Proteins associated with untransformed estrogen receptor in vitro. Perturbation of hydrophobic interactions induces alterations in quaternary structure and exposure of the DNA-binding site
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00392a005
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1. Estrogen response element binding induces alterations in estrogen receptor-alpha conformation as revealed by susceptibility to partial proteolysis;Journal of Molecular Endocrinology;2001-12-01
2. Estrogen response element sequence impacts the conformation and transcriptional activity of estrogen receptor α1Supported by NIH R01 DK 53220 and a University of Louisville School of Medicine Research Grant to C.M.K.1;Molecular and Cellular Endocrinology;2001-03
3. A ligand-induced conformational change in the estrogen receptor is localized in the steroid binding domain;Biochemistry;1992-07-16
4. Protein interactions with immobilized transition metal ions: Quantitative evaluations of variations in affinity and binding capacity;Analytical Biochemistry;1990-11
5. Ligand-binding properties of estrogen receptor proteins after interaction with surface-immobilized Zn(II) ions: Evidence for localized surface interactions and minimal conformational changes;Journal of Molecular Recognition;1990-08
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