Evidence map›Paper›PMID 41612406›Full record

ReviewGenome biology2026

Understanding liquid-liquid phase separation through TDP-43: fundamental principles, subcellular compartmentalisation, and role of solid inclusion formation.

Alessandra Bigi, Fabrizio Chiti

Abstract readReview
In one paragraph

Review in Genome biology, 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. TDP-43 Aggregation: The Healthy-Toxic Balance of the Prion-Like Domain.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
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

2 authors.

Alessandra BigiDepartment of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Florence, 50134, Italy. alessandra.bigi@unifi.it.
Fabrizio ChitiDepartment of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Florence, 50134, Italy. fabrizio.chiti@unifi.it.

Funding

Ministero dell'Università e della Ricerca #NEXTGENERATIONEU (NGEU) - National Recovery and Resilience Plan (NRRP), Investment PE8─Project Age-It: "Ageing Well in an Ageing Society" (D.R. 1557 11.10.2022).Università degli Studi di Firenze Fondi di Ateneo RICATEN 2023, RICATEN 2024 and RICATEN 2025Università degli Studi di Firenze Fondi di Ateneo RICATEN 2024 and RICATEN 2025
6 · The paper itself

Abstract

Phase separation is an important process in biology associated with formation of membraneless organelles but possibly related to the emergence of solid inclusions. TDP-43 is a largely studied paradigmatic case, as it forms neuronal cytoplasmic inclusions in neurodegenerative diseases and is an essential component of many membraneless organelles. Here, we review the physicochemical fundamentals of liquid-liquid phase separation (LLPS) of TDP-43 and its fragments in vitro, showing that full-length TDP-43 requires RNA or chaperones to form stable liquid droplets. We describe TDP-43-containing membraneless organelles and the debate on whether these assemblies represent reservoirs for pathological solid inclusion formation.

Indexed as

DNA-Binding ProteinsInclusion BodiesAmyotrophic Lateral SclerosisAnimalsCell CompartmentationHumansNeurodegenerative DiseasesPhase SeparationDNA-Binding ProteinsTARDBP protein, humanAmyotrophic lateral sclerosisAnisosomesFTLD-TDPLATE-NCParaspecklesStress granulesTAR DNA-binding protein 43

Identifiers

PMID41612406
PMCPMC12930980

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.