Evidence map›Paper›PMID 41179803›Full record

ReviewAutophagy reports2025

The role of autophagy in synucleinopathy: clearance versus spread of α-synuclein.

Emily Birnbaum, Zhenyu Yue

Abstract readReview
In one paragraph

Review in Autophagy reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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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

2 authors.

Emily BirnbaumDepartment of Neurology, The Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID https://orcid.org/0000-0002-0568-8786
Zhenyu YueDepartment of Neurology, The Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID https://orcid.org/0000-0001-8730-8515

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Emerging evidence suggests that the propagation of α-synuclein pathology underlies the progression of Parkinson's disease and supports the hypothesis that transmission of α-synuclein aggregates contributes to dopaminergic degeneration. Autophagy, a cellular degradation process, removes protein aggregates and damaged organelles and aids in α-synuclein clearance. However, fibrillar α-synuclein aggregates may evade and even disrupt autophagy, causing toxic spread. The role of autophagy may be multifaceted in the propagation of α-synuclein: clearing α-synuclein aggregates and damaged organelles (protective) versus the release of α-synuclein aggregates (harmful). Here we review how neuronal and glial autophagy regulate α-synuclein clearance and spreading. We also discuss the need for future research to address the interplay of autophagy and α-synuclein aggregates toward therapeutic development.

Indexed as

autophagyfibrilsParkinson’s diseasesynucleinopathyα-synuclein

Identifiers

PMID41179803
PMCPMC12578314

What OpenQuestion holds

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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.