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Volumn 217, Issue 1-2, 2004, Pages 167-179

Molecular mechanism of activation and nuclear translocation of the mineralocorticoid receptor upon binding of pregnanesteroids

Author keywords

11,19 Oxidoprogesterone; Aldosterone; Dynein; Immunophilins; Natriuresis; Trafficking

Indexed keywords

11,19 OXIDOPROGESTERONE; 11BETA HYDROXYPROGESTERONE; 5ALPHA PREGNANE 3,20 DIONE; 5BETA DIHYDROPROGESTERONE; 6,19 OXIDOPROGESTERONE; ALDOSTERONE; DEOXYCORTICOSTERONE; DYNEIN ADENOSINE TRIPHOSPHATASE; LIGAND; MINERALOCORTICOID; MINERALOCORTICOID RECEPTOR; PREGN 4 ENE 3,11,20 TRIONE; PREGNANE DERIVATIVE; PROGESTERONE DERIVATIVE; STEROID; UNCLASSIFIED DRUG;

EID: 2342586714     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2003.10.041     Document Type: Conference Paper
Times cited : (23)

References (57)
  • 1
    • 0032786877 scopus 로고    scopus 로고
    • General overview of mineralocorticoid action
    • Agarwal M.K., Mirashi M. General overview of mineralocorticoid action. Pharmacol. Ther. 84:2000;273-326
    • (2000) Pharmacol. Ther. , vol.84 , pp. 273-326
    • Agarwal, M.K.1    Mirashi, M.2
  • 2
    • 0036843129 scopus 로고    scopus 로고
    • Traffick jams II: An update of diseases of intracellular transport
    • Aridor A., Hannan L.A. Traffick jams II: an update of diseases of intracellular transport. Traffic. 3:2002;781-790
    • (2002) Traffic , vol.3 , pp. 781-790
    • Aridor, A.1    Hannan, L.A.2
  • 3
    • 0023221667 scopus 로고
    • Cloning of human mineralocorticoid receptor complementary DNA: Structural and functional kinship with the glucocorticoid receptor
    • Arriza J.L., Weinberger C., Cerelli G., Glaser T.M., Handelin B.L., Housman D.E., Evans R.M. Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor. Science. 237:1987;268-275
    • (1987) Science , vol.237 , pp. 268-275
    • Arriza, J.L.1    Weinberger, C.2    Cerelli, G.3    Glaser, T.M.4    Handelin, B.L.5    Housman, D.E.6    Evans, R.M.7
  • 4
    • 0026634731 scopus 로고
    • The cellular action of aldosterone in target epithelia
    • Bastl C.P., Hayslett J.P. The cellular action of aldosterone in target epithelia. Kidney Int. 42:1992;250-264
    • (1992) Kidney Int. , vol.42 , pp. 250-264
    • Bastl, C.P.1    Hayslett, J.P.2
  • 5
    • 0035856514 scopus 로고    scopus 로고
    • DNA binding domains in diverse nuclear receptors function as nuclear export signals
    • Black B.E., Holaska J.M., Rastinejad F., Paschal B.M. DNA binding domains in diverse nuclear receptors function as nuclear export signals. Curr. Biol. 11:2001;1749-1758
    • (2001) Curr. Biol. , vol.11 , pp. 1749-1758
    • Black, B.E.1    Holaska, J.M.2    Rastinejad, F.3    Paschal, B.M.4
  • 6
    • 0001179878 scopus 로고
    • An improved preparation of 11,19-oxidopregn-4-ene-3,20-dione and 6,19-oxidopregn-4-ene-3,11,20-tri-one
    • Brachet-Cota, A.L., Burton, G., 1990. An improved preparation of 11,19-oxidopregn-4-ene-3, 20-dione and 6,19-oxidopregn-4-ene-3,11,20-tri-one. Z. Naturforsch. 45, 711; 715.
