Evidence map›Paper›PMID 23454242›Full record

ReviewCancer letters2013

Phosphatase: PP2A structural importance, regulation and its aberrant expression in cancer.

Parthasarathy Seshacharyulu, Poomy Pandey, Kaustubh Datta, Surinder K Batra

Abstract readReview
In one paragraph

Review in Cancer letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 285 papers.

0numbers the graph read from it
0cells of the map it votes in
285citing papers in PubMed
16.6field-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

285 citing papers in PubMed, 468 citations in OpenAlex.

  1. Article
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  7. Lymphatic therapies open the valve in Marfan syndrome.The Journal of clinical investigation · 2026
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  10. Nitration in cancer signaling.Redox biology · 2026
    Review
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  16. Review
  17. Article
  18. Article
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225 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

4 authors at 1 institution in 1 country.

Parthasarathy SeshacharyuluDepartment of Biochemistry and Molecular Biology, Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA. p.seshacharyulu@unmc.edu
Poomy Pandey
Kaustubh Datta
Surinder K Batra
University of Nebraska Medical Center · US

Funding

Novel deregulated genes in the etiology and progression of human prostate cancerR01CA138791 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI BATRA, SURINDER K. · 2010 to 2014
$1.9M
The role of VEGF-C in resisting stress in prostate cancerR01CA140432 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI DATTA, KAUSTUBH · 2010 to 2014
$1.5M
NCI NIH HHS R01 CA 138791NCI NIH HHS R01 CA138791NCI NIH HHS R01 CA 140432NCI NIH HHS R01 CA140432
6 · The paper itself

Abstract

Protein Phosphatase 2A (PP2A) is an important and ubiquitously expressed serine threonine phosphatase and regulates the function by dephosphorylating many critical cellular molecules like Akt, p53, c-Myc and β-catenin. It plays a critical role in cellular processes, such as cell proliferation, signal transduction and apoptosis. Structurally, it is multifarious as it is composed of catalytic, scaffold and regulatory subunits. The catalytic and scaffold subunits have two isoforms and the regulatory subunit has four different families containing different isoforms. The regulatory subunit is the most diverse with temporal and spatial specificity. PP2A undergoes post-translational modifications (i.e. phosphorylation and methylation), which in turn, regulates its enzymatic activity. Aberrant expression, mutations and somatic alterations of the PP2A scaffold and regulatory subunits have been observed in various human malignancies, including lung, breast, skin and colon cancer, highlighting its role as a 'tumor suppressor'. This review is focused on the structural complexity of serine/threonine phosphatase PP2A and summarizes its expression pattern in cancer. Additionally, the PP2A interacting and regulatory proteins and substrates are also discussed. Finally, the mouse models developed to understand the biological role of PP2A subunits in an in vivo model system are also reviewed in this article.

Indexed as

Amino Acid SequenceAnimalsCell Transformation, NeoplasticConserved SequenceGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticHumansIsoenzymesNeoplasmsProtein Phosphatase 2Protein Processing, Post-TranslationalProtein SubunitsIsoenzymesProtein Phosphatase 2Protein Subunits

Identifiers

PMID23454242
PMCPMC3665613
OpenAlexW1992060900

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.