Steroid. Biochem. Mol. Biol. , vol.46 , pp. 269-279
    • Pratt, W.B.1    Czar, M.J.2    Stancato, L.F.3    Owens, J.K.4
  • 130
    • 0029681032 scopus 로고    scopus 로고
    • Molecular chaperoning of steroid hormone receptors
    • Feige U., Morimoto R.I., Yahara I., and Polla B.S. (Eds), Birkhauser, Basel
    • Pratt W.B., Gehring U., and Toft D.O. Molecular chaperoning of steroid hormone receptors. In: Feige U., Morimoto R.I., Yahara I., and Polla B.S. (Eds). Stress-Inducible Cellular Responses (1996), Birkhauser, Basel 79-95
    • (1996) Stress-Inducible Cellular Responses , pp. 79-95
    • Pratt, W.B.1    Gehring, U.2    Toft, D.O.3
  • 131
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the hsp90 molecular chaperone
    • Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., and Pearl L.H. Identification and structural characterization of the ATP/ADP-binding site in the hsp90 molecular chaperone. Cell 90 (1997) 65-75
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 132
    • 0020646901 scopus 로고
    • The glucocorticoid receptor in GH1 cells
    • Raaka B.M., and Samuels H.H. The glucocorticoid receptor in GH1 cells. J. Biol. Chem. 158 (1983) 417-425
    • (1983) J. Biol. Chem. , vol.158 , pp. 417-425
    • Raaka, B.M.1    Samuels, H.H.2
  • 133
    • 0028217326 scopus 로고
    • Direct demonstration of high affinity interactions of immunosuppressant drugs with the drug binding site of the human P-glycoprotein
    • Rao U.S., and Scarborough G.A. Direct demonstration of high affinity interactions of immunosuppressant drugs with the drug binding site of the human P-glycoprotein. Mol. Pharmacol. 45 (1994) 773-776
    • (1994) Mol. Pharmacol. , vol.45 , pp. 773-776
    • Rao, U.S.1    Scarborough, G.A.2
  • 134
    • 0030050335 scopus 로고    scopus 로고
    • Cyclophilin 40 (Cyp-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with Cyp-40 for hsp90 binding
    • Ratajczak T., and Carrello A. Cyclophilin 40 (Cyp-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with Cyp-40 for hsp90 binding. J. Biol. Chem. 271 (1996) 2961-2965
    • (1996) J. Biol. Chem. , vol.271 , pp. 2961-2965
    • Ratajczak, T.1    Carrello, A.2
  • 135
    • 0027438228 scopus 로고
    • The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59
    • Ratajczak T., Carrello A., Mark P.J., Warner B.J., Simpson R.J., Moritz R.L., and House A.K. The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59. J. Biol. Chem. 268 (1993) 13187-13192
    • (1993) J. Biol. Chem. , vol.268 , pp. 13187-13192
    • Ratajczak, T.1    Carrello, A.2    Mark, P.J.3    Warner, B.J.4    Simpson, R.J.5    Moritz, R.L.6    House, A.K.7
  • 136
    • 0029869782 scopus 로고    scopus 로고
    • Cyclosporin A potentiates estradiol-induced expression of the catepsin D gene in MCF7 breast cancer cells
    • Ratajczak T., Mark P.J., Martin R.L., and Minchin R.F. Cyclosporin A potentiates estradiol-induced expression of the catepsin D gene in MCF7 breast cancer cells. Biochem. Biophys. Res. Commun. 220 (1996) 208-212
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 208-212
    • Ratajczak, T.1    Mark, P.J.2    Martin, R.L.3    Minchin, R.F.4
  • 137
    • 0026687819 scopus 로고
    • Heterotetrameric structure of the human progesterone receptor
    • Rehberger P., Rexin M., and Gehring U. Heterotetrameric structure of the human progesterone receptor. Proc. Natl. Acad. Sci. USA 89 (1992) 8001-8005
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8001-8005
    • Rehberger, P.1    Rexin, M.2    Gehring, U.3
  • 138
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • Renaud J.-P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., and Moras D. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378 (1995) 681-689
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.-P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 139
