Evidence map›Paper›PMID 25591151›Full record

ArticleJournal of visualized experiments : JoVE2015

Investigating the spreading and toxicity of prion-like proteins using the metazoan model organism C. elegans.

Carmen I Nussbaum-Krammer, Mário F Neto, Renée M Brielmann, Jesper S Pedersen, Richard I Morimoto

Abstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

120 citing papers in PubMed, 188 citations in OpenAlex.

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  10. Ubiquitin Proteasome System Components, RAD23A and USP13, Modulate TDP-43 Solubility and Neuronal Toxicity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
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  20. Rescue of a Rotenone Model of Parkinson's Disease inInternational journal of molecular sciences · 2025
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60 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.

Carmen I Nussbaum-KrammerDepartment of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University; c.nussbaum@zmbh.uni-heidelberg.de.
Mário F NetoDepartment of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University.
Renée M BrielmannDepartment of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University.
Jesper S PedersenDepartment of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University.
Richard I MorimotoDepartment of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University.
Rice Institute · US

Funding

C. elegans Model for Neurodegenerative Diseases of AgingR37AG026647 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2010 to 2019
$3.9M
REGULATION AND EXPRESSION OF THE HUMAN HSP70 GENE FAMILYR01GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 1987 to 2013
$2.2M
C. Elegans Model for Neurodegenerative Diseases of AgingR01AG026647 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2005 to 2009
$2.0M
Small Molecule Screen for Novel Regulators of Chaperone ExpressionR21NS056337 · NINDS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I. · 2006 to 2007
$363k
NIA NIH HHS R01 AG026647NIA NIH HHS R37 AG026647NIGMS NIH HHS R01 GM038109NINDS NIH HHS R21 NS056337
6 · The paper itself

Abstract

Prions are unconventional self-propagating proteinaceous particles, devoid of any coding nucleic acid. These proteinaceous seeds serve as templates for the conversion and replication of their benign cellular isoform. Accumulating evidence suggests that many protein aggregates can act as self-propagating templates and corrupt the folding of cognate proteins. Although aggregates can be functional under certain circumstances, this process often leads to the disruption of the cellular protein homeostasis (proteostasis), eventually leading to devastating diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), Amyotrophic lateral sclerosis (ALS), or transmissible spongiform encephalopathies (TSEs). The exact mechanisms of prion propagation and cell-to-cell spreading of protein aggregates are still subjects of intense investigation. To further this knowledge, recently a new metazoan model in Caenorhabditis elegans, for expression of the prion domain of the cytosolic yeast prion protein Sup35 has been established. This prion model offers several advantages, as it allows direct monitoring of the fluorescently tagged prion domain in living animals and ease of genetic approaches. Described here are methods to study prion-like behavior of protein aggregates and to identify modifiers of prion-induced toxicity using C. elegans.

Indexed as

Disease Models, AnimalAnimalsCaenorhabditis elegansMicroscopy, FluorescencePrion DiseasesPrionsTime-Lapse ImagingPrions

Identifiers

PMID25591151
PMCPMC4354510
OpenAlexW2099496568

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.