Evidence map›Paper›PMID 20057357›Full record

ArticleThe EMBO journal2010

GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells.

Jonathan O Speare, Danielle K Offerdahl, Aaron Hasenkrug, Aaron B Carmody, Gerald S Baron

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  7. Review
  8. Cell-to-cell propagation of infectious cytosolic protein aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  9. Review
  10. Review
  11. Seeding plaques in Alzheimer's disease.Journal of neurochemistry · 2012
    Article
  12. Article
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  14. Article
  15. Review
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

Jonathan O SpeareNational Institute of Allergy and Infectious Diseases, National Institutes of Health, Rocky Mountain Laboratories, Laboratory of Persistent Viral Diseases, Hamilton, MT 59840, USA.
Danielle K Offerdahl
Aaron Hasenkrug
Aaron B Carmody
Gerald S Baron
National Institutes of Health · USNational Institute of Allergy and Infectious Diseases · US

Funding

Infectious Diseases Research Technologies Core - RMLZICAI001052 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CHERRY, JAMES · 2009 to 2025
$133.3M
Propagation of Lipid-Anchored Prion AggregatesZIAAI001112 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI BARON, GERALD · 2009 to 2015
$1.3M
Intramural NIH HHS
6 · The paper itself

Abstract

Prion diseases differ from other amyloid-associated protein misfolding diseases (e.g. Alzheimer's) because they are naturally transmitted between individuals and involve spread of protein aggregation between tissues. Factors underlying these features of prion diseases are poorly understood. Of all protein misfolding disorders, only prion diseases involve the misfolding of a glycosylphosphatidylinositol (GPI)-anchored protein. To test whether GPI anchoring can modulate the propagation and spread of protein aggregates, a GPI-anchored version of the amyloidogenic yeast protein Sup35NM (Sup35GPI) was expressed in neuronal cells. Treatment of cells with Sup35NM fibrils induced the GPI anchor-dependent formation of self-propagating, detergent-insoluble, protease-resistant, prion-like aggregates of Sup35GPI. Live-cell imaging showed intercellular spread of Sup35GPI aggregation to involve contact between aggregate-positive and aggregate-negative cells and transfer of Sup35GPI from aggregate-positive cells. These data demonstrate GPI anchoring facilitates the propagation and spread of protein aggregation and thus may enhance the transmissibility and pathogenesis of prion diseases relative to other protein misfolding diseases.

Indexed as

AnimalsCell LineGlycosylphosphatidylinositolsGreen Fluorescent ProteinsMiceNeuronsPeptide Termination FactorsPrionsProtein FoldingProtein MultimerizationRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransfectionGlycosylphosphatidylinositolsGreen Fluorescent ProteinsPeptide Termination FactorsPrionsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID20057357
PMCPMC2829165
OpenAlexW2056585385

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.