Evidence map›Paper›PMID 25419621›Full record

ReviewViruses2014

Cholesterol balance in prion diseases and Alzheimer's disease.

Samia Hannaoui, Su Yeon Shim, Yo Ching Cheng, Erica Corda, Sabine Gilch

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Parkinson's Disease: A Prionopathy?International journal of molecular sciences · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. 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

5 authors at 1 institution in 1 country.

Samia HannaouiDepartment of Ecosystem and Public Health, Faculty of Veterinary Medicine, and Hotchkiss Brain Institute, University of Calgary, 3280 Hospital Drive Northwest, Calgary, AB T2N 4Z6, Canada. shannaou@ucalgary.ca.
Su Yeon ShimDepartment of Ecosystem and Public Health, Faculty of Veterinary Medicine, and Hotchkiss Brain Institute, University of Calgary, 3280 Hospital Drive Northwest, Calgary, AB T2N 4Z6, Canada. syshim@ucalgary.ca.
Yo Ching ChengDepartment of Ecosystem and Public Health, Faculty of Veterinary Medicine, and Hotchkiss Brain Institute, University of Calgary, 3280 Hospital Drive Northwest, Calgary, AB T2N 4Z6, Canada. ycchen@ucalgary.ca.
Erica CordaDepartment of Ecosystem and Public Health, Faculty of Veterinary Medicine, and Hotchkiss Brain Institute, University of Calgary, 3280 Hospital Drive Northwest, Calgary, AB T2N 4Z6, Canada. ecorda@ucalgary.ca.
Sabine GilchDepartment of Ecosystem and Public Health, Faculty of Veterinary Medicine, and Hotchkiss Brain Institute, University of Calgary, 3280 Hospital Drive Northwest, Calgary, AB T2N 4Z6, Canada. sgilch@ucalgary.ca.
University of Calgary · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prion diseases are transmissible and fatal neurodegenerative disorders of humans and animals. They are characterized by the accumulation of PrPSc, an aberrantly folded isoform of the cellular prion protein PrPC, in the brains of affected individuals. PrPC is a cell surface glycoprotein attached to the outer leaflet of the plasma membrane by a glycosyl-phosphatidyl-inositol (GPI) anchor. Specifically, it is associated with lipid rafts, membrane microdomains enriched in cholesterol and sphinoglipids. It has been established that inhibition of endogenous cholesterol synthesis disturbs lipid raft association of PrPC and prevents PrPSc accumulation in neuronal cells. Additionally, prion conversion is reduced upon interference with cellular cholesterol uptake, endosomal export, or complexation at the plasma membrane. Altogether, these results demonstrate on the one hand the importance of cholesterol for prion propagation. On the other hand, growing evidence suggests that prion infection modulates neuronal cholesterol metabolism. Similar results were reported in Alzheimer's disease (AD): whereas amyloid β peptide formation is influenced by cellular cholesterol, levels of cholesterol in the brains of affected individuals increase during the clinical course of the disease. In this review, we summarize commonalities of alterations in cholesterol homeostasis and discuss consequences for neuronal function and therapy of prion diseases and AD.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBrainCholesterolHumansPrion DiseasesPrionsProtein FoldingAmyloid beta-PeptidesCholesterolPrions

Identifiers

PMID25419621
PMCPMC4246236
OpenAlexW2058045419

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.