메뉴 건너뛰기




Volumn 408, Issue , 2015, Pages 33-37

Novel interactions of the mineralocorticoid receptor

Author keywords

Aldosterone; Coactivators; Corticosteroids; Cortisol; N C interaction

Indexed keywords

LIGAND; MINERALOCORTICOID RECEPTOR; PROTEIN BINDING;

EID: 84938285139     PISSN: 03037207     EISSN: 18728057     Source Type: Journal    
DOI: 10.1016/j.mce.2015.01.027     Document Type: Review
Times cited : (37)

References (58)
  • 1
    • 24744451821 scopus 로고    scopus 로고
    • A ligand-mediated hydrogen bond network required for the activation of the mineralocorticoid receptor
    • Bledsoe R.K., Madauss K.P., Holt J.A., Apolito C.J., Lambert M.H., Pearce K.H., et al. A ligand-mediated hydrogen bond network required for the activation of the mineralocorticoid receptor. J. Biol. Chem 2005, 280:31283-31293.
    • (2005) J. Biol. Chem , vol.280 , pp. 31283-31293
    • Bledsoe, R.K.1    Madauss, K.P.2    Holt, J.A.3    Apolito, C.J.4    Lambert, M.H.5    Pearce, K.H.6
  • 2
    • 18444405534 scopus 로고    scopus 로고
    • Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition
    • Bledsoe R.K., Montana G., Stanley T.B., Delves C.J., Apolito C.J., McKee D.D., et al. Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell 2002, 110:93-105.
    • (2002) Cell , vol.110 , pp. 93-105
    • Bledsoe, R.K.1    Montana, G.2    Stanley, T.B.3    Delves, C.J.4    Apolito, C.J.5    McKee, D.D.6
  • 3
    • 33747154772 scopus 로고    scopus 로고
    • Anatomical profiling of nuclear receptor expression revealsa hierarchical transcriptional network
    • Bookout A.L., Jeong Y., Downes M., Yu R.T., Evans R.M., Mangelsdorf D.J. Anatomical profiling of nuclear receptor expression revealsa hierarchical transcriptional network. Cell 2006, 126:789-799.
    • (2006) Cell , vol.126 , pp. 789-799
    • Bookout, A.L.1    Jeong, Y.2    Downes, M.3    Yu, R.T.4    Evans, R.M.5    Mangelsdorf, D.J.6
  • 5
    • 0028909667 scopus 로고
    • Negative cross-talk between ReIA and the glucocorticoid receptor - a possible mechanism for the anti-inflammatory action of glucocorticoids
    • Caldenhoven E., Liden J., Wissink S., Vandestolpe A., Raaijmakers J., Koenderman L., et al. Negative cross-talk between ReIA and the glucocorticoid receptor - a possible mechanism for the anti-inflammatory action of glucocorticoids. Mol. Endocrinol 1995, 9:401-412.
    • (1995) Mol. Endocrinol , vol.9 , pp. 401-412
    • Caldenhoven, E.1    Liden, J.2    Wissink, S.3    Vandestolpe, A.4    Raaijmakers, J.5    Koenderman, L.6
  • 6
    • 44949169677 scopus 로고    scopus 로고
    • Functional mineralocorticoid receptors in human vascular endothelial cells regulate intercellular adhesion molecule-1 expression and promote leukocyte adhesion
    • Caprio M., Newfell B.G., la Sala A., Baur W., Fabbri A., Rosano G., et al. Functional mineralocorticoid receptors in human vascular endothelial cells regulate intercellular adhesion molecule-1 expression and promote leukocyte adhesion. Circ. Res 2008, 102:1359-1367.
