Evidence map›Paper›PMID 28826489›Full record

ArticleeLife2017

Acidic C-terminal domains autoregulate the RNA chaperone Hfq.

Andrew Santiago-Frangos, Jeliazko R Jeliazkov, Jeffrey J Gray, Sarah A Woodson

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed, 1 pooled it
7.0field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 1 synthesis or guideline pooled it, 69 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Article
  3. Article
  4. Competition for Hfq drives kinetic selection of mRNA targets byProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. What makes a small RNA work?Nucleic acids research · 2025
    Review
  7. Article
  8. TheFrontiers in cellular and infection microbiology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Andrew Santiago-FrangosCell, Molecular and Developmental Biology and Biophysics Program, Johns Hopkins University, Baltimore, United States.ORCID http://orcid.org/0000-0001-9615-065X
Jeliazko R JeliazkovProgram in Molecular Biophysics, Johns Hopkins University, Baltimore, United States.ORCID http://orcid.org/0000-0003-4249-1955
Jeffrey J GrayDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, United States.ORCID http://orcid.org/0000-0001-6380-2324
Sarah A WoodsonT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, United States.ORCID http://orcid.org/0000-0003-0170-1987
Johns Hopkins University · US

Funding

CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Prediction of the Structure of Therapeutic Antibodies with their AntigensR01GM078221 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GRAY, JEFFREY J · 2006 to 2020
$4.0M
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 GM078221NIGMS NIH HHS R01 GM120425NIGMS NIH HHS T32 GM007231NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

The RNA chaperone Hfq is an Sm protein that facilitates base pairing between bacterial small RNAs (sRNAs) and mRNAs involved in stress response and pathogenesis. Hfq possesses an intrinsically disordered C-terminal domain (CTD) that may tune the function of the Sm domain in different organisms. In

Indexed as

Crystallography, X-RayEscherichia coliEscherichia coli ProteinsHost Factor 1 ProteinModels, MolecularProtein BindingProtein ConformationProtein DomainsRNA, BacterialEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinRNA, BacterialautoregulationbiophysicsE. coliintrinsically disordered proteinRNA chaperoneRosettasmall non-coding RNASm proteinstructural biology

Identifiers

PMID28826489
PMCPMC5606850
OpenAlexW2744062290

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.