    • (1990) Z. Naturforsch. , vol.45 , pp. 711
    • Brachet-Cota, A.L.1    Burton, G.2
  • 8
    • 85047684372 scopus 로고    scopus 로고
    • Navigating steroid hormone receptors through the nuclear compartment
    • DeFranco D. Navigating steroid hormone receptors through the nuclear compartment. Mol. Endocrinol. 16:2002;1449-1455
    • (2002) Mol. Endocrinol. , vol.16 , pp. 1449-1455
    • Defranco, D.1
  • 9
    • 0034891982 scopus 로고    scopus 로고
    • Glucocorticoid-remediable aldosteronism
    • Dluhy R.G. Glucocorticoid-remediable aldosteronism. Endocrinilogist. 11:2001;2263-2268
    • (2001) Endocrinilogist , vol.11 , pp. 2263-2268
    • Dluhy, R.G.1
  • 11
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans R.M. The steroid and thyroid hormone receptor superfamily. Science. 240:1988;889-895
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 13
    • 0032539721 scopus 로고    scopus 로고
    • Subcellular localization of mineralocorticoid receptors in living cells: Effects of receptor agonists and antagonists
    • Fejes-Tóth G., Pearce D., Náray-Fejes-Tóth A. Subcellular localization of mineralocorticoid receptors in living cells: effects of receptor agonists and antagonists. Proc. Natl. Acad. Sci. U.S.A. 95:1998;2973-2978
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2973-2978
    • Fejes-Tóth, G.1    Pearce, D.2    Náray-Fejes-Tóth, A.3
  • 14
    • 0023743171 scopus 로고
    • Mineralocorticoid action: Target tissue specificity is enzyme, not receptor, mediated
    • Funder J.W., Pearce P., Smith R., Smith A.I. Mineralocorticoid action: target tissue specificity is enzyme, not receptor, mediated. Science. 242:1988;583-585
    • (1988) Science , vol.242 , pp. 583-585
    • Funder, J.W.1    Pearce, P.2    Smith, R.3    Smith, A.I.4
  • 15
    • 0030444810 scopus 로고    scopus 로고
    • Exclusion of corticosterone from epithelial mineralocorticoid receptors is insufficient for selectivity of aldosterone action: In vivo binding studies
    • Funder J.W., Miles K. Exclusion of corticosterone from epithelial mineralocorticoid receptors is insufficient for selectivity of aldosterone action: in vivo binding studies. Endocrinology. 137:1996;5264-5268
    • (1996) Endocrinology , vol.137 , pp. 5264-5268
    • Funder, J.W.1    Miles, K.2
  • 18
    • 0030952348 scopus 로고    scopus 로고
    • Features of the shuttle pair 11β-hydroxyprogesterone/11- ketoprogesterone
    • Galigniana M.D., Vicent G.P., Lantos C.P., Burton G. Features of the shuttle pair 11β-hydroxyprogesterone/11-ketoprogesterone. Steroids. 62:1997;358-364
    • (1997) Steroids , vol.62 , pp. 358-364
    • Galigniana, M.D.1    Vicent, G.P.2    Lantos, C.P.3    Burton, G.4
  • 19
    • 0032143407 scopus 로고    scopus 로고
    • Native rat kidney mineralocorticoid receptor is a phosphoprotein whose transformation to a DNA-binding form is induced by phosphatases
    • Galigniana M.D. Native rat kidney mineralocorticoid receptor is a phosphoprotein whose transformation to a DNA-binding form is induced by phosphatases. Biochem. J. 333:1998;555-563
    • (1998) Biochem. J. , vol.333 , pp. 555-563
    • Galigniana, M.D.1
  • 20
    • 0002478825 scopus 로고    scopus 로고
    • Functional regulation of corticosteroid receptors by phosphorylation and redox potential
    • Galigniana M.D. Functional regulation of corticosteroid receptors by phosphorylation and redox potential. Curr. Topics Steroid Res. 3:2000;1-22
    • (2000) Curr. Topics Steroid Res. , vol.3 , pp. 1-22
    • Galigniana, M.D.1
  • 22
    • 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., Pratt W.B. 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. 276:2001;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
  • 23
    • 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.M., Chinkers M., Radanyi C., Renoir J.M., Zhang M., Pratt W.B. 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. 41:2002;13602-13610
