Evidence map›Paper›PMID 41838907›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

The α-synuclein proteostasis network and its translational applications in Parkinson's disease.

Christine M Lim, Michele Vendruscolo

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. 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. Review
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

2 authors.

Christine M LimCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, Cambridgeshire CB2 1EW, United Kingdom.ORCID 0000-0002-5169-6672
Michele VendruscoloCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, Cambridgeshire CB2 1EW, United Kingdom.ORCID 0000-0002-3616-1610

Funding

UK Research and Innovation (UKRI) 10059436UK Research and Innovation (UKRI) 10061100
6 · The paper itself

Abstract

Parkinson's disease (PD) is a debilitating neurodegenerative condition that results in a loss of mobility and muscle control. A neuropathological hallmark of PD is the presence of aberrant inclusions, known as Lewy pathology, of which α-synuclein (α-Syn) is a major component. The accumulation of α-Syn may be due to an imbalance in the proteostasis system regulating α-Syn. To investigate this hypothesis, we delineated the proteostasis network (PN) of α-Syn in the human

Indexed as

alpha-SynucleinParkinson DiseaseProteostasisHumansProteomicsSubstantia NigraTranscriptomealpha-Synucleinalpha-synucleinParkinson’s diseaseprotein homeostasis

Identifiers

PMID41838907
PMCPMC13012101

What OpenQuestion holds

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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.