Evidence map›Paper›PMID 39827079›Full record

ReviewTrends in biochemical sciences2025

Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function.

Nathaniel Hess, Jerelle A Joseph

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Review
  3. Fusion protein condensate formation via coiled-coil domains.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Condensates as Conformation Editors of Disordered Client Proteins.Journal of the American Chemical Society · 2026
    Article
  6. Article
  7. Article
  8. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Biomolecular Condensates Dictate the Folding Landscape of Proteins.bioRxiv : the preprint server for biology · 2026
    Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article
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

2 authors.

Nathaniel HessDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544, USA.
Jerelle A JosephDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544, USA; Omenn-Darling Bioengineering Institute, Princeton University, Princeton, NJ 08544, USA. Electronic address: jerellejoseph@princeton.edu.

Funding

Inside Condensates: Bridging molecular structure and condensate material properties through simulationR35GM155259 · NIGMS · PRINCETON UNIVERSITY · PI Jerelle Aurelia Joseph · 2024 to 2026
$1.2M
NIGMS NIH HHS R35 GM155259
6 · The paper itself

Abstract

Biomolecular condensates are membraneless organelles that concentrate proteins and nucleic acids. One of the primary components of condensates is multidomain proteins, whose domains can be broadly classified as structured and disordered. While structured protein domains are ubiquitous within biomolecular condensates, the physical ramifications of their unique properties have been relatively underexplored. Therefore, this review synthesizes current literature pertaining to structured protein domains within the context of condensates. We examine how the propensity of structured domains for high interaction specificity and low conformational heterogeneity contributes to the formation, material properties, and functions of biomolecular condensates. Finally, we propose unanswered questions on the behavior of structured protein domains within condensates, the answers of which will contribute to a more complete understanding of condensate biophysics.

Indexed as

Biomolecular CondensatesProteinsAnimalsHumansProtein DomainsProteinsbiomolecular condensatesconformational heterogeneityinteraction specificityphase separationstructured protein domains

Identifiers

PMID39827079
PMCPMC12165725

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.