ArticleThe Journal of biological chemistry2020
Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways in
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- PexR is a noncanonical regulator of the peroxide stress response in bacteria.Nucleic acids research · 2025Article
- Targeting novel regulated cell death: disulfidptosis in cancer immunotherapy with immune checkpoint inhibitors.Biomarker research · 2025Review
- Altering the redox status ofeLife · 2025Article
- Regulation of fadR on the ROS defense mechanism in Shewanalla oneidensis.Biotechnology letters · 2024Article
- Production of selenium nanoparticles occurs through an interconnected pathway of sulphur metabolism and oxidative stress response in Pseudomonas putida KT2440.Microbial biotechnology · 2023Article
- Article
- NapB Restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants.Communications biology · 2022Article
- Proteomic Perspective of Cadmium Tolerance inFrontiers in microbiology · 2022Article
- Distinct HFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AhpC is a bacterial representative of 2-Cys peroxiredoxins (Prxs) with broad substrate specificity and functional plasticity. However, details underpinning these two important attributes of AhpC remain unclear. Here, we studied the functions and mechanisms of regulation of AhpC in the facultative Gram-negative anaerobic bacterium
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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.