메뉴 건너뛰기




Volumn 46, Issue 5, 2007, Pages 1389-1397

Evidence for NL1-independent nuclear translocation of the mineralocorticoid receptor

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BIOLOGICAL ORGANS; CELLS; CHEMICAL BONDS; DISSOCIATION; HORMONES; PROTEINS;

EID: 33846781599     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0621819     Document Type: Article
Times cited : (38)

References (53)
  • 1
    • 4143131953 scopus 로고    scopus 로고
    • Activation of the ligand-mineralocorticoid receptor functional unit by ancient, classical, and novel ligands. Structure-activity relationship
    • Galigniana, M. D., and Piwien Pilipuk, G. (2004) Activation of the ligand-mineralocorticoid receptor functional unit by ancient, classical, and novel ligands. Structure-activity relationship, Vitam. Horm. 69, 31-68.
    • (2004) Vitam. Horm , vol.69 , pp. 31-68
    • Galigniana, M.D.1    Piwien Pilipuk, G.2
  • 2
    • 22544466731 scopus 로고    scopus 로고
    • The new biology of aldosterone
    • Connell, J. M., and Davies, E. (2005) The new biology of aldosterone, J. Endocrinol. 186, 1-20.
    • (2005) J. Endocrinol , vol.186 , pp. 1-20
    • Connell, J.M.1    Davies, E.2
  • 3
    • 24344433108 scopus 로고    scopus 로고
    • The mineralocorticoid receptor: A journey exploring its diversity and specificity of action
    • Pascual-Le Tallec, L., and Lombes, M. (2005) The mineralocorticoid receptor: A journey exploring its diversity and specificity of action, Mol. Endocrinol. 19, 2211-2221.
    • (2005) Mol. Endocrinol , vol.19 , pp. 2211-2221
    • Pascual-Le Tallec, L.1    Lombes, M.2
  • 4
    • 0027982025 scopus 로고
    • Differential intracellular localization of human mineralocorticosteroid receptor on binding of agonists and antagonists
    • Lombes, M., Binart, N., Delahaye, F., Baulieu, E. E., and Rafestin-Oblin, M. E. (1994) Differential intracellular localization of human mineralocorticosteroid receptor on binding of agonists and antagonists, Biochem. J. 302 (Part 1), 191-197.
    • (1994) Biochem. J , vol.302 , Issue.PART 1 , pp. 191-197
    • Lombes, M.1    Binart, N.2    Delahaye, F.3    Baulieu, E.E.4    Rafestin-Oblin, M.E.5
  • 5
    • 0027420803 scopus 로고
    • Demonstration of nuclear translocation of the mineralocorticoid receptor (MR) using an anti-MR antibody and confocal laser scanning microscopy
    • Robertson, N. M., Schulman, G., Karnik, S., Alnemri, E., and Litwack, G. (1993) Demonstration of nuclear translocation of the mineralocorticoid receptor (MR) using an anti-MR antibody and confocal laser scanning microscopy, Mol. Endocrinol. 7, 1226-1239.
    • (1993) Mol. Endocrinol , vol.7 , pp. 1226-1239
    • Robertson, N.M.1    Schulman, G.2    Karnik, S.3    Alnemri, E.4    Litwack, G.5
  • 6
    • 0031721793 scopus 로고    scopus 로고
    • Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor
    • Piwien-Pilipuk, G., and Galigniana, M. D. (1998) Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor, Mol. Cell. Endocrinol. 144, 119-130.
    • (1998) Mol. Cell. Endocrinol , vol.144 , pp. 119-130
    • Piwien-Pilipuk, G.1    Galigniana, M.D.2
  • 7
    • 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
  • 8
    • 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
  • 9
    • 2342586714 scopus 로고    scopus 로고
    • Molecular mechanism of activation and nuclear translocation of the mineralocorticoid receptor upon binding of pregnanesteroids
    • Galigniana, M. D., Piwien Pilipuk, G., Kanelakis, K. C., Burton, G., and Lantos, C. P. (2004) Molecular mechanism of activation and nuclear translocation of the mineralocorticoid receptor upon binding of pregnanesteroids, Mol. Cell. Endocrinol. 217, 167-179.
