Thermodynamic Dissection of Estrogen Receptor–Promoter Interactions Reveals That Steroid Receptors Differentially Partition Their Self-Association and Promoter Binding Energetics-Reference-Cited by-同舟云学术

Thermodynamic Dissection of Estrogen Receptor–Promoter Interactions Reveals That Steroid Receptors Differentially Partition Their Self-Association and Promoter Binding Energetics

Published:2012-01-12 Issue:3 Volume:51 Page:739-749
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Moody Amie D.¹,Miura Michael T.¹,Connaghan Keith D.¹,Bain David L.¹

Affiliation:

1. Department of Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, Colorado 80045, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi2017156

Reference42 articles.

1. MOLECULAR MECHANISMS OF ACTION OF STEROID/THYROID RECEPTOR SUPERFAMILY MEMBERS

2. Differential Gene Regulation by the Two Progesterone Receptor Isoforms in Human Breast Cancer Cells

3. Overlapping but Distinct Gene Regulation Profiles by Glucocorticoids and Progestins in Human Breast Cancer Cells

4. Genome-Wide Dynamics of Chromatin Binding of Estrogen Receptors α and β: Mutual Restriction and Competitive Site Selection

5. Cooperative DNA Binding by the B-Isoform of Human Progesterone Receptor: Thermodynamic Analysis Reveals Strongly Favorable and Unfavorable Contributions to Assembly

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