Evidence map›Paper›PMID 20826672›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2010

Prion strain interactions are highly selective.

K Peter R Nilsson, Shivanjali Joshi-Barr, Olivia Winson, Christina J Sigurdson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Prion Strain Diversity.Cold Spring Harbor perspectives in medicine · 2016
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  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

4 authors at 3 institutions in 2 countries.

K Peter R NilssonDepartment of Physics, Chemistry, and Biology, Linköping University, Linköping, Sweden.
Shivanjali Joshi-Barr
Olivia Winson
Christina J Sigurdson
University of California, San Diego · USLinköping University · SEUniversity of California, Davis · US

Funding

Vaccines and Diagnostics TrialsU54AI065359 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI BARBOUR, ALAN G. · 2005 to 2013
$88.8M
Infectious prion generation by mouse transgenesisR21NS055116 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SIGURDSON, CHRISTINA · 2007 to 2009
$338k
NIAID NIH HHS U54 AI065359NIAID NIH HHS U54AI065359NINDS NIH HHS NS055116NINDS NIH HHS R21 NS055116
6 · The paper itself

Abstract

Various misfolded and aggregated neuronal proteins commonly coexist in neurodegenerative disease, but whether the proteins coaggregate and alter the disease pathogenesis is unclear. Here, we used mixtures of distinct prion strains, which are believed to differ in conformation, to test the hypothesis that two different aggregates interact and change the disease in vivo. We tracked two prion strains in mice histopathologically and biochemically, as well as by spectral analysis of plaque-bound PTAA (polythiophene acetic acid), a conformation-sensitive fluorescent amyloid ligand. We found that prion strains interacted in a highly selective and strain-specific manner, with (1) no interaction, (2) hybrid plaque formation, or (3) blockage of one strain by a second (interference). The hybrid plaques were maintained on additional passage in vivo and each strain seemed to maintain its original conformational properties, suggesting that one strain served only as a scaffold for aggregation of the second strain. These findings not only further our understanding of prion strain interactions but also directly demonstrate interactions that may occur in other protein aggregate mixtures.

Indexed as

AmyloidAnimalsBrainCattleDisease Models, AnimalEncephalopathy, Bovine SpongiformFemaleGlial Fibrillary Acidic ProteinMaleMiceMice, TransgenicPolymersPrion DiseasesPrionsProtein Structure, QuaternarySaccharomyces cerevisiae ProteinsAmyloidGlial Fibrillary Acidic ProteinPolymerspolythiophenePrionsSaccharomyces cerevisiae ProteinsThiophenes

Identifiers

PMID20826672
PMCPMC2951977
OpenAlexW2158945073

What OpenQuestion holds

Textmetadata
LicenceTDM
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.