Evidence map›Paper›PMID 37907238›Full record

ArticleLife science alliance2024

Cell cycle-dependent gene networks for cell proliferation activated by nuclear CK2α complexes.

Miwako Kato Homma, Ryuichiro Nakato, Atsushi Niida, Masashige Bando, Katsunori Fujiki, Naoko Yokota, So Yamamoto, Takeshi Shibata, Motoki Takagi, Junko Yamaki and 4 more

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 29% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Ellagic Acid Mediates the Delay of Dermal Fibroblast Senescence via CSNK2A1.Clinical, cosmetic and investigational dermatology · 2025
    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

14 authors at 3 institutions in 2 countries.

Miwako Kato HommaDepartment of Biomolecular Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan mkhomma@fmu.ac.jp.ORCID 0000-0002-5920-3596
Ryuichiro NakatoLaboratory of Computational Genomics, Institute for Quantitative Biosciences, University of Tokyo, Bunkyo, Japan.
Atsushi NiidaHuman Genome Center, The Institute of Medical Science, The University of Tokyo, Minato, Japan.
Masashige BandoInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo, Japan.
Katsunori FujikiInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo, Japan.
Naoko YokotaLaboratory of Computational Genomics, Institute for Quantitative Biosciences, University of Tokyo, Bunkyo, Japan.
So YamamotoDepartment of Biomolecular Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan.
Takeshi ShibataK.K. ABSciex, Shinagawa, Japan.
Motoki TakagiTranslational Research Center, Fukushima Medical University School of Medicine, Fukushima, Japan.ORCID 0000-0002-3534-2735
Junko YamakiDepartment of Biomolecular Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan.
Hiroko Kozuka-HataMedical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo, Minato, Japan.ORCID 0000-0002-9286-6594
Masaaki OyamaMedical Proteomics Laboratory, The Institute of Medical Science, The University of Tokyo, Minato, Japan.ORCID 0000-0001-6478-3735
Katsuhiko ShirahigeInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo, Japan.ORCID 0000-0002-7862-1144
Yoshimi HommaDepartment of Biomolecular Sciences, Fukushima Medical University School of Medicine, Fukushima, Japan.
The University of Tokyo · JPFukushima Medical University · JPKarolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear expression of protein kinase CK2α is reportedly elevated in human carcinomas, but mechanisms underlying its variable localization in cells are poorly understood. This study demonstrates a functional connection between nuclear CK2 and gene expression in relation to cell proliferation. Growth stimulation of quiescent human normal fibroblasts and phospho-proteomic analysis identified a pool of CK2α that is highly phosphorylated at serine 7. Phosphorylated CK2α translocates into the nucleus, and this phosphorylation appears essential for nuclear localization and catalytic activity. Protein signatures associated with nuclear CK2 complexes reveal enrichment of apparently unique transcription factors and chromatin remodelers during progression through the G

Indexed as

Gene Regulatory NetworksHistonesCasein Kinase IICell CycleCell ProliferationHumansProteomicsCasein Kinase IICSNK2A1 protein, humanHistones

Identifiers

PMID37907238
PMCPMC10618106
OpenAlexW4388079777

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.