    • (2004) Mol. Cell. Endocrinol , vol.217 , pp. 167-179
    • Galigniana, M.D.1    Piwien Pilipuk, G.2    Kanelakis, K.C.3    Burton, G.4    Lantos, C.P.5
  • 10
    • 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, 857-872.
    • (2004) Cell. Signalling , vol.16 , pp. 857-872
    • Pratt, W.B.1    Galigniana, M.D.2    Harrell, J.M.3    DeFranco, D.B.4
  • 11
    • 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
  • 12
    • 0037197660 scopus 로고    scopus 로고
    • All of the protein interactions that link steroid receptor·hsp90·immunophilin heterocomplexes to cytoplasmic dynein are common to plant and animal cells
    • Harrell, J. M., Kurek, I., Breiman, A., Radanyi, C., Renoir, J. M., Pratt, W. B., and Galigniana, M. D. (2002) All of the protein interactions that link steroid receptor·hsp90·immunophilin heterocomplexes to cytoplasmic dynein are common to plant and animal cells, Biochemistry 41, 5581-5587.
    • (2002) Biochemistry , vol.41 , pp. 5581-5587
    • Harrell, J.M.1    Kurek, I.2    Breiman, A.3    Radanyi, C.4    Renoir, J.M.5    Pratt, W.B.6    Galigniana, M.D.7
  • 13
    • 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
  • 14
    • 0031757167 scopus 로고    scopus 로고
    • Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton
    • Galigniana, M. D., Scruggs, J. L., Herrington, J., Welsh, M. J., Carter-Su, C., Housley, P. R., and Pratt, W. B. (1998) Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton, Mol. Endocrinol. 12, 1903-1913.
    • (1998) Mol. Endocrinol , vol.12 , pp. 1903-1913
    • Galigniana, M.D.1    Scruggs, J.L.2    Herrington, J.3    Welsh, M.J.4    Carter-Su, C.5    Housley, P.R.6    Pratt, W.B.7
  • 15
    • 1642392035 scopus 로고    scopus 로고
    • Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation
    • Galigniana, M. D., Harrell, J. M., Housley, P. R., Patterson, C., Fisher, S. K., and Pratt, W. B. (2004) Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation, Brain Res. Mol. Brain Res. 123, 27-36.
    • (2004) Brain Res. Mol. Brain Res , vol.123 , pp. 27-36
    • Galigniana, M.D.1    Harrell, J.M.2    Housley, P.R.3    Patterson, C.4    Fisher, S.K.5    Pratt, W.B.6
  • 16
    • 0032929622 scopus 로고    scopus 로고
    • Discrimination between NL1-and NL2-mediated nuclear localization of the glucocorticoid receptor
    • Savory, J. G., Hsu, B., Laquian, I. R., Giffin, W., Reich, T., Hache, R. J., and Lefebvre, Y. A. (1999) Discrimination between NL1-and NL2-mediated nuclear localization of the glucocorticoid receptor, Mol. Cell. Biol. 19, 1025-1037.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 1025-1037
    • Savory, J.G.1    Hsu, B.2    Laquian, I.R.3    Giffin, W.4    Reich, T.5    Hache, R.J.6    Lefebvre, Y.A.7
  • 17
    • 0033523006 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton
    • Galigniana, M. D., Housley, P. R., DeFranco, D. B., and Pratt, W. B. (1999) Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton, J. Biol. Chem. 274, 16222-16227.
