Evidence map›Paper›PMID 27037416›Full record

ReviewCold Spring Harbor perspectives in biology2016

The Role of Functional Prion-Like Proteins in the Persistence of Memory.

Kausik Si, Eric R Kandel

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Effect of the aggregated protein dye YAT2150 onAntimicrobial agents and chemotherapy · 2024
    Article
  11. Review
  12. Inhibition ofeLife · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. The elusive transcriptional memory trace.Oxford open neuroscience · 2022
    Review
  19. Review
  20. 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 2 institutions in 1 country.

Kausik SiStowers Institute for Medical Research, Kansas City, Missouri 64113 Department of Physiology, School of Medicine, University of Kansas Medical Center, Kansas City, Kansas 66160.
Eric R KandelHoward Hughes Medical Institute, Chevy Chase, Maryland 20815-6789 Departments of Neuroscience and Psychiatry, College of Physicians and Surgeons of Columbia University, New York, New York 10027 Zuckerman Mind Brain Behavior Institute, New York State Psychiatric Institute, New York, New York 10032 Kavli Institute for Brain Sciences, New York, New York 10032.
Columbia University · USStowers Institute for Medical Research · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Prions are a self-templating amyloidogenic state of normal cellular proteins, such as prion protein (PrP). They have been identified as the pathogenic agents, contributing to a number of diseases of the nervous system. However, the discovery that the neuronal RNA-binding protein, cytoplasmic polyadenylation element-binding protein (CPEB), has a prion-like state that is involved in the stabilization of memory raised the possibility that prion-like proteins can serve normal physiological functions in the nervous system. Here, we review recent experimental evidence of prion-like properties of neuronal CPEB in various organisms and propose a model of how the prion-like state may stabilize memory.

Indexed as

Models, BiologicalAnimalsCyclic AMP Response Element-Binding ProteinDrosophilaDrosophila ProteinsHippocampusMemorymRNA Cleavage and Polyadenylation FactorsPrion ProteinsProtein BiosynthesisSumoylationSynapsesTranscription FactorsUbiquitinationCPEB1 protein, humanCREB1 protein, humanCyclic AMP Response Element-Binding ProteinDrosophila ProteinsmRNA Cleavage and Polyadenylation FactorsOrb2 protein, DrosophilaPrion ProteinsTranscription Factors

Identifiers

PMID27037416
PMCPMC4817803
OpenAlexW2326995445

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.