메뉴 건너뛰기




Volumn 47, Issue 39, 2008, Pages 10471-10480

Control of glucocorticoid and progesterone receptor subcellular localization by the ligand-binding domain is mediated by distinct interactions with tetratricopeptide repeat proteins

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; CELLS; CHLORINE COMPOUNDS; ERROR ANALYSIS; FLOW INTERACTIONS; IMAGE SEGMENTATION; LIGANDS; PHOTORESISTS; PROTEINS; TESTING;

EID: 52949129878     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8011862     Document Type: Article
Times cited : (63)

References (49)
  • 2
    • 0034129679 scopus 로고    scopus 로고
    • Steroid hormone receptors: An update
    • Beato, M., and Klug, J. (2000) Steroid hormone receptors: An update. Hum. Reprod. Update 6 (3), 225-236.
    • (2000) Hum. Reprod. Update , vol.6 , Issue.3 , pp. 225-236
    • Beato, M.1    Klug, J.2
  • 3
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt, W. B., and Toft, D. O. (1997) Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 18 (3), 306-360.
    • (1997) Endocr. Rev , vol.18 , Issue.3 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 4
    • 2442537231 scopus 로고    scopus 로고
    • Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
    • Pratt, W. B., Galigniana, M. D., Harrell, J. M., and DeFranco, D. B. (2004) Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement. Cell. Signalling 16 (8), 857-872.
    • (2004) Cell. Signalling , vol.16 , Issue.8 , pp. 857-872
    • Pratt, W.B.1    Galigniana, M.D.2    Harrell, J.M.3    DeFranco, D.B.4
  • 5
    • 3543037605 scopus 로고    scopus 로고
    • Tetratricopeptide repeat cochaperones in steroid receptor complexes
    • Smith, D. F. (2004) Tetratricopeptide repeat cochaperones in steroid receptor complexes. Cell Stress Chaperones 9 (2), 109-121.
    • (2004) Cell Stress Chaperones , vol.9 , Issue.2 , pp. 109-121
    • Smith, D.F.1
  • 6
    • 0025922586 scopus 로고
    • The TPR snap helix: A novel protein repeat motif from mitosis to transcription
    • Goebl, M., and Yanagida, M. (1991) The TPR snap helix: A novel protein repeat motif from mitosis to transcription. Trends Biochem. Sci. 16 (5), 173-177.
    • (1991) Trends Biochem. Sci , vol.16 , Issue.5 , pp. 173-177
    • Goebl, M.1    Yanagida, M.2
  • 7
    • 0027962531 scopus 로고
    • The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain
    • Radanyi, C., Chambraud, B., and Baulieu, E. E. (1994) The ability of the immunophilin FKBP59-HBI to interact with the 90-kDa heat shock protein is encoded by its tetratricopeptide repeat domain. Proc. Natl. Acad. Sci. U.S.A. 91, 11197-11201.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 11197-11201
    • Radanyi, C.1    Chambraud, B.2    Baulieu, E.E.3
  • 8
    • 0033575232 scopus 로고    scopus 로고
    • Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90
    • Russell, L. C., Whitt, S. R., Chen, M. S., and Chinkers, M. (1999) Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90. J. Biol. Chem. 274, 20060-20063.
    • (1999) J. Biol. Chem , vol.274 , pp. 20060-20063
    • Russell, L.C.1    Whitt, S.R.2    Chen, M.S.3    Chinkers, M.4
  • 9
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufier, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hard, F. U., and Moarefi, I. (2000) Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufier, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hard, F.U.7    Moarefi, I.8
  • 10
    • 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., Le, B. S., Ning, Y. M., Sanchez, E. R., Handschumacher, R. E., and Baulieu, E. E. (1995) 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. U.S.A. 92, 4977-4981.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 4977-4981
    • Renoir, J.M.1    Mercier-Bodard, C.2    Hoffmann, K.3    Le, B.S.4    Ning, Y.M.5    Sanchez, E.R.6    Handschumacher, R.E.7    Baulieu, E.E.8
  • 11
    • 0033613950 scopus 로고    scopus 로고
    • The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90
    • Carrello, A., Ingley, E., Minchin, R. F., Tsai, S., and Ratajczak, T. (1999) The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90. J. Biol. Chem. 274, 2682-2689.
