Evidence map›Paper›PMID 29633565›Full record

ReviewWiley interdisciplinary reviews. RNA2018

Hfq chaperone brings speed dating to bacterial sRNA.

Andrew Santiago-Frangos, Sarah A Woodson

Abstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
16.6field-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

119 citing papers in PubMed, 184 citations in OpenAlex.

  1. Review
  2. Exchange dynamics and kinetic control of gene regulation complexes.Nature reviews. Molecular cell biology · 2026
    Review
  3. Bacterial small regulatory RNAs.Nature reviews. Microbiology · 2026
    Review
  4. Article
  5. Journal of molecular biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Competition for Hfq drives kinetic selection of mRNA targets byProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. What makes a small RNA work?Nucleic acids research · 2025
    Review
  19. Article
  20. Article

59 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.

Andrew Santiago-FrangosProgram in Cellular, Molecular and Developmental Biology and Biophysics, Johns Hopkins University, Baltimore, Maryland.ORCID 0000-0001-9615-065X
Sarah A WoodsonT. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland.ORCID 0000-0003-0170-1987
Johns Hopkins University · US

Funding

Hfq RNA Chaperone and the Mechanism of RNA-Dependent RegulationR01GM120425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WOODSON, SARAH A. · 2016 to 2019
$1.3M
NIGMS NIH HHS R01 GM120425
6 · The paper itself

Abstract

Hfq is a ubiquitous, Sm-like RNA binding protein found in most bacteria and some archaea. Hfq binds small regulatory RNAs (sRNAs), facilitates base pairing between sRNAs and their mRNA targets, and directly binds and regulates translation of certain mRNAs. Because sRNAs regulate many stress response pathways in bacteria, Hfq is essential for adaptation to different environments and growth conditions. The chaperone activities of Hfq arise from multipronged RNA binding by three different surfaces of the Hfq hexamer. The manner in which the structured Sm core of Hfq binds RNA has been well studied, but recent work shows that the intrinsically disordered C-terminal domain of Hfq modulates sRNA binding, creating a kinetic hierarchy of RNA competition for Hfq and ensuring the release of double-stranded sRNA-mRNA complexes. A combination of structural, biophysical, and genetic experiments reveals how Hfq recognizes its RNA substrates and plays matchmaker for sRNAs and mRNAs in the cell. The interplay between structured and disordered domains of Hfq optimizes sRNA-mediated post-transcriptional regulation, and is a common theme in RNA chaperones. This article is categorized under: Regulatory RNAs/RNAi/Riboswitches > Regulatory RNAs RNA Interactions with Proteins and Other Molecules > RNA-Protein Complexes RNA Structure and Dynamics > RNA Structure, Dynamics, and Chemistry.

Indexed as

BacteriaHost Factor 1 ProteinMolecular ChaperonesRNA, BacterialRNA, MessengerRNA Processing, Post-TranscriptionalRNA, Small UntranslatedHost Factor 1 ProteinMolecular ChaperonesRNA, BacterialRNA, MessengerRNA, Small UntranslatedautoinhibitionautoregulationE. coliintrinsically disordered proteinpost-transcriptional regulationRNA chaperonesmall non-coding RNASm protein

Identifiers

PMID29633565
PMCPMC6002925
OpenAlexW2807951024

What OpenQuestion holds

Textmetadata
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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.