Evidence map›Paper›PMID 39987501›Full record

ArticleACS sensors2025

Genetically-Encoded Phase Separation Sensors Enable High-Fidelity Live-Cell Probing of Biomolecular Condensates.

Alexa Regina Chua Avecilla, Jeremy Thomas, Felipe Garcia Quiroz

Abstract read
In one paragraph

Article in ACS sensors, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. A tunable affinity fusion tag for protein self-assembly.bioRxiv : the preprint server for biology · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Alexa Regina Chua AvecillaWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, Georgia 30322, United States.ORCID 0000-0001-6708-805X
Jeremy ThomasWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, Georgia 30322, United States.
Felipe Garcia QuirozWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory University, Atlanta, Georgia 30322, United States.ORCID 0000-0001-6454-9615

Funding

Multifunctional phase sensors for probing and manipulation of intracellular biomolecular condensatesDP2GM149749 · NIGMS · EMORY UNIVERSITY · PI GARCIA QUIROZ, FELIPE · 2022 to 2025
$2.3M
Toward therapeutic targeting of liquid-liquid phase separation dynamics in skinF31AR081697 · NIAMS · EMORY UNIVERSITY · PI AVECILLA, ALEXA REGINA CHUA · 2023 to 2025
$146k
NIAMS NIH HHS F31 AR081697NIGMS NIH HHS DP2 GM149749
6 · The paper itself

Abstract

Biomolecular condensates are membraneless compartments with enigmatic roles across intracellular phenomena. Intrinsically disordered proteins (IDPs) often function as condensate scaffolds, fueled by liquid-liquid phase separation (LLPS) dynamics. Intracellular probing of condensates relies on live-cell imaging of IDP-scaffolds tagged with fluorescent proteins. Conformational heterogeneity in IDPs, however, renders them uniquely susceptible to artifacts from tagging. Probing epidermal condensates in skin, we recently introduced genetically-encoded LLPS-sensors that circumvent the need for molecular-level tagging of skin IDPs. Departing from subcellular tracking of IDP-scaffolds, LLPS-sensors report on the assembly and liquid-like dynamics of their condensates. Here, we demonstrate biomolecular approaches for the evolution and tunability of epidermal LLPS-sensors and assess their impact in the early and late stages of intracellular phase separation. Benchmarking against scaffold-bound fluorescent reporters, we discovered that tunable ultraweak scaffold-sensor interactions uniquely enable the sensitive and innocuous probing of nascent and established biomolecular condensates. Our LLPS-sensitive tools pave the way for the high-fidelity intracellular probing of IDP-governed biomolecular condensates across biological systems.

Indexed as

Biomolecular CondensatesBiosensing TechniquesIntrinsically Disordered ProteinsAnimalsFluorescent DyesHumansPhase SeparationFluorescent DyesIntrinsically Disordered Proteinsbiomolecular condensatesintrinsically disordered proteinsliquid−liquid phase separationlive-cell imagingmembraneless organelles

Identifiers

PMID39987501
PMCPMC11959610

What OpenQuestion holds

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Registered trials

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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.