Zobrazeno 1 - 8
of 8
pro vyhledávání: '"J H, Brubaker"'
Autor:
Remco A. Spanjaard, Masato Ikeda, Akira Sugawara, J H Brubaker, William W. Chin, Paul M. Yen, Elizabeth C. Wilcox
Publikováno v:
Journal of Biological Chemistry. 269:12704-12709
Thyroid hormone receptors bind to thyroid hormone response elements (TREs) as heterodimers with 3,5,3'-L-triiodothyronine (T3) receptor auxiliary protein (TRAP) and retinoid X receptors (RXRs). Currently, it is not known whether TR/TRAP or TR/RXR het
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8eaf0e5883a67003937c397a2a407bcf
https://doi.org/10.1016/s0021-9258(18)99933-3
https://doi.org/10.1016/s0021-9258(18)99933-3
Publikováno v:
Endocrinology. 134:1075-1081
Thyroid hormone receptors (TRs) bind to thyroid hormone response elements (TREs) in the promoter region of target genes as monomers, homodimers, and heterodimers with nuclear proteins such as retinoid-X receptors (RXRs). Recently, we observed that T3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de7dfc0601cf58f59cf82a3422365b2f
https://doi.org/10.1210/endo.134.3.8119145
https://doi.org/10.1210/endo.134.3.8119145
Publikováno v:
Endocrinology. 134:543-548
Using both a protein phosphatase inhibitor, okadaic acid (OA), and a protein kinase inhibitor, H7, to modify phosphorylation events in the cell, we investigated the effects of these agents on transcriptional activation via exogenous rat thyroid hormo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac09e19f3414b1261b7c020db6432b89
https://doi.org/10.1210/endo.134.2.8299553
https://doi.org/10.1210/endo.134.2.8299553
Autor:
R F, Brubaker, J H, Brubaker
Publikováno v:
Archives of ophthalmology (Chicago, Ill. : 1960). 117(5)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::41e3bd029cd2313bfaab3a452b2eb407
https://pubmed.ncbi.nlm.nih.gov/10326980
https://pubmed.ncbi.nlm.nih.gov/10326980
Publikováno v:
Journal of molecular endocrinology. 16(2)
The sequences of the mouse and rat TRH receptors (TRH-Rs) show 94% similarity at the protein level. However, they differ significantly at their carboxy terminals, i.e. the mouse TRH-R ends with an asparagine at position 393 while, in the rat, residue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7bfba11835cfa500ed5074c7b562c11
https://pubmed.ncbi.nlm.nih.gov/9156522
https://pubmed.ncbi.nlm.nih.gov/9156522
Publikováno v:
The Journal of biological chemistry. 269(17)
Thyroid hormone receptors bind to thyroid hormone response elements (TREs) as heterodimers with 3,5,3'-L-triiodothyronine (T3) receptor auxiliary protein (TRAP) and retinoid X receptors (RXRs). Currently, it is not known whether TR/TRAP or TR/RXR het
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::96318973c8c1fc4c29080b58044bda22
https://pubmed.ncbi.nlm.nih.gov/8175681
https://pubmed.ncbi.nlm.nih.gov/8175681
Publikováno v:
The Journal of biological chemistry. 269(2)
v-erbA, a viral oncogenic homolog of thyroid hormone receptor (TR), blocks the effect of T3 in TR-mediated transcription. The mechanism(s) for this dominant negative effect by v-erbA on TRs is unknown but may involve competition between v-erbA and TR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4439682915c709f637c899726f53c976
https://pubmed.ncbi.nlm.nih.gov/7904604
https://pubmed.ncbi.nlm.nih.gov/7904604
Publikováno v:
Scopus-Elsevier
v-erbA, a viral oncogenic homolog of thyroid hormone receptor (TR), blocks the effect of T3 in TR-mediated transcription. The mechanism(s) for this dominant negative effect by v-erbA on TRs is unknown but may involve competition between v-erbA and TR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3913a9658a5ebc1092d84d6b74420aa0
http://www.scopus.com/inward/record.url?eid=2-s2.0-0027972575&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0027972575&partnerID=MN8TOARS