    • 0025337581 scopus 로고
    • The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein
    • Renoir J.-M., Radanyi C., Faber L.E., and Baulieu E.-E. The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein. J. Biol. Chem. 265 (1990) 10740-10745
    • (1990) J. Biol. Chem. , vol.265 , pp. 10740-10745
    • Renoir, J.-M.1    Radanyi, C.2    Faber, L.E.3    Baulieu, E.-E.4
  • 141
    • 0029067084 scopus 로고
    • Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyl-transferase 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., Le Bihan S., Ning Y.-M., Sanchez E.R., Handschumacher R.E., and Baulieu E.-E. Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyl-transferase 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    Le Bihan, S.4    Ning, Y.-M.5    Sanchez, E.R.6    Handschumacher, R.E.7    Baulieu, E.-E.8
  • 142
    • 0023711906 scopus 로고
    • Chemical cross-linking of heteromeric glucocorticoid receptors
    • Rexin M., Busch W., and Gehring U. Chemical cross-linking of heteromeric glucocorticoid receptors. Biochemistry 27 (1988) 5593-5601
    • (1988) Biochemistry , vol.27 , pp. 5593-5601
    • Rexin, M.1    Busch, W.2    Gehring, U.3
  • 143
    • 0024263207 scopus 로고
    • Tetrameric structure of the nonactivated glucocorticoid receptor in cell extracts and intact cells
    • Rexin M., Busch W., Segnitz B., and Gehring U. Tetrameric structure of the nonactivated glucocorticoid receptor in cell extracts and intact cells. FEBS Lett. 241 (1988) 234-238
    • (1988) FEBS Lett. , vol.241 , pp. 234-238
    • Rexin, M.1    Busch, W.2    Segnitz, B.3    Gehring, U.4
  • 144
    • 0026343608 scopus 로고
    • Protein components of the nonactivated glucocorticoid receptor
    • Rexin M., Busch W., and Gehring U. Protein components of the nonactivated glucocorticoid receptor. J. Biol. Chem. 266 (1991) 24601-24605
    • (1991) J. Biol. Chem. , vol.266 , pp. 24601-24605
    • Rexin, M.1    Busch, W.2    Gehring, U.3
  • 145
    • 0026667698 scopus 로고
    • Structure of the glucocorticoid receptor in intact cells in the absence of hormone
    • Rexin M., Busch W., Segnitz B., and Gehring U. Structure of the glucocorticoid receptor in intact cells in the absence of hormone. J. Biol. Chem. 267 (1992) 9619-9621
    • (1992) J. Biol. Chem. , vol.267 , pp. 9619-9621
    • Rexin, M.1    Busch, W.2    Segnitz, B.3    Gehring, U.4
  • 147
    • 0027418815 scopus 로고
    • Human P-glycoprotein transports cyclosporin A and FK506
    • Saeki T., Ueda K., Tanigawara Y., Hori R., and Komano T. Human P-glycoprotein transports cyclosporin A and FK506. J. Biol. Chem. 268 (1993) 6077-6080
    • (1993) J. Biol. Chem. , vol.268 , pp. 6077-6080
    • Saeki, T.1    Ueda, K.2    Tanigawara, Y.3    Hori, R.4    Komano, T.5
  • 148
    • 77956676382 scopus 로고
    • Hsp56: A novel heat shock protein associated with untransformed steroid receptor complexes
    • Sanchez E.R. Hsp56: A novel heat shock protein associated with untransformed steroid receptor complexes. J. Biol. Chem. 260 (1990) 12398-12401
    • (1990) J. Biol. Chem. , vol.260 , pp. 12398-12401
    • Sanchez, E.R.1
  • 149
    • 77956682226 scopus 로고
    • Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
    • Sanchez E.R., Toft D.O., Schlesinger M.J., and Pratt W.B. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem. 265 (1985) 20123-20130
    • (1985) J. Biol. Chem. , vol.265 , pp. 20123-20130
    • Sanchez, E.R.1    Toft, D.O.2    Schlesinger, M.J.3    Pratt, W.B.4
  • 150
    • 0025221344 scopus 로고
    • Hormone free glucocorticoid receptors overexpressed in Chinese hamster ovary cells are localized to the nucleus and are associated with both hsp70 and hsp90
