Monitoring ligand-mediated helix 12 transitions within the human estrogen receptor α using bipartite tetracysteine display-Reference-Cited by-同舟云学术

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Monitoring ligand-mediated helix 12 transitions within the human estrogen receptor α using bipartite tetracysteine display

Published:2020 Issue:31 Volume:18 Page:6063-6071
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Pokhrel Ranju¹²³⁴,Tang Tang¹²³⁴,Holub Justin M.¹²³⁴⁵^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry

2. Ohio University

3. Athens

4. USA

5. Molecular and Cellular Biology Program

Abstract

Fluorescent labeling coupled with bipartite tetracysteine display enables the surveillance of ligand-mediated helix 12 transitions within the estrogen receptor α ligand-binding domain.

Funder

Chemistry and Biochemistry Department, Ohio University

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/OB/D0OB01234C

Reference42 articles.

1. Mechanisms of Estrogen Receptor Signaling: Convergence of Genomic and Nongenomic Actions on Target Genes

2. Hormone Action in the Mammary Gland

3. Estrogen receptors and human disease

4. Molecular mechanism of estrogen-estrogen receptor signaling

5. Activation of Nuclear Receptors

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1. Mechanistic evidence from classical molecular dynamics and metadynamics revealed the mechanism of resistance to 4-hydroxy tamoxifen in estrogen receptor alpha Y537S mutant;Molecular Simulation;2022-07-12

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