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

The multiplicity of thioredoxin systems meets the specific lifestyles of Clostridia

8 Feb 2024

Abstract excerpt

Cells are unceasingly confronted by oxidative stresses that oxidize proteins on their cysteines. The thioredoxin (Trx) system, which is a ubiquitous system for thiol and protein repair, is composed of a thioredoxin (TrxA) and a thioredoxin reductase (TrxB). TrxAs reduce disulfide bonds of oxidized proteins and are then usually recycled by a single pleiotropic NAD(P)H-dependent TrxB (NTR). In this work, we first...

Read the complete abstract on PubMed

Topics

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

Share to Clostridium difficile and Clostridium perfringens research
Share to Gut microbiota and health
Share to Porphyrin Metabolism and Disorders

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 38330058
DOI: 10.1371/journal.ppat.1012001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The multiplicity of thioredoxin systems meets the specific lifestyles of ClostridiaPMID 38330058Read ↗

RstA Regulation of <i>Clostridioides difficile</i> Toxin Production and Sporulation in Phenotypically Diverse StrainsSemantic proximity Read ↗

Control of Clostridium difficile Physiopathology in Response to Cysteine AvailabilitySemantic proximity Read ↗

A rubrerythrin locus of <i>Clostridioides difficile</i> efficiently detoxifies reactive oxygen speciesSemantic proximity Read ↗

A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase.Semantic proximity Read ↗

Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.Semantic proximity Read ↗

Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways.Semantic proximity Read ↗

A conserved electron transport chain sensitizes Bacteroides to a pore-forming type VI secretion toxinSemantic proximity Read ↗

Clostridioides difficile strain-dependent and strain-independent adaptations to a microaerobic environmentSemantic proximity Read ↗

The tellurite resistance gene cluster of pathogenic bacteria and its effect on oxidative stress responseSemantic proximity Read ↗

The regulatory role of anti-sigma factor, RsbW, in <i>Clostridioides difficile</i> stress response, persistence and infectionSemantic proximity Read ↗

The monothiol glutaredoxin Grx4 interacts with the Cryptococcus iron regulator Cirl and regulates iron homeostasis and virulence in the <i>Cryptococcus neoformans</i>Semantic proximity Read ↗

The multidomain flavodiiron protein from Clostridium difficile 630 is an NADH:oxygen oxidoreductaseSemantic proximity Read ↗

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