Evidence map›Paper›PMID 21030659›Full record

ArticleScience (New York, N.Y.)2010

A size threshold limits prion transmission and establishes phenotypic diversity.

Aaron Derdowski, Suzanne S Sindi, Courtney L Klaips, Susanne DiSalvo, Tricia R Serio

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 100 citations in OpenAlex.

  1. Multiple aspects of amyloid dynamicsFrontiers in molecular neuroscience · 2024
    Article
  2. Measuring prion propagation in single bacteria elucidates a mechanism of loss.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  19. Study of Amyloids Using Yeast.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  20. Article

3 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

5 authors at 1 institution in 1 country.

Aaron DerdowskiDepartment of Molecular Biology, Cell Biology and Biochemistry, Brown University, 185 Meeting Street, Post Office Box G-L2, Providence, RI 02912, USA.
Suzanne S Sindi
Courtney L Klaips
Susanne DiSalvo
Tricia R Serio
Brown University · US

Funding

TRAINING IN MOLECULAR &CELL BIOLOGY &BIOCHEMISTRYT32GM007601 · NIGMS · BROWN UNIVERSITY · PI MOWRY, KIMBERLY L. · 1985 to 2019
$6.4M
Prion Cycle Regulation In VivoR01GM069802 · NIGMS · UNIVERSITY OF ARIZONA · PI SERIO, TRICIA R. · 2006 to 2014
$2.7M
Modeling Prion DynamicsF32GM089049 · NIGMS · BROWN UNIVERSITY · PI SINDI, SUZANNE · 2009 to 2011
$145k
Investigating the Mechanism of Sup35 Prion Curing by Excess Hsp104F31AG034754 · NIA · BROWN UNIVERSITY · PI KLAIPS, COURTNEY LEE · 2009 to 2011
$82k
Investigating the Mechanism of Prion Curing by [PSI+] No More MutationsF31AG032818 · NIA · BROWN UNIVERSITY · PI DISALVO, SUSANNE · 2008 to 2010
$81k
Role of the Actin Cytoskeleton in Yeast Prion PropagationF32GM085976 · NIGMS · BROWN UNIVERSITY · PI DERDOWSKI, AARON · 2008 to 2009
$72k
NIA NIH HHS AG032818NIA NIH HHS AG034754NIGMS NIH HHS GM069802NIGMS NIH HHS GM085976NIGMS NIH HHS GM089049NIGMS NIH HHS R01 GM069802NIGMS NIH HHS T32 GM007601
6 · The paper itself

Abstract

According to the prion hypothesis, atypical phenotypes arise when a prion protein adopts an alternative conformation and persist when that form assembles into self-replicating aggregates. Amyloid formation in vitro provides a model for this protein-misfolding pathway, but the mechanism by which this process interacts with the cellular environment to produce transmissible phenotypes is poorly understood. Using the yeast prion Sup35/[PSI(+)], we found that protein conformation determined the size distribution of aggregates through its interactions with a molecular chaperone. Shifts in this range created variations in aggregate abundance among cells because of a size threshold for transmission, and this heterogeneity, along with aggregate growth and fragmentation, induced age-dependent fluctuations in phenotype. Thus, prion conformations may specify phenotypes as population averages in a dynamic system.

Indexed as

AlgorithmsCell DivisionComputer SimulationPeptide Termination FactorsPhenotypePrionsProtein ConformationProtein FoldingRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPeptide Termination FactorsPrionsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiae

Identifiers

PMID21030659
PMCPMC3003433
OpenAlexW2036404841

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.