Evidence map›Paper›PMID 32711575›Full record

ReviewActa neuropathologica communications2020

Towards an improved early diagnosis of neurodegenerative diseases: the emerging role of in vitro conversion assays for protein amyloids.

Niccolò Candelise, Simone Baiardi, Alessia Franceschini, Marcello Rossi, Piero Parchi

Abstract readReview
In one paragraph

Review in Acta neuropathologica communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

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  9. Associations between misfolded alpha-synuclein aggregates and Alzheimer's disease pathology in vivo.Alzheimer's & dementia : the journal of the Alzheimer's Association · 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

5 authors.

Niccolò CandeliseDepartment of Experimental, Diagnostic and Specialty Medicine (DIMES), University of Bologna, Bologna, Italy.
Simone BaiardiIRCCS, Istituto delle Scienze Neurologiche di Bologna, Ospedale Bellaria, Via Altura 1/8, 40139, Bologna, Italy.
Alessia FranceschiniIRCCS, Istituto delle Scienze Neurologiche di Bologna, Ospedale Bellaria, Via Altura 1/8, 40139, Bologna, Italy.
Marcello RossiIRCCS, Istituto delle Scienze Neurologiche di Bologna, Ospedale Bellaria, Via Altura 1/8, 40139, Bologna, Italy.
Piero ParchiDepartment of Experimental, Diagnostic and Specialty Medicine (DIMES), University of Bologna, Bologna, Italy. piero.parchi@unibo.it.ORCID 0000-0002-9444-9524

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tissue accumulation of abnormal aggregates of amyloidogenic proteins such as prion protein, α-synuclein, and tau represents the hallmark of most common neurodegenerative disorders and precedes the onset of symptoms by years. As a consequence, the sensitive and specific detection of abnormal forms of these proteins in patients' accessible tissues or fluids as biomarkers may have a significant impact on the clinical diagnosis of these disorders. By exploiting seeded polymerization propagation mechanisms to obtain cell-free reactions that allow highly amplified detection of these amyloid proteins, novel emerging in vitro techniques, such as the real-time quaking-induced conversion assay (RT-QuIC) have paved the way towards this important goal. Given its high accuracy in identifying misfolded forms of prion protein from Creutzfeldt-Jakob disease (CJD) CSF, RT-QuIC has already been included in the diagnostic criteria for the clinical diagnosis of sporadic CJD, the most common human prion disease. By showing that this assay may also accurately discriminate between Lewy body disorders and other forms of parkinsonisms or dementias, more recent studies strongly suggested that CSF RT-QuIC can also be successfully applied to synucleinopathies. Finally, preliminary encouraging data also suggested that CSF RT-QuIC might also work for tau protein, and accurately distinguish between 3R- and 4R tauopathies, including Pick's disease, progressive supranuclear palsy, and corticobasal degeneration. Here we will review the state of the art of cell-free aggregation assays, their current diagnostic value and putative limitations, and the future perspectives for their expanded use in clinical practice.

Indexed as

Early DiagnosisAmyloidogenic ProteinsAnimalsBiological AssayCell-Free SystemHumansIn Vitro TechniquesNeurodegenerative DiseasesProtein Aggregation, PathologicalAmyloidogenic ProteinsAlzheimer’s diseaseBiomarkerDiagnosisLewy bodiesParkinson’s diseasePrion diseasePrion proteinRT-QuICTauα-Synuclein

Identifiers

PMID32711575
PMCPMC7382043

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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.