Evidence map›Paper›PMID 19290474›Full record

ReviewCellular and molecular life sciences : CMLS2009

For whom the bell tolls? DING proteins in health and disease.

Anne Berna, François Bernier, Eric Chabrière, Mikael Elias, Ken Scott, Andrew Suh

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. DING Proteins Extend to the Extremophilic World.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Sphingolipid transfer proteins defined by the GLTP-fold.Quarterly reviews of biophysics · 2015
    Article
  7. Article
  8. Article
  9. DING proteins: numerous functions, elusive genes, a potential for health.Cellular and molecular life sciences : CMLS · 2013
    Review
  10. Article
  11. Article
  12. Crystallization and preliminary X-ray diffraction analysis of a DING protein from Pseudomonas aeruginosa PA14.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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 at 5 institutions in 2 countries.

Anne BernaInstitut de Biologie Moléculaire des Plantes du CNRS, Institut de Botanique, Université de Strasbourg, 28 rue Goethe, Strasbourg Cedex, France. anne.berna@ibmp-ulp.u-strasbg.fr
François Bernier
Eric Chabrière
Mikael Elias
Ken Scott
Andrew Suh
University of Auckland · NZArchitecture et Fonction des Macromolécules Biologiques · FRCentre National de la Recherche Scientifique · FRInstitut de Biologie Moléculaire des Plantes · FRUniversité de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DING proteins, identified mainly by their eponymous N-terminal sequences, are ubiquitous in living organisms. Amongst bacteria, they are common in pseudomonads, and have been characterised with respect to genetics and structure. They form part of a wider family of phosphate-binding proteins, with emerging roles in phosphate acquisition and pathogenicity. Many DING proteins have been isolated in eukaryotes, in which they have been associated with very diverse biological activities, often in the context of possible signalling roles. Disease states in which DING proteins have been implicated include rheumatoid arthritis, lithiasis, atherosclerosis, some tumours and tumour-associated cachexia, and bacterial and viral adherence. Complete genetic and structural characterisation of eukaryotic DING genes and proteins is still lacking, though the phosphate-binding site seems to be conserved. Whether as bacterial proteins related to bacterial pathogenicity, or as eukaryotic components of biochemical signalling systems, DING proteins require further study.

Indexed as

DiseaseDNA-Binding ProteinsEscherichia coli ProteinsHealthRepressor ProteinsUbiquitin-Protein LigasesAnimalsForecastingHumansModels, MolecularPolycomb Repressive Complex 1Protein BindingProtein Structure, TertiaryStructure-Activity RelationshipdinG protein, E coliDNA-Binding ProteinsEscherichia coli ProteinsPolycomb Repressive Complex 1Repressor ProteinsRNF2 protein, humanRnf2 protein, mouseUbiquitin-Protein Ligases

Identifiers

PMID19290474
PMCPMC11115607
OpenAlexW2073480818

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.