Evidence map›Paper›PMID 41659424›Full record

ArticlebioRxiv : the preprint server for biology2026

Pathological TDP-43 filaments accumulate at synapses and cause synaptic dysfunction.

Renren Chen, Imogen Stockwell, Jessica C Pierce, Sew-Yeu Peak-Chew, Melissa Huang, Kathy Newell, Bernardino Ghetti, Michael A Cousin, Ingo H Greger, Benjamin Ryskeldi-Falcon

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Renren ChenMRC Laboratory of Molecular Biology, Cambridge, UK.
Imogen StockwellMRC Laboratory of Molecular Biology, Cambridge, UK.
Jessica C PierceInstitute for Neuroscience and Cardiovascular Research, University of Edinburgh, Edinburgh, UK.
Sew-Yeu Peak-ChewMRC Laboratory of Molecular Biology, Cambridge, UK.
Melissa HuangMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-0698-6996
Kathy NewellDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, USA.
Bernardino GhettiDepartment of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, USA.
Michael A CousinInstitute for Neuroscience and Cardiovascular Research, University of Edinburgh, Edinburgh, UK.
Ingo H GregerMRC Laboratory of Molecular Biology, Cambridge, UK.
Benjamin Ryskeldi-FalconMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0002-8176-2618

Funding

Research Education ComponentP30AG010133 · NIA · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI SAYKIN, ANDREW J · 1991 to 2020
$37.3M
Research Education ComponentP30AG072976 · NIA · INDIANA UNIVERSITY INDIANAPOLIS · PI ANDREW J SAYKIN · 2021 to 2026
$24.1M
Investigating the role of TDP-43 mislocalization, structure, and post-translational modifications in the neuropathologically heterogeneous TDP-43 proteinopathiesR01NS137469 · NINDS · INDIANA UNIVERSITY INDIANAPOLIS · PI Laura Cracco, Kathy L Newell · 2024 to 2026
$3.0M
Identification of novel four repeat tauopathies through analysis of network vulnerability, tau structure and propagation.R01AG080001 · NIA · INDIANA UNIVERSITY INDIANAPOLIS · PI BERNARDINO Francesco GHETTI, RUBEN VIDAL · 2023 to 2026
$2.7M
Structural analysis of tau associated with parenchymal and vascular prion protein amyloidosisRF1AG071177 · NIA · INDIANA UNIVERSITY INDIANAPOLIS · PI GHETTI, BERNARDINO FRANCESCO, JIANG, WEN · 2021 to 2021
$2.3M
Structure of amyloid fibrils in human neurodegenerative diseases and agingR01NS110437 · NINDS · INDIANA UNIVERSITY INDIANAPOLIS · PI BERNARDINO Francesco GHETTI, Wen Jiang · 2026 to 2026
$1.2M
NIA NIH HHS P30 AG010133NIA NIH HHS P30 AG072976NIA NIH HHS R01 AG080001NIA NIH HHS RF1 AG071177NINDS NIH HHS R01 NS110437NINDS NIH HHS R01 NS137469
6 · The paper itself

Abstract

The assembly of TAR DNA-binding protein 43 (TDP-43) into amyloid filaments within neurons is a hallmark of multiple neurodegenerative diseases, including motor neuron diseases (MND), frontotemporal dementias (FTD) and limbic-predominant age-related TDP-43 encephalopathy (LATE). These diseases result from the deterioration and loss of neurons, with synaptic dysfunction and neuronal hyperexcitability being prominent early events. Pathogenic mutations in the TDP-43 gene,

Indexed as

ALSamyloidcryo-ETFTDFTLD-TDPNeurodegenerationprion-like propagationprotein aggregationproximity labelling proteomicssynapseTDP-43

Identifiers

PMID41659424
PMCPMC12873875

What Socratic 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 Socratic graph.