    • (2002) Biochemistry , vol.41 , pp. 13602-13610
    • Galigniana, M.D.1    Harrell, J.M.2    Murphy, P.J.M.3    Chinkers, M.4    Radanyi, C.5    Renoir, J.M.6    Zhang, M.7    Pratt, W.B.8
  • 26
    • 0013955671 scopus 로고
    • Adrenal secretion rates of C19 and C21 steroids after hypophysectomy in the pig and the dog
    • Heap R.B., Holzbauer M., Newport H.M. Adrenal secretion rates of C19 and C21 steroids after hypophysectomy in the pig and the dog. J. Endocrinol. 36:1966;159-176
    • (1966) J. Endocrinol. , vol.36 , pp. 159-176
    • Heap, R.B.1    Holzbauer, M.2    Newport, H.M.3
  • 28
    • 0032548180 scopus 로고    scopus 로고
    • FKBP-type peptidyl-proplyl cis-trans isomerase from a sulfur-dependent hyperthermophilic archaeon, Thermococcus sp. KS-1
    • Iida T., Furutani M., Nishida F., Maruyama T. FKBP-type peptidyl-proplyl cis-trans isomerase from a sulfur-dependent hyperthermophilic archaeon, Thermococcus sp. KS-1. Gene. 222:1998;249-255
    • (1998) Gene , vol.222 , pp. 249-255
    • Iida, T.1    Furutani, M.2    Nishida, F.3    Maruyama, T.4
  • 30
    • 0015596205 scopus 로고
    • The effects of corticosterone, 18-OH-DOC, DOC and 11-hydroxyprogesterone on the adrenal pituitary axis of the stressed rat
    • Kraulis I., Traikov H., Li M., Birmingham M.K. The effects of corticosterone, 18-OH-DOC, DOC and 11-hydroxyprogesterone on the adrenal pituitary axis of the stressed rat. J. Steroid Biochem. 4:1973;129-137
    • (1973) J. Steroid Biochem. , vol.4 , pp. 129-137
    • Kraulis, I.1    Traikov, H.2    Li, M.3    Birmingham, M.K.4
  • 32
    • 0031451570 scopus 로고    scopus 로고
    • Evolution of the nuclear receptor superfamily: Early diversification from an ancestral orphan receptor
    • Laudet V. Evolution of the nuclear receptor superfamily: early diversification from an ancestral orphan receptor. J. Mol. Endocrinol. 19:1997;207-226
    • (1997) J. Mol. Endocrinol. , vol.19 , pp. 207-226
    • Laudet, V.1
  • 33
    • 0031733333 scopus 로고    scopus 로고
    • Intacellular signaling pathways confer specificity of transactivation by mineralocorticoid and glucocorticoid receptors
    • Lim-Tio S.S., Fuller P.J. Intacellular signaling pathways confer specificity of transactivation by mineralocorticoid and glucocorticoid receptors. Endocrinology. 139:1998;1653-1661
    • (1998) Endocrinology , vol.139 , pp. 1653-1661
    • Lim-Tio, S.S.1    Fuller, P.J.2
  • 34
    • 0029586681 scopus 로고
    • Steroid receptor heterodimerization demonstrated in vitro and in vivo
    • Liu W., Wang J., Sauter N.K., Pearce D. Steroid receptor heterodimerization demonstrated in vitro and in vivo. Proc. Natl. Acad. Sci. U.S.A. 92:1995;12480-12484
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 12480-12484
    • Liu, W.1    Wang, J.2    Sauter, N.K.3    Pearce, D.4
  • 35
    • 0027982025 scopus 로고
    • Differential intracellular localization of human mineralocorticoid receptor on binding of agonists and antagonists
    • Lombès M., Binart N., Delahaye F., Baulieu E.E., Rafestin-Oblin M.E. Differential intracellular localization of human mineralocorticoid receptor on binding of agonists and antagonists. Biochem. J. 302:1994;191-197
    • (1994) Biochem. J. , vol.302 , pp. 191-197
    • Lombès, M.1    Binart, N.2    Delahaye, F.3    Baulieu, E.E.4    Rafestin-Oblin, M.E.5
  • 36
    • 0029816659 scopus 로고    scopus 로고
    • Cellular functions of immunophilins
    • Marks A.R. Cellular functions of immunophilins. Physiol. Rev. 76:1996;631-649
    • (1996) Physiol. Rev. , vol.76 , pp. 631-649
    • Marks, A.R.1
  • 37
    • 0028358327 scopus 로고
    • Progesterone receptor A-form functions as a transcriptional modulator of mineralocorticoid receptor transcriptional activity
    • McDonnell D.P., Shabaz M.M., Vegeto E., Goldman M.E. Progesterone receptor A-form functions as a transcriptional modulator of mineralocorticoid receptor transcriptional activity. J. Steroid Biochem. Mol. Biol. 48:1994;425-432