    • (2008) Circ. Res , vol.102 , pp. 1359-1367
    • Caprio, M.1    Newfell, B.G.2    la Sala, A.3    Baur, W.4    Fabbri, A.5    Rosano, G.6
  • 7
    • 84870057420 scopus 로고    scopus 로고
    • Mineralocorticoid and glucocorticoid receptors differentially regulate NF-kappaB activity and pro-inflammatory cytokine production in murine BV-2 microglial cells
    • Chantong B., Kratschmar D.V., Nashev L.G., Balazs Z., Odermatt A. Mineralocorticoid and glucocorticoid receptors differentially regulate NF-kappaB activity and pro-inflammatory cytokine production in murine BV-2 microglial cells. J. Neuroinflammation 2012, 9:260.
    • (2012) J. Neuroinflammation , vol.9 , pp. 260
    • Chantong, B.1    Kratschmar, D.V.2    Nashev, L.G.3    Balazs, Z.4    Odermatt, A.5
  • 9
    • 0041324898 scopus 로고    scopus 로고
    • The interplay between the glucocorticoid receptor and nuclear factor-κB or activator protein-1: molecular mechanisms for gene repression
    • De Bosscher K., Vanden Berghe W., Haegeman G. The interplay between the glucocorticoid receptor and nuclear factor-κB or activator protein-1: molecular mechanisms for gene repression. Endocr. Rev 2003, 24:488-522.
    • (2003) Endocr. Rev , vol.24 , pp. 488-522
    • De Bosscher, K.1    Vanden Berghe, W.2    Haegeman, G.3
  • 10
    • 84855642277 scopus 로고    scopus 로고
    • Non-genomic actions of aldosterone: from receptors and signals to membrane targets
    • Dooley R., Harvey B.J., Thomas W. Non-genomic actions of aldosterone: from receptors and signals to membrane targets. Mol. Cell. Endocrinol 2012, 350:223-234.
    • (2012) Mol. Cell. Endocrinol , vol.350 , pp. 223-234
    • Dooley, R.1    Harvey, B.J.2    Thomas, W.3
  • 12
    • 77956909015 scopus 로고    scopus 로고
    • A new mode of mineralocorticoid receptor antagonism by a potent and selective nonsteroidal molecule
    • Fagart J., Hillisch A., Huyet J., Barfacker L., Fay M., Pleiss U., et al. A new mode of mineralocorticoid receptor antagonism by a potent and selective nonsteroidal molecule. J. Biol. Chem 2010, 285:29932-29940.
    • (2010) J. Biol. Chem , vol.285 , pp. 29932-29940
    • Fagart, J.1    Hillisch, A.2    Huyet, J.3    Barfacker, L.4    Fay, M.5    Pleiss, U.6
  • 13
    • 84888053233 scopus 로고    scopus 로고
    • Vascular effects of aldosterone: sorting out the receptors and the ligands
    • Feldman R.D., Gros R. Vascular effects of aldosterone: sorting out the receptors and the ligands. Clin. Exp. Pharmacol. Physiol 2013, 40:916-921.
    • (2013) Clin. Exp. Pharmacol. Physiol , vol.40 , pp. 916-921
    • Feldman, R.D.1    Gros, R.2
  • 14
    • 77957334372 scopus 로고    scopus 로고
    • Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure
    • Fischer K., Kelly S.M., Watt K., Price N.C., McEwan I.J. Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. Mol. Endocrinol 2010, 24:1935-1948.
    • (2010) Mol. Endocrinol , vol.24 , pp. 1935-1948
    • Fischer, K.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 15
    • 31944432423 scopus 로고    scopus 로고
    • Mechanisms of mineralocorticoid action
    • Fuller P.J., Young M.J. Mechanisms of mineralocorticoid action. Hypertension 2005, 46:1227-1235.
    • (2005) Hypertension , vol.46 , pp. 1227-1235
    • Fuller, P.J.1    Young, M.J.2
  • 17
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass C.K., Rosenfeld M.G. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 2000, 14:121-141.
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 18
    • 0025305295 scopus 로고
    • ICV infusion of corticosterone antagonizes ICV-aldosterone hypertension
    • Gomez-Sanchez E.P., Venkataraman M.T., Thwaites D., Fort C. ICV infusion of corticosterone antagonizes ICV-aldosterone hypertension. Am. J. Physiol 1990, 258:E649-E653.
