Evidence map›Paper›PMID 35380871›Full record

ReviewJournal of bacteriology2022

Dps Is a Universally Conserved Dual-Action DNA-Binding and Ferritin Protein.

Katie Orban, Steven E Finkel

Open access · greenAbstract readReview
In one paragraph

Review in Journal of bacteriology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
10.1field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Characterizing the Impact of Nucleoid-Associated Proteins on HU-DNA Interactions by Live-Cell Single-Molecule Tracking.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Physiological Changes and Transposition of Insertion Sequences in theInternational journal of molecular sciences · 2026
    Article
  8. Article
  9. Protein-centric mechanisms of typhoidalFrontiers in cellular and infection microbiology · 2026
    Review
  10. Review
  11. Article
  12. Dps binds and protects DNA in starvedbioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. The Mechanism of Mineral Nucleation and Growth in a Mini-Ferritin.Journal of the American Chemical Society · 2025
    Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Nucleoid-associated proteins: molecular mechanisms in microbial adaptation.World journal of microbiology & biotechnology · 2025
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Katie OrbanMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern Californiagrid.42505.36, Los Angeles, California, USA.
Steven E FinkelMolecular and Computational Biology Section, Department of Biological Sciences, University of Southern Californiagrid.42505.36, Los Angeles, California, USA.ORCID 0000-0003-1715-6696
University of Southern California · US

Funding

CBI: Chemistry Biology InterfaceT32GM118289 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FORSBURG, SUSAN L · 2016 to 2020
$1.2M
DOD | USAF | AMC | Air Force Office of Scientific Research (AFOSR) FA 9550-19-1-0249NIGMS NIH HHS T32 GM118289
6 · The paper itself

Abstract

The DNA-binding protein from starved cells, Dps, is a universally conserved prokaryotic ferritin that, in many species, also binds DNA. Dps homologs have been identified in the vast majority of bacterial species and several archaea. Dps also may play a role in the global regulation of gene expression, likely through chromatin reorganization. Dps has been shown to use both its ferritin and DNA-binding functions to respond to a variety of environmental pressures, including oxidative stress. One mechanism that allows Dps to achieve this is through a global nucleoid restructuring event during stationary phase, resulting in a compact, hexacrystalline nucleoprotein complex called the biocrystal that occludes damaging agents from DNA. Due to its small size, hollow spherical structure, and high stability, Dps is being developed for applications in biotechnology.

Indexed as

Escherichia coli ProteinsGene Expression Regulation, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsDNA-Binding ProteinsEscherichia coliFerritinsOxidative StressBacterial Outer Membrane ProteinsBacterial ProteinsDNA-Binding Proteinsdps protein, E coliEscherichia coli ProteinsFerritinsDNA-binding proteinDpsferritinnucleoid-associated proteinstationary phase

Identifiers

PMID35380871
PMCPMC9112962
OpenAlexW4226206744

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.