    • (1994) J. Steroid Biochem. Mol. Biol. , vol.48 , pp. 425-432
    • McDonnell, D.P.1    Shabaz, M.M.2    Vegeto, E.3    Goldman, M.E.4
  • 38
    • 0037047429 scopus 로고    scopus 로고
    • Dynamic remodeling of transcription complexes by molecular chaperones
    • Morimoto R.I. Dynamic remodeling of transcription complexes by molecular chaperones. Cell. 110:2002;281-284
    • (2002) Cell , vol.110 , pp. 281-284
    • Morimoto, R.I.1
  • 39
    • 0034973472 scopus 로고    scopus 로고
    • Dynamic changes in subcellular localization on mineralocorticoid receptor in living cells: In comparison with glucocorticoid receptor using dual-color labeling with green fluorescent protein spectral variants
    • Nishi M., Ogawa H., Ito T., Matsuda K.-I., Kawata M. Dynamic changes in subcellular localization on mineralocorticoid receptor in living cells: in comparison with glucocorticoid receptor using dual-color labeling with green fluorescent protein spectral variants. Mol. Endocrinol. 15:2001;1077-1092
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1077-1092
    • Nishi, M.1    Ogawa, H.2    Ito, T.3    Matsuda, K.-I.4    Kawata, M.5
  • 40
    • 0037059802 scopus 로고    scopus 로고
    • Determinants of subnuclear organization of mineralocorticoid receptor characterized through analysis of wild type and mutant receptors
    • Pearce D., Náray-Fejes-Tóth A., Fejes-Tóth G. Determinants of subnuclear organization of mineralocorticoid receptor characterized through analysis of wild type and mutant receptors. J. Biol. Chem. 277:2002;1451-1456
    • (2002) J. Biol. Chem. , vol.277 , pp. 1451-1456
    • Pearce, D.1    Náray-Fejes-Tóth, A.2    Fejes-Tóth, G.3
  • 41
    • 0031721793 scopus 로고    scopus 로고
    • Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor
    • Piwien-Pilipuk G., Galigniana M.D. Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor. Mol. Cell. Endocrinol. 144:1998;119-130
    • (1998) Mol. Cell. Endocrinol. , vol.144 , pp. 119-130
    • Piwien-Pilipuk, G.1    Galigniana, M.D.2
  • 42
    • 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., Galigniana M.D. 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. Biochem. Biophys. Acta. 1589:2000;31-48
    • (2000) Biochem. Biophys. Acta , vol.1589 , 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
  • 43
    • 0037111505 scopus 로고    scopus 로고
    • Correlation between pregnanesteroid conformation, receptor affinity, and anti-natriuretic effect
    • Piwien-Pilipuk G., Kanelakis K.C., Galigniana M.D. Correlation between pregnanesteroid conformation, receptor affinity, and anti-natriuretic effect. Eur. J. Pharmacol. 454:2002a;131-143
    • (2002) Eur. J. Pharmacol. , vol.454 , pp. 131-143
    • Piwien-Pilipuk, G.1    Kanelakis, K.C.2    Galigniana, M.D.3
  • 44
    • 0033961435 scopus 로고    scopus 로고
    • Oxidative stress by L-buthionine-(S,R)-sulfoximine, a selective inhibitor of glutathione metabolism, abrogates mouse kidney mineralocorticoid receptor function
    • Piwien-Pilipuk G., Galigniana M.D. Oxidative stress by L-buthionine-(S, R)-sulfoximine, a selective inhibitor of glutathione metabolism, abrogates mouse kidney mineralocorticoid receptor function. Biochem. Biophys. Acta. 1495:2002b;263-280
    • (2002) Biochem. Biophys. Acta , vol.1495 , pp. 263-280
    • Piwien-Pilipuk, G.1    Galigniana, M.D.2
  • 45
    • 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 elongation factor 2 in kidney cells
    • Piwien-Pilipuk G., Ayala A., Machado A., Galigniana M.D. 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 elongation factor 2 in kidney cells. J. Biol. Chem. 277:2002c;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
  • 46
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulationg the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt W.B. The role of heat shock proteins in regulationg 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
