ArticleJournal of bacteriology2002
An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed, 121 citations in OpenAlex.
- Air restriction enhancesMicrobiology spectrum · 2026Article
- Bacteriocin and Antioxidant Production, a Beneficial Properties of Lactic Acid Bacteria Isolated from Fermented Vegetables of Northwest Bulgaria.Probiotics and antimicrobial proteins · 2025Article
- Dpr-mediated HJournal of bacteriology · 2024Article
- Dps Functions as a Key Player in Bacterial Iron Homeostasis.ACS omega · 2023Review
- Article
- Dps Is a Universally Conserved Dual-Action DNA-Binding and Ferritin Protein.Journal of bacteriology · 2022Review
- Isolation and Characterization of Human Monoclonal Antibodies to Pneumococcal Capsular Polysaccharide 3.Microbiology spectrum · 2021Article
- Increased Oxidative Stress Tolerance of a Spontaneously OccurringJournal of bacteriology · 2021Article
- An Overview of Dps: Dual Acting Nanovehicles in Prokaryotes with DNA Binding and Ferroxidation Properties.Sub-cellular biochemistry · 2021Review
- Characterization of the Streptococcus mutansJournal of bacteriology · 2020Article
- Article
- Manganese Depletion Leads to Multisystem Changes in the Transcriptome of the Opportunistic PathogenFrontiers in microbiology · 2020Article
- What Happens in the Staphylococcal Nucleoid under Oxidative Stress?Microorganisms · 2019Review
- Differential biochemical properties of three canonical Dps proteins from the cyanobacteriumThe Journal of biological chemistry · 2018Article
- Disruption of a Novel Iron Transport System Reverses Oxidative Stress Phenotypes of aJournal of bacteriology · 2018Article
- A Capsular Polysaccharide-Specific Antibody Alters Streptococcus pneumoniae Gene Expression during Nasopharyngeal Colonization of Mice.Infection and immunity · 2018Article
- Streptococcus sanguinis biofilm formation & interaction with oral pathogens.Future microbiology · 2018Review
- Investigation of simulated microgravity effects onNPJ microgravity · 2017Article
- The copYAZ Operon Functions in Copper Efflux, Biofilm Formation, Genetic Transformation, and Stress Tolerance in Streptococcus mutans.Journal of bacteriology · 2015Article
- Manganese uptake and streptococcal virulence.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The dpr gene is an antioxidant gene which was isolated from the Streptococcus mutans chromosome by its ability to complement an alkyl hydroperoxide reductase-deficient mutant of Escherichia coli, and it was proven to play an indispensable role in oxygen tolerance in S. mutans. Here, we purified the 20-kDa dpr gene product, Dpr, from a crude extract of S. mutans as an iron-binding protein and found that Dpr formed a spherical oligomer about 9 nm in diameter. Molecular weight determinations of Dpr in solution by analytical ultracentrifugation and light-scattering analyses gave values of 223,000 to 292,000, consistent with a subunit composition of 11.5 to 15 subunits per molecule. The purified Dpr contained iron and zinc atoms and had an ability to incorporate up to 480 iron and 11.2 zinc atoms per molecule. Unlike E. coli Dps and two other members of the Dps family, Dpr was unable to bind DNA. One hundred nanomolar Dpr prevented by more than 90% the formation of hydroxyl radical generated by 10 microM iron(II) salt in vitro. The data shown in this study indicate that Dpr may act as a ferritin-like iron-binding protein in S. mutans and may allow this catalase- and heme-peroxidase-deficient bacterium to grow under air by limiting the iron-catalyzed Fenton reaction.
Indexed as
Identifiers
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.