All roads lead to PP 2A: exploiting the therapeutic potential of this phosphatase

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Renal and Extrarenal Effects of Gum Arabic (Acacia Senegal) - What Can be Learned from Animal Experiments?

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Programmed Cell Death Induced by Ceramide

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Alteration of Lymphocyte Trafficking by Sphingosine-1-Phosphate Receptor Agonists

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Forskolin: unique diterpene activator of adenylate cyclase in membranes and in intact cells.

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The Immune Modulator FTY720 Targets Sphingosine 1-Phosphate Receptors

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Serine/threonine phosphatases: mechanism through structure

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Proteasome inhibitors: a novel class of potent and effective antitumor agents.

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

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Recurrent R-spondin fusions in colon cancer

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The quantitative proteome of a human cell line

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Vitamin E: Antioxidant Activity, Biokinetics, and Bioavailability

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Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation

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The LDL–receptor–related protein, LRP, is an apolipoprotein E-binding protein

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CIP2A inhibits PP2A in human malignancies

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Ceramide activates heterotrimeric protein phosphatase 2A

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Molecular Understanding and Modern Application of Traditional Medicines: Triumphs and Trials

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HEAT repeats in the Huntington's disease protein

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Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins.

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Proteasome Inhibitors in Cancer Therapy: Lessons from the First Decade

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Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A

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Phosphoprotein Phosphatase Activities in Alzheimer Disease Brain

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Protein phosphatase 2A regulatory subunits and cancer

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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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Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme

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The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

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Phosphatase Activity Toward Abnormally Phosphorylated τ: Decrease in Alzheimer Disease Brain

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FTY720 (fingolimod) in Multiple Sclerosis: therapeutic effects in the immune and the central nervous system

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

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PP2A: the expected tumor suppressor

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

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Protein phosphatase 2A: a target for anticancer therapy

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PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)

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Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene.

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The B56 Family of Protein Phosphatase 2A (PP2A) Regulatory Subunits Encodes Differentiation-induced Phosphoproteins That Target PP2A to Both Nucleus and Cytoplasm

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Alterations of the PPP2R1B Gene in Human Lung and Colon Cancer

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FTY720, a new alternative for treating blast crisis chronic myelogenous leukemia and Philadelphia chromosome–positive acute lymphocytic leukemia

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Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins

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Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation

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A NOVEL IMMUNOSUPPRESSANT, FTY720, WITH A UNIQUE MECHANISM OF ACTION, INDUCES LONG-TERM GRAFT ACCEPTANCE IN RAT AND DOG ALLOTRANSPLANTATION1

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Induction of cancer cell apoptosis by α‐tocopheryl succinate: molecular pathways and structural requirements

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PP2A mRNA Expression Is Quantitatively Decreased in Alzheimer's Disease Hippocampus

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Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits

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Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure

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Involvement of PP2A in viral and cellular transformation

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Serine−Threonine Protein Phosphatase Inhibitors: Development of Potential Therapeutic Strategies

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Altered Expression Levels of the Protein Phosphatase 2A ABαC Enzyme Are Associated with Alzheimer Disease Pathology

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The recurrent SET-NUP214 fusion as a new HOXA activation mechanism in pediatric T-cell acute lymphoblastic leukemia

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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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Protein Ser/ Thr phosphatases – the ugly ducklings of cell signalling

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CIP2A Is Associated with Human Breast Cancer Aggressivity

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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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Direct interaction between the inhibitor 2 and ceramide via sphingolipid‐protein binding is involved in the regulation of protein phosphatase 2A activity and signaling

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Structural mechanism of demethylation and inactivation of protein phosphatase 2A

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The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity

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The Tumor Suppressor PP2A Aβ Regulates the RalA GTPase

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

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Prediction of the Coding Sequences of Unidentified Human Genes. XIV. The Complete Sequences of 100 New cDNA Clones from Brain Which Code for Large Proteins in vitro

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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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Comparison of heterotrimeric protein phosphatase 2A containing different B subunits.

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Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase.

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Targeting c-MYC by antagonizing PP2A inhibitors in breast cancer

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Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo

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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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Identification and characterization of SET, a nuclear phosphoprotein encoded by the translocation break point in acute undifferentiated leukemia.

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Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Bα subunit

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Targeting SET/I2PP2A oncoprotein functions as a multi-pathway strategy for cancer therapy

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Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A

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Critical Role for Protein Phosphatase 2A Heterotrimers in Mammalian Cell Survival*

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Methylation of the Protein Phosphatase 2A Catalytic Subunit Is Essential for Association of Bα Regulatory Subunit But Not SG2NA, Striatin, or Polyomavirus Middle Tumor Antigen

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A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation

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Role of Serine/Threonine Protein Phosphatase in Alzheimer’s Disease

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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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Vitamin E succinate inhibits the function of androgen receptor and the expression of prostate-specific antigen in prostate cancer cells

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A novel immunosuppressive agent FTY720 induced Akt dephosphorylation in leukemia cells

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The PP2A-Associated Protein α4 Is an Essential Inhibitor of Apoptosis

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Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the Aα subunit gene

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Apolipoprotein E is a biologically active constituent of the normal immunoregulatory lipoprotein, LDL-In.

