Evidence map›Paper›PMID 23639323›Full record

ReviewThe Lancet. Oncology2013

Protein phosphatase 2A: a target for anticancer therapy.

Danilo Perrotti, Paolo Neviani

Open access · greenAbstract readReview
In one paragraph

Review in The Lancet. Oncology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 242 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
242citing papers in PubMed, 1 pooled it
19.3field-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

242 citing papers in PubMed, 1 synthesis or guideline pooled it, 400 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Phosphoproteomic dysregulation promotes tumor proliferation in Cushing's disease.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

182 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

2 authors at 1 institution in 1 country.

Danilo PerrottiHuman Cancer Genetics Program, Department of Molecular Virology, Immunology, and Medical Genetics, and Comprehensive Cancer Center, Ohio State University, Columbus, OH 43210-2207, USA. danilo.perrotti@osumc.edu
Paolo Neviani
Cancer Genetics (United States) · US

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Tasleem J Padamsee · 1985 to 2026
$132.3M
SPORE Leukemia Tissue BankP50CA140158 · NCI · OHIO STATE UNIVERSITY · PI BLOOMFIELD, CLARA D · 2009 to 2013
$11.2M
Role of RNA-Binding Proteins in BCR/ABL LeukemogenesisR01CA095512 · NCI · OHIO STATE UNIVERSITY · PI PERROTTI, DANILO · 2003 to 2012
$2.2M
Role of microRNAs in the regulation of CML stem cell survival and self renewalR01CA163800 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI PERROTTI, DANILO · 2012 to 2017
$1.6M
NCI NIH HHS P30 CA016058NCI NIH HHS P50 CA140158NCI NIH HHS R01 CA095512NCI NIH HHS R01 CA163800
6 · The paper itself

Abstract

Protein phosphatase 2A (PP2A), one of the main serine-threonine phosphatases in mammalian cells, maintains cell homoeostasis by counteracting most of the kinase-driven intracellular signalling pathways. Unrestrained activation of oncogenic kinases together with inhibition of tumour suppressors is often required for development of cancer. PP2A has been shown to be genetically altered or functionally inactivated in many solid cancers and leukaemias, and is therefore a tumour suppressor. For example, the phosphatase activity of PP2A is suppressed in chronic myeloid leukaemia and other malignancies characterised by aberrant activity of oncogenic kinases. Preclinical studies show that pharmacological restoration of PP2A tumour-suppressor activity by PP2A-activating drugs (eg, FTY720) effectively antagonises cancer development and progression. Here, we discuss PP2A as a druggable tumour suppressor in view of the possible introduction of PP2A-activating drugs into anticancer therapeutic protocols.

Indexed as

Drug DesignMolecular Targeted TherapyAnimalsAntineoplastic AgentsEnzyme ActivationEnzyme ActivatorsHumansNeoplasmsProtein Phosphatase 2Signal TransductionAntineoplastic AgentsEnzyme ActivatorsProtein Phosphatase 2

Identifiers

PMID23639323
PMCPMC3913484
OpenAlexW1987474302

What OpenQuestion holds

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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.