Evidence map›Paper›PMID 24675871›Full record

ArticleScientific reports2014

Increased expression of p62/SQSTM1 in prion diseases and its association with pathogenic prion protein.

Takujiro Homma, Daisuke Ishibashi, Takehiro Nakagaki, Katsuya Satoh, Kazunori Sano, Ryuichiro Atarashi, Noriyuki Nishida

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 50 citations in OpenAlex.

  1. CpG oligodeoxynucleotide reduces PrPMolecules and cells · 2026
    Article
  2. Article
  3. Frontiers in neuroscience · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. An Update on Autophagy in Prion Diseases.Frontiers in bioengineering and biotechnology · 2020
    Review
  14. Impairment of autophagy in scrapie-infected transgenic mice at the clinical stage.Laboratory investigation; a journal of technical methods and pathology · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Lysosomal Quality Control in Prion Diseases.Molecular neurobiology · 2018
    Review
  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

7 authors at 1 institution in 1 country.

Takujiro HommaDepartment of Molecular Microbiology and immunology, Graduate School of Biomedical sciences, Nagasaki University, Nagasaki 852-8523, Japan.
Daisuke IshibashiDepartment of Molecular Microbiology and immunology, Graduate School of Biomedical sciences, Nagasaki University, Nagasaki 852-8523, Japan.
Takehiro NakagakiDepartment of Molecular Microbiology and immunology, Graduate School of Biomedical sciences, Nagasaki University, Nagasaki 852-8523, Japan.
Katsuya SatohDepartment of Molecular Microbiology and immunology, Graduate School of Biomedical sciences, Nagasaki University, Nagasaki 852-8523, Japan.
Kazunori SanoDepartment of Molecular Microbiology and immunology, Graduate School of Biomedical sciences, Nagasaki University, Nagasaki 852-8523, Japan.
Ryuichiro Atarashi1] Department of Molecular Microbiology and immunology, Graduate School of Biomedical sciences, Nagasaki University, Nagasaki 852-8523, Japan [2] Nagasaki University Research Centre for Genomic Instability and Carcinogenesis, Nagasaki 852-8523, Japan.
Noriyuki NishidaDepartment of Molecular Microbiology and immunology, Graduate School of Biomedical sciences, Nagasaki University, Nagasaki 852-8523, Japan.
Nagasaki University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prion diseases are neurodegenerative disorders characterized by the aggregation of abnormally folded prion protein (PrP(Sc)). In this study, we focused on the mechanism of clearance of PrP(Sc), which remains unclear. p62 is a cytosolic protein known to mediate both the formation and degradation of aggregates of abnormal proteins. The levels of p62 protein increased in prion-infected brains and persistently infected cell cultures. Upon proteasome inhibition, p62 co-localized with PrP(Sc), forming a large aggregate in the perinuclear region, hereafter referred to as PrP(Sc)-aggresome. These aggregates were surrounded with autophagosome marker LC3 and lysosomes in prion-infected cells. Moreover, transient expression of the phosphomimic form of p62, which has enhanced ubiquitin-binding activity, reduced the amount of PrP(Sc) in prion-infected cells, indicating that the activation of p62 could accelerate the clearance of PrP(Sc). Our findings would thus suggest that p62 could be a target for the therapeutic control of prion diseases.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsBrainCell Line, TumorDisease Models, AnimalGene ExpressionHeat-Shock ProteinsLysosomesMicePrion DiseasesPrionsProtein Aggregation, PathologicalProtein BindingProtein TransportProteolysisPrPSc ProteinsAdaptor Proteins, Signal TransducingHeat-Shock ProteinsPrionsPrPSc ProteinsSequestosome-1 ProteinSqstm1 protein, mouseUbiquitin

Identifiers

PMID24675871
PMCPMC3968452
OpenAlexW2126646764

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.