ReviewAntioxidants & redox signaling2013
Many roles of the bacterial envelope reducing pathways.
Review in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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.
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Who cites it
34 citing papers in PubMed, 55 citations in OpenAlex.
- A disulfide redox switch mechanism regulates glycoside hydrolase function.Nature communications · 2026Article
- Versatile roles of protein flavinylation in bacterial extracyotosolic electron transfer.mSystems · 2024Article
- The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli.Redox biology · 2023Article
- The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity.Acta crystallographica. Section D, Structural biology · 2022Article
- Biogenesis of secretory immunoglobulin M requires intermediate non-native disulfide bonds and engagement of the protein disulfide isomerase ERp44.The EMBO journal · 2022Article
- Article
- Comparative population genomic analyses of transporters within the Asgard archaeal superphylum.PloS one · 2021Article
- Suppressor Mutations in Type II Secretion Mutants of Vibrio cholerae: Inactivation of the VesC Protease.mSphere · 2020Article
- Local frustration determines loop opening during the catalytic cycle of an oxidoreductase.eLife · 2020Article
- Article
- C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning.PloS one · 2020Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Crystal Structure of the Apo-Form of NADPH-Dependent Thioredoxin Reductase from a Methane-Producing Archaeon.Antioxidants (Basel, Switzerland) · 2018Article
- Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens.The Journal of biological chemistry · 2018Article
- Transmembrane redox control and proteolysis of PdeC, a novel type of c-di-GMP phosphodiesterase.The EMBO journal · 2018Article
- Solution structure and elevator mechanism of the membrane electron transporter CcdA.Nature structural & molecular biology · 2018Article
- Article
- Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker.Free radical biology & medicine · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
significanceThe cell envelope of aerobic bacteria is an oxidizing environment in which most cysteine residues are involved in disulfide bonds. However, reducing redox pathways are also present in this cellular compartment where they provide electrons to a variety of cellular processes. The membrane protein DsbD plays a central role in these pathways by functioning as an electron hub that dispatches electrons received from the cytoplasmic thioredoxin system to periplasmic oxidoreductases. RECENT ADVANCES: Recent data have revealed that DsbD provides reducing equivalents to a large array of periplasmic redox proteins. Those proteins use the reducing power received from DsbD to correct non-native disulfides, mature c-type cytochromes, protect cysteines on secreted proteins from irreversible oxidation, reduce methionine sulfoxides, and scavenge reactive oxygen species such as hydrogen peroxide. CRITICAL ISSUES: Despite the prominent role played by DsbD, we have a poor understanding of how this protein transfers electrons across the inner membrane. Another critical issue will be to grasp the full physiological significance of the new reducing pathways that have been identified in the cell envelope such as the peroxide reduction pathway. FUTURE DIRECTIONS: A detailed understanding of DsbD's mechanism will require solving the structure of this intriguing protein. Moreover, bioinformatic, biochemical, and genetic approaches need to be combined for a better comprehension of the broad spectrum of periplasmic reducing systems present in bacteria, which will likely lead to the discovery of novel pathways.
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Registered trials
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