Evidence map›Paper›PMID 24509692›Full record

ArticlePrion

The GPI-anchoring of PrP: implications in sorting and pathogenesis.

Berta Puig, Hermann Altmeppen, Markus Glatzel

Open access · bronzeAbstract read
In one paragraph

Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

41 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
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  6. Review
  7. Therapeutic Trajectories in Human Prion Diseases.Sub-cellular biochemistry · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Major Surface Antigens in ZoonoticPathogens (Basel, Switzerland) · 2022
    Review
  15. Article
  16. What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022
    Review
  17. Article
  18. Review
  19. Article
  20. Review
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

3 authors at 2 institutions in 2 countries.

Berta Puig
Hermann Altmeppen
Markus Glatzel
Universität Hamburg · DEInstitute of Neuroimmunology of the Slovak Academy of Sciences · SK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cellular prion protein (PrP(C)) is an N-glycosylated GPI-anchored protein usually present in lipid rafts with numerous putative functions. When it changes its conformation to a pathological isoform (then referred to as PrP(Sc)), it is an essential part of the prion, the agent causing fatal and transmissible neurodegenerative prion diseases. There is growing evidence that toxicity and neuronal damage on the one hand and propagation/infectivity on the other hand are two distinct processes of the disease and that the GPI-anchor attachment of PrP(C) and PrP(Sc) plays an important role in protein localization and in neurotoxicity. Here we review how the signal sequence of the GPI-anchor matters in PrP(C) localization, how an altered cellular localization of PrP(C) or differences in GPI-anchor composition can affect prion infection, and we discuss through which mechanisms changes on the anchorage of PrP(C) can modify the disease process.

Indexed as

Protein TransportGlycosylphosphatidylinositolsProtein IsoformsProteolysisPrPC ProteinsSignal TransductionGlycosylphosphatidylinositolsProtein IsoformsPrPC Proteins

Identifiers

PMID24509692
PMCPMC7030901
OpenAlexW2038231428

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.