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ProteomicsIdentification of Cytosolic Protein Targets of Catechol Estrogens in Breast Cancer Cells Using a Click Chemistry-based Workflow
Catechol estrogens (CEs) are known to be toxic metabolites and the initiators in the oncogenesis of breast cancers via forming covalent adducts with DNAs. CEs shall also react with proteins but their cellular protein targets remain un-explored. Here we reported the identification of protein targets ...
ORGANISM(S): Homo sapiens (Human) 
2020-09-28 | PXD017731 | Pride
Affinity purification Catechol estrogens Breast cancer cells Mass spectrometry Proteomic 
ProteomicsIn-situ Click Reaction Coupled with Quantitative Proteomics for Identification of Protein Targets of Catechol Estrogens
Catechol estrogens (CEs) are metabolic electrophiles that actively undergo covalent interaction with cellular proteins, influencing molecular function. There is no feasible method to identify their binders in a living system. Herein, we developed a click chemistry-based approach using ethinylestradi...
ORGANISM(S): Rattus norvegicus (Rat) 
2022-02-28 | PXD009657 | Pride
Post translational modification Metabolites Proteomics Electrophiles Dimethyl labeling Lc/ms Catechol estrogens Oxidative stress Click chemistry Redox modification 
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Not available
S-EPMC9177730 | biostudies-literature
UnknownAssociation Between Telomere Length and Risk of Cancer and Non-Neoplastic Diseases: A Mendelian Randomization Study.
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S-EPMC5638008 | biostudies-literature
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S-EPMC5798588 | biostudies-literature
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S-EPMC9793579 | biostudies-literature
UnknownA multi-layer functional genomic analysis to understand noncoding genetic variation in lipids.
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S-EPMC9388392 | biostudies-literature
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S-EPMC5808456 | biostudies-literature
UnknownThe power of genetic diversity in genome-wide association studies of lipids.
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S-EPMC8730582 | biostudies-literature
UnknownPolygenic prediction of body mass index and obesity through the life course and across ancestries.
Not available
S-EPMC12443623 | biostudies-literature
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