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CIP2A is Overexpressed in Non-Small Cell Lung Cancer and Correlates with Poor Prognosis

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Purification of Porcine Brain Protein Phosphatase 2A Leucine Carboxyl Methyltransferase and Cloning of the Human Homologue,

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CIP2A Is Overexpressed in Gastric Cancer and Its Depletion Leads to Impaired Clonogenicity, Senescence, or Differentiation of Tumor Cells

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GSK-3β acts downstream of PP2A and the PI 3-kinase-Akt pathway, and upstream of caspase-2 in ceramide-induced mitochondrial apoptosis

Lin, C., Chen, C., Chiang, C.-W., Jan, M., Huang, W., & Lin, Y.-S. (2007) · Journal of Cell Science · doi:10.1242/jcs.03473 · Cited by 141 · see citing works

Vitamin E Analogs, a Novel Group of “Mitocans,” as Anticancer Agents: The Importance of Being Redox-Silent

Neužil, J., Tomasetti, M., Zhao, Y., Dong, L., Birringer, M., Wang, X., Low, P., Wu, K., Salvatore, B. A., & Ralph, S. J. (2007) · Molecular Pharmacology · doi:10.1124/mol.106.030122 · Cited by 139 · see citing works

PP2A impaired activity is a common event in acute myeloid leukemia and its activation by forskolin has a potent anti-leukemic effect

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A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain.

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The Dependence Receptor UNC5H2/B Triggers Apoptosis via PP2A-Mediated Dephosphorylation of DAP Kinase

Guenebeaud, C., Goldschneider, D., Castets, M., Guix, C., Chazot, G., Delloye-Bourgeois, C., Eisenberg-Lerner, A., Shohat, G., Zhang, M., Laudet, V., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.021 · Cited by 137 · see citing works

Vitamin E analogues as inducers of apoptosis: structure–function relation

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B56-Associated Protein Phosphatase 2A Is Required For Survival and Protects from Apoptosis in Drosophila melanogaster

Li, X., Scuderi, A., Letsou, A., & Virshup, D. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3674-3684.2002 · Cited by 135 · see citing works

Essential Requirement for PP2A Inhibition by the Oncogenic Receptor c-KIT Suggests PP2A Reactivation as a Strategy to Treat c-KIT+ Cancers

Roberts, K. G., Smith, A. M., McDougall, F. K., Carpenter, H., Horan, M. P., Neviani, P., Powell, J. A., Thomas, D., Guthridge, M. A., Perrotti, D., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2544 · Cited by 134 · see citing works

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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Subtype‐specific mutation of PPP2R1A in endometrial and ovarian carcinomas

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

Laine, A., Sihto, H., Come, C., Rosenfeldt, M. T., Zwolinska, A., Niemelä, M., Khanna, A., Chan, E. K., Kähäri, V.-M., Kellokumpu-Lehtinen, P.-L., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0292 · Cited by 130 · see citing works

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

Christensen, D. J., Chen, Y., Oddo, J., Matta, K. M., Neil, J. E., Davis, E. D., Volkheimer, A. D., Lanasa, M. C., Friedman, D. R., Goodman, B. K., et al. (2011) · Blood · doi:10.1182/blood-2011-04-351072 · Cited by 128 · see citing works

Carboxymethylation of the PP2A Catalytic Subunit in Saccharomyces cerevisiae Is Required for Efficient Interaction with the B-type Subunits Cdc55p and Rts1p

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Carnosic acid modulates Akt/IKK/NF-κB signaling by PP2A and induces intrinsic and extrinsic pathway mediated apoptosis in human prostate carcinoma PC-3 cells

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Apolipoprotein E and Peptide Mimetics Modulate Inflammation by Binding the SET Protein and Activating Protein Phosphatase 2A

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Phosphorylated PP2A (tyrosine 307) is associated with Alzheimer neurofibrillary pathology

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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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Activation of extracellular signal-regulated kinase and c-Jun-NH(2)-terminal kinase but not p38 mitogen-activated protein kinases is required for RRR-alpha-tocopheryl succinate-induced apoptosis of human breast cancer cells.

