ReviewNature microbiology2018
Disulfide bond formation in prokaryotes.
Review in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
87 citing papers in PubMed, 160 citations in OpenAlex.
- Genome-wide characterization of host factors involved in single-stranded RNA and DNA phage infection pathways.bioRxiv : the preprint server for biology · 2026Article
- Heterogeneous Indirect Redox Electrocatalysis in Electrolyte.Advanced materials (Deerfield Beach, Fla.) · 2026Review
- Engineering a Second Interchain Disulfide Bond in the αβ T-Cell Receptor Constant Domain: A Powerful Strategy to Enhance Stability, Pairing Fidelity, and Therapeutic Efficacy in TCR-T Cell Therapy.Pharmaceuticals (Basel, Switzerland) · 2026Review
- An improved fluorescent indicator for monitoring intracellular redox potential.Redox biology · 2026Article
- Antibiotic potentiation and inhibition of cross-resistance in pathogens associated with cystic fibrosis.eLife · 2026Article
- A universal cis-proline lock defines catalysis in thioredoxin-fold enzymes.Communications biology · 2026Article
- Unlocking the unexplored AMPSphere in marine rare species.Microbiome · 2026Article
- Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding.Protein science : a publication of the Protein Society · 2026Article
- A shared mechanism for Bacteroidota protein transport and gliding motility.Nature communications · 2025Article
- Disulphide bond-forming enzymes in clostridial species.Microbiology (Reading, England) · 2025Article
- A-to-I mRNA editing in bacteria can affect protein sequence, disulfide bond formation, and function.Nucleic acids research · 2025Article
- Toward Antibody Production in Genome-MinimizedACS synthetic biology · 2025Article
- Mitochondria-associated endoplasmic reticulum membranes and myocardial ischemia: from molecular mechanisms to therapeutic strategies.Journal of translational medicine · 2025Review
- Bacterial suppressor-of-copper-sensitivity proteins exhibit diverse thiol-disulfide oxidoreductase cellular functions.iScience · 2024Article
- Unveiling the versatility of the thioredoxin framework: Insights from the structural examination ofComputational and structural biotechnology journal · 2024Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Differential expression of "Candidatus Liberibacter solanacearum" genes and prophage loci in different life stages of potato psyllid.Scientific reports · 2024Article
- Warfarin analogs target disulfide bond-forming enzymes and suggest a residue important for quinone and coumarin binding.The Journal of biological chemistry · 2024Article
- Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art.Molecules (Basel, Switzerland) · 2024Review
- Cell envelope structural and functional contributions to antibiotic resistance inJournal of bacteriology · 2024Article
27 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
3 authors at 1 institution in 1 country.
Funding
Abstract
Interest in protein disulfide bond formation has recently increased because of the prominent role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that introduces disulfide bonds into cell envelope proteins consists of Escherichia coli enzymes DsbA and DsbB. Since its discovery, variations on the DsbAB pathway have been found in bacteria and archaea, probably reflecting specific requirements for survival in their ecological niches. One variation found amongst Actinobacteria and Cyanobacteria is the replacement of DsbB by a homologue of human vitamin K epoxide reductase. Many Gram-positive bacteria express enzymes involved in disulfide bond formation that are similar, but non-homologous, to DsbAB. While bacterial pathways promote disulfide bond formation in the bacterial cell envelope, some archaeal extremophiles express proteins with disulfide bonds both in the cytoplasm and in the extra-cytoplasmic space, possibly to stabilize proteins in the face of extreme conditions, such as growth at high temperatures. Here, we summarize the diversity of disulfide-bond-catalysing systems across prokaryotic lineages, discuss examples for understanding the biological basis of such systems, and present perspectives on how such systems are enabling advances in biomedical engineering and drug development.
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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.