    • (1990) Am. J. Physiol , vol.258 , pp. E649-E653
    • Gomez-Sanchez, E.P.1    Venkataraman, M.T.2    Thwaites, D.3    Fort, C.4
  • 19
    • 0023254634 scopus 로고
    • Oestradiol induction of a glucocorticoid-responsive gene by a chimaeric receptor
    • Green S., Chambon P. Oestradiol induction of a glucocorticoid-responsive gene by a chimaeric receptor. Nature 1987, 325:75-78.
    • (1987) Nature , vol.325 , pp. 75-78
    • Green, S.1    Chambon, P.2
  • 20
  • 21
    • 84856345106 scopus 로고    scopus 로고
    • Interaction between mineralocorticoid receptor and epidermal growth factor receptor signaling
    • Grossmann C., Gekle M. Interaction between mineralocorticoid receptor and epidermal growth factor receptor signaling. Mol. Cell. Endocrinol 2012, 350:235-241.
    • (2012) Mol. Cell. Endocrinol , vol.350 , pp. 235-241
    • Grossmann, C.1    Gekle, M.2
  • 22
    • 84906979408 scopus 로고    scopus 로고
    • Crystal structure of the mineralocorticoid receptor DNA binding domain in complex with DNA
    • Hudson W.H., Youn C., Ortlund E.A. Crystal structure of the mineralocorticoid receptor DNA binding domain in complex with DNA. PLoS ONE 2014, 9(9):e107000.
    • (2014) PLoS ONE , vol.9 , Issue.9 , pp. e107000
    • Hudson, W.H.1    Youn, C.2    Ortlund, E.A.3
  • 23
    • 22344444725 scopus 로고    scopus 로고
    • The ligand-dependent interaction of mineralocorticoid receptor with coactivator and corepressor peptides suggests multiple activation mechanisms
    • Hultman M.L., Krasnoperova N.V., Li S., Du S., Xia C., Dietz J.D., et al. The ligand-dependent interaction of mineralocorticoid receptor with coactivator and corepressor peptides suggests multiple activation mechanisms. Mol. Endocrinol 2005, 19:1460-1473.
    • (2005) Mol. Endocrinol , vol.19 , pp. 1460-1473
    • Hultman, M.L.1    Krasnoperova, N.V.2    Li, S.3    Du, S.4    Xia, C.5    Dietz, J.D.6
  • 24
    • 3442886513 scopus 로고    scopus 로고
    • Rates of hyperkalemia after publication of the Randomized Aldactone Evaluation Study
    • Juurlink D.N., Mamdani M.M., Lee D.S., Kopp A., Austin P.C., Laupacis A., et al. Rates of hyperkalemia after publication of the Randomized Aldactone Evaluation Study. N. Engl. J. Med 2004, 351:543-551.
    • (2004) N. Engl. J. Med , vol.351 , pp. 543-551
    • Juurlink, D.N.1    Mamdani, M.M.2    Lee, D.S.3    Kopp, A.4    Austin, P.C.5    Laupacis, A.6
  • 25
    • 0034327472 scopus 로고    scopus 로고
    • Inhibition of mineralocorticoid-mediated transcription by NF-[kappa]B
    • Kolla V., Litwack G. Inhibition of mineralocorticoid-mediated transcription by NF-[kappa]B. Arch. Biochem. Biophys 2000, 383:38-45.
    • (2000) Arch. Biochem. Biophys , vol.383 , pp. 38-45
    • Kolla, V.1    Litwack, G.2
  • 26
    • 0029560494 scopus 로고
    • Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer
    • Langley E., Zhou Z.X., Wilson E.M. Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer. J. Biol. Chem 1995, 270:29983-29990.