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α‐Tocopheryl succinate‐induced apoptosis in Jurkat T cells involves caspase‐3 activation, and both lysosomal and mitochondrial destabilisation

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Structural Basis of PP2A Inhibition by Small t Antigen

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Overexpression of SET is a recurrent event associated with poor outcome and contributes to protein phosphatase 2A inhibition in acute myeloid leukemia

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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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CIP2A is a target of bortezomib in human triple negative breast cancer cells

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Phosphoprotein Phosphatase 2A: A Novel Druggable Target for Alzheimer’s Disease

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

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A new immunosuppressant, FTY720, induces bcl‐2‐associated apoptotic cell death in human lymphocytes

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Mechanism of inhibition of PP2A activity and abnormal hyperphosphorylation of tau by I2PP2A/SET

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can , a Putative Oncogene Associated with Myeloid Leukemogenesis, May Be Activated by Fusion of Its 3‣ Half to Different Genes: Characterization of the set Gene

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Apoprotein E suppresses phytohemagglutinin-activated phospholipid turnover in peripheral blood mononuclear cells.

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Academic cross-fertilization by public screening yields a remarkable class of protein phosphatase methylesterase-1 inhibitors

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A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivoPreprint

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Cancerous inhibitor of PP2A is targeted by natural compound celastrol for degradation in non-small-cell lung cancer

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The Protein Phosphatase 2A Phosphatase Activator Is a Novel Peptidyl-Prolyl cis/trans-Isomerase

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A Novel cAMP-Stimulated Pathway in Protein Phosphatase 2A Activation

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Tissue‐specific expression of mRNAs encoding α‐ and β‐catalytic subunits of protein phosphatase 2A

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

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Prognostic role of CIP2A expression in serous ovarian cancer

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Genome-wide expression profiling reveals transcriptomic variation and perturbed gene networks in androgen-dependent and androgen-independent prostate cancer cells

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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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SV40 small T antigen and PP2A phosphatase in cell transformation

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

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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

Alterations of the PPP2R1B gene located at 11q23 in human colorectal cancers

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Low expression of PP2A regulatory subunit B55α is associated with T308 phosphorylation of AKT and shorter complete remission duration in acute myeloid leukemia patients

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Identification and functional analysis of two Ca2+-binding EF-hand motifs in the B″/PR72 subunit of protein phosphatase 2A

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Novel vitamin E analogue decreases syngeneic mouse mammary tumor burden and reduces lung metastasis.

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CIP2A expression is increased in prostate cancer

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cAMP Counter-regulates Insulin-mediated Protein Phosphatase-2A Inactivation in Rat Skeletal Muscle Cells

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Bortezomib Overcomes Tumor Necrosis Factor-related Apoptosis-inducing Ligand Resistance in Hepatocellular Carcinoma Cells in Part through the Inhibition of the Phosphatidylinositol 3-Kinase/Akt Pathway

Chen, K., Yeh, P.-Y., Hsu, C., Hsu, C., Lu, Y., Hsieh, H., Chen, P., & Cheng, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806268200 · Cited by 82 · see citing works

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

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Localization ofSaccharomyces cerevisiaeProtein Phosphatase 2A Subunits throughout Mitotic Cell Cycle

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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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PP2A: The Wolf in Sheep’s Clothing?

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Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits.

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Folate Deficiency Induces In Vitro and Mouse Brain Region-Specific Downregulation of Leucine Carboxyl Methyltransferase-1 and Protein Phosphatase 2A Bα Subunit Expression That Correlate with Enhanced Tau Phosphorylation

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Functional Domains of Template-Activating Factor-I as a Protein Phosphatase 2A Inhibitor

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IL-10 Promotes Tumor Aggressiveness via Upregulation of CIP2A Transcription in Lung Adenocarcinoma

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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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Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation

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Discovery and Optimization of Sulfonyl Acrylonitriles as Selective, Covalent Inhibitors of Protein Phosphatase Methylesterase-1

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RRR-alpha-tocopheryl succinate induces MDA-MB-435 and MCF-7 human breast cancer cells to undergo differentiation.

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CIP2A oncoprotein controls cell growth and autophagy through mTORC1 activation

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Vitamin E analogues as anticancer agents: Lessons from studies with α-tocopheryl succinate

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Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells

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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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Ser9 phosphorylation causes cytoplasmic detention of I2PP2A/SET in Alzheimer disease

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CIP2A overexpression is associated with c-Myc expression in colorectal cancer

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Evaluation of PPP2R2A as a prostate cancer susceptibility gene: A comprehensive germline and somatic study

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Structure-Activity Relationship Studies of Fostriecin, Cytostatin, and Key Analogs, with PP1, PP2A, PP5, and (β12–β13)-Chimeras (PP1/PP2A and PP5/PP2A), Provide Further Insight into the Inhibitory Actions of Fostriecin Family Inhibitors

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Aberrant intracellular localization of SET‐CAN fusion protein, associated with a leukemia, disorganizes nuclear export

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Modulation of Protein Phosphatase 2A Activity Alters Androgen-Independent Growth of Prostate Cancer Cells: Therapeutic Implications

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Reduced expression of the A? subunit of protein phosphatase 2A in human gliomas in the absence of mutations in the A? and A? subunit genes

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PPP2R1A mutations are common in the serous type of endometrial cancer

