Evidence map›Paper›PMID 33208041›Full record

ArticleCell cycle (Georgetown, Tex.)2020

Phase separation of the Cep63•Cep152 complex underlies the formation of dynamic supramolecular self-assemblies at human centrosomes.

Jong Il Ahn, Jung-Eun Park, Lingjun Meng, Liang Zhang, Tae-Sung Kim, Michael J Kruhlak, Bo Yeon Kim, Kyung S Lee

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. CytochromeiScience · 2024
    Article
  7. Cep57 regulates human centrosomes through multivalent interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Phase Transitions in Chemically Fueled, Multiphase Complex Coacervate Droplets.Angewandte Chemie (International ed. in English) · 2022
    Article
  14. Review
  15. Review
  16. Review
  17. 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

8 authors at 2 institutions in 2 countries.

Jong Il AhnLaboratory of Metabolism, National Cancer Institute, National Institutes of Health , Bethesda, MD, USA.ORCID 0000-0002-4600-3712
Jung-Eun ParkLaboratory of Metabolism, National Cancer Institute, National Institutes of Health , Bethesda, MD, USA.ORCID 0000-0001-9929-830X
Lingjun MengLaboratory of Metabolism, National Cancer Institute, National Institutes of Health , Bethesda, MD, USA.
Liang ZhangLaboratory of Metabolism, National Cancer Institute, National Institutes of Health , Bethesda, MD, USA.ORCID 0000-0002-8338-784X
Tae-Sung KimLaboratory of Metabolism, National Cancer Institute, National Institutes of Health , Bethesda, MD, USA.
Michael J KruhlakLaboratory of Cancer Biology and Genetics, National Cancer Institute, National Institutes of Health , Bethesda, MD, USA.
Bo Yeon KimChemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology , Ochang, Republic of Korea.
Kyung S LeeLaboratory of Metabolism, National Cancer Institute, National Institutes of Health , Bethesda, MD, USA.ORCID 0000-0001-8326-7162
National Institutes of Health · USKorea Research Institute of Bioscience and Biotechnology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The centrosome is a unique membraneless organelle that plays a pivotal role in the orderly progression of the cell cycle in animal cells. It has been shown that two pericentriolar scaffold proteins, Cep63 and Cep152, generate a heterotetrameric complex to self-assemble into a higher-order cylindrical architecture around a centriole. However, the mechanisms underlying how they reach their threshold concentrations in the vast intracellular space and generate a self-assembled architecture remain mysterious. Here we demonstrate that, like liquid-like assemblies, Cep63 and Cep152 cooperatively generate amorphous aggregates capable of undergoing dynamic turnover and inter-aggregate fusion

Indexed as

Cell CycleCell Cycle ProteinsCell Line, TumorCentriolesHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsLiquid-Liquid ExtractionMolecular WeightPlasmidsProtein AggregatesProtein Conformation, alpha-HelicalProtein DomainsTransfectionCell Cycle ProteinsCEP152 protein, humanCEP63 protein, humanProtein AggregatescentrosomeCep152Cep63PCMphase separation

Identifiers

PMID33208041
PMCPMC7781590
OpenAlexW3100359919

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.