    • Sanchez E.R., Hirst M., Scherrer L.C., Tang H.Y., Welsh M.J., Harmon J.M., Simons Jr. S.S., Ringold G.M., and Pratt W.B. Hormone free 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 (1990) 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 Jr., S.S.7    Ringold, G.M.8    Pratt, W.B.9
  • 151
    • 0025290187 scopus 로고
    • The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins
    • Sanchez E.R., Faber L.E., Henzel W.J., and Pratt W.B. The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins. Biochemistry 29 (1990) 5145-5152
    • (1990) Biochemistry , vol.29 , pp. 5145-5152
    • Sanchez, E.R.1    Faber, L.E.2    Henzel, W.J.3    Pratt, W.B.4
  • 152
    • 0028293935 scopus 로고
    • Potentiation of glucocorticoid receptor-mediated gene expression by heat and chemical shock
    • Sanchez E.R., Hu J.-L., Zhong S., Shen P., Greene M.J., and Housley P.R. Potentiation of glucocorticoid receptor-mediated gene expression by heat and chemical shock. Mol. Endocrinol. 8 (1994) 408-421
    • (1994) Mol. Endocrinol. , vol.8 , pp. 408-421
    • Sanchez, E.R.1    Hu, J.-L.2    Zhong, S.3    Shen, P.4    Greene, M.J.5    Housley, P.R.6
  • 153
    • 0026483950 scopus 로고
    • Energy-dependent conversion of transformed glucocorticoid receptors from soluble to particulate-bound form
    • Scherrer L.C., and Pratt W.B. Energy-dependent conversion of transformed glucocorticoid receptors from soluble to particulate-bound form. Biochemistry 31 (1992) 10879-10886
    • (1992) Biochemistry , vol.31 , pp. 10879-10886
    • Scherrer, L.C.1    Pratt, W.B.2
  • 154
    • 0025644194 scopus 로고
    • Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex
    • Scherrer L.C., Dalman F.C., Massa E., Meshinchi S., and Pratt W.B. Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex. J. Biol. Chem. 265 (1990) 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
  • 155
    • 0027256152 scopus 로고
    • Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat-shock protein hsp90
    • Scherrer L.C., Picard D., Massa E., Harmon J.M., Simons Jr. S.S., Yamamoto K.R., and Pratt W.B. Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat-shock protein hsp90. Biochemistry 32 (1993) 5381-5386
    • (1993) Biochemistry , vol.32 , pp. 5381-5386
    • Scherrer, L.C.1    Picard, D.2    Massa, E.3    Harmon, J.M.4    Simons Jr., S.S.5    Yamamoto, K.R.6    Pratt, W.B.7
  • 156
    • 0028825399 scopus 로고
    • Absence of the mdr1a P-glycoprotein in mice affects tissue distribution and pharmacokinetics of dexamethasone, digoxin, and cyclosporin A
    • Schinkel A.H., Wagenaar E., van Deemter L., Mol C.A.A.M., and Borst P. Absence of the mdr1a P-glycoprotein in mice affects tissue distribution and pharmacokinetics of dexamethasone, digoxin, and cyclosporin A. J. Clin. Invest. 96 (1995) 1698-1705
    • (1995) J. Clin. Invest. , vol.96 , pp. 1698-1705
    • Schinkel, A.H.1    Wagenaar, E.2    van Deemter, L.3    Mol, C.A.A.M.4    Borst, P.5
  • 157
    • 0029364576 scopus 로고
    • Protein folding. Prolyl isomerases join the fold
    • Schmid F.X. Protein folding. Prolyl isomerases join the fold. Curr. Biol. 5 (1995) 993-994
    • (1995) Curr. Biol. , vol.5 , pp. 993-994
    • Schmid, F.X.1
  • 158
    • 0027428602 scopus 로고
    • Cloning and expression of a mouse cDNA encoding p59, an immunophilin that associates with the glucocorticoid receptor
    • Schmitt J., Pohl J., and Stunnenberg H.G. Cloning and expression of a mouse cDNA encoding p59, an immunophilin that associates with the glucocorticoid receptor. Gene 132 (1993) 267-271
    • (1993) Gene , vol.132 , pp. 267-271
    • Schmitt, J.1    Pohl, J.2    Stunnenberg, H.G.3
  • 162
    • 0030113441 scopus 로고    scopus 로고
    • Transcriptional control: How nuclear receptors get turned on
    • Schwabe J.W.R. Transcriptional control: How nuclear receptors get turned on. Curr. Biol. 6 (1996) 372-374
    • (1996) Curr. Biol. , vol.6 , pp. 372-374
