Evidence map›Paper›PMID 34670846›Full record

ReviewRNA (New York, N.Y.)2022

Are stress granules the RNA analogs of misfolded protein aggregates?

Nina Ripin, Roy Parker

Abstract readReview
In one paragraph

Review in RNA (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
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  6. Review
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  8. Protein-RNA condensation kinetics via filamentous nanoclusters.Protein science : a publication of the Protein Society · 2025
    Article
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  14. Review
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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.

Nina RipinDepartment of Biochemistry and Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, Colorado 80303, USA.ORCID 0000-0001-6099-6506
Roy ParkerDepartment of Biochemistry and Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, Colorado 80303, USA.ORCID 0000-0002-8412-4152

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Ribonucleoprotein granules are ubiquitous features of eukaryotic cells. Several observations argue that the formation of at least some RNP granules can be considered analogous to the formation of unfolded protein aggregates. First, unfolded protein aggregates form from the exposure of promiscuous protein interaction surfaces, while some mRNP granules form, at least in part, by promiscuous intermolecular RNA-RNA interactions due to exposed RNA surfaces when mRNAs are not engaged with ribosomes. Second, analogous to the role of protein chaperones in preventing misfolded protein aggregation, cells contain abundant "RNA chaperones" to limit inappropriate RNA-RNA interactions and prevent mRNP granule formation. Third, analogous to the role of protein aggregates in diseases, situations where RNA aggregation exceeds the capacity of RNA chaperones to disaggregate RNAs may contribute to human disease. Understanding that RNP granules can be considered as promiscuous, reversible RNA aggregation events allow insight into their composition and how cells have evolved functions for RNP granules.

Indexed as

Biomolecular CondensatesEukaryotaEukaryotic CellsEukaryotic Initiation Factor-4AFlocculationHeat-Shock ProteinsMolecular ChaperonesPeptide Chain Initiation, TranslationalProtein AggregatesProtein FoldingRibonucleoproteinsRibosomesRNA, MessengerStress GranulesEukaryotic Initiation Factor-4AHeat-Shock ProteinsMolecular ChaperonesProtein AggregatesRibonucleoproteinsRNA, MessengereIF4ARNA aggregatesRNA chaperonesstress granules

Identifiers

PMID34670846
PMCPMC8675284

What OpenQuestion holds

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Registered trials

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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.