Evidence map›Paper›PMID 21926483›Full record

ReviewCell cycle (Georgetown, Tex.)2011

Pleiotropic functions of EAPII/TTRAP/TDP2: cancer development, chemoresistance and beyond.

Chunyang Li, Shi-Yong Sun, Fadlo R Khuri, Runzhao Li

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
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  9. Review
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  15. Article
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  17. Tyrosyl DNA phosphodiesterase 2, an enzyme fit for purpose.Nature structural & molecular biology · 2012
    Article
  18. Article
  19. An RNA virus hijacks an incognito function of a DNA repair enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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 3 institutions in 1 country.

Chunyang LiWinship Cancer Institute, Department of Hematology and Medical Oncology, School of Medicine, Emory University, Atlanta, GA, USA.
Shi-Yong Sun
Fadlo R Khuri
Runzhao Li
AID Atlanta · USEmory University · USIndiana University School of Medicine

Funding

TARGETING DEATH RECEPTOR-MEDIATED APOPTOSIS FOR HEAD AND NECK CANCERP50CA128613 · NCI · EMORY UNIVERSITY · PI KHURI, FADLO RAJA · 2007 to 2011
$12.0M
Modulation of EMT by ETS1 and EAPIIK22CA109577 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI LI, RUNZHAO · 2004 to 2006
$470k
NCI NIH HHS K22 CA109577NCI NIH HHS K22CA109577NCI NIH HHS P50 CA128613NCI NIH HHS P50CA128613
6 · The paper itself

Abstract

EAPII (also called TTRAP, TDP2), a protein identified a decade ago, has recently been shown to function as an oncogenic factor. This protein was also proven to be the first 5'- tyrosyl-DNA phosphodiesterase. EAPII has been demonstrated to have promiscuous protein associations, broad responsiveness to various extracellular signals, and pleiotropic functions in the development of human diseases including cancer and neurodegenerative disease. Emerging data suggest that EAPII is a multi-functional protein: EAPII repairs enzyme (topoisomerase)-mediated DNA damage by removing phosphotyrosine from DNA adducts; EAPII is involved in multiple signal transduction pathways such as TNF-TNFR, TGFβ and MAPK, and EAPII is responsive to immune defense, inflammatory response, virus infection and DNA toxins (chemo or radiation therapy). This review focuses on the current understanding of EAPII biology and its potential relations to many aspects of cancer development, including chromosome instability, tumorigenesis, tumor metastasis and chemoresistance, suggesting it as a potential target for intervention in cancer and other human diseases.

Indexed as

ApoptosisChromosomal InstabilityDNA-Binding ProteinsDNA RepairDrug Resistance, NeoplasmHumansNeoplasm MetastasisNeoplasmsNuclear ProteinsPhosphoric Diester HydrolasesSignal TransductionTranscription FactorsDNA-Binding ProteinsNuclear ProteinsPhosphoric Diester HydrolasesTDP2 protein, humanTranscription Factors

Identifiers

PMID21926483
PMCPMC3233625
OpenAlexW2054373267

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.