Non-genomic mechanisms of protein phosphatase 2A (PP2A) regulation in cancer

Cancer Genome Landscapes

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THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASES

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Pan-cancer patterns of somatic copy number alteration

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MYC, Metabolism, and Cancer

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Frequent Mutations of Chromatin Remodeling Gene ARID1A in Ovarian Clear Cell Carcinoma

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The PeptideAtlas project

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A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells

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CIP2A inhibits PP2A in human malignancies

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Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation

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Shugoshin collaborates with protein phosphatase 2A to protect cohesin

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The Vacuolating Virus, S.V.40

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Protein phosphatase 2A regulatory subunits and cancer

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The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation

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The Myeloid Leukemia-associated Protein SET Is a Potent Inhibitor of Protein Phosphatase 2A

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The tumor suppressor PP2A is functionally inactivated in blast crisis CML through the inhibitory activity of the BCR/ABL-regulated SET protein

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Tolerance of Whole-Genome Doubling Propagates Chromosomal Instability and Accelerates Cancer Genome Evolution

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Greatwall Phosphorylates an Inhibitor of Protein Phosphatase 2Α That Is Essential for Mitosis

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The Substrate of Greatwall Kinase, Arpp19, Controls Mitosis by Inhibiting Protein Phosphatase 2A

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Human Merkel cell polyomavirus small T antigen is an oncoprotein targeting the 4E-BP1 translation regulator

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SMYD3 links lysine methylation of MAP3K2 to Ras-driven cancer

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Multiple pathways regulated by the tumor suppressor PP2A in transformation

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The dynamic control of signal transduction networks in cancer cells

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Identification of specific PP2A complexes involved in human cell transformation

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Human polyomaviruses in disease and cancer

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Landscape of somatic single-nucleotide and copy-number mutations in uterine serous carcinoma

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Live-cell imaging RNAi screen identifies PP2A–B55α and importin-β1 as key mitotic exit regulators in human cells

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Use of mutation profiles to refine the classification of endometrial carcinomas

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A Conserved Motif Provides Binding Specificity to the PP2A-B56 Phosphatase

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Human mammary epithelial cell transformation through the activation of phosphatidylinositol 3-kinase

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Formation of stable attachments between kinetochores and microtubules depends on the B56-PP2A phosphatase

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Sphingosine analogue drug FTY720 targets I2PP2A/SET and mediates lung tumour suppression via activation of PP2A‐RIPK1‐dependent necroptosis

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Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts.

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Identification of Molecular Pathway Aberrations in Uterine Serous Carcinoma by Genome-wide Analyses

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Regulation of autophagy by coordinated action of mTORC1 and protein phosphatase 2A

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B56‐containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX‐1 and ERK

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Purification and Characterization of Two Potent Heat-Stable Protein Inhibitors of Protein Phosphatase 2A from Bovine Kidney

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PP2A-activating drugs selectively eradicate TKI-resistant chronic myeloid leukemic stem cells

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Phenothiazines induce PP2A-mediated apoptosis in T cell acute lymphoblastic leukemia

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

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Comprehensive assessment of cancer missense mutation clustering in protein structures

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The genomic landscape and evolution of endometrial carcinoma progression and abdominopelvic metastasis

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Structural mechanism of demethylation and inactivation of protein phosphatase 2A

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The Tumor Suppressor PP2A Aβ Regulates the RalA GTPase

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Targeting Mitotic Exit Leads to Tumor Regression In Vivo: Modulation by Cdk1, Mastl, and the PP2A/B55α,δ Phosphatase

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HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint

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Activation of tumor suppressor protein PP2A inhibits KRAS-driven tumor growth

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Identification of PP2A Complexes and Pathways Involved in Cell Transformation

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A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A

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A PP1-PP2A phosphatase relay controls mitotic progression

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Targeting c-MYC by antagonizing PP2A inhibitors in breast cancer

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MYC-Dependent Regulation and Prognostic Role of CIP2A in Gastric Cancer

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Selection of protein phosphatase 2A regulatory subunits is mediated by the C terminus of the catalytic Subunit

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Therapeutic targeting of PP2A

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Activation of the protein kinase B pathway by the HPV-16 E7 oncoprotein occurs through a mechanism involving interaction with PP2A

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SETBP1 overexpression is a novel leukemogenic mechanism that predicts adverse outcome in elderly patients with acute myeloid leukemia

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Principles behind the multifarious control of signal transduction

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Autophosphorylation-activated protein kinase phosphorylates and inactivates protein phosphatase 2A.

