ArticleMetallomics : integrated biometal science2023
Analysis of copper-induced protein precipitation across the E. coli proteome.
Article in Metallomics : integrated biometal science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- A cysteine-rich domain of themBio · 2026Article
- The Two Faces of Copper Capture Driven by the Internal His/Met-Rich and N-Terminal His-Rich Domains of CopI.Inorganic chemistry · 2026Article
- Data-Independent Acquisition (DIA) Strategy for Measuring Protein Stability Using Stability of Proteins from Rates of Oxidation (SPROX).Journal of the American Society for Mass Spectrometry · 2026Article
- Copper ionophore elicits calpain-dependent paraptosis coincident with proteotoxic stress.Cell communication and signaling : CCS · 2025Article
- Copper Activates a Redox Switch to Reversibly Inhibit Glyceraldehyde-3-Phosphate Dehydrogenase.Biochemistry · 2025Article
- Extrinsic and intrinsic factors affect copper-induced protein precipitation across eukaryotic and prokaryotic proteomes.Protein science : a publication of the Protein Society · 2025Article
- Copper homeostasis and pregnancy complications: a comprehensive review.Journal of assisted reproduction and genetics · 2025Review
- Protein Precipitation by Metal Hydroxides as a Convenient and Alternative Sample Preparation Procedure for Bioanalysis.Molecules (Basel, Switzerland) · 2024Article
- Proteomic strategies to interrogate the Fe-S proteome.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Liquid-Liquid Phase Separation-Mediated Photocatalytic Subcellular Hybrid System for Highly Efficient Hydrogen Production.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Glycyl-l-histidyl-l-lysine prevents copper- and zinc-induced protein aggregation and central nervous system cell death in vitro.Metallomics : integrated biometal science · 2024Article
- Revisiting the pro-oxidant activity of copper: interplay of ascorbate, cysteine, and glutathione.Metallomics : integrated biometal science · 2023Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Metal cations have been exploited for their precipitation properties in a wide variety of studies, ranging from differentiating proteins from serum and blood to identifying the protein targets of drugs. Despite widespread recognition of this phenomenon, the mechanisms of metal-induced protein aggregation have not been fully elucidated. Recent studies have suggested that copper's (Cu) ability to induce protein aggregation may be a main contributor to Cu-induced cell death. Here, we provide the first proteome-wide analysis of the relative sensitivities of proteins across the Escherichia coli proteome to Cu-induced aggregation. We utilize a metal-induced protein precipitation (MiPP) methodology that relies on quantitative bottom-up proteomics to define the metal concentration-dependent precipitation properties of proteins on a proteomic scale. Our results establish that Cu far surpasses other metals in promoting protein aggregation and that the protein aggregation is reversible upon metal chelation. The bulk of the Cu bound in the protein aggregates is Cu1+, regardless of the Cu2+ source. Analysis of our MiPP data allows us to investigate underlying biophysical characteristics that determine a protein's sensitivity to Cu-induced aggregation, which is independent of the relative concentration of protein in the lysate. Overall, this analysis provides new insights into the mechanism behind Cu cytotoxicity, as well as metal cation-induced protein aggregation.
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