Linked Life Data

3371551

Source:http://linkedlifedata.com/resource/pubmed/id/3371551

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-7-1
pubmed:abstractText
Glucocorticoid receptors of several rodent and human cell lines were subjected to mild proteolysis with several proteases. A hormone binding fragment of Mr approximately 40,000 was generated which had increased affinity for DNA as revealed by DNA-cellulose chromatography. It behaved similar to the truncated nti ('increased nuclear transfer') receptor of mutant mouse lymphoma cells. These data led to the view that wild-type receptors of Mr approximately 94,000 contain in addition to the functional domains for hormone binding and interaction with DNA a third domain ('modulation domain') which is essential for biological activity. Monoclonal antibodies against wild-type receptors were used in DNA binding experiments and increased affinity for DNA was observed. The data suggest that reacting the receptor with antibody leads to functional elimination of the modulation domain as if it were cleaved off by mild proteolysis. Antibody treatment neither caused nor inhibited receptor activation to a DNA binding form.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Modulation of DNA binding of glucocorticoid receptors.
pubmed:affiliation
Institut für Biologische Chemie, Universität Heidelberg, F.R.G.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't