pubmed-article:8612804 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8612804 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:8612804 | lifeskim:mentions | umls-concept:C0066563 | lld:lifeskim |
pubmed-article:8612804 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
pubmed-article:8612804 | lifeskim:mentions | umls-concept:C0026160 | lld:lifeskim |
pubmed-article:8612804 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:8612804 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
pubmed-article:8612804 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:8612804 | pubmed:dateCreated | 1996-6-4 | lld:pubmed |
pubmed-article:8612804 | pubmed:abstractText | The human mineralocorticoid receptor of the steroid receptor family contains a modular structure with domain E which is considered to be a hormone binding domain. Recombinant protein approaches enabled us to clearly determine that this domain is also able to interact with F-actin (Kd about 2 microM) and G-actin. Moreover, it was revealed that this mineralocorticoid receptor domain/actin interaction was modulated by specific mineralocorticoid ligands. Agonist (aldosterone) steroid binding almost totally (91%) abolished the interaction with F-actin, while antagonist (progesterone) binding allowed more than 30% of this binding. Steroid modulation of the interaction between domain E and actin indicated that this actin binding is specific and could be essential for cellular mineralocorticoid receptor activity. | lld:pubmed |
pubmed-article:8612804 | pubmed:language | eng | lld:pubmed |
pubmed-article:8612804 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8612804 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8612804 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8612804 | pubmed:month | Apr | lld:pubmed |
pubmed-article:8612804 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:8612804 | pubmed:author | pubmed-author:MornetDD | lld:pubmed |
pubmed-article:8612804 | pubmed:author | pubmed-author:LégerJ JJJ | lld:pubmed |
pubmed-article:8612804 | pubmed:author | pubmed-author:MesnierDD | lld:pubmed |
pubmed-article:8612804 | pubmed:author | pubmed-author:AuzouGG | lld:pubmed |
pubmed-article:8612804 | pubmed:author | pubmed-author:JalaguierSS | lld:pubmed |
pubmed-article:8612804 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8612804 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8612804 | pubmed:volume | 384 | lld:pubmed |
pubmed-article:8612804 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8612804 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8612804 | pubmed:pagination | 112-6 | lld:pubmed |
pubmed-article:8612804 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:8612804 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8612804 | pubmed:articleTitle | Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation. | lld:pubmed |
pubmed-article:8612804 | pubmed:affiliation | Institut National de la Santé et de la Recherche Médicale, Unité 300, Faculté de Pharmacie, Montpellier, France. | lld:pubmed |
pubmed-article:8612804 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8612804 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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