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October 9, 2025Open Access

A chemical proteomics method to quantify Cysteine S-acylation

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Authors

CFChloé FreyermuthJDJean‐William DupuyTRThibaud T. Renault

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Overview

A chemical proteomics approach quantifies s-acylation levels in proteins, suggesting insights into cellular function.

Key Points

  • The new workflow quantifies over 17,000 unique cysteine residues in biological samples, enhancing proteomic analysis.
  • Integration with high-field asymmetric waveform ion mobility spectrometry offers precise measurement of s-acylation levels.
  • This method reveals dynamic changes in s-acylation in response to autophagy induction in cellular proteomes.
  • Quantifying s-acylation is crucial for understanding protein functions and their implications in health and disease.

Cite This Study

Freyermuth et al. (2025) studied this question.

synapsesocial.com/papers/68e77f09d1c187e1c108faa9https://doi.org/10.26434/chemrxiv-2025-b43v1
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Also Consider

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  1. 1A mass spectrometry-based proteomics strategy to detect long-chain <i>S</i>-acylated peptides2025
  2. 2Analysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap)2024 · 7 citations
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  4. 4Deciphering protein long-chain S-acylation by mass spectrometry proteomics strategies2025
  5. 5Cysteine S-acetylation is a post-translational modification involved in metabolic regulation2024 · 1 citations