title: Structure and specific DNA binding of the rat liver glucocorticoid receptor.
abstract: During recent years major advances have been made in our understanding of glucocorticoid mechanism of action. This progress has been made possible by access to purified glucocorticoid receptor in significant amounts as well as by application of hybrid DNA technology within the field of glucocorticoid control of gene expression. Especially the mammary tumour virus genome has turned out to be a convenient experimental system suitable for such investigations. This paper summarizes some of the work carried out in our own laboratory, partially in collaboration with Dr Keith Yamamoto and his associates at the Department of Biochemistry and Biophysics, University of California, San Francisco, U.S.A.
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D002918:Chymotrypsin / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D005786:Gene Expression Regulation / Q000187:drug effects; D005938:Glucocorticoids / Q000494:pharmacology; D008099:Liver / Q000378:metabolism*; D008223:Lymphoma / Q000378:metabolism; D008324:Mammary Tumor Virus, Mouse / Q000235:genetics; D051379:Mice; D011817:Rabbits; D051381:Rats; D011965:Receptors, Glucocorticoid / Q000276:immunology / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
chemical_list: D000911:Antibodies, Monoclonal; D005938:Glucocorticoids; D011965:Receptors, Glucocorticoid; D011987:Receptors, Steroid; D004247:DNA; D002918:Chymotrypsin; D014357:Trypsin