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Frequent aberrant DNA methylation of ABCB1, FOXC1, PPP2R2B and PTEN in ductal carcinoma in situ and early invasive breast cancer

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Association analyses identify multiple new lung cancer susceptibility loci and their interactions with smoking in the Chinese population

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Is There a Role for SV40 in Human Cancer?

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Cancerous inhibitor of PP2A (CIP2A) at diagnosis of chronic myeloid leukemia is a critical determinant of disease progression

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Adiponectin-Activated AMPK Stimulates Dephosphorylation of AKT through Protein Phosphatase 2A Activation

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Protein phosphatase 2A subunit assembly: The catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen

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Senescence Sensitivity of Breast Cancer Cells Is Defined by Positive Feedback Loop between CIP2A and E2F1

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SET oncoprotein overexpression in B-cell chronic lymphocytic leukemia and non-Hodgkin lymphoma: a predictor of aggressive disease and a new treatment target

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Homozygous Deletions and Recurrent Amplifications Implicate New Genes Involved in Prostate Cancer

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The genomics and genetics of endometrial cancer

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Alterations in protein phosphatase 2A subunit interaction in human carcinomas of the lung and colon with mutations in the Aβ subunit gene

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B56δ-related protein phosphatase 2A dysfunction identified in patients with intellectual disability

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Recurrent <i>PPP2R1A</i> Mutations in Uterine Cancer Act through a Dominant-Negative Mechanism to Promote Malignant Cell Growth

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Antagonism of SET Using OP449 Enhances the Efficacy of Tyrosine Kinase Inhibitors and Overcomes Drug Resistance in Myeloid Leukemia

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SV40 and human cancer: A review of recent data

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B55β-Associated PP2A Complex Controls PDK1-Directed Myc Signaling and Modulates Rapamycin Sensitivity in Colorectal Cancer

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Targeting Inhibitors of the Tumor Suppressor PP2A for the Treatment of Pancreatic Cancer

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Antagonistic activities of the immunomodulator and PP2A-activating drug FTY720 (Fingolimod, Gilenya) in Jak2-driven hematologic malignancies

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PP2A inhibition determines poor outcome and doxorubicin resistance in early breast cancer and its activation shows promising therapeutic effects

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An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator

Longin, S., Jordens, J., MARTENS, E., Stevens, I., Janssens, V., Rondelez, E., BAERE, I. D., Derua, R., Waelkens, E., Goris, J., et al. (2004) · Biochemical Journal · doi:10.1042/bj20031643 · Cited by 101 · see citing works

Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit α4

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Human cancer-associated mutations in the Aα subunit of protein phosphatase 2A increase lung cancer incidence in Aα knock-in and knockout mice

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Tumor suppressive protein phosphatases in human cancer: Emerging targets for therapeutic intervention and tumor stratification

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Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56

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PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma

Puustinen, P., Junttila, M. R., Vanhatupa, S., Sablina, A. A., Hector-Greene, M., Teittinen, K. J., Raheem, O., Ketola, K., Lin, S., Kast, J., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2760 · Cited by 95 · see citing works

Overexpression of PP2A inhibitor SET oncoprotein is associated with tumor progression and poor prognosis in human non-small cell lung cancer

Liu, H., Gu, Y., Wang, H., Yin, J., Zheng, G., Zhang, Z., Lu, M., Wang, C., & He, Z. (2015) · Oncotarget · doi:10.18632/oncotarget.3818 · Cited by 94 · see citing works

Expression of SET, an inhibitor of protein phosphatase 2A, in renal development and Wilms' tumor.

