Evidence map›Paper›PMID 39139213›Full record

ArticleFrontiers in molecular neuroscience2024

Multiple aspects of amyloid dynamics

Jennifer Norton, Nicole Seah, Fabian Santiago, Suzanne S Sindi, Tricia R Serio

Abstract read
In one paragraph

Article in Frontiers in molecular neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Chemical reviews · 2026
    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

5 authors.

Jennifer NortonDepartment of Molecular and Cellular Biology, The University of Arizona, Tucson, AZ, United States.
Nicole SeahDepartment of Biochemistry, The University of Washington, Seattle, WA, United States.
Fabian SantiagoDepartment of Applied Mathematics, The University of California, Merced, Merced, CA, United States.
Suzanne S SindiDepartment of Applied Mathematics, The University of California, Merced, Merced, CA, United States.
Tricia R SerioDepartment of Biochemistry, The University of Washington, Seattle, WA, United States.

Funding

Cellular Mechanisms and Consequences of Protein Misfolding and ResolutionR35GM118042 · NIGMS · UNIVERSITY OF WASHINGTON · PI SERIO, TRICIA R. · 2016 to 2025
$3.3M
Mathematical Strategies to Uncover the Molecular Basis of Prion Transitions R01GM126548 · NIGMS · UNIVERSITY OF CALIFORNIA, MERCED · PI SINDI, SUZANNE · 2017 to 2020
$854k
NIGMS NIH HHS R01 GM126548NIGMS NIH HHS R35 GM118042
6 · The paper itself

Abstract

Prion variants are self-perpetuating conformers of a single protein that assemble into amyloid fibers and confer unique phenotypic states. Multiple prion variants can arise, particularly in response to changing environments, and interact within an organism. These interactions are often competitive, with one variant establishing phenotypic dominance over the others. This dominance has been linked to the competition for non-prion state protein, which must be converted to the prion state via a nucleated polymerization mechanism. However, the intrinsic rates of conversion, determined by the conformation of the variant, cannot explain prion variant dominance, suggesting a more complex interaction. Using the yeast prion system [

Indexed as

amyloidchaperoneHsp104prionSUP35variant competition

Identifiers

PMID39139213
PMCPMC11319303

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.