rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
1998-3-16
|
pubmed:databankReference |
|
pubmed:abstractText |
Human estrogen receptor beta (hER beta) cDNA that encodes the full-length amino acid sequence has been isolated from testis poly(A)+ RNA with the combination of cDNA screening and reverse transcription-PCR. It is composed of a 1590-bp open reading frame and a segment of the 5'- and 3'-untranslated region (UTR) and encodes an additional 53 amino acids in the N-terminal region compared with the previously reported one. Protein interaction between ER alpha and ER beta was demonstrated in vitro by GST pull-down assay and in vivo by immunoprecipitation. Thus, this study indicates that ER alpha and ER beta can interact in vivo, cross-signaling each other.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0006-291X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
4
|
pubmed:volume |
243
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
122-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9473491-Amino Acid Sequence,
pubmed-meshheading:9473491-Animals,
pubmed-meshheading:9473491-Base Sequence,
pubmed-meshheading:9473491-COS Cells,
pubmed-meshheading:9473491-Cloning, Molecular,
pubmed-meshheading:9473491-DNA, Complementary,
pubmed-meshheading:9473491-Dimerization,
pubmed-meshheading:9473491-Estrogen Receptor alpha,
pubmed-meshheading:9473491-Estrogen Receptor beta,
pubmed-meshheading:9473491-Humans,
pubmed-meshheading:9473491-Male,
pubmed-meshheading:9473491-Molecular Sequence Data,
pubmed-meshheading:9473491-Open Reading Frames,
pubmed-meshheading:9473491-RNA, Messenger,
pubmed-meshheading:9473491-Receptors, Estrogen,
pubmed-meshheading:9473491-Recombinant Fusion Proteins,
pubmed-meshheading:9473491-Testis
|
pubmed:year |
1998
|
pubmed:articleTitle |
The complete primary structure of human estrogen receptor beta (hER beta) and its heterodimerization with ER alpha in vivo and in vitro.
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pubmed:affiliation |
Department of Biochemistry, Saitama Medical School, Japan.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|