Zobrazeno 1 - 7
of 7
pro vyhledávání: '"F C, Dalman"'
Publikováno v:
The Journal of biological chemistry. 266(6)
In this work, we used two approaches to localize the 90-kDa heat shock protein (hsp90)-binding site within the hormone-binding domain of the glucocorticoid receptor. In the first approach, derivatives of the glucocorticoid receptor deleted for increa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0388b8f4d2098a17d1158b3e0c178bd5
https://pubmed.ncbi.nlm.nih.gov/1995612
https://pubmed.ncbi.nlm.nih.gov/1995612
Publikováno v:
The Journal of biological chemistry. 265(35)
Untransformed steroid receptors in cytosol preparations are associated with the 90-kDa heat shock protein hsp90, but the study of how hsp90 affects receptor function has been held back by the inability to reassociate steroid receptors with hsp90 in c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::149b1d60c4b731a312eaf641287e8ba5
https://pubmed.ncbi.nlm.nih.gov/2254299
https://pubmed.ncbi.nlm.nih.gov/2254299
Publikováno v:
The Journal of biological chemistry. 265(7)
We have recently reported that the glucocorticoid receptor (GR) becomes bound to the 90-kDa heat shock protein (hsp90) at or near the end of receptor translation in vitro (Dalman, F. C., Bresnick, E. H., Patel, P. D., Perdew, G. H., Watson, S. J., Jr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ef230924fdbc304bdf6503458d934e51
https://pubmed.ncbi.nlm.nih.gov/2303466
https://pubmed.ncbi.nlm.nih.gov/2303466
Autor:
W B, Pratt, E R, Sanchez, E H, Bresnick, S, Meshinchi, L C, Scherrer, F C, Dalman, M J, Welsh
Publikováno v:
Cancer research. 49
Reports from several laboratories support a model for glucocorticoid receptor (GR) transformation in cytosol in which a heteromeric 9S complex of GR and the Mr 90,000 heat shock protein undergo a temperature-dependent and hormone-promoted dissociatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ec62b4e9e3efcb09827354dc14f6dca9
https://pubmed.ncbi.nlm.nih.gov/2649237
https://pubmed.ncbi.nlm.nih.gov/2649237
Publikováno v:
The Journal of biological chemistry. 264(9)
Using L cell glucocorticoid receptors that have been immunopurified by adsorption to protein A Sepharose with a monoclonal antireceptor antibody, we have developed an assay to study the requirements for maintenance of steroid-binding capacity. After
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::936c37375a4413bea255733549d6c8aa
https://pubmed.ncbi.nlm.nih.gov/2647745
https://pubmed.ncbi.nlm.nih.gov/2647745
Publikováno v:
The Journal of biological chemistry. 263(25)
Digestion of the rat liver glucocorticoid receptor with chymotrypsin results in the generation of a 42-kDa fragment which contains the steroid-binding and DNA-binding domains and the antigenic site for the BuGR anti-glucocorticoid receptor monoclonal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2ac187f19009ee1fcf46556b88049c35
https://pubmed.ncbi.nlm.nih.gov/3045115
https://pubmed.ncbi.nlm.nih.gov/3045115
Publikováno v:
The Journal of biological chemistry. 264(33)
We have translated the rat glucocorticoid receptor in both reticulocyte lysate and in wheat germ extract. Receptor synthesized in the reticulocyte lysate is immunoadsorbed by the 8D3 monoclonal antibody directed against the 90-kDa heat shock protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b2a7f03440216ba4f43308d92d7b0e2c
https://pubmed.ncbi.nlm.nih.gov/2584195
https://pubmed.ncbi.nlm.nih.gov/2584195