The clinical potential of thiol redox proteomics

David Sheehan, Brian McDonagh

Research output: Contribution to journalReview articlepeer-review

6 Scopus citations


Introduction: Protein thiols are susceptible to oxidation in health and disease. Redox proteomics methods facilitate the identification, quantification, and rationalization of oxidation processes including those involving protein thiols. These residues are crucial to understanding redox homeostasis underpinning normal cell functioning and regulation as well as novel biomarkers of pathology and promising novel drug targets. Areas covered: This article reviews redox proteomic approaches to study of protein thiols in some important human pathologies and assesses the clinical potential of individual Cys residues as novel biomarkers for disease detection and as targets for novel treatments. Expert commentary: Although protein thiols are not as routinely used as redox biomarkers as some other lesions such as carbonylation, there has been growing recent interest in their potential. Driven largely by developments in high-resolution mass spectrometry it is possible now to identify proteins that are redox modified at thiol groups or that interact with regulatory oxidoreductases. Thiols that are specifically susceptible to modification by reactive oxygen species can be routinely identified now and quantitative MS can be used to quantify the proportion of a protein that is redox modified.

Original languageBritish English
Pages (from-to)41-48
Number of pages8
JournalExpert Review of Proteomics
Issue number1
StatePublished - 2 Jan 2020


  • biomarkers
  • druggable proteins
  • gel-based proteomics
  • ICAT
  • mass spectrometry
  • Protein oxidation


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