Evidence map›Paper›PMID 10713707›Full record

ArticleOncogene2000

Low frequency of alterations of the alpha (PPP2R1A) and beta (PPP2R1B) isoforms of the subunit A of the serine-threonine phosphatase 2A in human neoplasms.

G A Calin, M G di Iasio, E Caprini, I Vorechovsky, P G Natali, G Sozzi, C M Croce, G Barbanti-Brodano, G Russo, M Negrini

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 3% 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

97 citing papers in PubMed, 1 synthesis or guideline pooled it, 215 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025
    Review
  4. Effect of Propolis on PPP2R1A and Apoptosis in Cancer Cells.Biochemistry research international · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. The Pivotal Role of Protein Phosphatase 2A (PP2A) in Brain Tumors.International journal of molecular sciences · 2022
    Review
  10. Article
  11. Review
  12. Angiogenesis in gastrointestinal stromal tumors: From bench to bedside.World journal of gastrointestinal oncology · 2022
    Review
  13. Review
  14. PP2A is activated by cytochromeComputational and structural biotechnology journal · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Frontiers in cell and developmental biology · 2020
    Article

37 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

10 authors at 6 institutions in 3 countries.

G A CalinDipartimento di Medicina Sperimentale e Diagnostica, Sezione di Microbiologia, Universitá di Ferrara, via Luigi Borsari, 46, I-44100 Ferrara, Italy.
M G di Iasio
E Caprini
I Vorechovsky
P G Natali
G Sozzi
C M Croce
G Barbanti-Brodano
G Russo
M Negrini
University of Ferrara · ITFondazione IRCCS Istituto Nazionale dei Tumori · ITIstituto Dermopatico dell'Immacolata · ITIstituto di Istruzione Superiore I.T.C. Di Vittorio · ITKarolinska Institutet · SESidney Kimmel Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The phosphatase 2A (PP2A) is one of the major cellular serine-threonine phosphatases. It was recently shown that the gene encoding for the beta isoform of its subunit A, PPP2R1B, is altered in human lung and colorectal carcinomas, suggesting a role in human tumorigenesis. Here, we report the detection of mutations in breast, lung carcinomas and melanomas in the genes of both alpha (PPP2R1A) and beta isoforms. Mutations affecting PPP2R1B were found in four breast carcinomas, while mutations in PPP2R1A were found in carcinomas of the breast and of the lung and in one melanoma. Most of the mutations affecting PPP2R1B were exons deletions, suggesting abnormal splicing. These splicing abnormalities were detected in tumor samples in the absence of the normal splicing product, and were not found in several normal controls. In one case, a homozygous deletion present in tumor DNA, and not in the matched normal control was demonstrated. Mutations affecting the PPP2R1A gene were nucleotide substitutions changing highly conserved amino acids and one frame-shift. Although the frequency of alterations is low, the inclusion of both isoforms of subunit A in the genes mutated in human cancer and the addition of breast cancer to the list of neoplasms in which PPP2R1B is altered, strengthen the potential role of PP2A in human tumorogenesis.

Indexed as

MutationAmino Acid SubstitutionBase SequenceBreast NeoplasmsHumansLung NeoplasmsMelanomaMolecular Sequence DataPhosphoprotein PhosphatasesPolymerase Chain ReactionPolymorphism, GeneticPolymorphism, Single-Stranded ConformationalProtein IsoformsProtein Phosphatase 2RNA, NeoplasmSequence DeletionPhosphoprotein PhosphatasesProtein IsoformsProtein Phosphatase 2RNA, Neoplasm

Identifiers

PMID10713707
OpenAlexW2036495494

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.