ReviewAntioxidants & redox signaling2013
Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead.
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 66 papers, 1 of them a synthesis that pooled it.
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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
66 citing papers in PubMed, 1 synthesis or guideline pooled it, 127 citations in OpenAlex.
- Drug-resistantClinical microbiology reviews · 2025Pooled it
- Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- From Environmental Persistence to Host Adaptation: Differential Curli Regulation inMicroorganisms · 2026Review
- Antibiotic potentiation and inhibition of cross-resistance in pathogens associated with cystic fibrosis.eLife · 2026Article
- Endoplasmic Reticulum Redoxome: Protein Folding and Beyond.Biochemistry · 2026Review
- Biosensor that Detects Stress Caused by Periplasmic Proteins.ACS synthetic biology · 2024Article
- Radiotolerance of N-cycle bacteria and their transcriptomic response to low-dose space-analogue ionizing irradiation.iScience · 2024Article
- Solanum lycopersicum heme-binding protein 2 as a potent antimicrobial weapon against plant pathogens.Scientific reports · 2023Article
- A Shiga Toxin B-Subunit-Based Lectibody Boosts T Cell Cytotoxicity towards Gb3-Positive Cancer Cells.Cells · 2023Article
- Expression and Purification of scFvBio-protocol · 2023Article
- A cryptic oxidoreductase safeguards oxidative protein folding inProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Exposure ofJournal of fungi (Basel, Switzerland) · 2023Article
- In situ visualization of Braun's lipoprotein onScience advances · 2023Article
- Periplasmic stress contributes to a trade-off between protein secretion and cell growth inSynthetic biology (Oxford, England) · 2023Article
- Survival ofMicroorganisms · 2022Article
- Article
- ToxT Regulon Is Nonessential for Vibrio cholerae Colonization in Adult Mice.Applied and environmental microbiology · 2022Article
- Engineering of a synthetic antibody fragment for structural and functional studies of K+ channels.The Journal of general physiology · 2022Article
- Article
- Vascular thiol isomerases in thrombosis: The yin and yang.Journal of thrombosis and haemostasis : JTH · 2020Review
6 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
2 authors at 1 institution in 1 country.
Funding
Abstract
significanceThe discovery of the oxidoreductase disulfide bond protein A (DsbA) in 1991 opened the way to the unraveling of the pathways of disulfide bond formation in the periplasm of Escherichia coli and other Gram-negative bacteria. Correct oxidative protein folding in the E. coli envelope depends on both the DsbA/DsbB pathway, which catalyzes disulfide bond formation, and the DsbC/DsbD pathway, which catalyzes disulfide bond isomerization. RECENT ADVANCES: Recent data have revealed an unsuspected link between the oxidative protein-folding pathways and the defense mechanisms against oxidative stress. Moreover, bacterial disulfide-bond-forming systems that differ from those at play in E. coli have been discovered. CRITICAL ISSUES: In this review, we discuss fundamental questions that remain unsolved, such as what is the mechanism employed by DsbD to catalyze the transfer of reducing equivalents across the membrane and how do the oxidative protein-folding catalysts DsbA and DsbC cooperate with the periplasmic chaperones in the folding of secreted proteins. FUTURE DIRECTIONS: Understanding the mechanism of DsbD will require solving the structure of the membranous domain of this protein. Another challenge of the coming years will be to put the knowledge of the disulfide formation machineries into the global cellular context to unravel the interplay between protein-folding catalysts and chaperones. Also, a thorough characterization of the disulfide bond formation machineries at work in pathogenic bacteria is necessary to design antimicrobial drugs targeting the folding pathway of virulence factors stabilized by disulfide bonds.
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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.