    • (1995) J. Biol. Chem , vol.270 , pp. 29983-29990
    • Langley, E.1    Zhou, Z.X.2    Wilson, E.M.3
  • 27
    • 58149510602 scopus 로고    scopus 로고
    • Aldosterone activates NF-kappaB in the collecting duct
    • Leroy V., de Seigneux S., Agassiz V. Aldosterone activates NF-kappaB in the collecting duct. J. Am. Soc. Nephrol 2009, 20:131-144.
    • (2009) J. Am. Soc. Nephrol , vol.20 , pp. 131-144
    • Leroy, V.1    de Seigneux, S.2    Agassiz, V.3
  • 28
    • 63849261057 scopus 로고    scopus 로고
    • G protein-coupled receptor 30: estrogen receptors or collaboration?
    • Levin E.R. G protein-coupled receptor 30: estrogen receptors or collaboration?. Endocrinology 2009, 150:1563-1565.
    • (2009) Endocrinology , vol.150 , pp. 1563-1565
    • Levin, E.R.1
  • 29
    • 23044510503 scopus 로고    scopus 로고
    • Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor
    • Li Y., Suino K., Daugherty J., Xu H.E. Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor. Mol. Cell 2005, 19:367-380.
    • (2005) Mol. Cell , vol.19 , pp. 367-380
    • Li, Y.1    Suino, K.2    Daugherty, J.3    Xu, H.E.4
  • 30
    • 0030824266 scopus 로고    scopus 로고
    • A new function for the C-terminal zinc finger of the glucocorticoid receptor
    • Liden J., Delaunay F., Rafter I., Gustafsson J., Okret S. A new function for the C-terminal zinc finger of the glucocorticoid receptor. J. Biol. Chem 1997, 272:21467-21472.
    • (1997) J. Biol. Chem , vol.272 , pp. 21467-21472
    • Liden, J.1    Delaunay, F.2    Rafter, I.3    Gustafsson, J.4    Okret, S.5
  • 31
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto K.R., Sigler P.B. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 1991, 352:497-505.
    • (1991) Nature , vol.352 , pp. 497-505
    • Luisi, B.F.1    Xu, W.X.2    Otwinowski, Z.3    Freedman, L.P.4    Yamamoto, K.R.5    Sigler, P.B.6
  • 32
    • 24944440867 scopus 로고    scopus 로고
    • Analysis of the hormone-binding domain of steroid receptors using chimeras generated by homologous recombination
    • Martinez E.D., Pattabiraman N., Danielsen M. Analysis of the hormone-binding domain of steroid receptors using chimeras generated by homologous recombination. Exp. Cell Res 2005, 308:320-333.
    • (2005) Exp. Cell Res , vol.308 , pp. 320-333
    • Martinez, E.D.1    Pattabiraman, N.2    Danielsen, M.3
  • 34
    • 0034021821 scopus 로고    scopus 로고
    • Transcriptional repression of the 5-HTIA receptor promoter by corticosterone via mineralocorticoid receptors depends on the celllular context
    • Meijer O.C., Williamson A., Dallman M.F., Pearce D. Transcriptional repression of the 5-HTIA receptor promoter by corticosterone via mineralocorticoid receptors depends on the celllular context. J. Neuroendocrinol 2000, 12:245-254.
    • (2000) J. Neuroendocrinol , vol.12 , pp. 245-254
    • Meijer, O.C.1    Williamson, A.2    Dallman, M.F.3    Pearce, D.4
  • 35
    • 0034740164 scopus 로고    scopus 로고
    • Synergism between ER (alpha) transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1; requirement for the AF-1 (alpha)-helical core and for a direct interaction between the N- and C-terminal domains
    • Metivier R., Penot G., Flouriot G., Pakdel F. Synergism between ER (alpha) transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1; requirement for the AF-1 (alpha)-helical core and for a direct interaction between the N- and C-terminal domains. Mol. Endocrinol 2001, 15:1953-1970.
    • (2001) Mol. Endocrinol , vol.15 , pp. 1953-1970
    • Metivier, R.1    Penot, G.2    Flouriot, G.3    Pakdel, F.4
  • 36
    • 33645412965 scopus 로고    scopus 로고
    • Nongenomic actions of aldosterone: physiological or pathophysiological role?
