ArticleJournal of proteome research2025
An Optimized SP3 Sample Processing Workflow for In-Depth and Reproducible Phosphoproteomics.
Article in Journal of proteome research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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.
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Who cites it
1 citing paper in PubMed.
- Are Sulfates of the Hydroxyl Amino Acids Threonine and Serine Truly Extremely Rare or Do They Simply Escape Detection?Life (Basel, Switzerland) · 2026Article
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Authors and funding
7 authors.
Funding
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Abstract
Protein phosphorylation is a ubiquitous post-translational modification (PTM) found across the kingdoms of life and is critical for the regulation of protein function in health and disease. Advances in high-throughput mass spectrometry have transformed our ability to interrogate the phosphoproteome. However, sample preparation methodologies optimized for phosphoproteomics have not kept pace, compromising the ability to fully exploit these technological advances. In this study, we present an optimized phosphoproteomics workflow using carboxylated SP3 magnetic beads, which have simplified proteomics sample preparation. By employing a washing step with 8 M urea and omitting the conventional C
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