Evidence map›Paper›PMID 19231987›Full record

ReviewAnnual review of biochemistry2009

Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.

Byron Caughey, Gerald S Baron, Bruce Chesebro, Martin Jeffrey

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 187 papers.

0numbers the graph read from it
0cells of the map it votes in
187citing papers in PubMed
15.2field-weighted citation impact, top 1% 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

187 citing papers in PubMed, 325 citations in OpenAlex.

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  17. The Prion Basis of Progressive Neurodegenerative Disorders.Interdisciplinary perspectives on infectious diseases · 2023
    Review
  18. Review
  19. Review
  20. Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022
    Review

127 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Byron CaugheyLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA. bcaughey@nih.gov
Gerald S Baron
Bruce Chesebro
Martin Jeffrey
National Institutes of Health · USNational Institute of Allergy and Infectious Diseases · US

Funding

Biology of Prion Protein and the TSE DiseasesZIAAI000937 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CHESEBRO, BRUCE · 2009 to 2025
$16.9M
Structures and Activities of Prions and Prion Proteins ZIAAI000580 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CAUGHEY, BYRON · 2009 to 2025
$8.9M
TSE Prion Cell BiologyZIAAI000982 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI BARON, GERALD · 2009 to 2015
$3.7M
Intramural NIH HHS ZIA AI000580
6 · The paper itself

Abstract

The prion (infectious protein) concept has evolved with the discovery of new self-propagating protein states in organisms as diverse as mammals and fungi. The infectious agent of the mammalian transmissible spongiform encephalopathies (TSE) has long been considered the prototypical prion, and recent cell-free propagation and biophysical analyses of TSE infectivity have now firmly established its prion credentials. Other disease-associated protein aggregates, such as some amyloids, can also have prion-like characteristics under certain experimental conditions. However, most amyloids appear to lack the natural transmissibility of TSE prions. One feature that distinguishes the latter from the former is the glycophosphatidylinositol membrane anchor on prion protein, the molecule that is corrupted in TSE diseases. The presence of this anchor profoundly affects TSE pathogenesis, which involves major membrane distortions in the brain, and may be a key reason for the greater neurovirulence of TSE prions relative to many other autocatalytic protein aggregates.

Indexed as

AnimalsBrainHumansPrion DiseasesPrionsProtein FoldingPrions

Identifiers

PMID19231987
PMCPMC2794486
OpenAlexW2138390885

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.