    • (1999) J. Biol. Chem , vol.274 , pp. 16222-16227
    • Galigniana, M.D.1    Housley, P.R.2    DeFranco, D.B.3    Pratt, W.B.4
  • 18
    • 0027416853 scopus 로고
    • Bidirectional transport of glucocorticoid receptors across the nuclear envelope
    • Madan, A. P., and DeFranco, D. B. (1993) Bidirectional transport of glucocorticoid receptors across the nuclear envelope, Proc. Natl. Acad. Sci. U.S.A. 90, 3588-3592.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 3588-3592
    • Madan, A.P.1    DeFranco, D.B.2
  • 19
    • 0032763808 scopus 로고    scopus 로고
    • A model for the cytoplasmic trafficking of signalling proteins involving the hsp90-binding immunophilins and p50cdc37
    • Pratt, W. B., Silverstein, A. M., and Galigniana, M. D. (1999) A model for the cytoplasmic trafficking of signalling proteins involving the hsp90-binding immunophilins and p50cdc37, Cell. Signalling 11, 839-851.
    • (1999) Cell. Signalling , vol.11 , pp. 839-851
    • Pratt, W.B.1    Silverstein, A.M.2    Galigniana, M.D.3
  • 20
    • 0036357727 scopus 로고    scopus 로고
    • Functional implications of glucocorticoid receptor trafficking
    • DeFranco, D. B. (2002) Functional implications of glucocorticoid receptor trafficking, Ernst Schering Res. Found. Workshop, 91-109.
    • (2002) Ernst Schering Res. Found. Workshop , pp. 91-109
    • DeFranco, D.B.1
  • 21
    • 0029029232 scopus 로고
    • Nuclear localization signals overlap DNA- or RNA-binding domains in nucleic acid-binding proteins
    • LaCasse, E. C., and Lefebvre, Y. A. (1995) Nuclear localization signals overlap DNA- or RNA-binding domains in nucleic acid-binding proteins, Nucleic Acids Res. 23, 1647-1656.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1647-1656
    • LaCasse, E.C.1    Lefebvre, Y.A.2
  • 22
    • 0031008364 scopus 로고    scopus 로고
    • A role for HDJ-2/HSDJ in correcting subnuclear trafficking, transactivation, and transrepression defects of a glucocorticoid receptor zinc finger mutant
    • Tang, Y., Ramakrishnan, C., Thomas, J., and DeFranco, D. B. (1997) A role for HDJ-2/HSDJ in correcting subnuclear trafficking, transactivation, and transrepression defects of a glucocorticoid receptor zinc finger mutant, Mol. Biol. Cell 8, 795-809.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 795-809
    • Tang, Y.1    Ramakrishnan, C.2    Thomas, J.3    DeFranco, D.B.4
  • 23
    • 0032786877 scopus 로고    scopus 로고
    • General overview of mineralocorticoid hormone action
    • Agarwal, M. K., and Mirshahi, M. (1999) General overview of mineralocorticoid hormone action, Pharmacol. Ther. 84, 273-326.
    • (1999) Pharmacol. Ther , vol.84 , pp. 273-326
    • Agarwal, M.K.1    Mirshahi, M.2
  • 24
    • 20444484787 scopus 로고    scopus 로고
    • A serine/threonine-rich motif is one of three nuclear localization signals that determine unidirectional transport of the mineralocorticoid receptor to the nucleus
    • Walther, R. F., Atlas, E., Carrigan, A., Rouleau, Y., Edgecombe, A., Visentin, L., Lamprecht, C., Addicks, G. C., Hache, R. J., and Lefebvre, Y. A. (2005) A serine/threonine-rich motif is one of three nuclear localization signals that determine unidirectional transport of the mineralocorticoid receptor to the nucleus, J. Biol. Chem. 280, 17549-17561.
    • (2005) J. Biol. Chem , vol.280 , pp. 17549-17561
    • Walther, R.F.1    Atlas, E.2    Carrigan, A.3    Rouleau, Y.4    Edgecombe, A.5    Visentin, L.6    Lamprecht, C.7    Addicks, G.C.8    Hache, R.J.9    Lefebvre, Y.A.10
  • 25
    • 0020645078 scopus 로고
    • Translation of exogenous mRNAs in reticulocyte lysates
    • Merrick, W. C. (1983) Translation of exogenous mRNAs in reticulocyte lysates, Methods Enzymol. 101, 606-615.
