Evidence map›Paper›PMID 18729828›Full record

ArticleThe Biochemical journal2008

Depletion of nucleophosmin leads to distortion of nucleolar and nuclear structures in HeLa cells.

Mohammed Abdullahel Amin, Sachihiro Matsunaga, Susumu Uchiyama, Kiichi Fukui

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

57 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Noncatalytic regulation of 18Genes & development · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. The nucleolus as a multiphase liquid condensate.Nature reviews. Molecular cell biology · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Nucleophosmin Phosphorylation as a Diagnostic and Therapeutic Target for Ischemic AKI.Journal of the American Society of Nephrology : JASN · 2019
    Article
  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

4 authors at 1 institution in 1 country.

Mohammed Abdullahel AminDepartment of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871, Osaka, Japan.
Sachihiro Matsunaga
Susumu Uchiyama
Kiichi Fukui
Osaka University · JP

Funding

Texas Tech Center for Translational Research and Rural Health - Research Capacity CoreU54MD020892 · NIMHD · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI Lance R. McMahon, Naima Moustaid-Moussa · 2026 to 2026
$10.0M
NIMHD NIH HHS U54 MD020892
6 · The paper itself

Abstract

NPM (nucleophosmin; also known as B23) is an abundantly and ubiquitously expressed multifunctional nucleolar phosphoprotein, which is involved in numerous cellular processes, including ribosome biogenesis, protein chaperoning and centrosome duplication; however, the role of NPM in the cell cycle still remains unknown. In the present study, we show dynamic localization of NPM throughout the cell cycle of HeLa cells. Using a combination of RNAi (RNA interference) and three-dimensional microscopy we show that NPM is localized at the chromosome periphery during mitosis. We also demonstrate that depletion of NPM causes distortion of nucleolar structure as expected and leads to unexpected dramatic changes in nuclear morphology with multiple micronuclei formation. The defect in nuclear shape of NPM-depleted cells, which is clearly observed by live-cell imaging, is due to the distortion of cytoskeletal (alpha-tubulin and beta-actin) structure, resulting from the defects in centrosomal microtubule nucleation. These results indicate that NPM is an essential protein not only for the formation of normal nucleolar structure, but also for the maintenance of regular nuclear shape in HeLa cells.

Indexed as

Cell NucleolusCell NucleusHeLa CellsHumansMicroscopy, FluorescenceNuclear ProteinsNucleophosminRNA InterferenceNPM1 protein, humanNuclear ProteinsNucleophosmin

Identifiers

PMID18729828
PMCPMC2590675
OpenAlexW2070932926

What OpenQuestion holds

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LicenceCC BY-NC
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.