Evidence map›Paper›PMID 29676248›Full record

ReviewMicrobiology spectrum2018

RNase E and the High-Fidelity Orchestration of RNA Metabolism.

Katarzyna J Bandyra, Ben F Luisi

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology spectrum, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
27.5field-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

40 citing papers in PubMed, 183 citations in OpenAlex.

  1. Article
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  4. Review
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  18. Article
  19. Review
  20. Target recognition by RNase E RNA-binding domain AR2 drives sRNA decay in the absence of PNPase.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

2 authors at 1 institution in 1 country.

Katarzyna J BandyraDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
University of Cambridge · GB

Funding

Wellcome Trust 200873/Z/16/Z
6 · The paper itself

Abstract

The bacterial endoribonuclease RNase E occupies a pivotal position in the control of gene expression, as its actions either commit transcripts to an irreversible fate of rapid destruction or unveil their hidden functions through specific processing. Moreover, the enzyme contributes to quality control of rRNAs. The activity of RNase E can be directed and modulated by signals provided through regulatory RNAs that guide the enzyme to specific transcripts that are to be silenced. Early in its evolutionary history, RNase E acquired a natively unfolded appendage that recruits accessory proteins and RNA. These accessory factors facilitate the activity of RNase E and include helicases that remodel RNA and RNA-protein complexes, and polynucleotide phosphorylase, a relative of the archaeal and eukaryotic exosomes. RNase E also associates with enzymes from central metabolism, such as enolase and aconitase. RNase E-based complexes are diverse in composition, but generally bear mechanistic parallels with eukaryotic machinery involved in RNA-induced gene regulation and transcript quality control. That these similar processes arose independently underscores the universality of RNA-based regulation in life. Here we provide a synopsis and perspective of the contributions made by RNase E to sustain robust gene regulation with speed and accuracy.

Indexed as

Evolution, MolecularGene Expression Regulation, BacterialAconitate HydrataseArchaeaBacteriaEndoribonucleasesEukaryotic CellsExosomesPhosphopyruvate HydratasePolyribonucleotide NucleotidyltransferaseRNA, BacterialRNA HelicasesRNA Processing, Post-TranscriptionalAconitate HydrataseEndoribonucleasesPhosphopyruvate HydratasePolyribonucleotide Nucleotidyltransferaseribonuclease ERNA, BacterialRNA Helicases

Identifiers

PMID29676248
PMCPMC11633573
OpenAlexW2802607766

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.