Evidence map›Paper›PMID 42864345›Full record

ArticleNature communications2026

Mapping high resolution, multidimensional phase diagrams of near-physiological protein condensates.

Tanushree Agarwal, Tomas Sneideris, Fabian Svara, Klavs Jermakovs, Helena Coyle, Seema Qamar, Emanuel Kava, Rob Scrutton, Nicole Pleschka, Priyanka Peres and 8 more

Abstract read
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. 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

18 authors.

Tanushree AgarwalDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, UK.
Tomas SneiderisDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, UK.ORCID 0000-0001-5285-871X
Fabian Svaraariadne.ai ag, Buchrain, Switzerland.
Klavs JermakovsDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, UK.
Helena CoyleCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK.
Seema QamarCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK.
Emanuel KavaDepartment of Physics, Ribeirão Preto School of Philosophy, Science and Literature, University of São Paulo and National Institute of Science and Technology in Innovative Research in Health Sciences: from Nanotechnology to Artificial Intelligence, Ribeirão Preto, Brazil.
Rob ScruttonDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, UK.ORCID 0009-0008-0012-0703
Nicole PleschkaCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK.
Priyanka PeresCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK.
Gea CereghettiDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, UK.ORCID 0000-0001-7732-9435
Ewa AndrzejewskaDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, UK.
Alejandro Diaz-BarreiroDivision of Rheumatology, Department of Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland.
Gaby PalmerDivision of Rheumatology, Department of Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland.ORCID 0000-0001-7567-1798
Antonio J Costa-FilhoDepartment of Physics, Ribeirão Preto School of Philosophy, Science and Literature, University of São Paulo and National Institute of Science and Technology in Innovative Research in Health Sciences: from Nanotechnology to Artificial Intelligence, Ribeirão Preto, Brazil.ORCID 0000-0001-6730-8737
Georg KrainerDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, UK. georg.krainer@uni-graz.at.
Tuomas Pj KnowlesDepartment of Chemistry, Centre for Misfolding Disease, University of Cambridge, Cambridge, UK. tpjk2@cam.ac.uk.ORCID 0000-0002-7879-0140
Jonathon Nixon-AbellCambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge, UK. jjn36@cam.ac.uk.ORCID 0000-0003-4169-0012

Funding

Wellcome TrustWellcome Trust (Wellcome) 227745/Z/23/Z
6 · The paper itself

Abstract

Biomolecular condensates are membraneless compartments, crucial for organising and regulating diverse cellular processes. Current approaches to study condensate biology either use simplified recombinant protein systems with limited physiological relevance, or complex live-cell models with restricted experimental control and scalability. Here, we present ExVivo PhaseScan, a droplet microfluidics platform that couples mammalian lysate-based reconstitution with scalable analysis to generate high-resolution phase diagrams of compositionally complex protein condensates. We apply this approach to study two multicomponent condensate systems, stress granules and nucleoli, and dissect the physicochemical interactions that influence their stability. We further developed a machine learning pipeline to analyse condensate morphology which we use to reveal how mutations in the amyotrophic lateral sclerosis (ALS)-linked protein Fused in Sarcoma (FUS) remodels condensate properties. We identify liquid-to-solid transitions of mutant FUS within stress granules and nucleoli, and show that these transitions can be reversed by RNA aptamer-based interventions. Together, these findings establish ExVivo PhaseScan as a versatile tool for dissecting the physicochemical and pathological regulation of condensates, with potential to inform therapeutic strategies for diseases driven by aberrant phase transitions.

Indexed as

Biomolecular CondensatesRNA-Binding Protein FUSStress GranulesAmyotrophic Lateral SclerosisAnimalsAptamers, NucleotideCell NucleolusHumansMachine LearningMicrofluidicsMutationPhase SeparationAptamers, NucleotideFUS protein, humanRNA-Binding Protein FUS

Identifiers

PMID42864345
PMCPMC13658236

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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.