Evidence map›Paper›PMID 29930203›Full record

ArticleThe Journal of cell biology2018

The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged

Sandip Dey, Chiranjit Biswas, Jayati Sengupta

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Transcriptome analysis ofMicrobiology spectrum · 2026
    Article
  2. HflX mediates rifampicin resistance inFrontiers in microbiology · 2026
    Article
  3. Bio-protocol · 2025
    Article
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  15. HflX is a GTPase that controls hypoxia-induced replication arrest in slow-growing mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
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  18. Review
  19. Review
  20. Isolate Specific Cold Response ofFrontiers in microbiology · 2019
    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

3 authors at 1 institution in 1 country.

Sandip DeyStructural Biology and Bioinformatics Division, Council of Scientific and Industrial Research - Indian Institute of Chemical Biology, Kolkata, India.
Chiranjit BiswasStructural Biology and Bioinformatics Division, Council of Scientific and Industrial Research - Indian Institute of Chemical Biology, Kolkata, India.
Jayati SenguptaStructural Biology and Bioinformatics Division, Council of Scientific and Industrial Research - Indian Institute of Chemical Biology, Kolkata, India jayati@iicb.res.in.ORCID 0000-0003-3614-6047
Indian Institute of Chemical Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in

Indexed as

Adenosine TriphosphatasesEscherichia coliEscherichia coli ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateHeat-Shock ResponseProtein BindingRibosomesRibosome Subunits, Large, BacterialRNARNA HelicasesAdenosine TriphosphatasesEscherichia coli ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateHflX protein, E coliRNARNA Helicases

Identifiers

PMID29930203
PMCPMC6028529
OpenAlexW2809571448

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.