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MAPK kinase signalling dynamics regulate cell fate decisions and drug resistance

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Molecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells

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Analysis of 11q22–q23 deletion target genes in B-cell chronic lymphocytic leukaemia: Evidence for a pathogenic role of NPAT, CUL5, and PPP2R1B

Kalla, C., Scheuermann, M. O., Kube, I., Schlotter, M., Mertens, D., Döhner, H., Stilgenbauer, S., & Lichter, P. (2007) · European Journal of Cancer · doi:10.1016/j.ejca.2007.02.005 · Cited by 80 · see citing works

Identification of a PP2A-interacting protein that functions as a negative regulator of phosphatase activity in the ATM/ATR signaling pathway

McConnell, J. L., Gomez, R. J., McCorvey, L. R. A., Law, B. K., & Wadzinski, B. E. (2007) · Oncogene · doi:10.1038/sj.onc.1210406 · Cited by 80 · see citing works

Deregulation of the PP2A inhibitor SET shows promising therapeutic implications and determines poor clinical outcome in patients with metastatic colorectal cancer

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Expression of protein phosphatase 2A mutants and silencing of the regulatory Bα subunit induce a selective loss of acetylated and detyrosinated microtubules

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Bod1 regulates protein phosphatase 2A at mitotic kinetochores

Porter, I. M., Schleicher, K., Porter, M., & Swedlow, J. R. (2013) · Nature Communications · doi:10.1038/ncomms3677 · Cited by 70 · see citing works

Cell signaling pathways engaged by KSHV

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Genome‐wide analysis of primary plasma cell leukemia identifies recurrent imbalances associated with changes in transcriptional profiles

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Structural basis of protein phosphatase 2A stable latency

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ETS1 Mediates MEK1/2-Dependent Overexpression of Cancerous Inhibitor of Protein Phosphatase 2A (CIP2A) in Human Cancer Cells

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Restricted Protein Phosphatase 2A Targeting by Merkel Cell Polyomavirus Small T Antigen

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Complex Formation of JAK2 with PP2A, PI3K, and Yes in Response to the Hematopoietic Cytokine Interleukin-11

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A Protein Array Screen for Kaposi's Sarcoma-Associated Herpesvirus LANA Interactors Links LANA to TIP60, PP2A Activity, and Telomere Shortening

Shamay, M., Liu, J., Li, R., Liao, G., Li, S., Greenway, M., Hu, S., Zhu, J. K., Xie, Z., Ambinder, R. F., et al. (2012) · Journal of Virology · doi:10.1128/jvi.00169-12 · Cited by 61 · see citing works

Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling

Kauko, O., Laajala, T. D., Jumppanen, M., Hintsanen, P., Suni, V., Haapaniemi, P., Corthals, G., Aittokallio, T., Westermarck, J., & Imanishi, S. Y. (2015) · Scientific Reports · doi:10.1038/srep13099 · Cited by 61 · see citing works

Circumventing cellular control of PP2A by methylation promotes transformation in an Akt-dependent manner

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Serine 62-Phosphorylated MYC Associates with Nuclear Lamins and Its Regulation by CIP2A Is Essential for Regenerative Proliferation

Myant, K., Qiao, X., Halonen, T., Come, C., Laine, A., Janghorban, M., Partanen, J. I., Cassidy, J., Ogg, E.-L., Cammareri, P., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.003 · Cited by 59 · see citing works

Spatial control of protein phosphatase 2A (de)methylation

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PP2A targeting by viral proteins: A widespread biological strategy from DNA/RNA tumor viruses to HIV-1

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JC Virus Small t Antigen Binds Phosphatase PP2A and Rb Family Proteins and Is Required for Efficient Viral DNA Replication Activity

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CIP2A promotes proliferation of spermatogonial progenitor cells and spermatogenesis in mice

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Clinical significance of cancerous inhibitor of protein phosphatase 2A in human cancers

Khanna, A., & Pimanda, J. E. (2016) · International Journal of Cancer · doi:10.1002/ijc.29431 · Cited by 57 · see citing works

ATM-mediated phosphorylation activates the tumor-suppressive function of B56γ–PP2A

Shouse, G., Nobumori, Y., Panowicz, M. J., & Liu, X. (2011) · Oncogene · doi:10.1038/onc.2011.95 · Cited by 53 · see citing works

Association of cellular 56,000- and 32,000-molecular-weight protein with BK virus and polyoma virus t-antigens

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Regulation of protein phosphatase 2A (PP2A) tumor suppressor function by PME-1

