| pubmed-article:2734982 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2734982 | lifeskim:mentions | umls-concept:C0034786 | lld:lifeskim |
| pubmed-article:2734982 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:2734982 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2734982 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2734982 | pubmed:dateCreated | 1989-7-18 | lld:pubmed |
| pubmed-article:2734982 | pubmed:abstractText | The androgen receptor in several species (human, rat, calf) is a monomeric protein with a molecular mass of 100-110 kDa. The steroid binding domain is confined to a region of 30 kDa, while the DNA-binding domain has the size of approx. 10 kDa. A 40 kDa fragment containing both the DNA and steroid binding domain displayed a higher DNA binding activity than did the intact 100 kDa molecule. cDNA encoding the major part of the human androgen receptor was isolated. The cDNA contains an open reading frame of 2,277 bp but still lacks part of the 5'-coding sequence. Homology with the progesterone and glucocorticoid receptor was about 80% in the DNA binding domain and 50% in the steroid binding domain. The present data provide evidence that the androgen receptor belongs to the superfamily of ligand responsive transcriptional regulators and consists of three distinct domains each with a specialized function. | lld:pubmed |
| pubmed-article:2734982 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2734982 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2734982 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2734982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2734982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2734982 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2734982 | pubmed:issn | 0300-5623 | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:BoltJJ | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:de BoerWW | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:BrinkmannA... | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:Geurts van... | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:SmitAA | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:FaberP WPW | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:van der... | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:KuiperG GGG | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:van RooijH... | lld:pubmed |
| pubmed-article:2734982 | pubmed:author | pubmed-author:KlaasenPP | lld:pubmed |
| pubmed-article:2734982 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2734982 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:2734982 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2734982 | pubmed:authorsComplete | N | lld:pubmed |
| pubmed-article:2734982 | pubmed:pagination | 87-93 | lld:pubmed |
| pubmed-article:2734982 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:meshHeading | pubmed-meshheading:2734982-... | lld:pubmed |
| pubmed-article:2734982 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2734982 | pubmed:articleTitle | Structure and function of the androgen receptor. | lld:pubmed |
| pubmed-article:2734982 | pubmed:affiliation | Department of Biochemistry II, Erasmus University, Rotterdam, The Netherlands. | lld:pubmed |
| pubmed-article:2734982 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2734982 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2734982 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2734982 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2734982 | lld:pubmed |
