Evidence map›Paper›PMID 17584785›Full record

ArticleNucleic acids research2007

The novel PIAS-like protein hZimp10 is a transcriptional co-activator of the p53 tumor suppressor.

Jane Lee, Jason Beliakoff, Zijie Sun

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

47 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
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  7. The impact of dysregulation SUMOylation on prostate cancer.Journal of translational medicine · 2025
    Review
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  9. EndothelialFrontiers in cell and developmental biology · 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

3 authors at 2 institutions in 1 country.

Jane LeeDepartments of Urology and Genetics, Stanford University School of Medicine, Stanford, CA 94305-5118, USA.
Jason Beliakoff
Zijie Sun
Pediatrics and Genetics · USStanford University · US

Funding

Leveraging innovative technologies in basic and clinical cancer researchT32CA009302 · NCI · STANFORD UNIVERSITY · PI LAURA D ATTARDI, Aaron M Newman · 1985 to 2026
$19.1M
Roles of the androgen receptor and its co-regulators in prostate tumorigenesisR01CA070297 · NCI · STANFORD UNIVERSITY · PI SUN, ZIJIE · 2003 to 2025
$5.0M
Beta-catenin and Androgen Signaling in Prostate CancerR01DK061002 · NIDDK · STANFORD UNIVERSITY · PI SUN, ZIJIE · 2003 to 2007
$1.7M
TGF-Beta/Smads and Androgen Signaling in Prostate CancerR01CA087767 · NCI · STANFORD UNIVERSITY · PI SUN, ZIJIE · 2002 to 2006
$1.3M
Cytokine control of hematopoiesis and leukemiasZ01DK061002 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HENNIGHAUSEN, LOTHAR · 2007 to 2008
$1.1M
ANDROGEN RECEPTOR ASSOCIATED PROTEINS IN PROSTATE CANCERR29CA070297 · NCI · STANFORD UNIVERSITY · PI SUN, ZIJIE · 1997 to 2002
$329k
Androgen and Wnt Beta-catenin Signaling Pathways in Prostate CancerR56DK061002 · NIDDK · STANFORD UNIVERSITY · PI SUN, ZIJIE · 2008 to 2008
$36k
Intramural NIH HHS Z01 DK061002NCI NIH HHS 5T32 CA09302-27NCI NIH HHS CA070297NCI NIH HHS CA087767NCI NIH HHS R01 CA070297NCI NIH HHS R01 CA087767NCI NIH HHS R29 CA070297NCI NIH HHS T32 CA009302NIDDK NIH HHS DK061002NIDDK NIH HHS R01 DK061002NIDDK NIH HHS R56 DK061002
6 · The paper itself

Abstract

The tumor suppressor, p53, plays critical roles in the cell cycle progression, DNA repair and apoptosis. The PIAS proteins (protein inhibitor of activated STAT) were originally identified as inhibitors of the JAK-STAT pathway. Subsequently, crosstalk between the PIAS proteins and other signaling pathways has been shown to be involved in various cellular processes. Particularly, previous studies have demonstrated that PIAS proteins regulate p53-mediated transcription through sumoylation. hZimp10, also named zmiz1, is a novel PIAS-like protein and functions as a transcriptional co-activator. We recently identified p53 to be an hZimp10 interacting protein in the yeast two-hybrid screen. The interaction between p53 and hZimp10 was confirmed by GST pull-down and co-immunoprecipitation assays. Co-localization of p53 and hZimp10 proteins was also observed within cell nuclei by immunostaining. Moreover, we show that expression of exogenous hZimp10 enhances the transcriptional activity of p53 and knockdown of endogenous hZimp10 reduces the transcriptional activity of p53. Furthermore, using chromatin immunoprecipitation assays, we demonstrate that hZimp10 binds to p53 on the p21 promoter. Finally, p53-mediated transcription is significantly impaired in Zimp10 null embryonic fibroblasts. Taken together, these results provide the first line of evidence to demonstrate a role for Zimp10 in regulating p53 function.

Indexed as

Transcriptional ActivationAnimalsCell Line, TumorCell NucleusHumansMiceTrans-ActivatorsTranscription FactorsTumor Suppressor Protein p53Two-Hybrid System TechniquesTrans-ActivatorsTranscription FactorsTumor Suppressor Protein p53ZMIZ1 protein, human

Identifiers

PMID17584785
PMCPMC1935018
OpenAlexW2128833711

What OpenQuestion holds

Textmetadata
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.