Kaur, A., & Westermarck, J. K. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160161 · Cited by 53 · see citing works

G1/S transcriptional networks modulated by the HOX11/TLX1 oncogene of T-cell acute lymphoblastic leukemia

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Lyn sustains oncogenic signaling in chronic lymphocytic leukemia by strengthening SET-mediated inhibition of PP2A

Zonta, F., Pagano, M. A., Trentin, L., Tibaldi, E. V., Frezzato, F., Trimarco, V., Facco, M., Zagotto, G., Pavan, V., Ribaudo, G., et al. (2015) · Blood · doi:10.1182/blood-2014-12-619155 · Cited by 47 · see citing works

PP2A Inhibitor PME-1 Drives Kinase Inhibitor Resistance in Glioma Cells

Kaur, A., Denisova, O. V., Qiao, X., Jumppanen, M., Peuhu, E., Ahmed, S. U., Raheem, O., Haapasalo, H. K., Eriksson, J., Chalmers, A. J., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-1134 · Cited by 47 · see citing works

Involvement of Protein Phosphatase 2A in the Interleukin-3-Stimulated Jak2-Stat5 Signaling Pathway

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PP2A-B56α controls oncogene-induced senescence in normal and tumor human melanocytic cells

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PP2A Inactivation Mediated by <i>PPP2R4</i> Haploinsufficiency Promotes Cancer Development

Sents, W., Meeusen, B., Kalev, P., Radaelli, E., Sagaert, X., Miermans, E., Haesen, D., Lambrecht, C., Dewerchin, M., Carmeliet, P., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2911 · Cited by 42 · see citing works

ARPP-16 is a striatal-enriched inhibitor of protein phosphatase 2A regulated by microtubule-associated serine/threonine kinase 3 (Mast 3 kinase)

Andrade, E. C., Musante, V., Horiuchi, A., Matsuzaki, H., Brody, A. H., Wu, T., Greengard, P., Taylor, J. R., & Nairn, A. C. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.4559-15.2017 · Cited by 41 · see citing works

The glycine 90 to aspartate alteration in the Aβ subunit of PP2A (PPP2R1B) associates with breast cancer and causes a deficit in protein function

Esplin, E. D., Ramos, P., Martinez, B., Tomlinson, G. E., Mumby, M. C., & Evans, G. A. (2005) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20284 · Cited by 40 · see citing works

Inhibitors of the PI3K/mTOR pathway prevent STAT5 phosphorylation inJAK2V617Fmutated cells through PP2A/CIP2A axis

Bartalucci, N., Calabresi, L., Balliu, M., Martinelli, S., Rossi, M. C., Villeval, J., Annunziato, F., Guglielmelli, P., & Vannucchi, A. M. (2017) · Oncotarget · doi:10.18632/oncotarget.18073 · Cited by 39 · see citing works

Second generation tyrosine kinase inhibitors prevent disease progression in high-risk (high CIP2A) chronic myeloid leukaemia patients

Lucas, C. M., Harris, R. J., Holcroft, A. K., Scott, L. J., Carmell, N., McDonald, E., Polydoros, F., & Clark, R. E. (2015) · Leukemia · doi:10.1038/leu.2015.71 · Cited by 37 · see citing works

Mouse model for probing tumor suppressor activity of protein phosphatase 2A in diverse signaling pathways

Walter, G., & Ruediger, R. (2012) · Cell Cycle · doi:10.4161/cc.11.3.19057 · Cited by 37 · see citing works

Role of Protein Phosphatase 2A in the Regulation of Mitogen-Activated Protein Kinase Activity in Ventricular Cardiomyocytes

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Heterogeneous nuclear ribonucleoprotein A2 is a SET-binding protein and a PP2A inhibitor

Vera, J., Jaumot, M., Estanyol, J. M., Brun, S., Agell, N., & Bachs, O. (2005) · Oncogene · doi:10.1038/sj.onc.1209050 · Cited by 36 · see citing works

Molecular Pathways: Harnessing E2F1 Regulation for Prosenescence Therapy in p53-Defective Cancer Cells

Laine, A., & Westermarck, J. K. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1942 · Cited by 36 · see citing works

Anp32e/Cpd1 regulates protein phosphatase 2A activity at synapses during synaptogenesis

