ArticleThe journal of physical chemistry. B2026
Decoding the Post-translational Modification Crosstalk: Functional Implications of Phosphorylation, Acetylation, and Methylation.
Article in The journal of physical chemistry. B, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- PABPC1 in Cancer: From a Translational Housekeeper to a Stress-Responsive Regulatory Hub.Cancer science · 2026Review
- Lipid-Shell PARCH: A Physically Motivated Scale for Transmembrane Residue Hydropathy.The journal of physical chemistry. B · 2026Article
- Beyond acetylation: Evaluating the emerging biology of lysine acylation.Cell chemical biology · 2026Review
- Regulatory mechanisms of post-translational modifications on autophagic flux in neurons following ischemic stroke.Molecular biology reports · 2026Review
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Authors and funding
2 authors.
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Abstract
Post-translational modifications (PTMs) such as phosphorylation, acetylation, and methylation critically expand proteome function by regulating protein structure and interactions. Hydropathy changes serve as a main driving force; however, a quantitative, mechanistic understanding of how their distinct chemical changes alter local protein hydropathy remains limited. To bridge this gap, we extend the Protocol for Assigning a Residue's Character on a Hydropathy (PARCH) scale, a residue-level hydropathy scale, to systematically evaluate PTM-induced physicochemical changes. By applying this method, we quantify the effect and magnitude of hydropathy shifts at modification sites and map how these perturbations influence the local protein environment. Our analysis reveals that phosphorylation exerts a strong, consistent hydrophilic effect, significantly increasing PARCH values due to the introduction of a large, charged phosphate group. In contrast,
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