Evidence map›Paper›PMID 41340892›Full record

ArticleComputational and structural biotechnology journal2025

Modeling liquid-liquid phase separation and its impact on proteasomal substrate degradation.

Di Wu, Qi Ouyang, Hongli Wang

Abstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2025. 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. 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

3 authors.

Di WuThe State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Beijing, China.
Qi OuyangSchool of Physics, Zhejiang University, Hangzhou, China.
Hongli WangThe State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Beijing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proteasome, central to ubiquitin-proteasome mediated degradation of substrate proteins, undergoes liquid-liquid phase separation (LLPS) during substrate processing. However, the mechanisms governing proteasomal LLPS and its functional interplay with degradation dynamics remain elusive. Here, we developed a reaction-diffusion model with thermodynamic constraints to quantitatively characterize proteasome-associated LLPS mediated by the substrate-shuttling factor Radiation-sensitive 23 homolog B (RAD23B). The model successfully captures experimental LLPS dynamics, revealing a concentration-dependent phase transition boundary influenced by proteasome activity and molecular interactions. Significantly, LLPS was found to have bidirectional (enhancing or suppressing), context-dependent effects on degradation efficiency. This work elucidates regulatory mechanisms and functional roles of LLPS in proteasome-mediated degradation, offering a predictive quantitative model and testable hypotheses for future investigation.

Indexed as

Liquid-liquid phase separationProteasomeReaction-diffusion model

Identifiers

PMID41340892
PMCPMC12671354

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.