ArticleJournal of proteome research2021
Reversible Click Chemistry Tag for Universal Proteome Sample Preparation for Top-Down and Bottom-Up Analysis.
Article in Journal of proteome research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Development of an immobilized system for RNA modification analysis.Molecular omics · 2026Article
- Attachment of 2-Pyridyltetrazine Affinity Bioorthogonal Chemistry (ABC) Tags to Proteins for Site-Selective Bioorthogonal Chemistry.Methods in molecular biology (Clifton, N.J.) · 2026Article
- IP-to-MS: An Unbiased Workflow for Antigen Profiling.Journal of proteome research · 2025Article
- Influence of Aldehyde Dehydrogenase Inhibition on Stemness of Endometrial Cancer Stem Cells.Cancers · 2024Article
- One-pot method for preparing DNA, RNA, and protein for multiomics analysis.Communications biology · 2024Article
- Thiomethyltetrazines Are Reversible Covalent Cysteine Warheads Whose Dynamic Behavior can be "Switched Off"Journal of the American Chemical Society · 2023Article
- Expanding Glycomic Investigations through Thiol-Derivatized Glycans.Molecules (Basel, Switzerland) · 2023Article
- Affinity Bioorthogonal Chemistry (ABC) Tags for Site-Selective Conjugation, On-Resin Protein-Protein Coupling, and Purification of Protein Conjugates.Angewandte Chemie (International ed. in English) · 2022Article
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Authors and funding
6 authors.
Funding
Abstract
Successful proteome analysis requires reliable sample preparation beginning with protein solubilization and ending with a sample free of contaminants, ready for downstream analysis. Most proteome sample preparation technologies utilize precipitation or filter-based separation, both of which have significant disadvantages. None of the current technologies are able to prepare both intact proteins or digested peptides. Here, we introduce a reversible protein tag, ProMTag, that enables whole proteome capture, cleanup, and release of intact proteins for top-down analysis. Alternatively, the addition of a novel Trypsin derivative to the workflow generates peptides for bottom-up analysis. We show that the ProMTag workflow yields >90% for intact proteins and >85% for proteome digests. For top-down analysis, ProMTag cleanup improves resolution on 2D gels; for bottom-up exploration, this methodology produced reproducible mass spectrometry results, demonstrating that the ProMTag method is a truly universal approach that produces high-quality proteome samples compatible with multiple downstream analytical techniques. Data are available via ProteomeXchange with identifier PXD027799.
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