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Regulation of protein phosphatase 2A methylation by LCMT1 and PME‐1 plays a critical role in differentiation of neuroblastoma cells

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Over expression of PPP2R2C inhibits human glioma cells growth through the suppression of mTOR pathway

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Protein Phosphatase 2A Regulates Innate Immune and Proteolytic Responses to Cigarette Smoke Exposure in the Lung

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c-Jun involvement in vitamin E succinate induced apoptosis of reticuloendotheliosis virus transformed avian lymphoid cells

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Cardiac function is regulated by B56α-mediated targeting of protein phosphatase 2A (PP2A) to contractile relevant substrates

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PP2A activity is controlled by methylation and regulates oncoprotein expression in melanoma cells: A mechanism which participates in growth inhibition induced by chloroethylnitrosourea treatment

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The E3 Ubiquitin Ligase- and Protein Phosphatase 2A (PP2A)-binding Domains of the Alpha4 Protein Are Both Required for Alpha4 to Inhibit PP2A Degradation

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Leucine Carboxyl Methyltransferase 1 (LCMT1)-dependent Methylation Regulates the Association of Protein Phosphatase 2A and Tau Protein with Plasma Membrane Microdomains in Neuroblastoma Cells

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PPP2R2C Loss Promotes Castration-Resistance and Is Associated with Increased Prostate Cancer-Specific Mortality

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A Novel Assay for Protein Phosphatase 2A (PP2A) Complexes In Vivo Reveals Differential Effects of Covalent Modifications on Different Saccharomyces cerevisiae PP2A Heterotrimers

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Ceramide Produces Apoptosis Through Induction of p27kip1by Protein Phosphatase 2A-dependent Akt Dephosphorylation in PC-3 Prostate Cancer Cells

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

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Carnosic acid stimulates glucose uptake in skeletal muscle cells via a PME-1/PP2A/PKB signalling axis

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CIP2A is overexpressed in human ovarian cancer and regulates cell proliferation and apoptosis

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Sphingosine Interaction with Acidic Leucine-rich Nuclear Phosphoprotein-32A (ANP32A) Regulates PP2A Activity and Cyclooxygenase (COX)-2 Expression in Human Endothelial Cells

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

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Ethoxysanguinarine Induces Inhibitory Effects and Downregulates CIP2A in Lung Cancer Cells

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Development of erlotinib derivatives as CIP2A-ablating agents independent of EGFR activity

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CIP2A Influences Survival in Colon Cancer and Is Critical for Maintaining Myc Expression

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PCOTH, a Novel Gene Overexpressed in Prostate Cancers, Promotes Prostate Cancer Cell Growth through Phosphorylation of Oncoprotein TAF-Iβ/SET

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Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B)

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A high-resolution integrated map spanning the SDHD gene at 11q23: a 1.1-Mb BAC contig, a partial transcript map and 15 new repeat polymorphisms in a tumour-suppressor region

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Therapeutic Re-Activation of Protein Phosphatase 2A in Acute Myeloid Leukemia

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The biologic activity of the immunoregulatory lipoprotein, LDL-In is independent of its free fatty acid content.

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PTEN/MMAC1 expression in melanoma resection specimens

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PP2A: The Achilles Heal in MDS with 5q Deletion

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PP2A as a master regulator of the cell cycle

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Micropeptide CIP2A-BP encoded by LINC00665 inhibits triple-negative breast cancer progression

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

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Identification of Integrator-PP2A complex (INTAC), an RNA polymerase II phosphatase

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Arctigenin attenuates diabetic kidney disease through the activation of PP2A in podocytes

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Mission Possible: Advances in MYC Therapeutic Targeting in Cancer

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Selective Inhibition of STRN3-Containing PP2A Phosphatase Restores Hippo Tumor-Suppressor Activity in Gastric Cancer

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Targeting PP2A in cancer: Combination therapies

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Covalent Ligand Discovery against Druggable Hotspots Targeted by Anti-cancer Natural Products

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Targeting protein phosphatases for the treatment of inflammation-related diseases: From signaling to therapy

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miR-19b enhances proliferation and apoptosis resistance via the EGFR signaling pathway by targeting PP2A and BIM in non-small cell lung cancer

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Cathepsin S: investigating an old player in lung disease pathogenesis, comorbidities, and potential therapeutics

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

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Personalized medicine in breast cancer: pharmacogenomics approaches

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The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases

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K27-linked ubiquitination of BRAF by ITCH engages cytokine response to maintain MEK-ERK signaling

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Activation of PP2A and Inhibition of mTOR Synergistically Reduce MYC Signaling and Decrease Tumor Growth in Pancreatic Ductal Adenocarcinoma

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Treatment of inflammatory arthritis via targeting of tristetraprolin, a master regulator of pro-inflammatory gene expression

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Coordination of Protein Kinase and Phosphoprotein Phosphatase Activities in Mitosis

