Identification of the Porcine Intestinal Accessory Factor that Enables DNA Sequence Recognition by Vitamin D Receptor

The nuclear accessory protein in porcine intestinal nuclear extracts that activates the binding of the vitamin D receptor to its vitamin D response elements has been highly purified. It contains a protein that binds 9-cis-[3H]retinoic acid, was detected on immunoblots with an anti-retinoid X recepto...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1995-03, Vol.92 (7), p.2795-2799
Hauptverfasser:	Munder, Michael, Herzberg, Ian M., Zierold, Claudia, Moss, Valerie E., Hanson, Kris, Clagett-Dame, Margaret, DeLuca, Hector F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antibodies Base Sequence Biochemistry Cell Nucleus - metabolism Chromatography Chromatography, Affinity Cytochrome P-450 Enzyme System DNA - chemistry DNA - metabolism DNA-Binding Proteins - metabolism Gels Hogs Intestinal Mucosa - metabolism Intestines Mice Molecular Sequence Data Nuclear Proteins - isolation & purification Nuclear Proteins - metabolism Oligodeoxyribonucleotides Osteocalcin - genetics Osteocalcin - metabolism Proteins Rats Reading Frames Receptors Receptors, Calcitriol - metabolism Receptors, Retinoic Acid - immunology Receptors, Retinoic Acid - metabolism Resins Response elements Retinoic Acid Receptor gamma Retinoid X Receptors Steroid Hydroxylases - genetics Swine Transcription Factors - immunology Tretinoin - metabolism Vitamin D Vitamin D3 24-Hydroxylase
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