Evidence map›Paper›PMID 23535768›Full record

ReviewRNA biology2013

Structure and RNA-binding properties of the bacterial LSm protein Hfq.

Evelyn Sauer

Open access · bronzeAbstract readReview
In one paragraph

Review in RNA biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
10.7field-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

49 citing papers in PubMed, 107 citations in OpenAlex.

  1. RNA-Binding Proteins in Dinoflagellates.International journal of molecular sciences · 2026
    Review
  2. Competition for Hfq drives kinetic selection of mRNA targets byProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Unexpected Richness of the Bacterial Small RNA World.Journal of molecular biology · 2025
    Review
  4. Article
  5. Article
  6. TheFrontiers in cellular and infection microbiology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Analysis of Lsm Protein-Mediated Regulation in the HaloarchaeonInternational journal of molecular sciences · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

1 author at 1 institution in 1 country.

Evelyn SauerBiozentrum, University of Basel, Basel, Switzerland. evelyn.sauer@unibas.ch
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over the past years, small non-coding RNAs (sRNAs) emerged as important modulators of gene expression in bacteria. Guided by partial sequence complementarity, these sRNAs interact with target mRNAs and eventually affect transcript stability and translation. The physiological function of sRNAs depends on the protein Hfq, which binds sRNAs in the cell and promotes the interaction with their mRNA targets. This important physiological function of Hfq as a central hub of sRNA-mediated regulation made it one of the most intensely studied proteins in bacteria. Recently, a new model for sRNA binding by Hfq has been proposed that involves the direct recognition of the sRNA 3' end and interactions of the sRNA body with the lateral RNA-binding surface of Hfq. This review summarizes the current understanding of the RNA binding properties of Hfq and its (s)RNA complexes. Moreover, the implications of the new binding model for sRNA-mediated regulation are discussed.

Indexed as

AnimalsBacterial ProteinsBinding SitesEscherichia coliEscherichia coli ProteinsEukaryotaGene Expression Regulation, BacterialHost Factor 1 ProteinHumansPhylogenyProtein BindingProto-Oncogene ProteinsRNA, BacterialRNA-Binding ProteinsRNA, MessengerRNA, Small UntranslatedBacterial ProteinsEscherichia coli ProteinsHost Factor 1 ProteinLSM1 protein, humanProto-Oncogene ProteinsRNA, BacterialRNA-Binding ProteinsRNA, MessengerRNA, Small Untranslated3′ end recognitioncrystal structuregene regulationLSm ringnon-coding RNAsprokaryotesRNA chaperoneRNA degradation

Identifiers

PMID23535768
PMCPMC3710368
OpenAlexW2042739115

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.