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Crystal structure of a PP2A B56-BubR1 complex and its implications for PP2A substrate recruitment and localization

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Antiphospholipid antibodies induce thrombosis by PP2A activation via apoER2-Dab2-SHC1 complex formation in endothelium

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Eya3 partners with PP2A to induce c-Myc stabilization and tumor progression

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Loss of hepatic aldolase B activates Akt and promotes hepatocellular carcinogenesis by destabilizing the Aldob/Akt/PP2A protein complex

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

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Protein phosphatases in the RNAPII transcription cycle: erasers, sculptors, gatekeepers, and potential drug targetsPreprint

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Dysregulation of protein phosphatase 2A in parkinson disease and dementia with lewy bodies

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Role of Endoplasmic Reticulum-Mitochondria Communication in Type 2 Diabetes

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Transcriptional Effects of ApoE4: Relevance to Alzheimer’s Disease

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Direct activation of PP2A for the treatment of tyrosine kinase inhibitor–resistant lung adenocarcinoma

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MAP4K4 is a novel MAPK/ERK pathway regulator required for lung adenocarcinoma maintenance

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The Role of MicroRNAs in Muscle Tissue Development in Beef Cattle

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Cancer driver mutations in endometriosis: Variations on the major theme of fibrogenesis

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Uncovering BRD4 hyperphosphorylation associated with cellular transformation in NUT midline carcinoma

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PP2A: A Promising Biomarker and Therapeutic Target in Endometrial Cancer

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Cucurbitacin B Induces the Lysosomal Degradation of EGFR and Suppresses the CIP2A/PP2A/Akt Signaling Axis in Gefitinib-Resistant Non-Small Cell Lung Cancer

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CHK1 Inhibitor Blocks Phosphorylation of FAM122A and Promotes Replication Stress

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Netrin-1 promotes naive pluripotency through Neo1 and Unc5b co-regulation of Wnt and MAPK signalling

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PP2Ac Deficiency Enhances Tumor Immunogenicity by Activating STING–Type I Interferon Signaling in Glioblastoma

Mondal, I., Das, O., Sun, R., Jian, G., Yu, B., Diaz, A. A., Behnan, J., Dubey, A., Meng, Z., Eskandar, E. N., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-3382 · Cited by 52 · see citing works

Modulation of VEGF receptor 2 signaling by protein phosphatases

Corti, F., & Simons, M. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.11.022 · Cited by 50 · see citing works

Stemness Is Enhanced in Gastric Cancer by a SET/PP2A/E2F1 Axis

Enjoji, S., Yabe, R., Tsuji, S., Yoshimura, K., Kawasaki, H., Sakurai, M., Sakai, Y., Takenouchi, H., Yoshino, S., Hazama, S., et al. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0393 · Cited by 49 · see citing works

Loss of protein phosphatase 2A regulatory subunit B56δ promotes spontaneous tumorigenesis in vivo

Lambrecht, C., Libbrecht, L., Sagaert, X., Pauwels, P., Hoorne, Y., Crowther, J., Louis, J. V., Sents, W., Sablina, A., & Janssens, V (2018) · Oncogene · doi:10.1038/onc.2017.350 · Cited by 50 · see citing works

Prolyl oligopeptidase inhibition activates autophagy via protein phosphatase 2A

Svarcbahs, R., Jäntti, M. H., Kilpeläinen, T. P., Julku, U. H., Urvas, L., Kivioja, S., Norrbacka, S., & Myöhänen, T. T. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104558 · Cited by 50 · see citing works

Inactivation of PP2A by a recurrent mutation drives resistance to MEK inhibitors

O’Connor, C. M., Leonard, D., Wiredja, D., Avelar, R. A., Wang, Z., Schlatzer, D., Bryson, B., Tokala, E., Taylor, S. E., Upadhyay, A., et al. (2020) · Oncogene · doi:10.1038/s41388-019-1012-2 · Cited by 48 · see citing works

Protein phosphatase 2A activation as a therapeutic strategy for managing MYC-driven cancers

Farrington, C. C., Yuan, E., Mazhar, S., Izadmehr, S., Hurst, L., Allen-Petersen, B. L., Janghorban, M., Chung, E. M., Wolczanski, G., Galsky, M. D., et al. (2020) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)49933-9 · Cited by 47 · see citing works

The PHLPP2 phosphatase is a druggable driver of prostate cancer progression

Nowak, D. G., Cohen‐Katsenelson, K., Watrud, K. E., Chen, M., Mathew, G., D’Andrea, V. D., Lee, M. F., Swamynathan, M. M., Casanova‐Salas, I., Jibilian, M. C., et al. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201902048 · Cited by 48 · see citing works

Interaction of the Hippo Pathway and Phosphatases in Tumorigenesis

Emami, S. S., Zhang, D., & Yang, X. (2020) · Cancers · doi:10.3390/cancers12092438 · Cited by 46 · see citing works

