Evidence map›Paper›PMID 19738901›Full record

ArticlePloS one2009

Functionally relevant domains of the prion protein identified in vivo.

Frank Baumann, Jens Pahnke, Ivan Radovanovic, Thomas Rülicke, Juliane Bremer, Markus Tolnay, Adriano Aguzzi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Neurometals in the Pathogenesis of Prion Diseases.International journal of molecular sciences · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. Article
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  8. Review
  9. Membrane-anchored Aβ accelerates amyloid formation and exacerbates amyloid-associated toxicity in mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  10. Ataxia with cerebellar lesions in mice expressing chimeric PrP-Dpl protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
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  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

7 authors at 3 institutions in 3 countries.

Frank BaumannInstitute of Neuropathology, University Hospital of Zurich, Zurich, Switzerland.
Jens Pahnke
Ivan Radovanovic
Thomas Rülicke
Juliane Bremer
Markus Tolnay
Adriano Aguzzi
University Hospital of Zurich · CHHertie Institute for Clinical Brain Research · DEUniversity of Veterinary Medicine Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The prion consists essentially of PrP(Sc), a misfolded and aggregated conformer of the cellular protein PrP(C). Whereas PrP(C) deficient mice are clinically healthy, expression of PrP(C) variants lacking its central domain (PrP(DeltaCD)), or of the PrP-related protein Dpl, induces lethal neurodegenerative syndromes which are repressed by full-length PrP. Here we tested the structural basis of these syndromes by grafting the amino terminus of PrP(C) (residues 1-134), or its central domain (residues 90-134), onto Dpl. Further, we constructed a soluble variant of the neurotoxic PrP(DeltaCD) mutant that lacks its glycosyl phosphatidyl inositol (GPI) membrane anchor. Each of these modifications abrogated the pathogenicity of Dpl and PrP(DeltaCD) in transgenic mice. The PrP-Dpl chimeric molecules, but not anchorless PrP(DeltaCD), ameliorated the disease of mice expressing truncated PrP variants. We conclude that the amino proximal domain of PrP exerts a neurotrophic effect even when grafted onto a distantly related protein, and that GPI-linked membrane anchoring is necessary for both beneficial and deleterious effects of PrP and its variants.

Indexed as

AnimalsCell MembraneGenetic VariationGlycosylphosphatidylinositolsMiceMice, Inbred C57BLMice, TransgenicNeurodegenerative DiseasesNeurotoxinsPhenotypePrion ProteinsPrionsProtein Structure, TertiaryRecombinant Fusion ProteinsSignal TransductionTransgenesGlycosylphosphatidylinositolsNeurotoxinsPrion ProteinsPrionsPrnp protein, mouseRecombinant Fusion Proteins

Identifiers

PMID19738901
PMCPMC2733036
OpenAlexW2065060909

What OpenQuestion holds

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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.