    • (1999) J. Biol. Chem , vol.274 , pp. 2682-2689
    • Carrello, A.1    Ingley, E.2    Minchin, R.F.3    Tsai, S.4    Ratajczak, T.5
  • 12
    • 0033601331 scopus 로고    scopus 로고
    • Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein
    • Silverstein, A. M., Galigniana, M. D., Kanelakis, K. C., Radanyi, C., Renoir, J. M., and Pratt, W. B. (1999) Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein. J. Biol. Chem. 274, 36980-36986.
    • (1999) J. Biol. Chem , vol.274 , pp. 36980-36986
    • Silverstein, A.M.1    Galigniana, M.D.2    Kanelakis, K.C.3    Radanyi, C.4    Renoir, J.M.5    Pratt, W.B.6
  • 13
    • 0013801117 scopus 로고
    • Stereospecific binding of estrogens in the rat uterus
    • Noteboom, W. D., and Gorski, J. (1965) Stereospecific binding of estrogens in the rat uterus. Arch. Biochem. Biophys. 111, 559-568.
    • (1965) Arch. Biochem. Biophys , vol.111 , pp. 559-568
    • Noteboom, W.D.1    Gorski, J.2
  • 16
    • 0021878338 scopus 로고
    • Immunocytochemical study of mammalian progesterone receptor using monoclonal antibodies
    • Perrot-Applanat, M., Logeat, F., Groyer-Picard, M. T., and Milgrom, E. (1985) Immunocytochemical study of mammalian progesterone receptor using monoclonal antibodies. Endocrinology 116, 1473-1484.
    • (1985) Endocrinology , vol.116 , pp. 1473-1484
    • Perrot-Applanat, M.1    Logeat, F.2    Groyer-Picard, M.T.3    Milgrom, E.4
  • 17
    • 0023146969 scopus 로고
    • Intracellular localization of the glucocorticoid receptor: Evidence for cytoplasmic and nuclear localization
    • Wikstrom, A. C., Bakke, O., Okret, S., Bronnegard, M., and Gustafsson, J. A. (1987) Intracellular localization of the glucocorticoid receptor: Evidence for cytoplasmic and nuclear localization. Endocrinology 120, 1232-1242.
    • (1987) Endocrinology , vol.120 , pp. 1232-1242
    • Wikstrom, A.C.1    Bakke, O.2    Okret, S.3    Bronnegard, M.4    Gustafsson, J.A.5
  • 18
    • 0025037680 scopus 로고
    • Immunohistochemical localization of renal mineralocorticoid receptor by using an anti-idiotypic antibody that is an internal image of aldosterone
    • Lombes, M., Farman, N., Oblin, M. E., Baulieu, E. E., Bonvalet, J. P., Erlanger, B. F., and Gasc, J. M. (1990) Immunohistochemical localization of renal mineralocorticoid receptor by using an anti-idiotypic antibody that is an internal image of aldosterone. Proc. Natl. Acad. Sci. U.S.A. 87, 1086-1088.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 1086-1088
    • Lombes, M.1    Farman, N.2    Oblin, M.E.3    Baulieu, E.E.4    Bonvalet, J.P.5    Erlanger, B.F.6    Gasc, J.M.7
  • 19
    • 0030948745 scopus 로고    scopus 로고
    • Trafficking of the androgen receptor in living cells with fused green fluorescent protein-androgen receptor
    • Georget, V., Lobaccaro, J. M., Terouanne, B., Mangeat, P., Nicolas, J. C., and Sultan, C. (1997) Trafficking of the androgen receptor in living cells with fused green fluorescent protein-androgen receptor. Mol. Cell. Endocrinol. 129, 17-26.
