Identification of the Subdomain in the Nuclear Receptor for the Hormonal Form of Vitamin D3, 1α,25-Dihydroxyvitamin D3, Vitamin D Receptor, That Is Covalently Modified by an Affinity Labeling Reagent
Open Access
- 1 December 1997
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 348 (1) , 91-95
- https://doi.org/10.1006/abbi.1997.0389
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Differential Interaction of α,25-Dihydroxyvitamin D3 Analogues and Their 20-epi Homologues with the Vitamin D ReceptorPublished by Elsevier ,1997
- Aminopropylation of vitamin D hormone (1α,25-dihydroxyvitamin D3), its biological precursors, and other steroidal alcohols: An anchoring moiety for affinity studies of sterolsSteroids, 1995
- Purified Human Vitamin D Receptor Overexpressed in Escherichia coli and Baculovirus Systems Does Not Bind 1,25-Dihydroxyvitamin D3 Hormone Efficiently Unless Supplemented with a Rat Liver Nuclear ExtractBiochemical and Biophysical Research Communications, 1993
- Photoaffinity labeling of chick intestinal 1α,25-dihydroxyvitamin D3 receptorSteroids, 1993
- The expression of milligram amounts of functional human 1,25-dihydroxyvitamin D3 receptor in a bacterial expression systemBiochemical and Biophysical Research Communications, 1992
- Photoaffinity labeling of human serum vitamin D binding protein and chemical cleavages of the labeled protein: identification of an 11.5-KDa peptide containing the putative 25-hydroxyvitamin D3 binding siteBiochemistry, 1991
- A novel approach for the evaluation and treatment of psoriasis: Oral or topical use of 1,25-dihydroxyvitamin D3 can be a safe and effective therapy for psoriasisJournal of the American Academy of Dermatology, 1988
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- The synthesis of a radiolabeled photoaffinity analog of 1,25-dihyroxyvitamin D3Steroids, 1988
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970