Molecular mechanism of activation and nuclear translocation of the mineralocorticoid receptor upon binding of pregnanesteroids
The mineralocorticoid receptor (MR) is primarily localized in the cytoplasm of the cell in the absence of ligand. The first step in the genomic-dependent mechanism of action of mineralocorticoids is the binding of steroid to the MR, which in turn triggers MR nuclear translocation. The regulation of...
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2004
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| LEADER | 18094caa a22017177a 4500 | ||
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| 001 | PAPER-4631 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203412.0 | ||
| 008 | 190411s2004 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-2342586714 | |
| 024 | 7 | |2 cas |a 11beta hydroxyprogesterone, 600-57-7; 5alpha pregnane 3,20 dione, 566-65-4; 5beta dihydroprogesterone, 128-23-4; aldosterone, 52-39-1, 6251-69-0; deoxycorticosterone, 64-85-7; pregn 4 ene 3,11,20 trione, 516-15-4; Pregnenediones; Receptors, Mineralocorticoid; Transcription Factors | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a MCEND | ||
| 100 | 1 | |a Galigniana, M.D. | |
| 245 | 1 | 0 | |a Molecular mechanism of activation and nuclear translocation of the mineralocorticoid receptor upon binding of pregnanesteroids |
| 260 | |c 2004 | ||
| 270 | 1 | 0 | |m Galigniana, M.D.; Depto. de Quím. Biol., Fac. de Ciencias Exactas Y Naturales, Consejo Nac. de Invest., Cie. Y Tec., Buenos Aires, Argentina; email: mgali@umich.edu |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a The mineralocorticoid receptor (MR) is primarily localized in the cytoplasm of the cell in the absence of ligand. The first step in the genomic-dependent mechanism of action of mineralocorticoids is the binding of steroid to the MR, which in turn triggers MR nuclear translocation. The regulation of hormone-binding to MR is complex and involves a multifactorial mechanism, making it difficult to determine the optimal structure of a steroid for activating the MR and promoting its nuclear translocation. Here we review the structure-activity relationship for several pregnanesteroids that possess various functional groups, and suggest that a flat conformation of the ligand rather than the presence of particular chemical groups is a critical parameter for the final biological effect in vivo. We also discuss how the MR undergoes differential conformational changes according to the nature of the bound ligand, which in turn affects the dynein-dependent retrograde rate of movement for the steroid/receptor complex. © 2003 Elsevier Ireland Ltd. All rights reserved. |l eng | |
| 593 | |a Depto. de Quím. Biol., Fac. de Ciencias Exactas Y Naturales, Consejo Nac. de Invest., Cie. Y Tec., Buenos Aires, Argentina | ||
| 593 | |a Department of Pharmacology, Univ. of Michigan Medical School, 1301 Med. Sci. Research Building III, Ann Arbor, MI 48109-0632, United States | ||
| 593 | |a Depto. de Quím. Orgán., Fac. de Ciencias Exactas Y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a 11,19-OXIDOPROGESTERONE |
| 690 | 1 | 0 | |a ALDOSTERONE |
| 690 | 1 | 0 | |a DYNEIN |
| 690 | 1 | 0 | |a IMMUNOPHILINS |
| 690 | 1 | 0 | |a NATRIURESIS |
| 690 | 1 | 0 | |a TRAFFICKING |
| 690 | 1 | 0 | |a 11,19 OXIDOPROGESTERONE |
| 690 | 1 | 0 | |a 11BETA HYDROXYPROGESTERONE |
| 690 | 1 | 0 | |a 5ALPHA PREGNANE 3,20 DIONE |
| 690 | 1 | 0 | |a 5BETA DIHYDROPROGESTERONE |
| 690 | 1 | 0 | |a 6,19 OXIDOPROGESTERONE |
| 690 | 1 | 0 | |a ALDOSTERONE |
| 690 | 1 | 0 | |a DEOXYCORTICOSTERONE |
| 690 | 1 | 0 | |a DYNEIN ADENOSINE TRIPHOSPHATASE |
| 690 | 1 | 0 | |a LIGAND |
| 690 | 1 | 0 | |a MINERALOCORTICOID |
| 690 | 1 | 0 | |a MINERALOCORTICOID RECEPTOR |
| 690 | 1 | 0 | |a PREGN 4 ENE 3,11,20 TRIONE |
| 690 | 1 | 0 | |a PREGNANE DERIVATIVE |
| 690 | 1 | 0 | |a PROGESTERONE DERIVATIVE |
| 690 | 1 | 0 | |a STEROID |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a BINDING AFFINITY |
| 690 | 1 | 0 | |a CELL NUCLEUS |
| 690 | 1 | 0 | |a COMPLEX FORMATION |
| 690 | 1 | 0 | |a CONFERENCE PAPER |
| 690 | 1 | 0 | |a CONFORMATION |
| 690 | 1 | 0 | |a CYTOPLASM |
| 690 | 1 | 0 | |a DOSE RESPONSE |
| 690 | 1 | 0 | |a DRUG EFFECT |
| 690 | 1 | 0 | |a DRUG HALF LIFE |
| 690 | 1 | 0 | |a DRUG STRUCTURE |
| 690 | 1 | 0 | |a IN VIVO STUDY |
| 690 | 1 | 0 | |a LIGAND BINDING |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS |
| 690 | 1 | 0 | |a MOLECULAR INTERACTION |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN FUNCTION |
| 690 | 1 | 0 | |a STRUCTURE ACTIVITY RELATION |
| 690 | 1 | 0 | |a ACTIVE TRANSPORT, CELL NUCLEUS |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a CELL NUCLEUS |
| 690 | 1 | 0 | |a CYTOPLASM |
| 690 | 1 | 0 | |a GENE EXPRESSION REGULATION |
| 690 | 1 | 0 | |a HUMANS |
| 690 | 1 | 0 | |a PREGNENEDIONES |
| 690 | 1 | 0 | |a PROTEIN BINDING |
| 690 | 1 | 0 | |a PROTEIN CONFORMATION |
| 690 | 1 | 0 | |a RATS |
| 690 | 1 | 0 | |a RECEPTORS, MINERALOCORTICOID |
| 690 | 1 | 0 | |a SIGNAL TRANSDUCTION |
| 690 | 1 | 0 | |a STRUCTURE-ACTIVITY RELATIONSHIP |
| 690 | 1 | 0 | |a TRANSCRIPTION FACTORS |
| 700 | 1 | |a Pilipuk, G.P. | |
| 700 | 1 | |a Kanelakis, K.C. | |
| 700 | 1 | |a Burton, G. | |
| 700 | 1 | |a Lantos, C.P. | |
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