Evidence map›Paper›PMID 22888099›Full record

ArticleDisease models & mechanisms2013

A yeast model for amyloid-β aggregation exemplifies the role of membrane trafficking and PICALM in cytotoxicity.

Fabien D'Angelo, Hélène Vignaud, Julie Di Martino, Bénédicte Salin, Anne Devin, Christophe Cullin, Christelle Marchal

Open access · goldAbstract read
In one paragraph

Article in Disease models & mechanisms, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 73 citations in OpenAlex.

  1. Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025
    Review
  2. Review
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  4. Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023
    Review
  5. Article
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  7. Article
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  10. Proteome-Scale Mapping of Perturbed Proteostasis in Living Cells.Cold Spring Harbor perspectives in biology · 2020
    Review
  11. Article
  12. Article
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  16. Article
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  18. Recent Insights on Alzheimer's Disease Originating from Yeast Models.International journal of molecular sciences · 2018
    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

7 authors at 2 institutions in 1 country.

Fabien D'AngeloInstitut de Biochimie et Génétique Cellulaires, CNRS UMR 5095, Université Bordeaux 2, Victor Segalen, 33077 Bordeaux, France.
Hélène Vignaud
Julie Di Martino
Bénédicte Salin
Anne Devin
Christophe Cullin
Christelle Marchal
Centre National de la Recherche Scientifique · FRUniversité de Bordeaux · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease is the most common neurodegenerative disease, associated with aggregation of amyloid-β (Aβ) peptides. The exact mechanism of neuronal cell dysfunction in Alzheimer's disease is poorly understood and numerous models have been used to decipher the mechanisms leading to cellular death. Yeast cells might be a good model to understand the intracellular toxicity triggered by Aβ peptides. Indeed, yeast has been used as a model to examine protein functions or cellular pathways that mediate the secretion, aggregation and subsequent toxicity of proteins associated with human neurodegenerative disorders. In the present study, we use the yeast Saccharomyces cerevisiae as a model system to study the effects of intracellular Aβ in fusion with green fluorescent protein. We sent this fusion protein into the secretory pathway and showed that intracellular traffic pathways are necessary for the generation of toxic species. Yeast PICALM orthologs are involved in cellular toxicity, indicating conservation of the mechanisms of toxicity from mammals to yeast. Finally, our model demonstrates the capacity for intracellular Aβ to cross intracellular membranes and target mitochondrial organelles.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBiological Transport, ActiveEndocytosisGreen Fluorescent ProteinsHeat-Shock ProteinsHumansModels, BiologicalModels, NeurologicalMonomeric Clathrin Assembly ProteinsOxygen ConsumptionProtein MultimerizationProtein Processing, Post-TranslationalRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloid beta-PeptidesGreen Fluorescent ProteinsHeat-Shock ProteinsHsP104 protein, S cerevisiaeMonomeric Clathrin Assembly ProteinsPICALM protein, humanRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID22888099
PMCPMC3529352
OpenAlexW2118140245

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.