Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains-Reference-Cited by-同舟云学术

Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains

Published:2018-08-30 Issue:1 Volume:9 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Huang Wei,Peng Yi,Kiselar Janna,Zhao Xuan,Albaqami Aljawharah,Mendez Daniel,Chen Yinghua,Chakravarthy Srinivas,Gupta Sayan,Ralston Corie,Kao Hung-Ying,Chance Mark R.,Yang Sichun^ORCID

Funder

U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences

U.S. Department of Energy

U.S. Department of Health & Human Services | NIH | National Institute of Biomedical Imaging and Bioengineering

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-018-06034-2.pdf

Reference55 articles.

1. Kumar, V. et al. Functional domains of the human estrogen receptor. Cell 51, 941–951 (1987).

2. Deroo, B. J. & Korach, K. S. Estrogen receptors and human disease. J. Clin. Invest. 116, 561–570 (2006).

3. Kumar, V. & Chambon, P. The estrogen-receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell 55, 145–156 (1988).

4. Dahlman-Wright, K. et al. International union of pharmacology. LXIV. Estrogen receptors. Pharmacol. Rev. 58, 773–781 (2006).

5. Chandra, V. et al. Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. Nature 456, 350–356 (2008).

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