Downregulation of protein phosphatase 2A by apolipoprotein E: Implications for Alzheimer's disease

Theendakara, V. P., Bredesen, D. E., & Rao, R. V. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.07.002 · Cited by 46 · see citing works

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

PP2Ac/STRN4 negatively regulates STING-type I IFN signaling in tumor-associated macrophages

Ho, W. S., Mondal, I., Xu, B., Das, O., Sun, R., Chiou, P., Cai, X., Tahmasebinia, F., McFadden, E., Wu, C. Y.-J., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci162139 · Cited by 45 · see citing works

Transcriptional control of metabolism by interferon regulatory factors

Ahmad, Z., Kahloan, W., & Rosen, E. D. (2024) · Nature Reviews Endocrinology · doi:10.1038/s41574-024-00990-0 · Cited by 42 · see citing works

Altering phosphorylation in cancer through PP2A modifiers

Johnson, H., Narayan, S., & Sharma, A. K. (2024) · Cancer Cell International · doi:10.1186/s12935-023-03193-1 · Cited by 41 · see citing works

Distinct B subunits of PP 2A regulate the NF ‐κB signalling pathway through dephosphorylation of IKK β, IκBα and RelA

Tsuchiya, Y., Osaki, K., Kanamoto, M., Nakao, Y., Takahashi, E., Higuchi, T., & Kamata, H. (2017) · FEBS Letters · doi:10.1002/1873-3468.12912 · Cited by 40 · see citing works

The impact of phosphatases on proliferative and survival signaling in cancer

Narla, G., Sangodkar, J., & Ryder, C. B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2826-8 · Cited by 39 · see citing works

Protein phosphatase 2A (PP2A): a key phosphatase in the progression of chronic obstructive pulmonary disease (COPD) to lung cancer

Nader, C. P., Cidem, A., Verrills, N. M., & Ammit, A. J. (2019) · Respiratory Research · doi:10.1186/s12931-019-1192-x · Cited by 40 · see citing works

Protein phosphatase 2A activation as a therapeutic strategy for managing MYC-driven cancers

Farrington, C. C., Yuan, E., Mazhar, S., Izadmehr, S., Hurst, L., Allen-Petersen, B. L., Janghorban, M., Chung, E. M., Wolczanski, G., Galsky, M. D., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011443 · Cited by 38 · see citing works

Antihelminthic drug niclosamide inhibits CIP2A and reactivates tumor suppressor protein phosphatase 2A in non-small cell lung cancer cells

Kim, M.-O., Choe, M. H., Yoon, Y. N., Ahn, J., Yoo, M., Jung, K., An, S., Hwang, S., Oh, J. S., & Kim, J. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.08.009 · Cited by 38 · see citing works

STRIP1, a core component of STRIPAK complexes, is essential for normal mesoderm migration in the mouse embryo

Bazzi, H., Soroka, E., Alcorn, H. L., & Anderson, K. V. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713535114 · Cited by 37 · see citing works

MicroRNA-652 induces NED in LNCaP and EMT in PC3 prostate cancer cells

Nam, R. K., Benatar, T., Amemiya, Y., Wallis, C. J. D., Romero, J. M., Tsagaris, M., Sherman, C., Sugar, L., & Seth, A. K. (2018) · Oncotarget · doi:10.18632/oncotarget.24937 · Cited by 37 · see citing works

The Role of MYC and PP2A in the Initiation and Progression of Myeloid Leukemias

Pippa, R., & Odero, M. D. (2020) · Cells · doi:10.3390/cells9030544 · Cited by 36 · see citing works

The PP2A subunit PR130 is a key regulator of cell development and oncogenic transformation

Dzulko, M., Pons, M., Henke, A., Schneider, G., & Krämer, O. H. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188453 · Cited by 37 · see citing works

New Approaches to Difficult Drug Targets: The Phosphatase Story

Lazo, J. S., McQueeney, K. E., & Sharlow, E. R. (2017) · SLAS DISCOVERY · doi:10.1177/2472555217721142 · Cited by 36 · see citing works

Biased holoenzyme assembly of protein phosphatase 2A (PP2A): From cancer to small molecules

Haanen, T. J., O’Connor, C. M., & Narla, G. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102656 · Cited by 36 · see citing works

Regulation of the stability and activity of CDC25A and CDC25B by protein phosphatase PP2A and 14-3-3 binding

Kohama, Y., Saito, M., Yada, M., & Sakurai, H. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.11.017 · Cited by 35 · see citing works

Metformin Inhibit Lung Cancer Cell Growth and Invasion in Vitro as Well as Tumor Formation in Vivo Partially by Activating PP2A

Zhou, X., Liu, S., Lin, X., Xu, L., Mao, X., Liu, J., Zhang, Z., Jiang, W., & Zhou, H. (2019) · Medical Science Monitor · doi:10.12659/msm.912059 · Cited by 35 · see citing works

