Evidence map›Paper›PMID 9473058›Full record

ArticleJournal of bacteriology1998

The StpA protein functions as a molecular adapter to mediate repression of the bgl operon by truncated H-NS in Escherichia coli.

A Free, R M Williams, C J Dorman

Abstract read
In one paragraph

Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Histone-like nucleoid structuring (H-NS) protein silences the beta-glucoside (Computational and structural biotechnology journal · 2022
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. H-NS regulates DNA repair in Shigella.Journal of bacteriology · 1998
    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

3 authors.

A FreeDepartment of Microbiology, Moyne Institute of Preventive Medicine, Trinity College, Dublin 2, Republic of Ireland. Andrew.Free@ed.ac.uk
R M Williams
C J Dorman

Funding

Wellcome Trust
6 · The paper itself

Abstract

The mechanism of repression of the beta-glucoside utilization (bgl) operon of Escherichia coli by a carboxy-terminally truncated derivative of the nucleoid-associated protein H-NS which is defective in DNA binding was investigated. The DNA-binding function of the H-NS-like protein StpA was found to be necessary for repression, which is consistent with a role for StpA as a DNA-binding adapter for mutant derivatives of H-NS.

Indexed as

Amino Acid Transport SystemsEscherichia coli ProteinsMolecular ChaperonesOperonBacterial ProteinsCarrier ProteinsDNA-Binding ProteinsEnzyme RepressionEscherichia coliGene Expression Regulation, BacterialGenes, ReporterGlucosidesMutationPeptide FragmentsSequence DeletionAmino Acid Transport SystemsBacterial ProteinsCarrier ProteinsDNA-Binding ProteinsEscherichia coli ProteinsGlucosidesH-NS protein, bacteriaMolecular ChaperonesPeptide FragmentsProU protein, BacteriaStpA protein, E coli

Identifiers

PMID9473058
PMCPMC106983

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.