Evidence map›Paper›PMID 36310213›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils.

Thomas Skamris, Bente Vestergaard, Kenneth L Madsen, Annette E Langkilde, Vito Foderà

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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. Article
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.

Thomas SkamrisDepartment of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark.
Bente VestergaardDepartment of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark.
Kenneth L MadsenDepartment of Neuroscience, University of Copenhagen, Copenhagen, Denmark.
Annette E LangkildeDepartment of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark. annette.langkilde@sund.ku.dk.
Vito FoderàDepartment of Pharmacy, University of Copenhagen, Copenhagen, Denmark. vito.fodera@sund.ku.dk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregates, hereunder amyloid fibrils, can undergo a maturation process, whereby early formed aggregates undergo a structural and physicochemical transition leading to more mature species. In the case of amyloid-related diseases, such maturation confers distinctive biological properties of the aggregates, which may account for a range of diverse pathological subtypes. Here, we present a protocol for the preparation of α-synuclein amyloid fibrils differing in the level of their maturation. We utilize widely accessible biophysical techniques to characterize the structure and morphology and a simple thermal treatment procedure to test their thermodynamic stability. Their biological properties are probed by means of binding to native plasma membrane sheets originating from mammalian cell lines.

Indexed as

alpha-SynucleinAmyloidosisAmyloidAnimalsBiophysicsHumansMammalsProtein Aggregatesalpha-SynucleinAmyloidProtein AggregatesAmyloid fibril maturationAmyloid polymorphismFibril stabilityMembrane bindingα-synuclein

Identifiers

PMID36310213

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.