    • (1997) Mol. Cell. Endocrinol , vol.129 , pp. 17-26
    • Georget, V.1    Lobaccaro, J.M.2    Terouanne, B.3    Mangeat, P.4    Nicolas, J.C.5    Sultan, C.6
  • 20
    • 0032539721 scopus 로고    scopus 로고
    • Subcellular localization of mineralocorticoid receptors in living cells: Effects of receptor agonists and antagonists
    • Fejes-Toth, G., Pearce, D., and Naray-Fejes-Toth, A. (1998) Subcellular localization of mineralocorticoid receptors in living cells: Effects of receptor agonists and antagonists. Proc. Natl. Acad. Sci. U.S.A. 95, 2973-2978.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 2973-2978
    • Fejes-Toth, G.1    Pearce, D.2    Naray-Fejes-Toth, A.3
  • 21
    • 0025382801 scopus 로고
    • Signal transduction by steroid hormones: Nuclear localization is differentially regulated in estrogen and glucocorticoid receptors
    • Picard, D., Kumar, V., Chambon, P., and Yamamoto, K. R. (1990) Signal transduction by steroid hormones: Nuclear localization is differentially regulated in estrogen and glucocorticoid receptors. Cell Regul. 1, 291-299.
    • (1990) Cell Regul , vol.1 , pp. 291-299
    • Picard, D.1    Kumar, V.2    Chambon, P.3    Yamamoto, K.R.4
  • 22
    • 0035136885 scopus 로고    scopus 로고
    • Separable features of the ligand-binding domain determine the differential subcellular localization and ligand-binding specificity of glucocorticoid receptor and progesterone receptor
    • Wan, Y., Coxe, K. K., Thackray, V. G., Housley, P. R., and Nordeen, S. K. (2001) Separable features of the ligand-binding domain determine the differential subcellular localization and ligand-binding specificity of glucocorticoid receptor and progesterone receptor. Mol. Endocrinol. 15, 17-31.
    • (2001) Mol. Endocrinol , vol.15 , pp. 17-31
    • Wan, Y.1    Coxe, K.K.2    Thackray, V.G.3    Housley, P.R.4    Nordeen, S.K.5
  • 23
    • 0023441954 scopus 로고
    • Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor
    • Picard, D., and Yamamoto, K. R. (1987) Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J. 6, 3333-3340.
    • (1987) EMBO J , vol.6 , pp. 3333-3340
    • Picard, D.1    Yamamoto, K.R.2
  • 24
    • 0024372113 scopus 로고
    • Mechanisms of nuclear localization of the progesterone receptor: Evidence for interaction between monomers
    • Guiochon-Mantel, A., Loosfelt, H., Lescop, P., Sar, S., Atger, M., Perrot-Applanat, M., and Milgrom, E. (1989) Mechanisms of nuclear localization of the progesterone receptor: Evidence for interaction between monomers. Cell 57, 1147-1154.
    • (1989) Cell , vol.57 , pp. 1147-1154
    • Guiochon-Mantel, A.1    Loosfelt, H.2    Lescop, P.3    Sar, S.4    Atger, M.5    Perrot-Applanat, M.6    Milgrom, E.7
  • 25
    • 0026713869 scopus 로고
    • Cooperation of proto-signals for nuclear accumulation of estrogen and progesterone receptors
    • Ylikomi, T., Bocquel, M. T., Berry, M., Gronemeyer, H., and Chambon, P. (1992) Cooperation of proto-signals for nuclear accumulation of estrogen and progesterone receptors. EMBO J. 11, 3681-3694.
    • (1992) EMBO J , vol.11 , pp. 3681-3694
    • Ylikomi, T.1    Bocquel, M.T.2    Berry, M.3    Gronemeyer, H.4    Chambon, P.5
  • 27
    • 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 90
    • Scherrer, L. C., Picard, D., Massa, E., Harmon, J. M., Simons, S. S. J., Yamamoto, K. R., and Pratt, W. B. (1993) 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 90. Biochemistry 32, 5381-5386.
