Evidence map›Paper›PMID 27226089›Full record

ReviewClinical microbiology reviews2016

Prions: Beyond a Single Protein.

Alvin S Das, Wen-Quan Zou

Open access · bronzeAbstract readReview
In one paragraph

Review in Clinical microbiology reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Upregulated PrPNPJ precision oncology · 2024
    Article
  3. Article
  4. RNA-Seq Analysis of Mammalian Prion Disease.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Direct interaction of DNMT inhibitors to PrPActa pharmaceutica Sinica. B · 2019
    Article
  19. Proteasome Activation to Combat Proteotoxicity.Molecules (Basel, Switzerland) · 2019
    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

2 authors at 1 institution in 1 country.

Alvin S DasDepartments of Pathology and Neurology, National Prion Disease Pathology Surveillance Center, National Center for Regenerative Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Wen-Quan ZouDepartments of Pathology and Neurology, National Prion Disease Pathology Surveillance Center, National Center for Regenerative Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA wxz6@case.edu.
Case Western Reserve University · US

Funding

Pathogenicity of prion protein aggregates from uninfected cells and brainsR01NS062787 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI ZOU, WEN-QUAN · 2009 to 2013
$1.4M
Generating iPSC-derived Neurons to Explore Formation & Inhibition of Human PrionsR21NS087588 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI QI, XIN, TESAR, PAUL JOSEPH · 2014 to 2015
$436k
Accessing transmissibility and diagnostic marker of skin prions.R21NS096626 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI KONG, QINGZHONG, SAFAR, JIRI G. · 2016 to 2017
$436k
NINDS NIH HHS NS062787NINDS NIH HHS NS087588NINDS NIH HHS NS096626NINDS NIH HHS R01 NS062787NINDS NIH HHS R21 NS087588NINDS NIH HHS R21 NS096626
6 · The paper itself

Abstract

Since the term protein was first coined in 1838 and protein was discovered to be the essential component of fibrin and albumin, all cellular proteins were presumed to play beneficial roles in plants and mammals. However, in 1967, Griffith proposed that proteins could be infectious pathogens and postulated their involvement in scrapie, a universally fatal transmissible spongiform encephalopathy in goats and sheep. Nevertheless, this novel hypothesis had not been evidenced until 1982, when Prusiner and coworkers purified infectious particles from scrapie-infected hamster brains and demonstrated that they consisted of a specific protein that he called a "prion." Unprecedentedly, the infectious prion pathogen is actually derived from its endogenous cellular form in the central nervous system. Unlike other infectious agents, such as bacteria, viruses, and fungi, prions do not contain genetic materials such as DNA or RNA. The unique traits and genetic information of prions are believed to be encoded within the conformational structure and posttranslational modifications of the proteins. Remarkably, prion-like behavior has been recently observed in other cellular proteins-not only in pathogenic roles but also serving physiological functions. The significance of these fascinating developments in prion biology is far beyond the scope of a single cellular protein and its related disease.

Indexed as

AnimalsHumansPrion ProteinsPrionsPrion ProteinsPrions

Identifiers

PMID27226089
PMCPMC4978610
OpenAlexW2406357427

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.