ArticleMolecular & cellular proteomics : MCP2009
Systematic mapping of posttranslational modifications in human estrogen receptor-alpha with emphasis on novel phosphorylation sites.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed, 71 citations in OpenAlex.
- Site-specific ERα phosphorylation determines sex-dependent metabolic, reproductive, and body-compositional phenotypes in mice.iScience · 2025Article
- Decoding estrogen receptor and GPER biology: structural insights and therapeutic advances in ERα-positive breast cancer.Frontiers in oncology · 2025Review
- Estrogen Receptor Signaling in Breast Cancer.Cancers · 2023Review
- Review
- Decoding the Therapeutic Implications of the ERα Stability and Subcellular Distribution in Breast Cancer.Frontiers in endocrinology · 2022Review
- The Interplay of Sex Steroids, the Immune Response, and the Intestinal Microbiota.Trends in microbiology · 2021Review
- GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer.Science advances · 2021Article
- Ancient Evolutionary Origin of Intrinsically Disordered Cancer Risk Regions.Biomolecules · 2020Article
- Decoding the PTM-switchboard of Notch.Biochimica et biophysica acta. Molecular cell research · 2019Review
- Quantification of Breast Cancer Protein Biomarkers at Different Expression Levels in Human Tumors.Methods in molecular biology (Clifton, N.J.) · 2018Article
- ERpS294 is a biomarker of ligand or mutational ERα activation and a breast cancer target for CDK2 inhibition.Oncotarget · 2017Article
- Quantitative proteomics of breast tumors: Tissue quality assessment to clinical biomarkers.Proteomics · 2017Article
- Estrogens, Neuroinflammation, and Neurodegeneration.Endocrine reviews · 2016Review
- Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α.The Journal of biological chemistry · 2015Article
- A kinetic model identifies phosphorylated estrogen receptor-α (ERα) as a critical regulator of ERα dynamics in breast cancer.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- ERα, SKP2 and E2F-1 form a feed forward loop driving late ERα targets and G1 cell cycle progression.Oncogene · 2014Article
- The functional diversity of protein lysine methylation.Molecular systems biology · 2014Review
- Pin1 modulates ERα levels in breast cancer through inhibition of phosphorylation-dependent ubiquitination and degradation.Oncogene · 2014Article
- pRb controls estrogen receptor alpha protein stability and activity.Oncotarget · 2013Article
- Derailed estrogen signaling and breast cancer: an authentic couple.Endocrine reviews · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
A systematic study of posttranslational modifications of the estrogen receptor isolated from the MCF-7 human breast cancer cell line is reported. Proteolysis with multiple enzymes, mass spectrometry, and tandem mass spectrometry achieved very high sequence coverage for the full-length 66-kDa endogenous protein from estradiol-treated cell cultures. Nine phosphorylated serine residues were identified, three of which were previously unreported and none of which were previously observed by mass spectrometry by any other laboratory. Two additional modified serine residues were identified in recombinant protein, one previously reported but not observed here in endogenous protein and the other previously unknown. Although major emphasis was placed on identifying new phosphorylation sites, N-terminal loss of methionine accompanied by amino acetylation and a lysine side chain acetylation (or possibly trimethylation) were also detected. The use of both HPLC-ESI and MALDI interfaced to different mass analyzers gave higher sequence coverage and identified more sites than could be achieved by either method alone. The estrogen receptor is critical in the development and progression of breast cancer. One previously unreported phosphorylation site identified here was shown to be strongly dependent on estradiol, confirming its potential significance to breast cancer. Greater knowledge of this array of posttranslational modifications of estrogen receptor, particularly phosphorylation, will increase our understanding of the processes that lead to estradiol-induced activation of this protein and may aid the development of therapeutic strategies for management of hormone-dependent breast cancer.
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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.