Evidence map›Paper›PMID 41299034›Full record

ArticleCommunications biology2025

Structural and cellular properties of human prion protein oligomers.

Alessandro Emendato, Giuseppina Divisato, Emilia Giannino, Silvia Mansueto, Maria Chiara Zizolfi, Rosa Peltrini, Silvia Parisi, Alfonso De Simone

Abstract read
In one paragraph

Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Alessandro EmendatoDepartment of Pharmacy, University of Naples Federico II, Naples, Italy.ORCID http://orcid.org/0000-0001-8605-2183
Giuseppina DivisatoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples "Federico II", Naples, Italy.ORCID http://orcid.org/0000-0003-4014-1716
Emilia GianninoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples "Federico II", Naples, Italy.
Silvia MansuetoDepartment of Pharmacy, University of Naples Federico II, Naples, Italy.ORCID http://orcid.org/0009-0001-9675-7096
Maria Chiara ZizolfiDepartment of Molecular Medicine and Medical Biotechnology, University of Naples "Federico II", Naples, Italy.ORCID http://orcid.org/0009-0008-7181-3152
Rosa PeltriniDepartment of Pharmacy, University of Naples Federico II, Naples, Italy.ORCID http://orcid.org/0000-0003-2671-8996
Silvia ParisiDepartment of Molecular Medicine and Medical Biotechnology, University of Naples "Federico II", Naples, Italy.ORCID http://orcid.org/0000-0002-1944-9110
Alfonso De SimoneDepartment of Pharmacy, University of Naples Federico II, Naples, Italy. alfonso.desimone@unina.it.ORCID http://orcid.org/0000-0001-8789-9546

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) BioDisOrder - 819644
6 · The paper itself

Abstract

The misfolding of the human prion protein (hPrP) and the consequent self-assembly into insoluble amyloid fibrils are associated with neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs). In this study, we investigated the stability and aggregation behaviour of the folded C-terminal domain of hPrP (hPrP

Indexed as

Prion ProteinsProtein MultimerizationAmyloidCell SurvivalHumansMembrane Potential, MitochondrialNeural Stem CellsProtein AggregatesProtein FoldingAmyloidPrion ProteinsProtein Aggregates

Identifiers

PMID41299034
PMCPMC12657908

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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.