    • (1983) Methods Enzymol , vol.101 , pp. 606-615
    • Merrick, W.C.1
  • 26
    • 0037070088 scopus 로고    scopus 로고
    • Modification of an essential amino group in the mineralocorticoid receptor evidences a differential conformational change of the receptor protein upon binding of antagonists, natural agonists and the synthetic agonist 11,19-oxidoprogesterone
    • Piwien-Pilipuk, G., Kanelakis, K. C., Ghini, A. A., Lantos, C. P., Litwack, G., Burton, G., and Galigniana, M. D. (2002) Modification of an essential amino group in the mineralocorticoid receptor evidences a differential conformational change of the receptor protein upon binding of antagonists, natural agonists and the synthetic agonist 11,19-oxidoprogesterone, Biochim. Biophys. Acta 1539, 31-48.
    • (2002) Biochim. Biophys. Acta , vol.1539 , pp. 31-48
    • Piwien-Pilipuk, G.1    Kanelakis, K.C.2    Ghini, A.A.3    Lantos, C.P.4    Litwack, G.5    Burton, G.6    Galigniana, M.D.7
  • 27
    • 0033961435 scopus 로고    scopus 로고
    • Oxidative stress induced by L-buthionine-(S,R)-sulfoximine, a selective inhibitor of glutathione metabolism, abrogates mouse kidney mineralocorticoid receptor function
    • Piwien-Pilipuk, G., and Galigniana, M. D. (2000) Oxidative stress induced by L-buthionine-(S,R)-sulfoximine, a selective inhibitor of glutathione metabolism, abrogates mouse kidney mineralocorticoid receptor function, Biochim. Biophys. Acta 1495, 263-280.
    • (2000) Biochim. Biophys. Acta , vol.1495 , pp. 263-280
    • Piwien-Pilipuk, G.1    Galigniana, M.D.2
  • 28
    • 0037023775 scopus 로고    scopus 로고
    • Impairment of mineralocorticoid receptor (MR)-dependent biological response by oxidative stress and aging: Correlation with post-translational modification of MR and decreased ADP-ribosylatable level of elongating factor 2 in kidney cells
    • Piwien-Pilipuk, G., Ayala, A., Machado, A., and Galigniana, M. D. (2002) Impairment of mineralocorticoid receptor (MR)-dependent biological response by oxidative stress and aging: Correlation with post-translational modification of MR and decreased ADP-ribosylatable level of elongating factor 2 in kidney cells, J. Biol. Chem. 277, 11896-11903.
    • (2002) J. Biol. Chem , vol.277 , pp. 11896-11903
    • Piwien-Pilipuk, G.1    Ayala, A.2    Machado, A.3    Galigniana, M.D.4
  • 29
    • 33746044924 scopus 로고    scopus 로고
    • Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and System N (SNAT5) amino acid transporter activity involving a conserved histidine residue
    • Baird, F. E., Pinilla-Tenas, J. J., Ogilvie, W. L., Ganapathy, V., Hundal, H. S., and Taylor, P. M. (2006) Evidence for allosteric regulation of pH-sensitive System A (SNAT2) and System N (SNAT5) amino acid transporter activity involving a conserved histidine residue, Biochem. J. 397, 369-375.
    • (2006) Biochem. J , vol.397 , pp. 369-375
    • Baird, F.E.1    Pinilla-Tenas, J.J.2    Ogilvie, W.L.3    Ganapathy, V.4    Hundal, H.S.5    Taylor, P.M.6
  • 31
    • 33645517425 scopus 로고    scopus 로고
    • Functional contribution of a conserved, mobile loop histidine of phosphoribulokinase
    • Runquist, J. A., and Miziorko, H. M. (2006) Functional contribution of a conserved, mobile loop histidine of phosphoribulokinase, Protein Sci. 15, 837-842.
    • (2006) Protein Sci , vol.15 , pp. 837-842
    • Runquist, J.A.1    Miziorko, H.M.2
  • 33
    • 0032553440 scopus 로고    scopus 로고
    • Localization of critical histidyl residues required for vinblastine-induced tubulin polymerization and for microtubule assembly
    • Rai, S. S., and Wolff, J. (1998) Localization of critical histidyl residues required for vinblastine-induced tubulin polymerization and for microtubule assembly, J. Biol. Chem. 273, 31131-31137.
