Evidence map›Paper›PMID 31988747›Full record

ReviewTranslational neurodegeneration2020

Effect of the micro-environment on α-synuclein conversion and implication in seeded conversion assays.

Niccolo Candelise, Matthias Schmitz, Katrin Thüne, Maria Cramm, Alberto Rabano, Saima Zafar, Erik Stoops, Hugo Vanderstichele, Anna Villar-Pique, Franc Llorens and 1 more

Abstract readReview
In one paragraph

Review in Translational neurodegeneration, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed, 2 pooled it
–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

48 citing papers in PubMed, 2 syntheses or guidelines pooled it.

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  18. Posttranslational Modifications ofPharmacological reviews · 2024
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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

11 authors.

Niccolo Candelise *1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
Matthias Schmitz *1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.ORCID 0000-0002-5502-681X
Katrin Thüne1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
Maria Cramm1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
Alberto Rabano4Departamento de Neuropatología y Banco de Tejidos (BT-CIEN), Fundación CIEN, Instituto de Salud Carlos III Centro Alzheimer Fundación Reina Sofíac, Valderrebollo n° 5, 28031 Madrid, Spain.
Saima Zafar1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
Erik StoopsADx NeuroSciences, Technologiepark 4, Ghent, Belgium.
Hugo VandersticheleADx NeuroSciences, Technologiepark 4, Ghent, Belgium.
Anna Villar-Pique1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
Franc Llorens1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.
Inga Zerr1Department of Neurology, University Medicine Goettingen and the German Center for Neurodegenerative Diseases (DZNE), Robert-Koch -Straße 40, 37075 Göttingen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: α-Synuclein is a small soluble protein, whose physiological function in the healthy brain is poorly understood. Intracellular inclusions of α-synuclein, referred to as Lewy bodies (LBs), are pathological hallmarks of α-synucleinopathies, such as Parkinson's disease (PD) or dementia with Lewy bodies (DLB). Main body: Understanding of the molecular basis as well as the factors or conditions promoting α-synuclein misfolding and aggregation is an important step towards the comprehension of pathological mechanism of α-synucleinopathies and for the development of efficient therapeutic strategies. Based on the conversion and aggregation mechanism of α-synuclein, novel diagnostic tests, such as protein misfolding seeded conversion assays, e.g. the real-time quaking-induced conversion (RT-QuIC), had been developed. In diagnostics, α-synuclein RT-QuIC exhibits a specificity between 82 and 100% while the sensitivity varies between 70 and 100% among different laboratories. In addition, the α-synuclein RT-QuIC can be used to study the α-synuclein-seeding-characteristics of different α-synucleinopathies and to differentiate between DLB and PD. Conclusion: The variable diagnostic accuracy of current α-synuclein RT-QuIC occurs due to different protocols, cohorts and material etc.. An impact of micro-environmental factors on the α-synuclein aggregation and conversion process and the occurrence and detection of differential misfolded α-synuclein types or strains might underpin the clinical heterogeneity of α-synucleinopathies

Indexed as

Cellular Microenvironmentalpha-SynucleinAnimalsHumansProteostasis DeficienciesSynucleinopathiesalpha-SynucleinSNCA protein, humanProtein misfoldingProtein strainsRT-QuICα-Synucleinopathies

Identifiers

PMID31988747
PMCPMC6966864

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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.