Evidence map›Paper›PMID 35314000›Full record

ReviewTranslational neurodegeneration2022

Propagation of tau and α-synuclein in the brain: therapeutic potential of the glymphatic system.

Douglas M Lopes, Sophie K Llewellyn, Ian F Harrison

Open access · goldAbstract readReview
In one paragraph

Review in Translational neurodegeneration, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Glymphatic dysfunction in cerebellar neurodegeneration: mechanistic insights and emerging clinical implications.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
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  15. Article
  16. MRI markers of cerebrospinal fluid dynamics predict dementia and mediate the impact of cardiovascular risk.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
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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.

Douglas M LopesDivision of Medicine, Department of Imaging, Centre for Advanced Biomedical Imaging, Faculty of Medical Sciences, University College London, Paul O'Gorman Building, 72 Huntley Street, London, WC1E 6DD, UK.
Sophie K LlewellynDivision of Medicine, Department of Imaging, Centre for Advanced Biomedical Imaging, Faculty of Medical Sciences, University College London, Paul O'Gorman Building, 72 Huntley Street, London, WC1E 6DD, UK.
Ian F HarrisonDivision of Medicine, Department of Imaging, Centre for Advanced Biomedical Imaging, Faculty of Medical Sciences, University College London, Paul O'Gorman Building, 72 Huntley Street, London, WC1E 6DD, UK. ian.harrison@ucl.ac.uk.ORCID 0000-0003-1250-4911
University College London · GBAdvanced Imaging Research (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease, are characterised by the accumulation of misfolded protein deposits in the brain, leading to a progressive destabilisation of the neuronal network and neuronal death. Among the proteins that can abnormally accumulate are tau and α-synuclein, which can propagate in a prion-like manner and which upon aggregation, represent the most common intracellular proteinaceous lesions associated with neurodegeneration. For years it was thought that these intracellular proteins and their accumulation had no immediate relationship with extracellular homeostasis pathways such as the glymphatic clearance system; however, mounting evidence has now suggested that this is not the case. The involvement of the glymphatic system in neurodegenerative disease is yet to be fully defined; however, it is becoming increasingly clear that this pathway contributes to parenchymal solute clearance. Importantly, recent data show that proteins prone to intracellular accumulation are subject to glymphatic clearance, suggesting that this system plays a key role in many neurological disorders. In this review, we provide a background on the biology of tau and α-synuclein and discuss the latest findings on the cell-to-cell propagation mechanisms of these proteins. Importantly, we discuss recent data demonstrating that manipulation of the glymphatic system may have the potential to alleviate and reduce pathogenic accumulation of propagation-prone intracellular cytotoxic proteins. Furthermore, we will allude to the latest potential therapeutic opportunities targeting the glymphatic system that might have an impact as disease modifiers in neurodegenerative diseases.

Indexed as

Alzheimer DiseaseGlymphatic SystemNeurodegenerative Diseasesalpha-SynucleinBrainHumansalpha-SynucleinAquaporin-4ClearanceGlymphaticPropagationSynucleinopathyTauopathy

Identifiers

PMID35314000
PMCPMC8935752
OpenAlexW4220909881

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.