Evidence map›Paper›PMID 20802533›Full record

ArticleOncogene2011

Identification of FUSE-binding protein 1 as a regulatory mRNA-binding protein that represses nucleophosmin translation.

M E Olanich, B L Moss, D Piwnica-Worms, R R Townsend, J D Weber

Open access · greenAbstract read
In one paragraph

Article in Oncogene, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. A dual effect of FUBP1 onRNA (New York, N.Y.) · 2025
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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

5 authors at 2 institutions in 1 country.

M E OlanichBRIGHT Institute, Washington University School of Medicine, St Louis, MO 63110, USA.
B L Moss
D Piwnica-Worms
R R Townsend
J D Weber
Washington University in St. Louis · USImaging Center · US

Funding

Washington University Center for Cellular ImagingP30CA091842 · NCI · WASHINGTON UNIVERSITY · PI TIMOTHY J. EBERLEIN · 2001 to 2026
$128.0M
Washington University Institute of Clinical and Translational Sciences (UL1)UL1RR024992 · NCRR · WASHINGTON UNIVERSITY · PI EVANOFF, BRADLEY A · 2007 to 2011
$45.4M
WU-MDACC Inter-Institutional Molecular Imaging CenterP50CA094056 · NCI · WASHINGTON UNIVERSITY · PI KOPAN, RAPHAEL · 2002 to 2016
$26.3M
TRAINING PROGRAM IN CELLULAR AND MOLECULAR BIOLOGYT32GM007067 · NIGMS · WASHINGTON UNIVERSITY · PI TRUE-KROB, HEATHER L · 1985 to 2020
$20.4M
YOGA LIFESTYLE INTERVENTION REDUCES BLOOD PRESSURE IN HIV-INFECTED ADULTSP41RR000954 · NCRR · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 1985 to 2011
$16.0M
REGULATION AND ROLE OF MTOR IN NEUROFIBROMIN GROWTH CONTROLR01CA127008 · NCI · WASHINGTON UNIVERSITY · PI GUTMANN, DAVID H, PIWNICA-WORMS, DAVID · 2008 to 2011
$1.6M
NCI NIH HHS CA128007NCI NIH HHS P30 CA091842NCI NIH HHS P30 CA91842NCI NIH HHS P50 CA094056NCI NIH HHS P50 CA94056NCI NIH HHS R01 CA127008NCRR NIH HHS P41 RR000954NCRR NIH HHS P41RR000954NCRR NIH HHS UL1 RR024992NIGMS NIH HHS 5T32 GM007067NIGMS NIH HHS T32 GM007067
6 · The paper itself

Abstract

Nucleophosmin (NPM/B23) is a multifunctional oncoprotein whose protein expression levels dictate cellular growth and proliferation rates. NPM is translationally responsive to hyperactive mammalian target of rapamycin (mTOR) signals, but the mechanism of this regulation is not understood. Using chimeric translational reporters, we found that the 3' untranslated region (UTR) of the NPM messenger (m)RNA is sufficient to mediate its translational modulation by mTOR signalling. We show that far upstream element (FUSE)-binding protein 1 (FBP1) interacts specifically with the 3' UTR of NPM to repress translation. Overexpression of FBP1 resulted in translational repression of NPM mRNAs, whereas depletion of FBP1 caused a dramatic increase in NPM translation and resulted in enhanced overall cell proliferation. Thus, we propose that FBP1 is a key regulator of cell growth and proliferation through its ability to selectively bind the NPM 3' UTR and repress NPM translation.

Indexed as

5' Untranslated RegionsCell Growth ProcessesDNA-Binding ProteinsDNA HelicasesHumansNuclear ProteinsNucleophosminProtein BindingProtein BiosynthesisRNA-Binding ProteinsRNA, MessengerSignal TransductionSirolimus5' Untranslated RegionsDNA-Binding ProteinsDNA HelicasesFUBP1 protein, humanNPM1 protein, humanNuclear ProteinsNucleophosminRNA-Binding ProteinsRNA, MessengerSirolimus

Identifiers

PMID20802533
PMCPMC3190308
OpenAlexW2030693010

What OpenQuestion holds

Textmetadata
LicenceTDM
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.