Evidence map›Paper›PMID 32209660›Full record

ArticleThe Journal of biological chemistry2020

The hibernating 100S complex is a target of ribosome-recycling factor and elongation factor G in

Arnab Basu, Kathryn E Shields, Mee-Ngan F Yap

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Structural insights into RNA recognition by theProceedings of the National Academy of Sciences of the United States of America · 2026
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  12. Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. Transcription regulates ribosome hibernation.Molecular microbiology · 2021
    Article
  17. 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 2 institutions in 1 country.

Arnab BasuDepartment of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, Missouri 63104.
Kathryn E ShieldsDepartment of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, Missouri 63104.
Mee-Ngan F YapDepartment of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, Saint Louis, Missouri 63104; Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611. Electronic address: frances.yap@northwestern.edu.
Saint Louis University · USNorthwestern University · US

Funding

Regulation and function of bacterial hibernating 100S ribosomeR01GM121359 · NIGMS · SAINT LOUIS UNIVERSITY · PI YAP, M.-N. FRANCES · 2017 to 2025
$3.2M
NIGMS NIH HHS R01 GM121359
6 · The paper itself

Abstract

The formation of translationally inactive 70S dimers (called 100S ribosomes) by hibernation-promoting factor is a widespread survival strategy among bacteria. Ribosome dimerization is thought to be reversible, with the dissociation of the 100S complexes enabling ribosome recycling for participation in new rounds of translation. The precise pathway of 100S ribosome recycling has been unclear. We previously found that the heat-shock GTPase HflX in the human pathogen

Indexed as

Guanosine TriphosphateModels, MolecularPeptide Elongation Factor GProtein ConformationRibosomal ProteinsRibosomesStaphylococcus aureusGuanosine TriphosphatePeptide Elongation Factor GRibosomal Proteinsribosome releasing factor100S ribosomebacterial persistenceelongation factor G (EF-G)GTPasehibernationribosomeribosome-recycling factor (RRF)Staphylococcus aureus (S. aureus)translation elongation factortranslation regulation

Identifiers

PMID32209660
PMCPMC7196661
OpenAlexW3014008569

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.