    • Mihailidou A.S. Nongenomic actions of aldosterone: physiological or pathophysiological role?. Steroids 2006, 71:277-280.
    • (2006) Steroids , vol.71 , pp. 277-280
    • Mihailidou, A.S.1
  • 37
    • 84856335862 scopus 로고    scopus 로고
    • Tissue-specific modulation of mineralocorticoid receptor function by 11β-hydroxysteroid dehydrogenases: an overview
    • Odermatt A., Kratschmar D.V. Tissue-specific modulation of mineralocorticoid receptor function by 11β-hydroxysteroid dehydrogenases: an overview. Mol. Cell. Endocrinol 2012, 350:168-186.
    • (2012) Mol. Cell. Endocrinol , vol.350 , pp. 168-186
    • Odermatt, A.1    Kratschmar, D.V.2
  • 38
    • 0027394555 scopus 로고
    • Mineralocorticoid and glucocorticoid receptor activities distinguished by nonreceptor factors at a composite response element
    • Pearce D., Yamamoto K.R. Mineralocorticoid and glucocorticoid receptor activities distinguished by nonreceptor factors at a composite response element. Science 1993, 259:1161-1165.
    • (1993) Science , vol.259 , pp. 1161-1165
    • Pearce, D.1    Yamamoto, K.R.2
  • 39
    • 69449087342 scopus 로고    scopus 로고
    • Structural and functional characterization of the interdomain interaction in the mineralocorticoid receptor
    • Pippal J.B., Yao Y.-Z., Rogerson F.M., Fuller P.J. Structural and functional characterization of the interdomain interaction in the mineralocorticoid receptor. Mol. Endocrinol 2009, 23:1360-1370.
    • (2009) Mol. Endocrinol , vol.23 , pp. 1360-1370
    • Pippal, J.B.1    Yao, Y.-Z.2    Rogerson, F.M.3    Fuller, P.J.4
  • 41
    • 70349257487 scopus 로고    scopus 로고
    • Deletion of mineralocorticoid receptors from macrophages protects against DOC/salt-induced cardiac fibrosis and increased blood pressure
    • Rickard A.J., Morgan J., Tesch G., Funder J.W., Fuller P.J., Young M.J. Deletion of mineralocorticoid receptors from macrophages protects against DOC/salt-induced cardiac fibrosis and increased blood pressure. Hypertens 2009, 54:537-543.
    • (2009) Hypertens , vol.54 , pp. 537-543
    • Rickard, A.J.1    Morgan, J.2    Tesch, G.3    Funder, J.W.4    Fuller, P.J.5    Young, M.J.6
  • 42
    • 0034465234 scopus 로고    scopus 로고
    • Residues in the ligand binding domain that confer progestin or glucocorticoid specificity and nodulate the receptor transactivation capacity
    • Robin-Jagerschmidt C., Wurtz J.-M., Guillot B., Gofflo D., Benhamou B., Vergezac A., et al. Residues in the ligand binding domain that confer progestin or glucocorticoid specificity and nodulate the receptor transactivation capacity. Mol. Endocrinol 2000, 14:1028-1037.
    • (2000) Mol. Endocrinol , vol.14 , pp. 1028-1037
    • Robin-Jagerschmidt, C.1    Wurtz, J.-M.2    Guillot, B.3    Gofflo, D.4    Benhamou, B.5    Vergezac, A.6
  • 43
    • 0037469632 scopus 로고    scopus 로고
    • Interdomain interactions in the mineralocorticoid receptor
    • Rogerson F.M., Fuller P.J. Interdomain interactions in the mineralocorticoid receptor. Mol. Cell. Endocrinol 2003, 200:45-55.
