Evidence map›Paper›PMID 42035512›Full record

ArticleRedox biology2026

Making HEDS or tails of glutaredoxin catalysis: Direct reduction of bis(2-hydroxyethyl) disulfide as a non-glutathione disulfide substrate.

Lukas Lang, Cedric Diaz, Erik Matonia, Marcel Deponte

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Redox biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Lukas LangFaculty of Chemistry, Comparative Biochemistry, RPTU Kaiserslautern, Kaiserslautern, D-67663, Germany.
Cedric DiazFaculty of Chemistry, Comparative Biochemistry, RPTU Kaiserslautern, Kaiserslautern, D-67663, Germany.
Erik MatoniaFaculty of Chemistry, Comparative Biochemistry, RPTU Kaiserslautern, Kaiserslautern, D-67663, Germany.
Marcel DeponteFaculty of Chemistry, Comparative Biochemistry, RPTU Kaiserslautern, Kaiserslautern, D-67663, Germany. Electronic address: deponte@rptu.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bis(2-hydroxyethyl) disulfide (HEDS) steady-state assay is the most commonly used assay to measure the activity and kinetic parameters of glutaredoxins. Despite its widespread use, the HEDS assay is often misinterpreted, and the exact enzyme mechanism has remained unclear. Here we used stopped-flow kinetic measurements to show that the active-site cysteinyl residue of mono- and dithiol class I glutaredoxins from Saccharomyces cerevisiae and Plasmodium falciparum reduces HEDS with a second-order rate constant around 10

Indexed as

DisulfidesGlutaredoxinsCatalysisCatalytic DomainEthanolGlutathioneKineticsOxidation-ReductionPlasmodium falciparumSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate Specificity2-hydroxyethyl disulfideDisulfidesEthanolGlutaredoxinsGlutathioneSaccharomyces cerevisiae ProteinsCatalysisDisulfideEnzyme mechanismGlutaredoxinGlutathione

Identifiers

PMID42035512
PMCPMC13133953

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.