Evidence map›Paper›PMID 22472622›Full record

ReviewNature structural & molecular biology2012

High-resolution structure of infectious prion protein: the final frontier.

Rodrigo Diaz-Espinoza, Claudio Soto

Abstract readReview
In one paragraph

Review in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
–field-weighted citation impact
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

51 citing papers in PubMed.

  1. Article
  2. Excess PrPNature communications · 2023
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Catalytic Amyloids as Novel Synthetic Hydrolases.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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.

Rodrigo Diaz-EspinozaDepartment of Neurology, Mitchell Center for Alzheimer's Disease and Related Brain Disorders, University of Texas Medical School, Houston, Texas, USA.
Claudio Soto

Funding

Cyclic Amplification of Prion Protein MisfoldingR01NS049173 · NINDS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI SOTO, CLAUDIO · 2005 to 2014
$3.2M
NINDS NIH HHS R01NS041973NINDS NIH HHS R01 NS049173
6 · The paper itself

Abstract

Prions are the proteinaceous infectious agents responsible for the transmission of prion diseases. The main or sole component of prions is the misfolded prion protein (PrP(Sc)), which is able to template the conversion of the host's natively folded form of the protein (PrP(C)). The detailed mechanism of prion replication and the high-resolution structure of PrP(Sc) are unknown. The currently available information on PrP(Sc) structure comes mostly from low-resolution biophysical techniques, which have resulted in quite divergent models. Recent advances in the production of infectious prions, using very pure recombinant protein, offer new hope for PrP(Sc) structural studies. This review highlights the importance of, challenges for and recent progress toward elucidating the elusive structure of PrP(Sc), arguably the major pending milestone to reach in understanding prions.

Indexed as

AnimalsHumansModels, MolecularPrion DiseasesProtein FoldingProtein Structure, SecondaryPrPSc ProteinsPrPSc Proteins

Identifiers

PMID22472622
PMCPMC4049221

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.