Evidence map›Paper›PMID 31866823›Full record

ReviewFrontiers in molecular neuroscience2019

Targeting Alpha-Synuclein as a Therapy for Parkinson's Disease.

Carroll Rutherford Fields, Nora Bengoa-Vergniory, Richard Wade-Martins

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular neuroscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed, 1 pooled it
22.4field-weighted citation impact, top 1% of its field
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

166 citing papers in PubMed, 1 synthesis or guideline pooled it, 321 citations in OpenAlex.

  1. Pooled it
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  7. Acteoside exerts neuroprotective effects by preventing α-synuclein aggregation and oxidative stress in models of Parkinson's disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2026
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  13. High-Fat Diet Alters Behavior and Hippocampal Gene Expression.International journal of molecular sciences · 2025
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106 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Carroll Rutherford FieldsDepartment of Neuroscience at Johns Hopkins University, Baltimore, MD, United States.
Nora Bengoa-VergnioryDepartment of Physiology, Oxford Parkinson's Disease Center, Anatomy and Genetics, Oxford, United Kingdom.
Richard Wade-MartinsDepartment of Physiology, Oxford Parkinson's Disease Center, Anatomy and Genetics, Oxford, United Kingdom.
Parkinson's UK · GBJohns Hopkins University · US

Funding

Medical Research Council MC_EX_MR/N50192X/1Medical Research Council MR/L023784/2Medical Research Council MR/M024962/1Medical Research Council MR/P007058/1Parkinson's UK H-1301Parkinson's UK J-0901
6 · The paper itself

Abstract

Parkinson's disease (PD) is one of the most common neurodegenerative disorders with a global burden of approximately 6.1 million patients. Alpha-synuclein has been linked to both the sporadic and familial forms of the disease. Moreover, alpha-synuclein is present in Lewy-bodies, the neuropathological hallmark of PD, and the protein and its aggregation have been widely linked to neurotoxic pathways that ultimately lead to neurodegeneration. Such pathways include autophagy/lysosomal dysregulation, synaptic dysfunction, mitochondrial disruption, and endoplasmic reticulum (ER) and oxidative stress. Alpha-synuclein has not only been shown to alter cellular pathways but also to spread between cells, causing aggregation in host cells. Therapeutic approaches will need to address several, if not all, of these angles of alpha-synuclein toxicity. Here we review the current advances in therapeutic efforts for PD that aim to produce a disease-modifying therapy by targeting the spread, production, aggregation, and degradation of alpha-synuclein. These include: receptor blocking strategies whereby putative alpha-synuclein receptors could be blocked inhibiting alpha-synuclein spread, an alpha-synuclein reduction which will decrease the amount alpha-synuclein available for aggregation and pathway disruption, the use of small molecules in order to target alpha-synuclein aggregation, immunotherapy and the increase of alpha-synuclein degradation by increasing autophagy/lysosomal flux. The research discussed here may lead to a disease-modifying therapy that tackles disease onset and progression in the future.

Indexed as

aggregationalpha-synucleinfibrilsoligomersParkinson’s diseasetherapy

Identifiers

PMID31866823
PMCPMC6906193
OpenAlexW2992485745

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.