Evidence map›Paper›PMID 42897149›Full record

ArticleNature communications2026

Imaging nanoscopic co-assemblies of α-synuclein and Tau in human samples.

Yu P Zhang, Amber Wallis, Clara Obensa Bertroli, Cherida Zhang, Melanie Burke, Florence Layburn, Evgeniia Lobanova, Martin Furlepa, Shekhar Kedia, Yuhao Cui and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 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. Article
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

16 authors.

Yu P ZhangDepartment of Chemistry, University of Cambridge, Cambridge, UK. yz566@cam.ac.uk.
Amber WallisUK Dementia Research Institute at University College London, London, UK.
Clara Obensa BertroliUK Dementia Research Institute at University College London, London, UK.
Cherida ZhangDepartment of Chemistry, University of Cambridge, Cambridge, UK.
Melanie BurkeDepartment of Chemistry, University of Cambridge, Cambridge, UK.
Florence LayburnDepartment of Chemistry, University of Cambridge, Cambridge, UK.
Evgeniia LobanovaDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-7605-5820
Martin FurlepaDepartment of Chemistry, University of Cambridge, Cambridge, UK.
Shekhar KediaDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-9322-979X
Yuhao CuiDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0009-0007-5761-8222
Prasanna SureshDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0009-0001-5298-5994
Woo Suk YangDepartment of Chemistry, University of Cambridge, Cambridge, UK.
Annelies QuaegebeurDepartment of Clinical Neurosciences, University of Cambridge, Cambridge, UK.
Tim BartelsUK Dementia Research Institute at University College London, London, UK.ORCID 0000-0002-4071-5612
Caroline H Williams-GrayDepartment of Clinical Neurosciences, University of Cambridge, Cambridge, UK.ORCID 0000-0002-2648-9743
David KlenermanDepartment of Chemistry, University of Cambridge, Cambridge, UK. dk10012@cam.ac.uk.ORCID 0000-0001-7116-6954

Funding

Royal Society RSRP\R\210003
6 · The paper itself

Abstract

α-synuclein (αS), amyloid-β (Aβ), and Tau aggregates are hallmarks of many neurodegenerative diseases, yet the prevalence and nature of their nanoscopic co-assemblies remain poorly understood. Here, we adapt a single-molecule pull-down (SiMPull) assay to profile αS, Aβ, and Tau co-assemblies across post-mortem brain tissue homogenates, soluble brain fractions, human serum, cerebrospinal fluid, and saliva. We show that αS-Tau co-assemblies are abundant across all sample matrices, accounting for ~10-70% of total αS aggregates in both Parkinson's disease (PD) and control samples. Notably, αS-Tau co-assemblies in soluble brain fractions from controls exhibit higher Proteinase K (PK) resistance than those from PD cases. Biophysically, Tau accelerates αS aggregation in simple in vitro systems, but this effect is suppressed in complex environments. Together, this work establishes a framework for probing co-assemblies, revealing that αS-Tau species possess heterogeneous biophysical features and are unlikely to act as a single, uniformly toxic species in PD pathology.

Indexed as

alpha-SynucleinBrainParkinson Diseasetau ProteinsAmyloid beta-PeptidesEndopeptidase KFemaleHumansMaleProtein AggregatesProtein Aggregation, PathologicalSalivaSingle Molecule Imagingalpha-SynucleinAmyloid beta-PeptidesEndopeptidase KProtein Aggregatestau Proteins

Identifiers

PMID42897149
PMCPMC13680374

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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.