Evidence map›Paper›PMID 33349060›Full record

ReviewCritical reviews in biochemistry and molecular biology2021

HEPN RNases - an emerging class of functionally distinct RNA processing and degradation enzymes.

Monica C Pillon, Jacob Gordon, Meredith N Frazier, Robin E Stanley

Abstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. The isolated HEPN domain of SACSIN exhibits RNA-binding activity.Cellular and molecular life sciences : CMLS · 2026
    Article
  3. Article
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  10. Strategies for plant-virus disease management from gene editing to nanotechnology.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025
    Review
  11. Article
  12. Article
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  15. Article
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  18. Review
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  20. Review
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.

Monica C PillonDepartment of Health and Human Services, Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA.ORCID 0000-0001-8571-6873
Jacob GordonDepartment of Health and Human Services, Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA.ORCID 0000-0001-7199-7416
Meredith N FrazierDepartment of Health and Human Services, Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA.ORCID 0000-0003-3205-8832
Robin E StanleyDepartment of Health and Human Services, Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA.ORCID 0000-0002-2106-3102

Funding

Structure and Function of RNA Processing MachinesZIAES103247 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI STANLEY, ROBIN · 2015 to 2025
$22.9M
Defining Environmental Influence on RNA ProcessingR00ES030735 · NIEHS · BAYLOR COLLEGE OF MEDICINE · PI PILLON, MONICA · 2021 to 2023
$747k
Intramural NIH HHS ZIA ES103247NIEHS NIH HHS R00 ES030735
6 · The paper itself

Abstract

HEPN (Higher Eukaryotes and Prokaryotes Nucleotide-binding) RNases are an emerging class of functionally diverse RNA processing and degradation enzymes. Members are defined by a small α-helical bundle encompassing a short consensus RNase motif. HEPN dimerization is a universal requirement for RNase activation as the conserved RNase motifs are precisely positioned at the dimer interface to form a composite catalytic center. While the core HEPN fold is conserved, the organization surrounding the HEPN dimer can support large structural deviations that contribute to their specialized functions. HEPN RNases are conserved throughout evolution and include bacterial HEPN RNases such as CRISPR-Cas and toxin-antitoxin associated nucleases, as well as eukaryotic HEPN RNases that adopt large multi-component machines. Here we summarize the canonical elements of the growing HEPN RNase family and identify molecular features that influence RNase function and regulation. We explore similarities and differences between members of the HEPN RNase family and describe the current mechanisms for HEPN RNase activation and inhibition.

Indexed as

ProteolysisRNA Processing, Post-TranscriptionalAmino Acid SequenceAnimalsCatalytic DomainCRISPR-Cas SystemsEndoribonucleasesHumansProtein Conformation, alpha-HelicalProtein MultimerizationRNA-Binding ProteinsRNA StabilityToxin-Antitoxin SystemsEndoribonucleasesRNA-Binding ProteinsCRISPR-CasEndoribonucleaseHEPNNiKsRNA degradationRNA processingToxin-Antitoxin

Identifiers

PMID33349060
PMCPMC7856873

What OpenQuestion holds

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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.