    • Schwabe, J.W.R.1
  • 163
    • 0025272959 scopus 로고
    • Mechanism of action of a steroidal antiglucocorticoid in lymphoid cells
    • Segnitz B., and Gehring U. Mechanism of action of a steroidal antiglucocorticoid in lymphoid cells. J. Biol. Chem. 265 (1990) 2789-2796
    • (1990) J. Biol. Chem. , vol.265 , pp. 2789-2796
    • Segnitz, B.1    Gehring, U.2
  • 164
    • 0028911171 scopus 로고
    • Subunit structure of the nonactivated human estrogen receptor
    • Segnitz B., and Gehring U. Subunit structure of the nonactivated human estrogen receptor. Proc. Natl. Acad. Sci. USA 92 (1995) 2179-2183
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2179-2183
    • Segnitz, B.1    Gehring, U.2
  • 165
    • 0030810984 scopus 로고    scopus 로고
    • The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin
    • Segnitz B., and Gehring U. The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin. J. Biol. Chem. 272 (1997) 18694-18701
    • (1997) J. Biol. Chem. , vol.272 , pp. 18694-18701
    • Segnitz, B.1    Gehring, U.2
  • 166
    • 0019725640 scopus 로고
    • Chromatographic studies on interconversions of "non-activated" and "activated" forms of glucocorticoid-receptor complexes from rat heart cytosol
    • Seleznev Y.M., Shnyra A.A., Volkova N.G., Smirnov V.N., Djozdjevic-Markovic R., Lan N., and Baxter J.D. Chromatographic studies on interconversions of "non-activated" and "activated" forms of glucocorticoid-receptor complexes from rat heart cytosol. J. Steroid Biochem. 15 (1981) 55-61
    • (1981) J. Steroid Biochem. , vol.15 , pp. 55-61
    • Seleznev, Y.M.1    Shnyra, A.A.2    Volkova, N.G.3    Smirnov, V.N.4    Djozdjevic-Markovic, R.5    Lan, N.6    Baxter, J.D.7
  • 167
    • 0029008487 scopus 로고
    • Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases
    • Sepp-Lorenzino L., Ma Z., Lebwohl D.E., Vinitzky A., and Rosen N. Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases. J. Biol. Chem. 270 (1995) 16580-16587
    • (1995) J. Biol. Chem. , vol.270 , pp. 16580-16587
    • Sepp-Lorenzino, L.1    Ma, Z.2    Lebwohl, D.E.3    Vinitzky, A.4    Rosen, N.5
  • 168
    • 0021288961 scopus 로고
    • Structure of mammalian steroid receptors: Evolving concepts and methodological developments
    • Sherman M.R., and Stevens J. Structure of mammalian steroid receptors: Evolving concepts and methodological developments. Annu. Rev. Physiol. 46 (1984) 83-105
    • (1984) Annu. Rev. Physiol. , vol.46 , pp. 83-105
    • Sherman, M.R.1    Stevens, J.2
  • 169
    • 0028713459 scopus 로고
    • Function/activity of specific amino acids in glucocorticoid receptors
    • Litwack G. (Ed), Academic Press, San Diego
    • Simons Jr. S.S. Function/activity of specific amino acids in glucocorticoid receptors. In: Litwack G. (Ed). Vitamins and Hormones 49 (1994), Academic Press, San Diego 49-130
    • (1994) Vitamins and Hormones , vol.49 , pp. 49-130
    • Simons Jr., S.S.1
  • 170
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and disactivation loop model for steroid receptor complexes
    • Smith D.F. Dynamics of heat shock protein 90-progesterone receptor binding and disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7 (1993) 1418-1429
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 171
    • 12044259947 scopus 로고
    • Steroid receptors and their associated proteins
    • Smith D.F., and Toft D.O. Steroid receptors and their associated proteins. Mol. Endocrinol. 7 (1993) 4-11
    • (1993) Mol. Endocrinol. , vol.7 , pp. 4-11
    • Smith, D.F.1    Toft, D.O.2
  • 172
    • 0025640051 scopus 로고
    • Reconstitution of progesterone receptor with heat shock proteins
    • Smith D.F., Schowalter D.B., Kost S.L., and Toft D.O. Reconstitution of progesterone receptor with heat shock proteins. Mol. Endocrinol. 4 (1990) 1704-1711