    • (2003) Mol. Cell. Endocrinol , vol.200 , pp. 45-55
    • Rogerson, F.M.1    Fuller, P.J.2
  • 44
    • 0033579510 scopus 로고    scopus 로고
    • Structural determinants of aldosterone binding selectivity in the mineralocorticoid receptor
    • Rogerson F.M., Dimopoulos N., Sluka P., Chu S., Curtis A.J., Fuller P.J. Structural determinants of aldosterone binding selectivity in the mineralocorticoid receptor. J. Biol. Chem 1999, 274:36305-36311.
    • (1999) J. Biol. Chem , vol.274 , pp. 36305-36311
    • Rogerson, F.M.1    Dimopoulos, N.2    Sluka, P.3    Chu, S.4    Curtis, A.J.5    Fuller, P.J.6
  • 45
    • 34247897054 scopus 로고    scopus 로고
    • A critical region in the mineralocorticoid receptor for aldosterone binding and activation by cortisol: evidence for a common mechanism governing ligand binding specificity in steroid hormone receptors
    • Rogerson F.M., Yao Y.-Z., Elsass R.E., Dimopoulos N., Smith B.J., Fuller P.J. A critical region in the mineralocorticoid receptor for aldosterone binding and activation by cortisol: evidence for a common mechanism governing ligand binding specificity in steroid hormone receptors. Mol. Endocrinol 2007, 21:817-828.
    • (2007) Mol. Endocrinol , vol.21 , pp. 817-828
    • Rogerson, F.M.1    Yao, Y.-Z.2    Elsass, R.E.3    Dimopoulos, N.4    Smith, B.J.5    Fuller, P.J.6
  • 46
    • 84907709951 scopus 로고    scopus 로고
    • Identification and characterization of a ligand-selective mineralocorticoid receptor coactivator
    • Rogerson F.M., Yao Y.-Z., Young M.J., Fuller P.J. Identification and characterization of a ligand-selective mineralocorticoid receptor coactivator. FASEB J. 2014, 28:4200-4210.
    • (2014) FASEB J. , vol.28 , pp. 4200-4210
    • Rogerson, F.M.1    Yao, Y.-Z.2    Young, M.J.3    Fuller, P.J.4
  • 47
    • 0029762716 scopus 로고    scopus 로고
    • High glucose stimulates aldosterone-induced hypertrophy via type 1 mineralocorticoid receptors in neonatal rat cardiomyocytes
    • Sato A., Funder J.W. High glucose stimulates aldosterone-induced hypertrophy via type 1 mineralocorticoid receptors in neonatal rat cardiomyocytes. Endocrinology 1996, 137:4145-4153.
    • (1996) Endocrinology , vol.137 , pp. 4145-4153
    • Sato, A.1    Funder, J.W.2
  • 48
    • 84887432790 scopus 로고    scopus 로고
    • Mineralocorticoid receptor phosphorylation regulates ligand binding and renal response to volume depletion and hyperkalemia
    • Shibata S., Rinehart J., Zhang J., Moeckel G., Castaňeda-Bueno M., Stiegler A.L., et al. Mineralocorticoid receptor phosphorylation regulates ligand binding and renal response to volume depletion and hyperkalemia. Cell Metab 2013, 18:660-671.
    • (2013) Cell Metab , vol.18 , pp. 660-671
    • Shibata, S.1    Rinehart, J.2    Zhang, J.3    Moeckel, G.4    Castaňeda-Bueno, M.5    Stiegler, A.L.6
  • 49
    • 84858293934 scopus 로고    scopus 로고
    • Aldosterone stimulates nuclear factor-kappaB activity and transcription of intercellular adhesion molecule-1 and connective tissue browth factor in rat mesangial cells via serum- and glucocorticoid-inducible protein kinase-1
    • Terada Y., Ueda S., Hamada K., Shimamura Y., Ogata K., Inoue K., et al. Aldosterone stimulates nuclear factor-kappaB activity and transcription of intercellular adhesion molecule-1 and connective tissue browth factor in rat mesangial cells via serum- and glucocorticoid-inducible protein kinase-1. Clin. Exp. Nephrol 2012, 16:81-88.
