ArticleChembiochem : a European journal of chemical biology2020
Isotopically Labeled Clickable Glutathione to Quantify Protein S-Glutathionylation.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Protein phosphatase PP2Cα S-glutathionylation regulates cell migration.The Journal of biological chemistry · 2024Article
- Chemoproteomic strategy identified p120-catenin glutathionylation regulates E-cadherin degradation and cell migration.Cell chemical biology · 2023Article
- Clickable Glutathione-Based Identification of Cysteine Glutathionylation.Current protocols · 2023Article
- Desmin Reorganization by Stimuli Inducing Oxidative Stress and Electrophiles: Role of Its Single Cysteine Residue.Antioxidants (Basel, Switzerland) · 2023Article
- Chemistry and biology of enzymes in protein glutathionylation.Current opinion in chemical biology · 2023Review
- Functional Analysis of GSTK1 in Peroxisomal Redox Homeostasis in HEK-293 Cells.Antioxidants (Basel, Switzerland) · 2023Article
- Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022Review
- Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.Antioxidants (Basel, Switzerland) · 2022Review
- Hsp70 in Redox Homeostasis.Cells · 2022Review
- Identification and Quantification of Glutathionylated Cysteines under Ischemic Stress.Journal of proteome research · 2021Article
- Contemporary proteomic strategies for cysteine redoxome profiling.Plant physiology · 2021Review
- Characterization of cellular oxidative stress response by stoichiometric redox proteomics.American journal of physiology. Cell physiology · 2021Review
- S-glutathionylation proteome profiling reveals a crucial role of a thioredoxin-like protein in interspecies competition and cariogenecity of Streptococcus mutans.PLoS pathogens · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein S-glutathionylation is one of the important cysteine oxidation events that regulate various redox-mediated biological processes. Despite several existing methods, there are few proteomic approaches to identify and quantify specific cysteine residues susceptible to S-glutathionylation. We previously developed a clickable glutathione approach that labels intracellular glutathione with azido-Ala by using a mutant form of glutathione synthetase. In this study, we developed a quantification strategy with clickable glutathione by using isotopically labeled heavy and light derivatives of azido-Ala, which provides the relative quantification of glutathionylated peptides in mass spectrometry-based proteomic analysis. We applied isotopically labeled clickable glutathione to HL-1 cardiomyocytes, quantifying relative levels of 1398 glutathionylated peptides upon addition of hydrogen peroxide. Importantly, we highlight elevated levels of glutathionylation on sarcomere-associated muscle proteins while validating glutathionylation of two structural proteins, α-actinin and desmin. Our report provides a chemical proteomic strategy to quantify specific glutathionylated cysteines.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.