  • 47
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W.B., Toft D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocrinol. Rev. 18:1997;306-360
    • (1997) Endocrinol. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 49
    • 0027420803 scopus 로고
    • Demonstration of nuclear translocation of the mineralocorticoid receptor (MR) using anti-MR antibody and confocal scanning microscopy
    • Robertson N.M., Schulman G., Karnik S., Alnemri E., Litwack G. Demonstration of nuclear translocation of the mineralocorticoid receptor (MR) using anti-MR antibody and confocal scanning microscopy. Mol. Endocrinol. 7:1993;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
  • 50
    • 0029085868 scopus 로고
    • Glucocorticoid receptor expression is down-regulated by Lp(a) lipoprotein in vascular smooth muscle cells
    • Sato A., Sheppard K.E., Fullerton M.J., Sviridov D.D., Funder J.W. Glucocorticoid receptor expression is down-regulated by Lp(a) lipoprotein in vascular smooth muscle cells. Endocrinology. 136:1995;3707-3713
    • (1995) Endocrinology , vol.136 , pp. 3707-3713
    • Sato, A.1    Sheppard, K.E.2    Fullerton, M.J.3    Sviridov, D.D.4    Funder, J.W.5
  • 51
    • 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., Pratt W.B. Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein. J. Biol. Chem. 274:1999;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
  • 52
    • 0028988075 scopus 로고
    • 11α- and 11β-Hydroxyprogesterone, potent inhibitors of 11β-hydroxysteroid dehydrogenase (isoforms 1 and 2), confer marked mineralocorticoid activity on corticosterone in the ADX rats
    • Souness G., Latif S., Laurenzo J., Morris D.J. 11α- and 11β-Hydroxyprogesterone, potent inhibitors of 11β-hydroxysteroid dehydrogenase (isoforms 1 and 2), confer marked mineralocorticoid activity on corticosterone in the ADX rats. Endocrinology. 136:1995;1809-1812
    • (1995) Endocrinology , vol.136 , pp. 1809-1812
    • Souness, G.1    Latif, S.2    Laurenzo, J.3    Morris, D.J.4
  • 53
    • 0028588118 scopus 로고
    • Heterodimerization between mineralocorticoid and glucocorticoid receptor: A new principle of glucocorticoid action in the CNS
    • Trapp T., Rupprecht R., Castren M., Reul M., Holsboer F. Heterodimerization between mineralocorticoid and glucocorticoid receptor: a new principle of glucocorticoid action in the CNS. Neuron. 13:1994;1457-1462
    • (1994) Neuron , vol.13 , pp. 1457-1462
    • Trapp, T.1    Rupprecht, R.2    Castren, M.3    Reul, M.4    Holsboer, F.5
  • 55
    • 0036352904 scopus 로고    scopus 로고
    • Differences in nuclear retention characteristics of agonist-activated glucocorticoid receptor may determine specific biological responses
    • Vicent G.P., Pecci A., Ghini A.A., Piwien-Pilipuk G., Galigniana M.D. Differences in nuclear retention characteristics of agonist-activated glucocorticoid receptor may determine specific biological responses. Exp. Cell Res. 276:2002;142-154
    • (2002) Exp. Cell Res. , vol.276 , pp. 142-154
    • Vicent, G.P.1    Pecci, A.2    Ghini, A.A.3    Piwien-Pilipuk, G.4    Galigniana, M.D.5
  • 56
    • 0024208510 scopus 로고
    • Quantitative analysis of aldosterone's role in potassium regulation
    • Young D.B. Quantitative analysis of aldosterone's role in potassium regulation. Am. J. Physiol. 255:1988;F811-F822
    • (1988) Am. J. Physiol. , vol.255 , pp. 811-F822
    • Young, D.B.1
  • 57
    • 0028290539 scopus 로고
    • Mineralocorticoids, hypertension, and cardiac fibrosis
    • Young M., Fullerton M., Dilley R., Funder J. Mineralocorticoids, hypertension, and cardiac fibrosis. J. Clin. Invest. 93:1994;2578-2583
    • (1994) J. Clin. Invest. , vol.93 , pp. 2578-2583
    • Young, M.1    Fullerton, M.2    Dilley, R.3    Funder, J.4


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