Costanzo, R. V., Vilá‐Ortíz, G. J., Perandones, C., Carminatti, H., Matilla‐Dueñas, A., & Radrizzani, M. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04555.x · Cited by 35 · see citing works

An Endogenous Serine/Threonine Protein Phosphatase Inhibitor, G-Substrate, Reduces Vulnerability in Models of Parkinson's Disease

Chung, C. Y., Koprich, J. B., Endo, S., & Ole Isacson, A. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1972-07.2007 · Cited by 35 · see citing works

Combined targeting of SET and tyrosine kinases provides an effective therapeutic approach in human T-cell acute lymphoblastic leukemia

Richard, N. P., Pippa, R., Cleary, M. M., Puri, A., Tibbitts, D., Mahmood, S., Christensen, D. J., Jeng, S., McWeeney, S. K., Look, A. T., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.12394 · Cited by 34 · see citing works

Inhibition of DNA methyltransferase as a novel therapeutic strategy to overcome acquired resistance to dual PI3K/mTOR inhibitors

Qian, X.-J., Li, Y.-T., Yu, Y., Yang, F., Deng, R., Ji, J., Jiao, L., Li, X., Wu, R.-Y., Chen, W.-D., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3016 · Cited by 33 · see citing works

B56γ Tumor-Associated Mutations Provide New Mechanisms for B56γ-PP2A Tumor Suppressor Activity

Nobumori, Y., Shouse, G., Wu, Y., Lee, K. J., Shen, B., & Liu, X. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0633 · Cited by 33 · see citing works

FAM122A, a new endogenous inhibitor of protein phosphatase 2A

Fan, L., Liu, M.-H., Guo, M., Hu, C. X., Yan, Z.-W., Chen, J., Chen, G., & Huang, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.11698 · Cited by 33 · see citing works

MYC-dependent recruitment of RUNX1 and GATA2 on the SET oncogene promoter enhances PP2A inactivation in acute myeloid leukemia

Pippa, R., Dominguez, A., Malumbres, R., Endo, A., Arriazu, E., Marcotegui, N., Guruceaga, E., & Odero, M. D. (2016) · Oncotarget · doi:10.18632/oncotarget.9840 · Cited by 32 · see citing works

Inhibition of Src by direct interaction with protein phosphatase 2A

Yokoyama, N. N., & Miller, W. T. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02874-5 · Cited by 31 · see citing works

Tyrosine phosphorylation of PP2A is regulated by HER-2 signalling and correlates with breast cancer progression

Zhang (2009) · International Journal of Oncology · doi:10.3892/ijo_00000256 · Cited by 30 · see citing works

Novel B55α-PP2A mutations in AML promote AKT T308 phosphorylation and sensitivity to AKT inhibitor-induced growth arrest

Shouse, G., de Necochea-Campion, R., Mirshahidi, S., Liu, X., & Chen, C.-S. (2016) · Oncotarget · doi:10.18632/oncotarget.11209 · Cited by 30 · see citing works

A fine balancing act: A delicate kinase-phosphatase equilibrium that protects against chromosomal instability and cancer

Cordeiro, M. H., Smith, R. J., & Saurin, A. T. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.017 · Cited by 29 · see citing works

A genetic variant in a PP2A regulatory subunit encoded by the PPP2R2B gene associates with altered breast cancer risk and recurrence

Vázquez, A., Kulkarni, D. A., Grochola, L. F., Bond, G. L., Barnard, N., Toppmeyer, D., Levine, A. J., & Hirshfield, K. M. (2010) · International Journal of Cancer · doi:10.1002/ijc.25582 · Cited by 26 · see citing works

Immunohistochemistry-based prognostic biomarkers in NSCLC: novel findings on the road to clinical use?

Lindskog, C., Edlund, K., Mattsson, J. S. M., & Micke, P. (2015) · Expert Review of Molecular Diagnostics · doi:10.1586/14737159.2015.1002772 · Cited by 25 · see citing works

Determinants for the interaction between Janus kinase 2 and protein phosphatase 2A

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Alterations of tumour suppressor gene PPP2R1B in hepatocellular carcinoma

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Cellular inhibitors of Protein Phosphatase PP2A in cancer.

