Evidence map›Paper›PMID 23416301›Full record

ArticleFEBS letters2013

DksA2, a zinc-independent structural analog of the transcription factor DksA.

Ran Furman, Tapan Biswas, Eric M Danhart, Mark P Foster, Oleg V Tsodikov, Irina Artsimovitch

Abstract read
In one paragraph

Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
  2. A genome-wide screen inJournal of bacteriology · 2026
    Article
  3. Cobalt mitigates zinc-starvation effects in Pseudomonas aeruginosa.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  4. Calprotectin protectsmSystems · 2025
    Article
  5. Review
  6. Convergent evolution in toxin detection and resistance provides evidence for conserved bacterial-fungal interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Strategies for Zinc Uptake inFrontiers in microbiology · 2021
    Review
  17. Article
  18. Puzzling conformational changes affecting proteins binding to the RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. DksA-DnaJ redox interactions provide a signal for the activation of bacterial RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  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

6 authors.

Ran FurmanDepartment of Microbiology, The Ohio State University, Columbus, OH, USA.
Tapan Biswas
Eric M Danhart
Mark P Foster
Oleg V Tsodikov
Irina Artsimovitch

Funding

Mechnanism of transcript elongation control by RfaHR01GM067153 · NIGMS · OHIO STATE UNIVERSITY · PI IRINA ARTSIMOVITCH · 2003 to 2026
$8.0M
Structural and Dynamics in Allosteric Gene RegulationR01GM077234 · NIGMS · OHIO STATE UNIVERSITY · PI FOSTER, MARK P. · 2007 to 2010
$1.2M
NIGMS NIH HHS R01 GM067153NIGMS NIH HHS R01 GM077234
6 · The paper itself

Abstract

Transcription factor DksA contains a four-Cys Zn(2 +)-finger motif thought to be responsible for structural integrity and the relative disposition of its domains. Pseudomonas aeruginosa encodes an additional DksA paralog (DksA2) that is expressed selectively under Zn(2+) limitation. Although DksA2 does not bind Zn(2+), it complements the Escherichia coli dksA deletion and has similar effects on transcription in vitro. In this study, structural and biochemical analyses reveal that DksA2 has a similar fold, domain structure and RNA polymerase binding properties to those of the E. coli DksA despite the lack of the stabilizing metal ion.

Indexed as

Crystallography, X-RayCysteineDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein IsoformsProtein Structure, SecondaryProtein Structure, TertiaryPseudomonas aeruginosaRecombinant ProteinsStructural Homology, ProteinTranscription, GeneticZincCysteinedksA protein, E coliDNA-Directed RNA PolymerasesEscherichia coli ProteinsProtein IsoformsRecombinant ProteinsRNA polymerase alpha subunitZinc

Identifiers

PMID23416301
PMCPMC5525025

What OpenQuestion holds

Textmetadata
LicenceTDM
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.