Evidence map›Paper›PMID 32165583›Full record

ArticleScience (New York, N.Y.)2020

Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in

Ruben Hervas, Michael J Rau, Younshim Park, Wenjuan Zhang, Alexey G Murzin, James A J Fitzpatrick, Sjors H W Scheres, Kausik Si

Open access · bronzeAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
14.9field-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

113 citing papers in PubMed, 200 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Review
  9. Article
  10. A J-domain protein enhances memory by promoting physiological amyloid formation inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Review
  13. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

53 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Ruben HervasStowers Institute for Medical Research, Kansas City, MO 64110, USA.ORCID 0000-0001-6393-6058
Michael J RauWashington University Center for Cellular Imaging, Washington University School of Medicine, St. Louis, MO 63110, USA.ORCID 0000-0001-5170-2000
Younshim ParkStowers Institute for Medical Research, Kansas City, MO 64110, USA.ORCID 0000-0001-6364-2383
Wenjuan ZhangMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Alexey G MurzinMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
James A J FitzpatrickWashington University Center for Cellular Imaging, Washington University School of Medicine, St. Louis, MO 63110, USA.ORCID 0000-0002-7907-3602
Sjors H W ScheresMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.ORCID 0000-0002-0462-6540
Kausik SiStowers Institute for Medical Research, Kansas City, MO 64110, USA. ksi@stowers.org.ORCID 0000-0002-9613-6273
MRC Laboratory of Molecular Biology · GBStowers Institute for Medical Research · USWashington University in St. Louis · US

Funding

Structure and function of mammalian CPEB2 aggregates in normal and AD brainR01AG066189 · NIA · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI SI, KAUSIK · 2021 to 2025
$2.2M
Medical Research Council MC_UP_A025_1013NIA NIH HHS R01 AG066189UK Medical Research
6 · The paper itself

Abstract

How long-lived memories withstand molecular turnover is a fundamental question. Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element-binding (CPEB) protein, is a putative substrate of long-lasting memories. We isolated aggregated

Indexed as

Memory, Long-TermProtein AggregatesAmyloidAnimalsCryoelectron MicroscopyDrosophila melanogasterDrosophila ProteinsGlutamineHydrophobic and Hydrophilic InteractionsmRNA Cleavage and Polyadenylation FactorsNeuronsProtein ConformationRNA-Binding ProteinsTranscription FactorsAmyloidDrosophila ProteinsGlutaminemRNA Cleavage and Polyadenylation FactorsOrb2 protein, DrosophilaProtein AggregatesRNA-Binding ProteinsTranscription Factors

Identifiers

PMID32165583
PMCPMC7182444
OpenAlexW3011713314

What OpenQuestion holds

Textmetadata
LicenceTDM
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.