Evidence map›Paper›PMID 24493590›Full record

ArticleThe Journal of cell biology2014

Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and webs.

Alexander Rouvinski, Sharon Karniely, Maria Kounin, Sanaa Moussa, Miri D Goldberg, Gabriela Warburg, Roman Lyakhovetsky, Dulce Papy-Garcia, Janine Kutzsche, Carsten Korth and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022
    Review
  10. Review
  11. Article
  12. Neuroinflammation in Prion Disease.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Cellular mechanisms responsible for cell-to-cell spreading of prions.Cellular and molecular life sciences : CMLS · 2018
    Review
  20. Lysosomal Quality Control in Prion Diseases.Molecular neurobiology · 2018
    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

16 authors at 5 institutions in 5 countries.

Alexander RouvinskiDepartment of Microbiology and Molecular Genetics, Institute for Medical Research Israel-Canada, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel.
Sharon Karniely
Maria Kounin
Sanaa Moussa
Miri D Goldberg
Gabriela Warburg
Roman Lyakhovetsky
Dulce Papy-Garcia
Janine Kutzsche
Carsten Korth
George A Carlson
Susan F Godsave
Peter J Peters
Katarina Luhr
Krister Kristensson
Albert Taraboulos
Heinrich Heine University Düsseldorf · DEKarolinska Institutet · SEThe Netherlands Cancer Institute · NLLaboratoire de Recherche sur la Croissance Cellulaire, la Réparation et la Régénération Tissulaires · FRMcLaughlin Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian prions refold host glycosylphosphatidylinositol-anchored PrP(C) into β-sheet-rich PrP(Sc). PrP(Sc) is rapidly truncated into a C-terminal PrP27-30 core that is stable for days in endolysosomes. The nature of cell-associated prions, their attachment to membranes and rafts, and their subcellular locations are poorly understood; live prion visualization has not previously been achieved. A key obstacle has been the inaccessibility of PrP27-30 epitopes. We overcame this hurdle by focusing on nascent full-length PrP(Sc) rather than on its truncated PrP27-30 product. We show that N-terminal PrP(Sc) epitopes are exposed in their physiological context and visualize, for the first time, PrP(Sc) in living cells. PrP(Sc) resides for hours in unexpected cell-surface, slow moving strings and webs, sheltered from endocytosis. Prion strings observed by light and scanning electron microscopy were thin, micrometer-long structures. They were firmly cell associated, resisted phosphatidylinositol-specific phospholipase C, aligned with raft markers, fluoresced with thioflavin, and were rapidly abolished by anti-prion glycans. Prion strings and webs are the first demonstration of membrane-anchored PrP(Sc) amyloids.

Indexed as

Imaging, Three-DimensionalActinsAmyloidAnimalsAntibodiesBenzothiazolesCell SurvivalEndocytosisHippocampusMembrane MicrodomainsMiceModels, BiologicalPhosphoinositide Phospholipase CPolysaccharidesProtein BindingProtein DenaturationActinsAmyloidAntibodiesBenzothiazolesPhosphoinositide Phospholipase CPolysaccharidesPrPSc ProteinsThiazolesthioflavin T

Identifiers

PMID24493590
PMCPMC3912534
OpenAlexW2082672533

What OpenQuestion holds

Textmetadata
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.