Evidence map›Paper›PMID 26507691›Full record

ReviewThe FEBS journal2016

All roads lead to PP2A: exploiting the therapeutic potential of this phosphatase.

Jaya Sangodkar, Caroline C Farrington, Kimberly McClinch, Matthew D Galsky, David B Kastrinsky, Goutham Narla

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed, 1 pooled it
12.1field-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

190 citing papers in PubMed, 1 synthesis or guideline pooled it, 304 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Phosphoproteomic dysregulation promotes tumor proliferation in Cushing's disease.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
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  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Protein Phosphatase 2A Promotes CD8Research (Washington, D.C.) · 2025
    Article
  19. Article
  20. Article

130 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

6 authors at 2 institutions in 1 country.

Jaya SangodkarDepartment of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York City, NY, USA.
Caroline C FarringtonDepartment of Medicine and Institute for Transformative Molecular Medicine, Case Western Reserve University, Cleveland, OH, USA.
Kimberly McClinchDepartment of Hematology and Medical Oncology, Icahn School of Medicine at Mount Sinai, New York City, NY, USA.
Matthew D GalskyDepartment of Hematology and Medical Oncology, Icahn School of Medicine at Mount Sinai, New York City, NY, USA.
David B KastrinskyDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York City, NY, USA.
Goutham NarlaDepartment of Medicine and Institute for Transformative Molecular Medicine, Case Western Reserve University, Cleveland, OH, USA.
Icahn School of Medicine at Mount Sinai · USCase Western Reserve University · US

Funding

Small Molecule Activators of PP2A (SMAPs) for Prostate Cancer TherapyR01CA181654 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NARLA, GOUTHAM · 2015 to 2019
$1.9M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA181654NCI NIH HHS R01CA181654
6 · The paper itself

Abstract

Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase involved in the regulation of many cellular processes. A confirmed tumor suppressor protein, PP2A is genetically altered or functionally inactivated in many cancers highlighting a need for its therapeutic reactivation. In this review we discuss recent literature on PP2A: the elucidation of its structure and the functions of its subunits, and the identification of molecular lesions and post-translational modifications leading to its dysregulation in cancer. A final section will discuss the proteins and small molecules that modulate PP2A and how these might be used to target dysregulated forms of PP2A to treat cancers and other diseases.

Indexed as

Catalytic DomainEnzyme InhibitorsGene DeletionGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticHumansModels, MolecularMutationNeoplasmsPhosphorylationProtein Phosphatase 2Protein Processing, Post-TranslationalProtein SubunitsTumor Suppressor ProteinsEnzyme InhibitorsProtein Phosphatase 2Protein SubunitsTumor Suppressor Proteinscancercancer biologycell signalingCIP2Adrug developmentPP2Aprotein phosphatasesSETstructural biologytumor suppressors

Identifiers

PMID26507691
PMCPMC4803620
OpenAlexW1819171550

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.