    • (1993) Biochemistry , vol.32 , pp. 5381-5386
    • Scherrer, L.C.1    Picard, D.2    Massa, E.3    Harmon, J.M.4    Simons, S.S.J.5    Yamamoto, K.R.6    Pratt, W.B.7
  • 28
    • 0028596331 scopus 로고
    • The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptor
    • Czar, M. J., Owens-Grillo, J. K., Yem, A. W., Leach, K. L., Deibel, M. R., Jr., Welsh, M. J., and Pratt, W. B. (1994) The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptor. Mol. Endocrinol. 8, 1731-1741.
    • (1994) Mol. Endocrinol , vol.8 , pp. 1731-1741
    • Czar, M.J.1    Owens-Grillo, J.K.2    Yem, A.W.3    Leach, K.L.4    Deibel Jr., M.R.5    Welsh, M.J.6    Pratt, W.B.7
  • 29
    • 0035805599 scopus 로고    scopus 로고
    • Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus
    • Galigniana, M. D., Radanyi, C., Renoir, J. M., Housley, P. R., and Pratt, W. B. (2001) Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus. J. Biol. Chem. 276, 14884-14889.
    • (2001) J. Biol. Chem , vol.276 , pp. 14884-14889
    • Galigniana, M.D.1    Radanyi, C.2    Renoir, J.M.3    Housley, P.R.4    Pratt, W.B.5
  • 30
    • 0037085381 scopus 로고    scopus 로고
    • A new first step in activation of steroid receptors: Hormone-induced switching of FKBP51 and FKBP52 immunophilins
    • Davies, T. H., Ning, Y. M., and Sanchez, E. R. (2002) A new first step in activation of steroid receptors: Hormone-induced switching of FKBP51 and FKBP52 immunophilins. J. Biol. Chem. 277, 4597-4600.
    • (2002) J. Biol. Chem , vol.277 , pp. 4597-4600
    • Davies, T.H.1    Ning, Y.M.2    Sanchez, E.R.3
  • 31
    • 14244262261 scopus 로고    scopus 로고
    • FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells
    • Wochnik, G. M., Ruegg, J., Abel, G. A., Schmidt, U., Holsboer, F., and Rein, T. (2005) FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells. J. Biol. Chem. 280, 4609-4616.
    • (2005) J. Biol. Chem , vol.280 , pp. 4609-4616
    • Wochnik, G.M.1    Ruegg, J.2    Abel, G.A.3    Schmidt, U.4    Holsboer, F.5    Rein, T.6
  • 32
    • 13544267438 scopus 로고    scopus 로고
    • Differential Control of Glucocorticoid Receptor Hormone-Binding Function by Tetratricopeptide Repeat (TPR) Proteins and the Immunosuppressive Ligand FK506
    • Davies, T. H., Ning, Y. M., and Sanchez, E. R. (2005) Differential Control of Glucocorticoid Receptor Hormone-Binding Function by Tetratricopeptide Repeat (TPR) Proteins and the Immunosuppressive Ligand FK506. Biochemistry 44, 2030-2038.
    • (2005) Biochemistry , vol.44 , pp. 2030-2038
    • Davies, T.H.1    Ning, Y.M.2    Sanchez, E.R.3
  • 33
    • 0025221344 scopus 로고
    • Hormone-free mouse glucocorticoid receptors overexpressed in Chinese hamster ovary cells are localized to the nucleus and are associated with both hsp70 and hsp90
    • Sanchez, E. R., Hirst, M., Scherrer, L. C., Tang, H. Y., Welsh, M. J., Harmon, J. M., Simons, S. S. J., Ringold, G. M., and Pratt, W. B. (1990) Hormone-free mouse glucocorticoid receptors overexpressed in Chinese hamster ovary cells are localized to the nucleus and are associated with both hsp70 and hsp90. J. Biol. Chem. 265, 20123-20130.
