Evidence map›Paper›PMID 24833341›Full record

ArticleBiology2014

Dancing to another tune-adhesive moonlighting proteins in bacteria.

Veera Kainulainen, Timo K Korhonen

Open access · goldAbstract read
In one paragraph

Article in Biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed, 1 pooled it
19.7field-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

87 citing papers in PubMed, 1 synthesis or guideline pooled it, 150 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Review
  5. Frontiers in cellular and infection microbiology · 2026
    Article
  6. Article
  7. Evaluation of Salivary GAPDH as a Predictor Biomarker for Periodontitis.International journal of molecular sciences · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Molecular Identification and Bioinformatics Analysis ofPathogens (Basel, Switzerland) · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Moonlighting Proteins: Diverse Functions Found in Fungi.Journal of fungi (Basel, Switzerland) · 2023
    Review
  16. The Enolase of theInternational journal of molecular sciences · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Article

27 more citing papers are in PubMed but not listed here.

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.

Veera KainulainenDepartment of Veterinary Biosciences, University of Helsinki, P.O. Box 66, FI-00014 Helsinki, Finland. veera.kainulainen@helsinki.fi.
Timo K KorhonenGeneral Microbiology, Department of Biosciences, University of Helsinki, P.O. Box 56, FI-00014 Helsinki, Finland. timo.korhonen@helsinki.fi.
University of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological moonlighting refers to proteins which express more than one function. Moonlighting proteins occur in pathogenic and commensal as well as in Gram-positive and Gram-negative bacteria. The canonical functions of moonlighting proteins are in essential cellular processes, i.e., glycolysis, protein synthesis, chaperone activity, and nucleic acid stability, and their moonlighting functions include binding to host epithelial and phagocytic cells, subepithelia, cytoskeleton as well as to mucins and circulating proteins of the immune and hemostatic systems. Sequences of the moonlighting proteins do not contain known motifs for surface export or anchoring, and it has remained open whether bacterial moonlighting proteins are actively secreted to the cell wall or whether they are released from traumatized cells and then rebind onto the bacteria. In lactobacilli, ionic interactions with lipoteichoic acids and with cell division sites are important for surface localization of the proteins. Moonlighting proteins represent an abundant class of bacterial adhesins that are part of bacterial interactions with the environment and in responses to environmental changes. Multifunctionality in bacterial surface proteins appears common: the canonical adhesion proteins fimbriae express also nonadhesive functions, whereas the mobility organelles flagella as well as surface proteases express adhesive functions.

Identifiers

PMID24833341
PMCPMC4009768
OpenAlexW2047808858

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.