ArticleChemical science2015
Systematic re-evaluation of the bis(2-hydroxyethyl)disulfide (HEDS) assay reveals an alternative mechanism and activity of glutaredoxins.
Article in Chemical science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 39 citations in OpenAlex.
- Making HEDS or tails of glutaredoxin catalysis: Direct reduction of bis(2-hydroxyethyl) disulfide as a non-glutathione disulfide substrate.Redox biology · 2026Article
- HAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Aromatic Residue Variations in the Central β‑Sheet Influence Stability and Activity of E. coli Glutaredoxin 3.ACS omega · 2025Article
- Molecular basis for the enzymatic inactivity of class III glutaredoxin ROXY9 on standard glutathionylated substrates.Nature communications · 2025Article
- Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction.Nature communications · 2024Article
- Chloroplasts lacking class I glutaredoxins are functional but show a delayed recovery of protein cysteinyl redox state after oxidative challenge.Redox biology · 2024Article
- Article
- Characterization of the glutathione-dependent reduction of the peroxiredoxin 5 homolog PfAOP from Plasmodium falciparum.Protein science : a publication of the Protein Society · 2022Article
- Biochemical and structural characterizations of thioredoxin reductase selenoproteins of the parasitic filarial nematodes Brugia malayi and Onchocerca volvulus.Redox biology · 2022Article
- Comparative study of His- and Non-His-tagged CLIC proteins, reveals changes in their enzymatic activity.Biochemistry and biophysics reports · 2021Article
- A glutaredoxin domain fused to the radical-generating subunit of ribonucleotide reductase (RNR) functions as an efficient RNR reductant.The Journal of biological chemistry · 2018Article
- Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides.Chemical science · 2018Article
- The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?Antioxidants & redox signaling · 2017Review
- Glutaredoxin catalysis requires two distinct glutathione interaction sites.Nature communications · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The reduction of bis(2-hydroxyethyl)disulfide (HEDS) by reduced glutathione (GSH) is the most commonly used assay to analyze the presence and properties of enzymatically active glutaredoxins (Grx), a family of central redox proteins in eukaryotes and glutathione-utilizing prokaryotes. Enzymatically active Grx usually prefer glutathionylated disulfide substrates. These are converted
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Registered trials
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.