    • (2012) Clin. Exp. Nephrol , vol.16 , pp. 81-88
    • Terada, Y.1    Ueda, S.2    Hamada, K.3    Shimamura, Y.4    Ogata, K.5    Inoue, K.6
  • 50
    • 0033305373 scopus 로고    scopus 로고
    • Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo
    • Tetel M.J., Giangrande P.H., Leonhardt S.A., McDonnell D.P., Edwards D.P. Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo. Mol. Endocrinol 1999, 13:910-924.
    • (1999) Mol. Endocrinol , vol.13 , pp. 910-924
    • Tetel, M.J.1    Giangrande, P.H.2    Leonhardt, S.A.3    McDonnell, D.P.4    Edwards, D.P.5
  • 51
    • 0034982410 scopus 로고    scopus 로고
    • Disrupted amino- and carboxyl-terminal interactions of the androgen receptor are linked to androgen insensitivity
    • Thompson J., Saatcioglu F., Janne O.A., Palvimo J.J. Disrupted amino- and carboxyl-terminal interactions of the androgen receptor are linked to androgen insensitivity. Mol. Endocrinol 2001, 15:923-935.
    • (2001) Mol. Endocrinol , vol.15 , pp. 923-935
    • Thompson, J.1    Saatcioglu, F.2    Janne, O.A.3    Palvimo, J.J.4
  • 52
    • 0031004099 scopus 로고    scopus 로고
    • Sequences in the ligand-binding domains of the human androgen and progesterone receptors which determine their distinct ligand identities
    • Vivat V., Gofflo D., Wurtz J.-M., Bourguet W., Philibert D., Gronemeyer H. Sequences in the ligand-binding domains of the human androgen and progesterone receptors which determine their distinct ligand identities. J. Mol. Endocrinol 1997, 18:147-160.
    • (1997) J. Mol. Endocrinol , vol.18 , pp. 147-160
    • Vivat, V.1    Gofflo, D.2    Wurtz, J.-M.3    Bourguet, W.4    Philibert, D.5    Gronemeyer, H.6
  • 54
    • 84856315210 scopus 로고    scopus 로고
    • Interactions of the mineralocorticoid receptor - Within and without
    • Yang J., Fuller P.J. Interactions of the mineralocorticoid receptor - Within and without. Mol. Cell. Endocrinol 2012, 350:196-205.
    • (2012) Mol. Cell. Endocrinol , vol.350 , pp. 196-205
    • Yang, J.1    Fuller, P.J.2
  • 55
    • 78650923654 scopus 로고    scopus 로고
    • Identification of ligand-selective peptide antagonists of the mineralocorticoid receptor using phage display
    • Yang J., Chang C.Y., Safi R., Morgan J., McDonnell D.P., Fuller P.J., et al. Identification of ligand-selective peptide antagonists of the mineralocorticoid receptor using phage display. Mol. Endocrinol 2011, 25:32-43.
    • (2011) Mol. Endocrinol , vol.25 , pp. 32-43
    • Yang, J.1    Chang, C.Y.2    Safi, R.3    Morgan, J.4    McDonnell, D.P.5    Fuller, P.J.6
  • 56
    • 84856346254 scopus 로고    scopus 로고
    • Mechanisms of mineralocorticoid salt-induced hypertension and cardiac fibrosis
    • Young M.J., Rickard A.J. Mechanisms of mineralocorticoid salt-induced hypertension and cardiac fibrosis. Mol. Cell. Endocrinol 2012, 350:248-255.
    • (2012) Mol. Cell. Endocrinol , vol.350 , pp. 248-255
    • Young, M.J.1    Rickard, A.J.2
  • 58
    • 0028809317 scopus 로고
    • Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability
    • Zhou Z.X., Lane M.V., Kemppainen J.A., French F.S., Wilson E.M. Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability. Mol. Endocrinol 1995, 9:208-218.
    • (1995) Mol. Endocrinol , vol.9 , pp. 208-218
    • Zhou, Z.X.1    Lane, M.V.2    Kemppainen, J.A.3    French, F.S.4    Wilson, E.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.