    • (1998) J. Biol. Chem , vol.273 , pp. 31131-31137
    • Rai, S.S.1    Wolff, J.2
  • 34
    • 0036352904 scopus 로고    scopus 로고
    • Differences in nuclear retention characteristics of agonist-activated glucocorticoid receptor may determine specific responses
    • Vicent, G. P., Pecci, A., Ghini, A., Piwien-Pilipuk, G., and Galigniana, M. D. (2002) Differences in nuclear retention characteristics of agonist-activated glucocorticoid receptor may determine specific responses, Exp. Cell Res. 276, 142-154.
    • (2002) Exp. Cell Res , vol.276 , pp. 142-154
    • Vicent, G.P.1    Pecci, A.2    Ghini, A.3    Piwien-Pilipuk, G.4    Galigniana, M.D.5
  • 35
    • 0024452915 scopus 로고
    • Isolation and characterization of a mouse L cell variant deficient in glucocorticoid receptors
    • Housley, P. R., and Forsthoefel, A. M. (1989) Isolation and characterization of a mouse L cell variant deficient in glucocorticoid receptors, Biochem. Biophys. Res. Commun. 164, 480-487.
    • (1989) Biochem. Biophys. Res. Commun , vol.164 , pp. 480-487
    • Housley, P.R.1    Forsthoefel, A.M.2
  • 36
    • 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. (1997) 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, 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
  • 37
    • 0030581094 scopus 로고    scopus 로고
    • Stability study on renal type I mineralocorticoid receptor
    • Galigniana, M. D. (1996) Stability study on renal type I mineralocorticoid receptor, Life Sci. 59, 511-521.
    • (1996) Life Sci , vol.59 , pp. 511-521
    • Galigniana, M.D.1
  • 38
    • 0032168389 scopus 로고    scopus 로고
    • Cysteines 849 and 942 of human mineralocorticoid receptor are crucial for steroid binding
    • Lupo, B., Mesnier, D., and Auzou, G. (1998) Cysteines 849 and 942 of human mineralocorticoid receptor are crucial for steroid binding, Biochemistry 37, 12153-12159.
    • (1998) Biochemistry , vol.37 , pp. 12153-12159
    • Lupo, B.1    Mesnier, D.2    Auzou, G.3
  • 39
    • 0033179116 scopus 로고    scopus 로고
    • Comparative inhibition by hard and soft metal ions of steroid-binding capacity of renal mineralocorticoid receptor cross-linked to the 90-kDa heat-shock protein heterocomplex
    • Galigniana, M. D., and Piwien-Pilipuk, G. (1999) Comparative inhibition by hard and soft metal ions of steroid-binding capacity of renal mineralocorticoid receptor cross-linked to the 90-kDa heat-shock protein heterocomplex, Biochem. J. 341 (Part 3), 585-592.
    • (1999) Biochem. J , vol.341 , Issue.PART 3 , pp. 585-592
    • Galigniana, M.D.1    Piwien-Pilipuk, G.2
  • 40
    • 0017632673 scopus 로고
    • Modification of histidyl residues in proteins by diethylpyrocarbonate
    • Miles, E. W. (1977) Modification of histidyl residues in proteins by diethylpyrocarbonate, Methods Enzymol. 47, 431-442.
    • (1977) Methods Enzymol , vol.47 , pp. 431-442
    • Miles, E.W.1
  • 42
    • 0034061186 scopus 로고    scopus 로고
    • Nuclear transport and transcription
    • Komeili, A., and O'Shea, E. K. (2000) Nuclear transport and transcription, Curr. Opin. Cell Biol. 12, 355-360.
