Evidence map›Paper›PMID 36175485›Full record

ReviewExperimental & molecular medicine2022

Phase separation of low-complexity domains in cellular function and disease.

Jiwon Lee, Hana Cho, Ilmin Kwon

Open access · goldAbstract readReview
In one paragraph

Review in Experimental & molecular medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 51 citations in OpenAlex.

  1. Mechanistic Insights into HIV-1 Capsid Interactions with CPSF6.bioRxiv : the preprint server for biology · 2026
    Article
  2. Fusion protein condensate formation via coiled-coil domains.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Making sense of low-complexity domains: The 2025 Lasker Basic Science Award.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Mammalian oocytes receive maternal-effect RNAs from granulosa cells.bioRxiv : the preprint server for biology · 2025
    Article
  18. Article
  19. Screening of CCDC43 molecular partners by BioID2-based proximity labeling.Turkish journal of biology = Turk biyoloji dergisi · 2025
    Article
  20. Enhanced HSP70 binding to mBMC plant biology · 2024
    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

3 authors at 1 institution in 1 country.

Jiwon LeeDepartment of Anatomy and Cell Biology, Sungkyunkwan University School of Medicine, Suwon, 16419, Korea.
Hana ChoDepartment of Physiology, Sungkyunkwan University School of Medicine, Suwon, 16419, Korea. hanacho@skku.edu.
Ilmin KwonDepartment of Anatomy and Cell Biology, Sungkyunkwan University School of Medicine, Suwon, 16419, Korea. ilmin.kwon@skku.edu.
Sungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this review, we discuss the ways in which recent studies of low-complexity (LC) domains have challenged our understanding of the mechanisms underlying cellular organization. LC sequences, long believed to function in the absence of a molecular structure, are abundant in the proteomes of all eukaryotic organisms. Over the past decade, the phase separation of LC domains has emerged as a fundamental mechanism driving dynamic multivalent interactions of many cellular processes. We review the key evidence showing the role of phase separation of individual proteins in organizing cellular assemblies and facilitating biological function while implicating the dynamics of phase separation as a key to biological validity and functional utility. We also highlight the evidence showing that pathogenic LC proteins alter various phase separation-dependent interactions to elicit debilitating human diseases, including cancer and neurodegenerative diseases. Progress in understanding the biology of phase separation may offer useful hints toward possible therapeutic interventions to combat the toxicity of pathogenic proteins.

Indexed as

Neurodegenerative DiseasesProteomeHumansProteome

Identifiers

PMID36175485
PMCPMC9534829
OpenAlexW4297999505

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.