    • (1990) J. Biol. Chem , vol.265 , pp. 20123-20130
    • Sanchez, E.R.1    Hirst, M.2    Scherrer, L.C.3    Tang, H.Y.4    Welsh, M.J.5    Harmon, J.M.6    Simons, S.S.J.7    Ringold, G.M.8    Pratt, W.B.9
  • 34
    • 0026787403 scopus 로고
    • Tissue distribution and cellular localization of hsp56, an FK506-binding protein. Characterization using a highly specific polyclonal antibody
    • Ruff, V. A., Yem, A. W., Munns, P. L., Adams, L. D., Reardon, I. M., Deibel, M. R., Jr., and Leach, K. L. (1992) Tissue distribution and cellular localization of hsp56, an FK506-binding protein. Characterization using a highly specific polyclonal antibody. J. Biol. Chem. 267, 21285-21288.
    • (1992) J. Biol. Chem , vol.267 , pp. 21285-21288
    • Ruff, V.A.1    Yem, A.W.2    Munns, P.L.3    Adams, L.D.4    Reardon, I.M.5    Deibel Jr., M.R.6    Leach, K.L.7
  • 35
    • 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. (1995) 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, 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
  • 36
    • 0032941272 scopus 로고    scopus 로고
    • Differential localization and activity of the A- and B-forms of the human progesterone receptor using green fluorescent protein chimeras
    • Lim, C. S., Baumann, C. T., Htun, H., Xian, W., Irie, M., Smith, C. L., and Hager, G. L. (1999) Differential localization and activity of the A- and B-forms of the human progesterone receptor using green fluorescent protein chimeras. Mol. Endocrinol. 13, 366-375.
    • (1999) Mol. Endocrinol , vol.13 , pp. 366-375
    • Lim, C.S.1    Baumann, C.T.2    Htun, H.3    Xian, W.4    Irie, M.5    Smith, C.L.6    Hager, G.L.7
  • 37
    • 0022549929 scopus 로고
    • Ultrastructural localization of the progesterone receptor by an immunogold method: Effect of hormone administration
    • Perrot-Applanat, M., Groyer-Picard, M. T., Logeat, F., and Milgrom, E. (1986) Ultrastructural localization of the progesterone receptor by an immunogold method: Effect of hormone administration. J. Cell Biol. 102, 1191-1199.
    • (1986) J. Cell Biol , vol.102 , pp. 1191-1199
    • Perrot-Applanat, M.1    Groyer-Picard, M.T.2    Logeat, F.3    Milgrom, E.4
  • 40
    • 0037137181 scopus 로고    scopus 로고
    • Binding of hsp90-associated immunophilins to cytoplasmic dynein: Direct binding and in vivo evidence that the peptidylprolyl isomerase domain is a dynein interaction domain
    • Galigniana, M. D., Harrell, J. M., Murphy, P. J., Chinkers, M., Radanyi, C., Renoir, J. M., Zhang, M., and Pratt, W. B. (2002) Binding of hsp90-associated immunophilins to cytoplasmic dynein: Direct binding and in vivo evidence that the peptidylprolyl isomerase domain is a dynein interaction domain. Biochemistry 41, 13602-13610.
    • (2002) Biochemistry , vol.41 , pp. 13602-13610
    • Galigniana, M.D.1    Harrell, J.M.2    Murphy, P.J.3    Chinkers, M.4    Radanyi, C.5    Renoir, J.M.6    Zhang, M.7    Pratt, W.B.8
  • 41
    • 2342666137 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatase 5 (PP5) participates in the regulation of glucocorticoid receptor nucleocytoplasmic shuttling
    • Dean, D. A., Urban, G., Aragon, I. V., Swingle, M., Miller, B., Rusconi, S., Bueno, M., Dean, N. M., and Honkanen, R. E. (2001) Serine/threonine protein phosphatase 5 (PP5) participates in the regulation of glucocorticoid receptor nucleocytoplasmic shuttling. BMC Cell Biol. 2, 6.
