Evidence map›Paper›PMID 35484036›Full record

ReviewTrends in cell biology2022

Ectopic biomolecular phase transitions: fusion proteins in cancer pathologies.

Richoo B Davis, Mahdi Muhammad Moosa, Priya R Banerjee

Open access · greenAbstract readReview
In one paragraph

Review in Trends in cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Driving forces of RNA condensation revealed through coarse-grained modeling with explicit MgProceedings of the National Academy of Sciences of the United States of America · 2025
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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 at 2 institutions in 1 country.

Richoo B DavisDepartment of Physics, State University of New York (SUNY) at Buffalo, Buffalo, NY 14260, USA.
Mahdi Muhammad MoosaDepartment of Physics, State University of New York (SUNY) at Buffalo, Buffalo, NY 14260, USA. Electronic address: mahdi.moosa@gmail.com.
Priya R BanerjeeDepartment of Physics, State University of New York (SUNY) at Buffalo, Buffalo, NY 14260, USA. Electronic address: prbanerj@buffalo.edu.
University at Buffalo, State University of New York · USBuffalo State University · US

Funding

Quantifying Physiologic and Pathologic Viscoelastic Phases of Biomolecular Condensates by Correlative Force and Fluorescence MicroscopyR35GM138186 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI BANERJEE, PRIYA R. · 2020 to 2025
$4.4M
Mechanism of liquid phase homeostasis of prion-like RNA binding proteinsR21AG064258 · NIA · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI BANERJEE, PRIYA R. · 2019 to 2020
$435k
Developing a screening platform to identify inhibitors of pathological self-assembly of TauR03AG070510 · NIA · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI BANERJEE, PRIYA R. · 2021 to 2022
$315k
Deciphering the role of low complexity domains in dual specificity kinase functionR03TR003387 · NCATS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI BANERJEE, PRIYA R. · 2021 to 2021
$158k
NCATS NIH HHS R03 TR003387NIA NIH HHS R03 AG070510NIA NIH HHS R21 AG064258NIGMS NIH HHS R35 GM138186
6 · The paper itself

Abstract

Biomolecular condensates are membraneless organelles (MLOs) that are enriched in specific proteins and nucleic acids, compartmentalized to perform biochemical functions. Such condensates are formed by phase separation (PS) enabled by protein domains that allow multivalent interactions. Chromosomal translocation-derived in-frame gene fusions often generate proteins with non-native domain combinations that rewire protein-protein interaction networks. Several recent studies have shown that, for a subset of these fusion proteins, pathogenesis can be driven by the ability of the fusion protein to undergo phase transitions at non-physiological cellular locations to form ectopic condensates. We highlight how such ectopic phase transitions can alter biological processes and posit that dysfunction via protein PS at non-physiological locations represents a generic route to oncogenic transformation.

Indexed as

NeoplasmsNucleic AcidsHumansOrganellesPhase TransitionProteinsNucleic AcidsProteinsbiomolecular condensatesliquid–liquid phase separationoncofusiononcogenesisprion-like domain

Identifiers

PMID35484036
PMCPMC9288518
OpenAlexW4224497442

What OpenQuestion holds

Textmetadata
LicenceTDM
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.