RABL6A inhibits tumor-suppressive PP2A/AKT signaling to drive pancreatic neuroendocrine tumor growth

Umesalma, S., Kaemmer, C. A., Kohlmeyer, J. L., Letney, B. L., Schab, A. M., Reilly, J. A., Sheehy, R. M., Hagen, J., Tiwari, N., Zhan, F., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci123049 · Cited by 35 · see citing works

To be or not to be: PP2A as a dual player in CNS functions, its role in neurodegeneration, and its interaction with brain insulin signaling

Javadpour, P., Dargahi, L., Ahmadiani, A., & Ghasemi, R. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03063-y · Cited by 35 · see citing works

Protein phosphatase 2A-B55β mediated mitochondrial p-GPX4 dephosphorylation promoted sorafenib-induced ferroptosis in hepatocellular carcinoma via regulating p53 retrograde signaling

Qian, B., Che, L., Du, Z., Guo, N.-J., Wu, X.-M., Yang, L., Zheng, Z.-X., Gao, Y., Wang, M., Chen, X., et al. (2023) · Theranostics · doi:10.7150/thno.82132 · Cited by 34 · 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

Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition

Musante, V., Li, L., Kanyo, J. E., Lam, T. T., Colangelo, C. M., Cheng, S. K., Brody, A. H., Greengard, P., Novère, N. G. L., & Nairn, A. C. (2017) · eLife · doi:10.7554/elife.24998 · Cited by 33 · see citing works

PPP2R2A prostate cancer haploinsufficiency is associated with worse prognosis and a high vulnerability to B55α/PP2A reconstitution that triggers centrosome destabilization

Zhao, Z., Kurimchak, A., Nikonova, A. S., Feiser, F., Wasserman, J. S., Fowle, H. A., Varughese, T., Connors, M., Johnson, K. J., Makhov, P. B., et al. (2019) · Oncogenesis · doi:10.1038/s41389-019-0180-9 · Cited by 31 · see citing works

ATM-associated signalling triggers the unfolded protein response and cell death in response to stress

Hotokezaka, Y., Katayama, I., & Nakamura, T. (2020) · Communications Biology · doi:10.1038/s42003-020-1102-2 · Cited by 32 · see citing works

A Quantitative Chemical Proteomic Strategy for Profiling Phosphoprotein Phosphatases from Yeast to Humans

Lyons, S. P., Jenkins, N. P., Nasa, I., Choy, M. S., Adamo, M. E., Page, R., Peti, W., Moorhead, G. B. G., & Kettenbach, A. N. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000822 · Cited by 29 · see citing works

Perturbation of Specific Signaling Pathways Is Involved in Initiation of Mouse Liver Fibrosis

Chen, L., Guo, P., Li, W., Fang, F., Zhu, W., Fan, J., Wang, F., Gao, Y., Zhao, Q., Wang, Q., et al. (2020) · Hepatology · doi:10.1002/hep.31457 · Cited by 31 · see citing works

Emerging insights into serine/threonine-specific phosphoprotein phosphatase function and selectivity

Kokot, T., & Köhn, M. (2022) · Journal of Cell Science · doi:10.1242/jcs.259618 · Cited by 30 · see citing works

PPP2R5A: A multirole protein phosphatase subunit in regulating cancer development

Mao, Z., Liu, C., Lin, X., Sun, B., & Su, C. (2018) · Cancer Letters · doi:10.1016/j.canlet.2017.11.024 · Cited by 30 · see citing works

Protein phosphatase 2A activation mechanism contributes to JS-K induced caspase-dependent apoptosis in human hepatocellular carcinoma cells

Liu, L., Huang, Z., Chen, J., Wang, J., & Wang, S. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0823-2 · Cited by 30 · see citing works

Protein Phosphatase 2A as a Drug Target in the Treatment of Cancer and Alzheimer’s Disease

Wei, H., Zhang, H., Xie, J., Meng, D., Wang, X., Ke, D., Zeng, J., & Liu, R. (2020) · Current Medical Science · doi:10.1007/s11596-020-2140-1 · Cited by 29 · see citing works

Role of Protein Phosphatase 2A in Osteoblast Differentiation and Function

Okamura, H., Yoshida, K., Morimoto, H., Teramachi, J., Ochiai, K., Haneji, T., & Yamamoto, A. (2017) · Journal of Clinical Medicine · doi:10.3390/jcm6030023 · Cited by 28 · see citing works

Piecing Together a Broken Tumor Suppressor Phosphatase for Cancer Therapy

Westermarck, J. K., & Neel, B. G. (2020) · Cell · doi:10.1016/j.cell.2020.04.005 · Cited by 28 · see citing works

Curcumin and derivatives function through protein phosphatase 2A and presenilin orthologues in Dictyostelium discoideum

