Source:http://linkedlifedata.com/resource/pubmed/id/12088282
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2002-6-28
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pubmed:abstractText |
This review aims to evaluate the impact that human estrogen receptor-alpha (ER-alpha) synthesis, modification and degradation has on estrogen-dependant physiological and pathological processes within the body. Estrogen signaling is transduced through estrogen receptors, which act as ligand-inducible transcription factors. The significance of different isoforms of ER-alpha that lack structural features of full-length ER-alpha are discussed. The influence of differential promoter usage on the amount and isoform of ER-alpha within individual cell types is also reviewed. Moreover, the potential role of phosphorylation, ubiquitination and acetylation in the function and dynamic turnover of ER-alpha is presented.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1420-682X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
821-31
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading |
pubmed-meshheading:12088282-Acetylation,
pubmed-meshheading:12088282-Estrogen Receptor alpha,
pubmed-meshheading:12088282-Exons,
pubmed-meshheading:12088282-Gene Expression Regulation,
pubmed-meshheading:12088282-Humans,
pubmed-meshheading:12088282-Models, Biological,
pubmed-meshheading:12088282-Phosphorylation,
pubmed-meshheading:12088282-Protein Isoforms,
pubmed-meshheading:12088282-Receptors, Estrogen
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pubmed:year |
2002
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pubmed:articleTitle |
Human estrogen receptor-alpha: regulation by synthesis, modification and degradation.
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pubmed:affiliation |
European Molecular Biology Laboratory, EMBL, Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Review
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