Evidence map›Paper›PMID 27499269›Full record

ArticleScientific reports2016

Nanoscale studies link amyloid maturity with polyglutamine diseases onset.

F S Ruggeri, S Vieweg, U Cendrowska, G Longo, A Chiki, H A Lashuel, G Dietler

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

84 citing papers in PubMed, 148 citations in OpenAlex.

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  20. The liquid-to-solid transition of FUS is promoted by the condensate surface.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article

24 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

7 authors at 2 institutions in 2 countries.

F S RuggeriLaboratory of Physics of Living Matter, École Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
S ViewegLaboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, École Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
U CendrowskaLaboratory of Physics of Living Matter, École Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
G LongoLaboratory of Physics of Living Matter, École Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
A ChikiLaboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, École Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
H A LashuelLaboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, École Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
G DietlerLaboratory of Physics of Living Matter, École Polytechnique Fédérale de Lausanne (EPFL), 1015 Lausanne, Switzerland.
École Polytechnique Fédérale de Lausanne · CHUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The presence of expanded poly-glutamine (polyQ) repeats in proteins is directly linked to the pathogenesis of several neurodegenerative diseases, including Huntington's disease. However, the molecular and structural basis underlying the increased toxicity of aggregates formed by proteins containing expanded polyQ repeats remain poorly understood, in part due to the size and morphological heterogeneity of the aggregates they form in vitro. To address this knowledge gap and technical limitations, we investigated the structural, mechanical and morphological properties of fibrillar aggregates at the single molecule and nanometer scale using the first exon of the Huntingtin protein as a model system (Exon1). Our findings demonstrate a direct correlation of the morphological and mechanical properties of Exon1 aggregates with their structural organization at the single aggregate and nanometric scale and provide novel insights into the molecular and structural basis of Huntingtin Exon1 aggregation and toxicity.

Indexed as

Huntington DiseaseProtein Aggregation, PathologicalAmyloidHumansHuntingtin ProteinPeptidesAmyloidHTT protein, humanHuntingtin ProteinPeptidespolyglutamine

Identifiers

PMID27499269
PMCPMC4976327
OpenAlexW2518449720

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.