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 355-360
    • Komeili, A.1    O'Shea, E.K.2
  • 43
    • 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
  • 44
    • 0034791787 scopus 로고    scopus 로고
    • The C-terminal half of Hsp90 is responsible for its cytoplasmic localization
    • Passinen, S., Valkila, J., Manninen, T., Syvala, H., and Ylikomi, T. (2001) The C-terminal half of Hsp90 is responsible for its cytoplasmic localization, Eur. J. Biochem. 268, 5337-5342.
    • (2001) Eur. J. Biochem , vol.268 , pp. 5337-5342
    • Passinen, S.1    Valkila, J.2    Manninen, T.3    Syvala, H.4    Ylikomi, T.5
  • 45
    • 0028156864 scopus 로고
    • In vivo functional protein-protein interaction: Nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus
    • Kang, K. I., Devin, J., Cadepond, F., Jibard, N., Guiochon-Mantel, A., Baulieu, E. E., and Catelli, M. G. (1994) In vivo functional protein-protein interaction: Nuclear targeted hsp90 shifts cytoplasmic steroid receptor mutants into the nucleus, Proc. Natl. Acad. Sci. U.S.A. 91, 340-344.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 340-344
    • Kang, K.I.1    Devin, J.2    Cadepond, F.3    Jibard, N.4    Guiochon-Mantel, A.5    Baulieu, E.E.6    Catelli, M.G.7
  • 47
    • 4344615011 scopus 로고    scopus 로고
    • A single subunit of a heterotrimeric CCAAT-binding complex carries a nuclear localization signal: Piggy back transport of the pre-assembled complex to the nucleus
    • Steidl, S., Tuncher, A., Goda, H., Guder, C., Papadopoulou, N., Kobayashi, T., Tsukagoshi, N., Kato, M., and Brakhage, A. A. (2004) A single subunit of a heterotrimeric CCAAT-binding complex carries a nuclear localization signal: Piggy back transport of the pre-assembled complex to the nucleus, J. Mol. Biol. 342, 515-524.
    • (2004) J. Mol. Biol , vol.342 , pp. 515-524
    • Steidl, S.1    Tuncher, A.2    Goda, H.3    Guder, C.4    Papadopoulou, N.5    Kobayashi, T.6    Tsukagoshi, N.7    Kato, M.8    Brakhage, A.A.9
  • 48
    • 2442642835 scopus 로고    scopus 로고
    • Ploski, J. E., Shamsher, M. K., and Radu, A. (2004) Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13, Mol. Cell. Biol. 24, 4824-4834.
    • Ploski, J. E., Shamsher, M. K., and Radu, A. (2004) Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13, Mol. Cell. Biol. 24, 4824-4834.
  • 49
    • 29544437089 scopus 로고    scopus 로고
    • Effect of initial subcellular localization of progesterone receptor on import kinetics and transcriptional activity
    • Li, H., Fidler, M. L., and Lim, C. S. (2005) Effect of initial subcellular localization of progesterone receptor on import kinetics and transcriptional activity, Mol. Pharm. 2, 509-518.
    • (2005) Mol. Pharm , vol.2 , pp. 509-518
    • Li, H.1    Fidler, M.L.2    Lim, C.S.3
  • 50
    • 0033756012 scopus 로고    scopus 로고
    • Nucleocytoplasmic protein traffic and its significance to cell function
    • Yoneda, Y. (2000) Nucleocytoplasmic protein traffic and its significance to cell function, Genes Cells 5, 777-787.
    • (2000) Genes Cells , vol.5 , pp. 777-787
    • Yoneda, Y.1
  • 52
    • 21244456015 scopus 로고    scopus 로고
    • Imaging analysis of mineralocorticoid receptor and importins in single living cells by using GFP color variants
    • Tanaka, M., Nishi, M., Morimoto, M., Sugimoto, T., and Kawata, M. (2005) Imaging analysis of mineralocorticoid receptor and importins in single living cells by using GFP color variants, Cell Tissue Res. 320, 447-453.
    • (2005) Cell Tissue Res , vol.320 , pp. 447-453
    • Tanaka, M.1    Nishi, M.2    Morimoto, M.3    Sugimoto, T.4    Kawata, M.5
  • 53


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.