    • (2001) BMC Cell Biol , vol.2 , pp. 6
    • Dean, D.A.1    Urban, G.2    Aragon, I.V.3    Swingle, M.4    Miller, B.5    Rusconi, S.6    Bueno, M.7    Dean, N.M.8    Honkanen, R.E.9
  • 42
    • 0033018628 scopus 로고    scopus 로고
    • Glucocorticoid resistance in the squirrel monkey is associated with overexpression of the immunophilin FKBP51
    • Reynolds, P. D., Ruan, Y., Smith, D. F., and Scammell, J. G. (1999) Glucocorticoid resistance in the squirrel monkey is associated with overexpression of the immunophilin FKBP51. J. Clin. Endocrinol. Metab. 84, 663-669.
    • (1999) J. Clin. Endocrinol. Metab , vol.84 , pp. 663-669
    • Reynolds, P.D.1    Ruan, Y.2    Smith, D.F.3    Scammell, J.G.4
  • 43
    • 0033712280 scopus 로고    scopus 로고
    • Squirrel monkey immunophilin FKBP51 is a potent inhibitor of glucocorticoid receptor binding
    • Denny, W. B., Valentine, D. L., Reynolds, P. D., Smith, D. F., and Scammell, J. G. (2000) Squirrel monkey immunophilin FKBP51 is a potent inhibitor of glucocorticoid receptor binding. Endocrinology 141, 4107-4113.
    • (2000) Endocrinology , vol.141 , pp. 4107-4113
    • Denny, W.B.1    Valentine, D.L.2    Reynolds, P.D.3    Smith, D.F.4    Scammell, J.G.5
  • 45
    • 0034622974 scopus 로고    scopus 로고
    • Subgroup of reproductive functions of progesterone mediated by progesterone receptor-B isoform
    • Mulac-Jericevic, B., Mullinax, R. A., DeMayo, F. J., Lydon, J. P., and Conneely, O. M. (2000) Subgroup of reproductive functions of progesterone mediated by progesterone receptor-B isoform. Science 289, 1751-1754.
    • (2000) Science , vol.289 , pp. 1751-1754
    • Mulac-Jericevic, B.1    Mullinax, R.A.2    DeMayo, F.J.3    Lydon, J.P.4    Conneely, O.M.5
  • 46
    • 0042693019 scopus 로고    scopus 로고
    • Defective mammary gland morphogenesis in mice lacking the progesterone receptor B isoform
    • Mulac-Jericevic, B., Lydon, J. P., DeMayo, F. J., and Conneely, O. M. (2003) Defective mammary gland morphogenesis in mice lacking the progesterone receptor B isoform. Proc. Natl. Acad. Sci. U.S.A. 100, 9744-9749.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 9744-9749
    • Mulac-Jericevic, B.1    Lydon, J.P.2    DeMayo, F.J.3    Conneely, O.M.4
  • 47
    • 0025092188 scopus 로고
    • High level expression of wild-type and variant mouse glucocorticoid receptors in chinese hamster ovary cells
    • Hirst, M. A., Northrop, J. P., Danielsen, M., and Ringold, G. M. (1990) High level expression of wild-type and variant mouse glucocorticoid receptors in chinese hamster ovary cells. Mol. Endocrinol. 4, 162-170.
    • (1990) Mol. Endocrinol , vol.4 , pp. 162-170
    • Hirst, M.A.1    Northrop, J.P.2    Danielsen, M.3    Ringold, G.M.4
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 34447525646 scopus 로고    scopus 로고
    • Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia mutated (ATM)-mediated cell cycle arrest
    • Yong, W., Bao, S., Chen, H., Li, D., Sanchez, E. R., and Shou, W. (2007) Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia mutated (ATM)-mediated cell cycle arrest. J. Biol. Chem. 282, 14690-14694.
    • (2007) J. Biol. Chem , vol.282 , pp. 14690-14694
    • Yong, W.1    Bao, S.2    Chen, H.3    Li, D.4    Sanchez, E.R.5    Shou, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.