ArticleJournal of bacteriology2001
Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
What it found
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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.
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.
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Who cites it
90 citing papers in PubMed, 191 citations in OpenAlex.
- Metronidazole and ether derivatives target Helicobacter pylori via simultaneous stress induction and inhibition.Nature microbiology · 2026Article
- Article
- Linoleic Hydroperoxides Are Potent Hyperoxidative Agents of Sensitive and Robust Typical 2-Cys Peroxiredoxins.Antioxidants (Basel, Switzerland) · 2025Article
- Asphaltene biotransformation by a novel enzyme thiol peroxidase fromApplied and environmental microbiology · 2025Article
- A Physiological Approach to Explore How Thioredoxin-Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate HAntioxidants (Basel, Switzerland) · 2024Article
- The multiplicity of thioredoxin systems meets the specific lifestyles of Clostridia.PLoS pathogens · 2024Article
- Gold complex compounds that inhibit drug-resistantFrontiers in antibiotics · 2023Article
- Reactive sulfur and selenium species in the regulation of bone homeostasis.Free radical biology & medicine · 2022Review
- Positive Selection of Mutations in the Helicobacter pyloriInfection and immunity · 2022Article
- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
- Helicobacter pylori Thioredoxin1 May Play a Highly Pathogenic Role via the IL6/STAT3 Pathway.Gastroenterology research and practice · 2022Article
- Structural and Biochemical Characterization of Thioredoxin-2 fromAntioxidants (Basel, Switzerland) · 2021Article
- Relevance of peroxiredoxins in pathogenic microorganisms.Applied microbiology and biotechnology · 2021Review
- Distinct HFrontiers in microbiology · 2021Article
- Thioredoxin Reductase Is a Valid Target for Antimicrobial Therapeutic Development Against Gram-Positive Bacteria.Frontiers in microbiology · 2021Article
- Thiol Peroxidases as Major Regulators of Intracellular Levels of Peroxynitrite in LiveAntioxidants (Basel, Switzerland) · 2020Article
- The thermophilic biomass-degrading bacteriumThe Journal of biological chemistry · 2019Article
- Structure, Mechanism, and Inhibition ofAntimicrobial agents and chemotherapy · 2019Article
- Analysis of core protein clusters identifies candidate variable sites conferring metronidazole resistance inGastroenterology report · 2019Article
- Tyrosine substitution of a conserved active-site histidine residue activates Plasmodium falciparum peroxiredoxin 6.Protein science : a publication of the Protein Society · 2019Article
30 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Helicobacter pylori, an oxygen-sensitive microaerophile, contains an alkyl hydroperoxide reductase homologue (AhpC, HP1563) that is more closely related to 2-Cys peroxiredoxins of higher organisms than to most other eubacterial AhpC proteins. Allelic replacement mutagenesis revealed ahpC to be essential, suggesting a critical role for AhpC in defending H. pylori against oxygen toxicity. Characterization of the ahpC promoter region divulged two putative regulatory elements and identified the transcription initiation site, which was mapped to 96 and 94 bp upstream of the initiation codon. No homologue of ahpF, which encodes the dedicated AhpC reductase in most eubacteria, was found in the H. pylori genome. Instead, homologues of Escherichia coli thioredoxin (Trx) reductase (TrxR, HP0825) and Trx (Trx1, HP0824) formed a reductase system for H. pylori AhpC. A second Trx homologue (Trx2, HP1458) was identified but was incapable of AhpC reduction, although Trx2 exhibited disulfide reductase activity with other substrates [insulin and 5,5'-dithiobis(2-nitrobenzoic acid)]. AhpC interactions with each substrate, Trx1 and hydroperoxide, were bimolecular and nonsaturable (infinite V(max) and K(m) values) but rapid enough (at 1 x 10(5) to 2 x 10(5) M(-1) s(-1)) to suggest an important role for AhpC in cellular peroxide metabolism. AhpC also exhibited a wide specificity for hydroperoxide substrates, which, taken together with the above results, suggests a minimal binding site for hydroperoxides composed of little more than the cysteinyl (Cys49) active site. H. pylori AhpC was not reduced by Salmonella typhimurium AhpF and was slightly more active with E. coli TrxR and Trx1 than was S. typhimurium AhpC, demonstrating the specialized catalytic properties of this peroxiredoxin.
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What OpenQuestion holds
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.