Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Glutathione oxidation in response to intracellular H2O2: Key but overlapping roles for dehydroascorbate reductases.

Plant signaling & behavior - 3 Aug 2017

Rahantaniaina Marie-Sylviane, Li Shengchun, Chatel-Innocenti Gilles, Tuzet Andrée, Mhamdi Amna, Vanacker Hélène, Noctor Graham

Abstract excerpt

Glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H2O2 detoxification. We have investigated the response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Gene Expression Regulation, Plant
Share to Glutathione

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Peroxide

Share to Intracellular Space

Share to Oxidants

Share to Oxidation-Reduction

Share to Oxidative Stress

Share to Oxidoreductases

Source

Open in PubMed Open full text

Identifiers

PMID: 28782990
DOI: 10.1080/15592324.2017.1356531
PMCID: PMC5616140

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Glutathione oxidation in response to intracellular H2O2: Key but overlapping roles for dehydroascorbate reductases.PMID 28782990Read ↗

Arabidopsis dehydroascorbate reductase 1 and 2 modulate redox states of ascorbate-glutathione cycle in the cytosol in response to photooxidative stress.Semantic proximity Read ↗

Cytosolic and Chloroplastic DHARs Cooperate in Oxidative Stress-Driven Activation of the Salicylic Acid Pathway.Semantic proximity Read ↗

Arabidopsis GLUTATHIONE REDUCTASE1 plays a crucial role in leaf responses to intracellular hydrogen peroxide and in ensuring appropriate gene expression through both salicylic acid and jasmonic acid signaling pathways.Semantic proximity Read ↗

Selective silencing of 2Cys and type-IIB Peroxiredoxins discloses their roles in cell redox state and stress signaling.Semantic proximity Read ↗

Functional analysis of Arabidopsis mutants points to novel roles for glutathione in coupling H(2)O(2) to activation of salicylic acid accumulation and signaling.Semantic proximity Read ↗

Hydrogen sulfide attenuates intracellular oxidative stress via repressing glycolate oxidase activities in Arabidopsis thaliana.Semantic proximity Read ↗

Analysis of cytosolic isocitrate dehydrogenase and glutathione reductase 1 in photoperiod-influenced responses to ozone using Arabidopsis knockout mutants.Semantic proximity Read ↗

Plastid-localized glutathione reductase2-regulated glutathione redox status is essential for Arabidopsis root apical meristem maintenance.Semantic proximity Read ↗

A Coupled GSH/GSNOR System Denitrosylates TRXh5 to Allow Activation of SA Signalling by Oxidative Stress.Semantic proximity Read ↗

Cytosolic dehydroascorbate reductase is important for ozone tolerance in Arabidopsis thaliana.Semantic proximity Read ↗

Role of yeast glutaredoxins as glutathione S-transferases.Semantic proximity Read ↗

The Arabidopsis glutathione transferase gene family displays complex stress regulation and co-silencing multiple genes results in altered metabolic sensitivity to oxidative stress.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.