Evidence map›Paper›PMID 40521644›Full record

ArticleProtein science : a publication of the Protein Society2025

A tool to dissect heterotypic determinants of homotypic protein phase behavior.

Hannah Kimbrough, Jacob Jensen, Caleb Weber, Tayla Miller, Lucinda E Maddera, Jillian F Blanck, Vignesh M P Babu, William B Redwine, Randal Halfmann

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. A tool to dissect heterotypic determinants of homotypic protein phase behavior.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
  5. A tunable affinity fusion tag for protein self-assembly.bioRxiv : the preprint server for biology · 2025
    Article
  6. Functional constraints ofbioRxiv : the preprint server for biology · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Hannah KimbroughStowers Institute for Medical Research, Kansas City, Missouri, USA.
Jacob JensenStowers Institute for Medical Research, Kansas City, Missouri, USA.
Caleb WeberStowers Institute for Medical Research, Kansas City, Missouri, USA.
Tayla MillerStowers Institute for Medical Research, Kansas City, Missouri, USA.
Lucinda E MadderaStowers Institute for Medical Research, Kansas City, Missouri, USA.
Jillian F BlanckStowers Institute for Medical Research, Kansas City, Missouri, USA.
Vignesh M P BabuStowers Institute for Medical Research, Kansas City, Missouri, USA.
William B RedwineStowers Institute for Medical Research, Kansas City, Missouri, USA.
Randal HalfmannStowers Institute for Medical Research, Kansas City, Missouri, USA.ORCID 0000-0002-6592-1471

Funding

Elucidating mechanisms of amyloid nucleation in vivoR01GM130927 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI HALFMANN, RANDAL ARTHUR · 2020 to 2023
$1.3M
NIGMS NIH HHS R01 GM130927NIGMS NIH HHS R01GM130927Stowers Institute for Medical Research
6 · The paper itself

Abstract

Proteins commonly self-assemble to create liquid or solid condensates with diverse biological activities. The mechanisms of assembly are determined by each protein's sequence and cellular context. We previously developed distributed amphifluoric FRET (DAmFRET) to analyze sequence determinants of self-assembly in cells. Here, we extend the utility of DAmFRET by creating a nanobody (mEosNb) against the fluorescent protein mEos3 to physically tether other proteins to DAmFRET-enabled query proteins. This tool allows us to rapidly screen for effects on the phase behavior of query proteins by modulating the expression level and valence of mEosNb-fused modifier proteins. We use our system to identify thresholds of valence for liquid-liquid phase separation and to discriminate nucleation mechanisms of amyloid and other paracrystalline assemblies in cells. Our approach adds a new experimental dimension for interrogating the mechanisms of intracellular phase transitions.

Indexed as

Fluorescence Resonance Energy TransferSingle-Domain AntibodiesHumansLuminescent ProteinsPhase TransitionLuminescent ProteinsSingle-Domain Antibodiesamyloidbiomolecular condensatemultivalencynanobodynucleationsynthetic biology

Identifiers

PMID40521644
PMCPMC12168132

What OpenQuestion holds

Textmetadata
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.