ReviewNature reviews. Microbiology2009
DSB proteins and bacterial pathogenicity.
Review in Nature reviews. Microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 162 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
162 citing papers in PubMed, 0 citations in OpenAlex.
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- A universal cis-proline lock defines catalysis in thioredoxin-fold enzymes.Communications biology · 2026Article
- Revealing Cell Envelope Heterogeneity in Two StableInternational journal of molecular sciences · 2026Article
- Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding.Protein science : a publication of the Protein Society · 2026Article
- Disulphide bond-forming enzymes in clostridial species.Microbiology (Reading, England) · 2025Article
- The Extracytoplasmic Protein Quality Control System in Pathogenic Campylobacterota: Its Role in Bacterial Virulence and Maintaining Cellular Envelope Proteostasis.International journal of molecular sciences · 2025Review
- Antimicrobial peptide class that forms discrete β-barrel stable pores anchored by transmembrane helices.Nature communications · 2025Article
- 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
- RcsF-independent mechanisms of signaling within the Rcs phosphorelay.PLoS genetics · 2024Article
- RcsF-independent mechanisms of signaling within the Rcs Phosphorelay.bioRxiv : the preprint server for biology · 2024Article
- Fluoromethylketone-Fragment Conjugates Designed as Covalent Modifiers of EcDsbA are Atypical Substrates.ChemMedChem · 2024Article
- Warfarin analogs target disulfide bond-forming enzymes and suggest a residue important for quinone and coumarin binding.The Journal of biological chemistry · 2024Article
- Development of a sensor for disulfide bond formation in diverse bacteria.Journal of bacteriology · 2024Article
- Structural insights into the disulfide isomerase and chaperone activity of TrbB of the F plasmid type IV secretion system.Current research in structural biology · 2024Article
- A Buried Water Network Modulates the Activity of theAntioxidants (Basel, Switzerland) · 2023Article
- Distinct enzymatic strategies forCritical reviews in biochemistry and molecular biology · 2023Article
- Fragment screening libraries for the identification of protein hot spots and their minimal binding pharmacophores.RSC medicinal chemistry · 2023Article
102 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
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
If DNA is the information of life, then proteins are the machines of life--but they must be assembled and correctly folded to function. A key step in the protein-folding pathway is the introduction of disulphide bonds between cysteine residues in a process called oxidative protein folding. Many bacteria use an oxidative protein-folding machinery to assemble proteins that are essential for cell integrity and to produce virulence factors. Although our current knowledge of this machinery stems largely from Escherichia coli K-12, this view must now be adjusted to encompass the wider range of disulphide catalytic systems present in bacteria.
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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.