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1704-1711
    • Smith, D.F.1    Schowalter, D.B.2    Kost, S.L.3    Toft, D.O.4
  • 173
    • 0025233648 scopus 로고
    • Purification of unactivated progesterone receptor and identification of novel receptor-associating proteins
    • Smith D.F., Faber L.E., and Toft D.O. Purification of unactivated progesterone receptor and identification of novel receptor-associating proteins. J. Biol. Chem. 265 (1990) 3996-4003
    • (1990) J. Biol. Chem. , vol.265 , pp. 3996-4003
    • Smith, D.F.1    Faber, L.E.2    Toft, D.O.3
  • 174
    • 0026543821 scopus 로고
    • Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events
    • Smith D.F., Stensgard B.A., Welch W.J., and Toft D.O. Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events. J. Biol. Chem. 267 (1992) 1350-1356
    • (1992) J. Biol. Chem. , vol.267 , pp. 1350-1356
    • Smith, D.F.1    Stensgard, B.A.2    Welch, W.J.3    Toft, D.O.4
  • 176
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith D.F., Whitesell L., Nair S.C., Chen S., Prapapanich V., and Rimerman R.A. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol. 15 (1995) 6804-6812
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6804-6812
    • Smith, D.F.1    Whitesell, L.2    Nair, S.C.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.A.6
  • 177
    • 0027403603 scopus 로고
    • Reconstitution of ligand-mediated glucocorticoid receptor activity by trans-acting functional domains
    • Spanjaard R.A., and 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
  • 179
    • 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., Hutchison K.A., Krishna P., and Pratt W.B. Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90. Biochemistry 35 (1996) 554-561
    • (1996) Biochemistry , vol.35 , pp. 554-561
    • Stancato, L.F.1    Hutchison, K.A.2    Krishna, P.3    Pratt, W.B.4
  • 180
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., and Pavletich N.P. Crystal structure of an hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent. Cell 89 (1997) 239-250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 181
    • 0027239861 scopus 로고
    • Mutational analysis of hsp90 binding to the progesterone receptor
    • Sullivan W.P., and Toft D.O. Mutational analysis of hsp90 binding to the progesterone receptor. J. Biol. Chem. 268 (1993) 20373-20379
    • (1993) J. Biol. Chem. , vol.268 , pp. 20373-20379
    • Sullivan, W.P.1    Toft, D.O.2
  • 182
    • 0026095725 scopus 로고
    • Hormone-dependent transcriptional regulation and cellular transformation by Fos-steroid receptor fusion proteins
    • Superti-Furga G., Bergers G., Picard D., and Busslinger M. Hormone-dependent transcriptional regulation and cellular transformation by Fos-steroid receptor fusion proteins. Proc. Natl. Acad. Sci. USA 88 (1991) 5114-5118
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5114-5118
    • Superti-Furga, G.1    Bergers, G.2    Picard, D.3    Busslinger, M.4
  • 183
    • 0021956164 scopus 로고
    • Isolation of dissimilar components of the 8.5S non-activated uterine progestin receptor
    • Tai P.-K.K., and Faber L.E. Isolation of dissimilar components of the 8.5S non-activated uterine progestin receptor. Can. J. Biochem. Cell. Biol. 63 (1985) 41-49
    • (1985) Can. J. Biochem. Cell. Biol. , vol.63 , pp. 41-49
    • Tai, P.-K.K.1    Faber, L.E.2
  • 184
    • 0022918191 scopus 로고
    • A 59-kilodalton protein associated with progestin, estrogen, androgen and glucocorticoid receptors
    • Tai P.-K.K., Maeda Y., Nakao K., Wakim N.G., Duhring J.L., and Faber L.E. A 59-kilodalton protein associated with progestin, estrogen, androgen and glucocorticoid receptors. Biochemistry 25 (1986) 5269-5275
    • (1986) Biochemistry , vol.25 , pp. 5269-5275
