ReviewJournal of bacteriology2015
Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.
Review in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed, 75 citations in OpenAlex.
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- The conserved two-component systems CutRS and CssRS control the protein secretion stress response inmBio · 2026Article
- The natural symbiotic bacterium Enterococcus faecalis LX10 drives Bombyx mori refractoriness to Nosema bombycis infection via the secretion of enterococcin.BMC microbiology · 2025Article
- Current Knowledge of Enterococcal Endocarditis: A Disease Lurking in Plain Sight of Health Providers.Pathogens (Basel, Switzerland) · 2024Review
- Article
- Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in Paenibacillus lautus missing a conserved disulfide bond.The Journal of biological chemistry · 2023Article
- Mechanism of 5-chloro-2-methyl-4-isothiazolin-3-one (CMIT) in controlling microbial problems in aircraft fuel systems.RSC advances · 2023Article
- A cryptic oxidoreductase safeguards oxidative protein folding inProceedings of the National Academy of Sciences of the United States of America · 2023Article
- A cell wall-anchored glycoprotein confers resistance to cation stress in Actinomyces oris biofilms.Molecular oral microbiology · 2022Article
- An Apoplastic Effector Pat-1Frontiers in plant science · 2022Article
- OsnR is an autoregulatory negative transcription factor controlling redox-dependent stress responses in Corynebacterium glutamicum.Microbial cell factories · 2021Article
- Identification of a Thiol-Disulfide Oxidoreductase (SdbA) Catalyzing Disulfide Bond Formation in the Superantigen SpeA in Streptococcus pyogenes.Journal of bacteriology · 2021Article
- Anchoring surface proteins to the bacterial cell wall by sortase enzymes: how it started and what we know now.Current opinion in microbiology · 2021Review
- Optimized Genetic Tools Allow the Biosynthesis of Glycocin F and Analogues Designed To Test the Roles ofJournal of bacteriology · 2021Article
- Cardiac Microlesions Form During Severe Bacteremic Enterococcus faecalis Infection.The Journal of infectious diseases · 2021Article
- Antibiofilm Activity of Heather and Manuka Honeys and Antivirulence Potential of Some of Their Constituents on the DsbA1 Enzyme ofAntibiotics (Basel, Switzerland) · 2020Article
- The pathogenesis of cardiac microlesion formation during severe bacteremic infection.PLoS pathogens · 2020Review
- Genetic Manipulation of Corynebacterium diphtheriae and Other Corynebacterium Species.Current protocols in microbiology · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Disulfide bonds are important for the stability and function of many secreted proteins. In Gram-negative bacteria, these linkages are catalyzed by thiol-disulfide oxidoreductases (Dsb) in the periplasm. Protein oxidation has been well studied in these organisms, but it has not fully been explored in Gram-positive bacteria, which lack traditional periplasmic compartments. Recent bioinformatics analyses have suggested that the high-GC-content bacteria (i.e., actinobacteria) rely on disulfide-bond-forming pathways. In support of this, Dsb-like proteins have been identified in Mycobacterium tuberculosis, but their functions are not known. Actinomyces oris and Corynebacterium diphtheriae have recently emerged as models to study disulfide bond formation in actinobacteria. In both organisms, disulfide bonds are catalyzed by the membrane-bound oxidoreductase MdbA. Remarkably, unlike known Dsb proteins, MdbA is important for pathogenesis and growth, which makes it a potential target for new antibacterial drugs. This review will discuss disulfide-bond-forming pathways in bacteria, with a special focus on Gram-positive 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.