Evidence map›Paper›PMID 33836595›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in

Tessa Sinnige, Georg Meisl, Thomas C T Michaels, Michele Vendruscolo, Tuomas P J Knowles, Richard I Morimoto

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. A New Soaking Protocol to Live StainbioRxiv : the preprint server for biology · 2026
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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

6 authors.

Tessa SinnigeDepartment of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University, Evanston, IL 60208-3500; t.sinnige1@uu.nl r-morimoto@northwestern.edu.ORCID 0000-0002-9353-126X
Georg MeislCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.ORCID 0000-0002-6562-7715
Thomas C T MichaelsCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.ORCID 0000-0001-6931-5041
Michele VendruscoloCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.ORCID 0000-0002-3616-1610
Tuomas P J KnowlesCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.
Richard I MorimotoDepartment of Molecular Biosciences, Rice Institute for Biomedical Research, Northwestern University, Evanston, IL 60208-3500; t.sinnige1@uu.nl r-morimoto@northwestern.edu.ORCID 0000-0002-3431-445X

Funding

Tissue resident macrophages regulate proteostasis in the aging lungP01AG049665 · NIA · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GR Scott Budinger · 2015 to 2026
$26.9M
The proteasome in aging and neurodegenerative diseaseP01AG054407 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2018 to 2022
$14.0M
C. elegans Model for Neurodegenerative Diseases of AgingR37AG026647 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2010 to 2019
$3.9M
Regulation of Peripheral ProteostasisRF1AG057296 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2017 to 2017
$3.0M
Cell non-autonomous regulation of proteostasis in aging and longevityR56AG059579 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2018 to 2018
$377k
NIA NIH HHS P01 AG049665NIA NIH HHS P01 AG054407NIA NIH HHS R37 AG026647NIA NIH HHS R56 AG059579NIA NIH HHS RF1 AG057296
6 · The paper itself

Abstract

Protein aggregation is associated with a wide range of degenerative human diseases with devastating consequences, as exemplified by Alzheimer's, Parkinson's, and Huntington's diseases. In vitro kinetic studies have provided a mechanistic understanding of the aggregation process at the molecular level. However, it has so far remained largely unclear to what extent the biophysical principles of amyloid formation learned in vitro translate to the complex environment of living organisms. Here, we take advantage of the unique properties of a

Indexed as

AmyloidAnimalsCaenorhabditis elegansKineticsModels, MolecularMuscle CellsPeptidesProtein AggregatesProtein Aggregation, PathologicalAmyloidPeptidespolyglutamineProtein AggregatesamyloidC. eleganschemical kineticspolyglutamineprotein aggregation

Identifiers

PMID33836595
PMCPMC7980373

What OpenQuestion holds

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Registered trials

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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.