    • Tai, P.-K.K.1    Maeda, Y.2    Nakao, K.3    Wakim, N.G.4    Duhring, J.L.5    Faber, L.E.6
  • 185
    • 0026710278 scopus 로고
    • Association of a 59 kilodalton immunophilin with the glucocorticoid receptor complex
    • Tai P.-K.K., Albers M.W., Chang H., Faber L.E., and Schreiber S.L. Association of a 59 kilodalton immunophilin with the glucocorticoid receptor complex. Science 256 (1992) 1315-1318
    • (1992) Science , vol.256 , pp. 1315-1318
    • Tai, P.-K.K.1    Albers, M.W.2    Chang, H.3    Faber, L.E.4    Schreiber, S.L.5
  • 186
    • 0028037857 scopus 로고
    • Potentiation of progesterone receptor-mediated transcription by the immunosuppressant FK506
    • Tai P.-K.K., Albers M.W., McDonnell D.P., Chang H., Schreiber S.L., and Faber L.E. Potentiation of progesterone receptor-mediated transcription by the immunosuppressant FK506. Biochemistry 33 (1994) 10666-10671
    • (1994) Biochemistry , vol.33 , pp. 10666-10671
    • Tai, P.-K.K.1    Albers, M.W.2    McDonnell, D.P.3    Chang, H.4    Schreiber, S.L.5    Faber, L.E.6
  • 187
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai M.-J., and O'Malley B.W. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63 (1994) 451-486
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-486
    • Tsai, M.-J.1    O'Malley, B.W.2
  • 188
    • 0023940887 scopus 로고
    • Inhibition of transforming activity of tyrosine kinase oncogens by herbimycin A
    • Uehara Y., Murakami Y., Mizuno S., and Kawai S. Inhibition of transforming activity of tyrosine kinase oncogens by herbimycin A. Virology 164 (1988) 294-298
    • (1988) Virology , vol.164 , pp. 294-298
    • Uehara, Y.1    Murakami, Y.2    Mizuno, S.3    Kawai, S.4
  • 189
    • 0026591729 scopus 로고
    • Antiandrogens and the mutated androgen receptor of LNCaP cells: Differential effects on binding affinity, heat-shock protein interaction, and transcription activation
    • Veldscholte J., Berrevoets C.A., Brinkmann A.O., Grootegoed J.A., and Mulder E. Antiandrogens and the mutated androgen receptor of LNCaP cells: Differential effects on binding affinity, heat-shock protein interaction, and transcription activation. Biochemistry 31 (1992) 2393-2399
    • (1992) Biochemistry , vol.31 , pp. 2393-2399
    • Veldscholte, J.1    Berrevoets, C.A.2    Brinkmann, A.O.3    Grootegoed, J.A.4    Mulder, E.5
  • 191
    • 0029855010 scopus 로고    scopus 로고
    • Steroid hormone receptors and their regulation by phosphorylation
    • Weigel N.L. Steroid hormone receptors and their regulation by phosphorylation. Biochem. J. 319 (1996) 657-667
    • (1996) Biochem. J. , vol.319 , pp. 657-667
    • Weigel, N.L.1
  • 192
    • 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., and 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
  • 193
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L., Mimnaugh E.G., DeCosta B., Myers C.E., and Neckers L.M. Inhibition of heat shock protein hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 91 (1994) 8324-8328
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    DeCosta, B.3    Myers, C.E.4    Neckers, L.M.5
  • 195
    • 0029829893 scopus 로고    scopus 로고
    • Modular structure of glucocorticoid receptor domains is not equivalent to functional independence
    • Xu M., Chakraborti P.K., Garabedian M.J., Yamamoto K.R., and Simons Jr. S.S. Modular structure of glucocorticoid receptor domains is not equivalent to functional independence. J. Biol. Chem. 271 (1996) 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 Jr., S.S.5
  • 196
    • 0030046766 scopus 로고    scopus 로고
    • Assessment of glucocorticoid receptor-heat shock protein 90 interactions in vivo during nucleocytoplasmic trafficking
    • Yang J., and 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
  • 197


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.