Haesen, D., Sents, W., Ivanova, E., Lambrecht, C., & Janssens, V. (2012) · Lirias · Cited by 24 · see citing works

Phosphorylation of SET Protein at Ser171 by Protein Kinase D2 Diminishes Its Inhibitory Effect on Protein Phosphatase 2A

Irie, A., Harada, K., Araki, N., & Nishimura, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051242 · Cited by 23 · see citing works

Protein phosphatase 2A interacts with the Src kinase substrate p130CAS

Yokoyama, N. N., & Miller, W. T. (2001) · Oncogene · doi:10.1038/sj.onc.1204735 · Cited by 23 · see citing works

FTY 720 (Fingolimod) sensitizes hepatocellular carcinoma cells to sorafenib‐mediated cytotoxicity

Ahmed, D., de Verdier, P. J., Ryk, C., Lunqe, O., Stal, P. I., & Flygare, J. (2015) · Pharmacology Research & Perspectives · doi:10.1002/prp2.171 · Cited by 21 · see citing works

Relevance Rank Platform (RRP) for Functional Filtering of High Content Protein–Protein Interaction Data*

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Important Role for Phylogenetically Invariant PP2Acα Active Site and C-Terminal Residues Revealed by Mutational Analysis in Saccharomyces cerevisiae

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Cyclin E and SV40 Small t Antigen Cooperate to Bypass Quiescence and Contribute to Transformation by Activating CDK2 in Human Fibroblasts*

Sotillo, E., Garriga, J., Kurimchak, A., & Graña, X. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709055200 · Cited by 19 · see citing works

Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A

Löw, C., Quistgaard, E. M., Kovermann, M., Anandapadamanaban, M., Balbach, J., & Nordlund, P. (2014) · Biological Chemistry · doi:10.1515/hsz-2014-0106 · Cited by 18 · see citing works

Using passenger mutations to estimate the timing of driver mutations and identify mutator alterations

Youn, A., & Simon, R. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-363 · Cited by 17 · see citing works

A stress survival response in retinal cells mediated through inhibition of the serine / threonine phosphatase PP2A

Finnegan, S., Mackey, A. M., & Cotter, T. G. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07301.x · Cited by 16 · see citing works

Papillomavirus E7 Oncoproteins Share Functions with Polyomavirus Small T Antigens

White, E. A., Kramer, R. E., Hwang, J. H., Pores‐Fernando, A. T., Naetar, N., Hahn, W. C., Roberts, T. M., Schaffhausen, B. S., Livingston, D. M., & Howley, P. M. (2014) · Journal of Virology · doi:10.1128/jvi.03282-14 · Cited by 16 · see citing works

PR65A Phosphorylation Regulates PP2A Complex Signaling

Kumar, K. U., Xing, Y., Lather, S., Grillon, J. M., Johnson, K. R., Skidgel, R. A., Solaro, R. J., & Danziger, R. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085000 · Cited by 15 · see citing works

Germline variation in TP53 regulatory network genes associates with breast cancer survival and treatment outcome

Jamshidi, M., Schmidt, M. K., Dörk, T., et al. (2012) · International Journal of Cancer · doi:10.1002/ijc.27884 · Cited by 12 · see citing works

Specificity of research antibodies: “trust is good, validation is better”

Ogris, E., Sontag, E., Wadzinski, B. E., & Narla, G. (2017) · Human Pathology · doi:10.1016/j.humpath.2017.12.003 · Cited by 6 · see citing works

PP2A inhibition is a druggable MEK inhibitor resistance mechanism in KRAS-mutant lung cancer cells

Kauko, O., O’Connor, C. M., Kulesskiy, E., Sangodkar, J., Aakula, A., Izadmehr, S., Yetukuri, L., Yadav, B., Padzik, A., Laajala, T. D., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aaq1093 · Cited by 149 · see citing works

Physiologic functions of PP2A: Lessons from genetically modified mice

Reynhout, S., & Janssens, V. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.07.010 · Cited by 124 · see citing works

Phosphoproteome and drug-response effects mediated by the three protein phosphatase 2A inhibitor proteins CIP2A, SET, and PME-1

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CIP2A interacts with TopBP1 and is selectively essential for DNA damage-induced basal-like breast cancer tumorigenesis

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