Evidence map›Paper›PMID 33068411›Full record

ReviewNucleic acids research2020

RNA as the stone guest of protein aggregation.

Alexandra Louka, Elsa Zacco, Piero Andrea Temussi, Gian Gaetano Tartaglia, Annalisa Pastore

Open access · goldAbstract readReview
In one paragraph

Review in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
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  17. Article
  18. Nuclear Organization in Response to Stress: A Special Focus on Nucleoli.Results and problems in cell differentiation · 2022
    Article
  19. Article
  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

5 authors at 3 institutions in 3 countries.

Alexandra LoukaUK Dementia Research Institute at the Maurice Wohl Institute of King's College London, London SE5 9RT, UK.
Elsa ZaccoCenter for Human Technologies, Central RNA laboratory, Istituto Italiano di Tecnologia, Genova 16152, Italy.
Piero Andrea TemussiUK Dementia Research Institute at the Maurice Wohl Institute of King's College London, London SE5 9RT, UK.
Gian Gaetano TartagliaCenter for Human Technologies, Central RNA laboratory, Istituto Italiano di Tecnologia, Genova 16152, Italy.
Annalisa PastoreUK Dementia Research Institute at the Maurice Wohl Institute of King's College London, London SE5 9RT, UK.
King's College London · GBInstitució Catalana de Recerca i Estudis Avançats · ESItalian Institute of Technology · IT

Funding

Medical Research Council MC_PC_13054Motor Neurone Disease Association PASTORE/APR15/840-791
6 · The paper itself

Abstract

The study of prions as infectious aggregates dates several decades. From its original formulation, the definition of a prion has progressively changed to the point that many aggregation-prone proteins are now considered bona fide prions. RNA molecules, not included in the original 'protein-only hypothesis', are also being recognized as important factors contributing to the 'prion behaviour', that implies the transmissibility of an aberrant fold. In particular, an association has recently emerged between aggregation and the assembly of prion-like proteins in RNA-rich complexes, associated with both physiological and pathological events. Here, we discuss the historical rising of the concept of prion-like domains, their relation to RNA and their role in protein aggregation. As a paradigmatic example, we present the case study of TDP-43, an RNA-binding prion-like protein associated with amyotrophic lateral sclerosis. Through this example, we demonstrate how the current definition of prions has incorporated quite different concepts making the meaning of the term richer and more stimulating. An important message that emerges from our analysis is the dual role of RNA in protein aggregation, making RNA, that has been considered for many years a 'silent presence' or the 'stone guest' of protein aggregation, an important component of the process.

Indexed as

Amyotrophic Lateral SclerosisBinding SitesDNA-Binding ProteinsGene ExpressionHumansModels, MolecularPrionsProtein AggregatesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsRNARNA-Binding Protein FUSRNA-Binding ProteinsTATA-Binding Protein Associated FactorsDNA-Binding ProteinsFUS protein, humanPrionsProtein AggregatesRNARNA-Binding Protein FUSRNA-Binding ProteinsTAF15 protein, humanTARDBP protein, humanTATA-Binding Protein Associated Factors

Identifiers

PMID33068411
PMCPMC7708036
OpenAlexW3092767112

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.