The DOI matches its Crossref record; 100 of the 103 references it cites were found in a registry or an index.
Protein phosphatase 2A: a target for anticancer therapy
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“PP2A complex components are mutated at a relatively low frequency in most types of human cancer”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [2]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Among them, cancerous inhibitor of PP2A (CIP2A) is the most prevalent oncoprotein”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [2]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“This establishes the reactivation of PP2A as an attractive novel approach in cancer therapy [2,6]”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [2]
The cited source says what the claim attributes to it.
In the citing paper
“whereas its inhibition promotes the various malignant characteristics of human cancer cells [1,2]”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [2]
In the citing paper
“Restoring PP2A activity (e.g., with FTY720 in leukemia) can counteract cancer, while transient PP2A inhibition (e.g., LB100 in GBM) may sensitize tumors to therapy [ 180 ].”
From Targeting PP2A in cancer: an underrated option (2025) · cites this paper as [180]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Antitumor effects of OSU-2S, a nonimmunosuppressive analogue of FTY720, in hepatocellular carcinoma
Omar, H. A., Chou, C.-C., Berman-Booty, L. D., Ma, Y., Hung, J., Wang, D.-S., Kogure, T., Patel, T. C., Terracciano, L., Muthusamy, N., et al. (2011) · Hepatology · doi:10.1002/hep.24293 · Cited by 74
RetractedThe genomic and transcriptomic architecture of 2,000 breast tumours reveals novel subgroups
METABRIC Group, Curtis, C., Shah, S. P., Chin, S.-F., Turashvili, G., Rueda, O. M., Dunning, M. J., Speed, D., Lynch, A. G., Samarajiwa, S., et al. (2012) · Nature · doi:10.1038/nature10983 · Cited by 6,097
Oncogenic Transcription Factors in the Human Acute Leukemias
Look, A. T. (1997) · Science · doi:10.1126/science.278.5340.1059 · Cited by 1,181
Principles of Tumor Suppression
Sherr, C. J. (2004) · Cell · doi:10.1016/s0092-8674(03)01075-4 · Cited by 1,028
Bcl-2 family proteins and cancer
Yip, K. W., & Reed, J. C. (2008) · Oncogene · doi:10.1038/onc.2008.307 · Cited by 913
Ubiquitination regulates PTEN nuclear import and tumor suppression
Trotman, L. C., Wang, X., Alimonti, A., Chen, Z., Teruya-Feldstein, J., Yang, H., Pavletich, N. P., Carver, B. S., Cordon-Cardo, C., Erdjument-Bromage, H., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.040 · Cited by 748
CIP2A inhibits PP2A in human malignancies
Junttila, M. R., Puustinen, P., Niemelä, M., Ahola, R., Arnold, H., Böttzauw, T., Ala-aho, R., Nielsen, C., Ivaska, J., Taya, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.044 · Cited by 677
The biology of CML blast crisis
Calabretta, B., & Perrotti, D. (2004) · Blood · doi:10.1182/blood-2003-12-4111 · Cited by 608
Self-citationProtein phosphatase 2A regulatory subunits and cancer
Eichhorn, P. J. A., Creyghton, M. P., & Bernards, R. (2009) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.05.005 · Cited by 513
Neviani, P., Santhanam, R., Trotta, R., Notari, M., Blaser, B. W., Liu, S., Mao, H. C., Chang, J. S., Galietta, A., Uttam, A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.015 · Cited by 481
Self-citation
Cited by
Sorted by citations
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
All roads lead to PP 2A: exploiting the therapeutic potential of this phosphatase
Sangodkar, J., Farrington, C. C., McClinch, K., Galsky, M. D., Kastrinsky, D. B., & Narla, G. (2016) · The FEBS Journal · doi:10.1111/febs.13573 · Cited by 312
Zhai, B., Hu, F., Jiang, X. L., Xu, J., Zhao, D., Liu, B., Pan, S., Dong, X., Tan, G., Wei, Z., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-1043 · Cited by 286
Platelets reduce anoikis and promote metastasis by activating YAP1 signaling
Haemmerle, M., Taylor, M., Gutschner, T., Pradeep, S., Cho, M. S., Sheng, J., Lyons, Y., Nagaraja, A. S., Dood, R. L., Wen, Y., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00411-z · Cited by 274
PP2A-activating drugs selectively eradicate TKI-resistant chronic myeloid leukemic stem cells
Neviani, P., Harb, J. G., Oaks, J. J., Santhanam, R., Walker, C. J., Ellis, J. J., Ferenchak, G. J., Dorrance, A. M., Paisie, C. A., Eiring, A. M., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci68951 · Cited by 227
Self-citation
Metadata
- Authors
- Perrotti, D., & Neviani, P.
- Affiliations
- The Ohio State University (US)
- Corresponding author
- Perrotti, Danilo
- Venue
- The Lancet Oncology
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 14
- Issue
- 6
- Pages
- e229-e238
- ISSN
- 1470-2045 (ISSN-L)
- PMC
- PMC3913484
- OpenAlex
- W1987474302
- Cited by
- 400
- References
- 103
- Citations by year
- 2026: 13 · 2025: 17 · 2024: 16 · 2023: 33 · 2022: 31 · 2021: 26 · 2020: 33 · 2019: 35 · 2018: 29 · 2017: 37 · 2016: 62 · 2015: 29 · 2014: 28 · 2013: 11
- FWCI
- 3.99
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The Lancet Oncology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (P50CA140158, R01CA163800, R01CA095512, P30CA016058)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- protein phosphatase 2A, tumour suppressor, cancer therapy, fingolimod, oncogenic kinase, serine/threonine phosphatase, chronic myeloid leukemia, therapeutic target
- MeSH terms
- Animals, Antineoplastic Agents, Enzyme Activation, Humans, Neoplasms, Drug Design, Signal Transduction, Enzyme Activators, Protein Phosphatase 2, Molecular Targeted Therapy
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
