Evidence map›Paper›PMID 14729947›Full record

ArticleMolecular and cellular biology2004

Physical and functional interactions of the Arf tumor suppressor protein with nucleophosmin/B23.

David Bertwistle, Masataka Sugimoto, Charles J Sherr

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 193 papers.

0numbers the graph read from it
0cells of the map it votes in
193citing papers in PubMed
18.9field-weighted citation impact, top 1% 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

193 citing papers in PubMed, 377 citations in OpenAlex.

  1. Tyrosine phosphorylation unfolds nucleophosmin and disrupts its integration into the nucleolus.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. p14Nature communications · 2024
    Article
  10. Article
  11. Article
  12. Review
  13. p14Research square · 2023
    Article
  14. Article
  15. Article
  16. Liquid-liquid phase separation in tumor biology.Signal transduction and targeted therapy · 2022
    Review
  17. The Role of Nucleophosmin 1 (Life (Basel, Switzerland) · 2022
    Review
  18. Review
  19. Review
  20. Article

133 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

David BertwistleHoward Hughes Medical Institute and Department of Genetics & Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
Masataka Sugimoto
Charles J Sherr
Howard Hughes Medical Institute · USSt. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
NCI NIH HHS CA-21765NCI NIH HHS P30 CA021765
6 · The paper itself

Abstract

The Arf tumor suppressor inhibits cell cycle progression through both p53-dependent and p53-independent mechanisms, including interference with rRNA processing. Using tandem-affinity-tagged p19(Arf), we purified Arf-associated proteins from mouse NIH 3T3 fibroblasts undergoing cell cycle arrest. Tagged p19(Arf) associated with nucleolar and ribosomal proteins, including nucleophosmin/B23 (NPM), a protein thought to foster the maturation of preribosomal particles. NPM is an abundant protein, only a minor fraction of which binds to p19(Arf); however, a significant proportion of p19(Arf) associates with NPM. The interaction between p19(Arf) and NPM requires amino acid sequences at the Arf amino terminus, which are also required for Mdm2 binding, as well as the central acidic domain of NPM and an adjacent segment that regulates NPM oligomerization. The interaction between p19(Arf) and NPM occurs in primary mouse embryonic fibroblasts, including those lacking both Mdm2 and p53. In an NIH 3T3 derivative cell line (MT-Arf) engineered to conditionally express an Arf transgene, induced p19(Arf) associates with NPM and colocalizes with it in high-molecular-weight complexes (2 to 5 MDa). An NPM mutant lacking its carboxyl-terminal nucleic acid-binding domain oligomerizes with endogenous NPM, inhibits p19(Arf) from entering into 2- to 5-MDa particles, and overrides the ability of p19(Arf) to retard rRNA processing.

Indexed as

AnimalsCyclin-Dependent Kinase Inhibitor p16Genes, ReporterMiceMutationNIH 3T3 CellsNuclear ProteinsNucleophosminProtein BindingRibosomesRNA, RibosomalTransfectionTumor Suppressor Protein p14ARFCdkn2a protein, mouseCyclin-Dependent Kinase Inhibitor p16Npm1 protein, mouseNuclear ProteinsNucleophosminRNA, RibosomalTumor Suppressor Protein p14ARF

Identifiers

PMID14729947
PMCPMC321449
OpenAlexW1965912619

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.