Surface Mapping of the Ligand‐Filled C‐Terminal Half of the Porcine Estradiol Receptor by Restricted Proteolysis
- 1 July 1995
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 231 (2) , 510-516
- https://doi.org/10.1111/j.1432-1033.1995.0510e.x
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- The Ligand-Binding Site of the Estradiol-Receptor Resides in a Noncovalent Complex of Two Consecutive Peptides of 17 and 7 kDaBiochemical and Biophysical Research Communications, 1994
- Detection of Zn-Binding in Domain E of the Porcine Estradiol ReceptorBiochemical and Biophysical Research Communications, 1993
- Structure of the hormone binding domain of human .beta.1 thyroid hormone nuclear receptor: Is it an .alpha./.beta. barrel?Biochemistry, 1993
- Assignment of the ligand binding site of the porcine estradiol receptor to the N‐terminal 17 kDa part of domain EFEBS Letters, 1993
- Microsequence analysis of winged bean seed proteins electroblotted from two-dimensional gelProtein Journal, 1989
- The steroid binding domain of porcine estrogen receptorBiochemistry, 1987
- Purification of the Steroid-Binding Core of Porcine Estrogen ReceptorHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1983
- Prediction of protein antigenic determinants from amino acid sequences.Proceedings of the National Academy of Sciences, 1981
- Conformation of amino acid side-chains in proteinsJournal of Molecular Biology, 1978
- THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONSAnnals of the New York Academy of Sciences, 1949