ArticleMolecular & cellular proteomics : MCP2010
Proteomics analysis of the estrogen receptor alpha receptosome.
Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Ferguson analysis of protein electromigration during single-cell electrophoresis in an open microfluidic device.The Analyst · 2020Article
- Differential recruitment of co-regulatory proteins to the human estrogen receptor 1 in response to xenoestrogens.Comparative biochemistry and physiology. Part D, Genomics & proteomics · 2016Article
- A meta-analysis to evaluate the cellular processes regulated by the interactome of endogenous and over-expressed estrogen receptor alpha.Oncoscience · 2015Article
- Identification of estrogen receptor proteins in breast cancer cells using matrix-assisted laser desorption/ionization time of flight mass spectrometry (Review).Oncology letters · 2014Article
- Age-dependent Effects of 17β-estradiol on the dynamics of estrogen receptor β (ERβ) protein-protein interactions in the ventral hippocampus.Molecular & cellular proteomics : MCP · 2014Article
- Proteomic analysis of coregulators bound to ERα on DNA and nucleosomes reveals coregulator dynamics.Molecular cell · 2013Article
- In-depth proteomic characterization of endogenous nuclear receptors in mouse liver.Molecular & cellular proteomics : MCP · 2013Article
- Estrogen signaling and the aging brain: context-dependent considerations for postmenopausal hormone therapy.ISRN endocrinology · 2013Article
- Estrogen receptor alpha interacts with mitochondrial protein HADHB and affects beta-oxidation activity.Molecular & cellular proteomics : MCP · 2012Article
- The Effects of 17β-estradiol in Cancer are Mediated by Estrogen Receptor Signaling at the Plasma Membrane.Frontiers in physiology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The estrogen receptors (ERs) are ligand-dependent transcription factors that activate transcription by binding to estrogen response elements. Estrogen-mediated effects are tissue- and cell type-specific, determined by the cofactor recruitment to the ERs among other factors. To understand these differences in estrogen action, it is important to identify the various compositions of the ER complexes (ER receptosomes). In this report, we describe a fast and efficient method for the isolation of the ERalpha receptosome for proteomics analysis. Using immobilized estrogen response element on a Sepharose column in combination with two-dimensional electrophoresis and MALDI-TOF MS, significant amounts of proteins could be isolated and identified. Differences in ERalpha complex composition with the ER ligands 17beta-estradiol, 4-hydroxytamoxifen, and ICI-182,780 could also be observed. Thus, this approach provides an easy and relevant way of identifying ERalpha cofactor and transcription factor recruitment under different conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.