Evidence map›Paper›PMID 34885933›Full record

ReviewMolecules (Basel, Switzerland)2021

Toward a Disease-Modifying Therapy of Alpha-Synucleinopathies: New Molecules and New Approaches Came into the Limelight.

Mae Upcott, Kirill D Chaprov, Vladimir L Buchman

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

7 citing papers in PubMed, 8 citations in OpenAlex.

  1. A Randomized First-in-Human Study With UB-312, a UBITh® α-Synuclein Peptide Vaccine.Movement disorders : official journal of the Movement Disorder Society · 2022
    Trial
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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

3 authors at 2 institutions in 2 countries.

Mae UpcottSchool of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, UK.
Kirill D ChaprovInstitute of Physiologically Active Compounds Russian Academy of Sciences (IPAC RAS), 1 Severniy Proezd, Chernogolovk, 142432 Moscow, Russia.ORCID 0000-0002-0258-1879
Vladimir L BuchmanSchool of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, UK.
Belgorod National Research University · RUCardiff University · GB

Funding

Ministry of Science and Higher Education of Russian Federation grant agreement № 075-15-2020-795, state contract № 13.1902.21.0027 of 29.09.2020, unique project ID: RF-190220X0027
6 · The paper itself

Abstract

The accumulation of the various products of alpha-synuclein aggregation has been associated with the etiology and pathogenesis of several neurodegenerative conditions, including both familial and sporadic forms of Parkinson's disease (PD) and dementia with Lewy bodies (DLB). It is now well established that the aggregation and spread of alpha-synuclein aggregation pathology activate numerous pathogenic mechanisms that contribute to neurodegeneration and, ultimately, to disease progression. Therefore, the development of a safe and effective disease-modifying therapy that limits or prevents the accumulation of the toxic intermediate products of alpha-synuclein aggregation and the spread of alpha-synuclein aggregation pathology could provide significant positive clinical outcomes in PD/DLB cohorts. It has been suggested that this goal can be achieved by reducing the intracellular and/or extracellular levels of monomeric and already aggregated alpha-synuclein. The principal aim of this review is to critically evaluate the potential of therapeutic strategies that target the post-transcriptional steps of alpha-synuclein production and immunotherapy-based approaches to alpha-synuclein degradation in PD/DLB patients. Strategies aimed at the downregulation of alpha-synuclein production are at an early preclinical stage of drug development and, although they have shown promise in animal models of alpha-synuclein aggregation, many limitations need to be resolved before in-human clinical trials can be seriously considered. In contrast, many strategies aimed at the degradation of alpha-synuclein using immunotherapeutic approaches are at a more advanced stage of development, with some in-human Phase II clinical trials currently in progress. Translational barriers for both strategies include the limitations of alpha-synuclein aggregation models, poor understanding of the therapeutic window for the alpha-synuclein knockdown, and variability in alpha-synuclein pathology across patient cohorts. Overcoming such barriers should be the main focus of further studies. However, it is already clear that these strategies do have the potential to achieve a disease-modifying effect in PD and DLB.

Indexed as

alpha-SynucleinAnimalsDisease ManagementDrug Delivery SystemsGenetic TherapyHumansImmunotherapyProtein AggregatesSynucleinopathiesalpha-SynucleinProtein AggregatesSNCA protein, humanalpha-synucleinbiomarkerParkinson’s diseaserodent modelstherapeutic/therapytranslational research

Identifiers

PMID34885933
PMCPMC8658846
OpenAlexW4200016408

What OpenQuestion holds

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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.