Evidence map›Paper›PMID 41854301›Full record

ArticleProtein science : a publication of the Protein Society2026

Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP-43 low-complexity domain.

Thomas B Walker, Joshua W Trowbridge, Shannon McMahon, Nicholas R Marzano, Lauren Rice, Justin J Yerbury, Heath Ecroyd, Luke McAlary

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. 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

8 authors.

Thomas B WalkerMolecular Horizons and School of Science, University of Wollongong, Wollongong, New South Wales, Australia.ORCID https://orcid.org/0009-0002-7197-8420
Joshua W TrowbridgeMolecular Horizons and School of Science, University of Wollongong, Wollongong, New South Wales, Australia.
Shannon McMahonMolecular Horizons and School of Science, University of Wollongong, Wollongong, New South Wales, Australia.
Nicholas R MarzanoMolecular Horizons and School of Science, University of Wollongong, Wollongong, New South Wales, Australia.
Lauren RiceMolecular Horizons and School of Science, University of Wollongong, Wollongong, New South Wales, Australia.
Justin J YerburyMolecular Horizons and School of Science, University of Wollongong, Wollongong, New South Wales, Australia.
Heath EcroydMolecular Horizons and School of Science, University of Wollongong, Wollongong, New South Wales, Australia.ORCID https://orcid.org/0000-0001-7574-0044
Luke McAlaryMolecular Horizons and School of Science, University of Wollongong, Wollongong, New South Wales, Australia.

Funding

FightMNDMotor Neurone Disease AustraliaNational Health and Medical Research Council APP1194872
6 · The paper itself

Abstract

TAR DNA-binding protein 43 (TDP-43) is a nucleic acid-binding protein that regulates processes of mRNA metabolism, during which it undergoes condensation mediated by its C-terminal low-complexity domain (TDP-43

Indexed as

DNA-Binding ProteinsHeat-Shock ProteinsHSP27 Heat-Shock ProteinsProtein AggregatesHumansMolecular ChaperonesPhosphorylationProtein DomainsDNA-Binding ProteinsHeat-Shock ProteinsHSP27 Heat-Shock ProteinsHSPB1 protein, humanMolecular ChaperonesProtein AggregatesTARDBP protein, humanamyotrophic lateral sclerosischaperonesfibrillationliquid–liquid phase separationproteostasis

Identifiers

PMID41854301
PMCPMC13140710

What OpenQuestion holds

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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.