Evidence map›Paper›PMID 15684379›Full record

ArticleMolecular and cellular biology2005

Nucleophosmin (B23) targets ARF to nucleoli and inhibits its function.

Chandrashekhar Korgaonkar, Jussara Hagen, Van Tompkins, April A Frazier, Chantal Allamargot, Frederick W Quelle, Dawn E Quelle

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
13.6field-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

150 citing papers in PubMed, 290 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
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  5. p14Nature communications · 2024
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  9. p14Research square · 2023
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90 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

7 authors at 1 institution in 1 country.

Chandrashekhar KorgaonkarDepartment of Pharmacology, The University of Iowa, College of Medicine, Iowa City, IA 52242, USA.
Jussara Hagen
Van Tompkins
April A Frazier
Chantal Allamargot
Frederick W Quelle
Dawn E Quelle
University of Iowa · US

Funding

PROGRAM IN HEMOSTASIS AND THROMBOSIS FOR ACADEMICT32HL007344 · NHLBI · UNIVERSITY OF IOWA · PI Anil Kumar Chauhan, Steven R Lentz · 1985 to 2026
$6.5M
Growth Inhibition by the ARF Tumor SuppressorR01CA090367 · NCI · UNIVERSITY OF IOWA · PI QUELLE, DAWN E · 2002 to 2011
$2.9M
CYTOKINE SIGNALING PATHWAYS REGULATING A G1 CHECKPOINTR01CA079889 · NCI · UNIVERSITY OF IOWA · PI QUELLE, FREDERICK W · 1999 to 2003
$794k
NCI NIH HHS R01 CA079889NCI NIH HHS R01 CA090367NCI NIH HHS R01-CA79889NCI NIH HHS R01-CA90367
6 · The paper itself

Abstract

The ARF tumor suppressor is a nucleolar protein that activates p53-dependent checkpoints by binding Mdm2, a p53 antagonist. Despite persuasive evidence that ARF can bind and inactivate Mdm2 in the nucleoplasm, the prevailing view is that ARF exerts its growth-inhibitory activities from within the nucleolus. We suggest ARF primarily functions outside the nucleolus and provide evidence that it is sequestered and held inactive in that compartment by a nucleolar phosphoprotein, nucleophosmin (NPM). Most cellular ARF is bound to NPM regardless of whether cells are proliferating or growth arrested, indicating that ARF-NPM association does not correlate with growth suppression. Notably, ARF binds NPM through the same domains that mediate nucleolar localization and Mdm2 binding, suggesting that NPM could control ARF localization and compete with Mdm2 for ARF association. Indeed, NPM knockdown markedly enhanced ARF-Mdm2 association and diminished ARF nucleolar localization. Those events correlated with greater ARF-mediated growth suppression and p53 activation. Conversely, NPM overexpression antagonized ARF function while increasing its nucleolar localization. These data suggest that NPM inhibits ARF's p53-dependent activity by targeting it to nucleoli and impairing ARF-Mdm2 association.

Indexed as

AnimalsCell NucleolusCell ProliferationChlorocebus aethiopsCOS CellsCyclin-Dependent Kinase Inhibitor p16HumansMiceNIH 3T3 CellsNuclear ProteinsNucleophosminProtein BindingProtein TransportProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Tumor Cells, CulturedCdkn2a protein, mouseCyclin-Dependent Kinase Inhibitor p16MDM2 protein, humanMdm2 protein, mouseNPM1 protein, humanNpm1 protein, mouseNuclear ProteinsNucleophosminProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p14ARFTumor Suppressor Protein p53

Identifiers

PMID15684379
PMCPMC548001
OpenAlexW2155781667

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.