Evidence map›Paper›PMID 24769839›Full record

ArticleThe Journal of general virology2014

Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, α-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys.

Pedro Piccardo, Juraj Cervenak, Ming Bu, Lindsay Miller, David M Asher

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of general virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

4 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Aggregation of MBP in chronic demyelination.Annals of clinical and translational neurology · 2015
    Article
  4. 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 1 institution in 1 country.

Pedro PiccardoLaboratory of Bacterial and TSE Agents, Division of Emerging Transfusion Transmitted Diseases, Office of Blood Research and Review, Center for Biologics Evaluation and Research, Food and Drug Administration, 1401 Rockville Pike, HFM-313, Rockville, MD 20852, USA.
Juraj CervenakLaboratory of Bacterial and TSE Agents, Division of Emerging Transfusion Transmitted Diseases, Office of Blood Research and Review, Center for Biologics Evaluation and Research, Food and Drug Administration, 1401 Rockville Pike, HFM-313, Rockville, MD 20852, USA.
Ming BuLaboratory of Bacterial and TSE Agents, Division of Emerging Transfusion Transmitted Diseases, Office of Blood Research and Review, Center for Biologics Evaluation and Research, Food and Drug Administration, 1401 Rockville Pike, HFM-313, Rockville, MD 20852, USA.
Lindsay MillerLaboratory of Bacterial and TSE Agents, Division of Emerging Transfusion Transmitted Diseases, Office of Blood Research and Review, Center for Biologics Evaluation and Research, Food and Drug Administration, 1401 Rockville Pike, HFM-313, Rockville, MD 20852, USA.
David M AsherLaboratory of Bacterial and TSE Agents, Division of Emerging Transfusion Transmitted Diseases, Office of Blood Research and Review, Center for Biologics Evaluation and Research, Food and Drug Administration, 1401 Rockville Pike, HFM-313, Rockville, MD 20852, USA.
Center for Biologics Evaluation and Research · US

Funding

Biotechnology and Biological Sciences Research Council BBS/E/D/20251967Biotechnology and Biological Sciences Research Council BBS/E/D/20251968NIAID NIH HHS Y01 AI004893NIAID NIH HHS Y1-AI-4893-02
6 · The paper itself

Abstract

Proteins aggregate in several slowly progressive neurodegenerative diseases called 'proteinopathies'. Studies with cell cultures and transgenic mice overexpressing mutated proteins suggested that aggregates of one protein induced misfolding and aggregation of other proteins as well - a possible common mechanism for some neurodegenerative diseases. However, most proteinopathies are 'sporadic', without gene mutation or overexpression. Thus, proteinopathies in WT animals genetically close to humans might be informative. Squirrel monkeys infected with the classical bovine spongiform encephalopathy agent developed an encephalopathy resembling variant Creutzfeldt-Jakob disease with accumulations not only of abnormal prion protein (PrP(TSE)), but also three other proteins: hyperphosphorylated tau (p-tau), α-synuclein and ubiquitin; β-amyloid protein (Aβ) did not accumulate. Severity of brain lesions correlated with spongiform degeneration. No amyloid was detected. These results suggested that PrP(TSE) enhanced formation of p-tau and aggregation of α-synuclein and ubiquitin, but not Aβ, providing a new experimental model for neurodegenerative diseases associated with complex proteinopathies.

Indexed as

alpha-SynucleinAnimalsBrainCattleDisease Models, AnimalEncephalopathy, Bovine SpongiformPrionsSaimiritau ProteinsUbiquitinalpha-SynucleinPrionstau ProteinsUbiquitin

Identifiers

PMID24769839
PMCPMC4059271
OpenAlexW2032193472

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.