Cocorocchio, M., Baldwin, A. J., Stewart, B., Kim, L. W., Harwood, A. J., Thompson, C. R. L., Andrews, P. L. R., & Williams, R. S. B. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.032375 · Cited by 28 · see citing works

Berberine attenuates pulmonary arterial hypertension via protein phosphatase 2A signaling pathway both in vivo and in vitro

Luo, J., Gu, Y., Liu, P., Jiang, X., Yu, W., Ye, P., Chao, Y., Yang, H., Zhu, L., Zhou, L., et al. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26940 · Cited by 28 · see citing works

Regulation and role of the PP2A-B56 holoenzyme family in cancer

Peris, I., Romero-Murillo, S., Vicente, C., Narla, G., & Odero, M. D. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188953 · Cited by 29 · see citing works

Chronic Cigarette Smoke Exposure Subdues PP2A Activity by Enhancing Expression of the Oncogene CIP2A

Nath, S., Ohlmeyer, M. H. J., Salathe, M. A., Poon, J., Baumlin, N., Foronjy, R., & Geraghty, P. M. (2018) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2018-0173oc · Cited by 27 · see citing works

MEF2A Regulates the MEG3-DIO3 miRNA Mega Cluster-Targeted PP2A Signaling in Bovine Skeletal Myoblast Differentiation

Wang, Y., Mei, C., Su, X., Wang, H., Yang, W., & Zan, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112748 · Cited by 27 · see citing works

Hypoxia-Induced miR-675-5p Supports β-Catenin Nuclear Localization by Regulating GSK3-β Activity in Colorectal Cancer Cell Lines

Saieva, L., Barreca, M. M., Zichittella, C., Prado, M. G., Tripodi, M., Alessandro, R., & Conigliaro, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113832 · Cited by 27 · see citing works

Sphingolipids inhibit endosomal recycling of nutrient transporters by inactivating ARF6

Finicle, B. T., Ramirez, M. U., Liu, G., Selwan, E. M., McCracken, A. N., Yu, J., Joo, Y., Nguyen, J., Ou, K., Roy, S. G., et al. (2018) · Journal of Cell Science · doi:10.1242/jcs.213314 · Cited by 26 · see citing works

PTEN deficiency facilitates gemcitabine efficacy in cancer by modulating the phosphorylation of PP2Ac and DCK

Jiang, T., Cui, X.-W., Zeng, T., Pan, Y., Lin, Y., Feng, X., Tan, Y., Yuan, Z., Dong, L., & Wang, H. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.add7464 · Cited by 26 · see citing works

The evolution of small molecule enzyme activators

Dow, L. F., Case, A. M., Paustian, M. P., Pinkerton, B. R., Simeon, P., & Trippier, P. C. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00399j · Cited by 29 · see citing works

The Cell Cycle Checkpoint System MAST(L)-ENSA/ARPP19-PP2A is Targeted by cAMP/PKA and cGMP/PKG in Anucleate Human Platelets

Kumm, E. J., Pagel, O., Gambaryan, S. P., Walter, U., Zahedi, R. P., Smolenski, A., & Jurk, K. (2020) · Cells · doi:10.3390/cells9020472 · Cited by 26 · see citing works

Activated Protein Phosphatase 2A Disrupts Nutrient Sensing Balance Between Mechanistic Target of Rapamycin Complex 1 and Adenosine Monophosphate–Activated Protein Kinase, Causing Sarcopenia in Alcohol‐Associated Liver Disease

Davuluri, G., Welch, N., Sekar, J., Gangadhariah, M. H., Alchirazi, K. A., Mohan, M. L., Kumar, A., Kant, S., Thapaliya, S., Stine, M., et al. (2020) · Hepatology · doi:10.1002/hep.31524 · Cited by 26 · see citing works

PP2A and Its Inhibitors in Helper T-Cell Differentiation and Autoimmunity

Khan, M. M., Ullah, U., Khan, M. H., & Lahesmaa, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.786857 · Cited by 25 · see citing works

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

Seshacharyulu, P., Pandey, P., Datta, K., & Batra, S. K. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.02.036 · Cited by 479 · see citing works

Therapeutic targeting of PP2A

O’Connor, C. M., Perl, A. L., Léonard, D., Sangodkar, J., & Narla, G. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.008 · Cited by 181 · see citing works

Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

Lambrecht, C., Haesen, D., Sents, W., Ivanova, E., & Janssens, V. (2013) · Methods in Molecular Biology · doi:10.1007/978-1-62703-562-0_17 · Cited by 140 · see citing works

Targeting PP2A in cancer: an underrated option

Sarais, F., Krempien, F., Koehn, C., Brewing, L., Classen, C. F., Walter, M., & Shokraie, O. (2025) · Journal of Experimental &amp; Clinical Cancer Research · doi:10.1186/s13046-025-03560-y · Cited by 8 · see citing works

PP2A-Mediated Anticancer Therapy

Chen, W., Wang, Z., Jiang, C., & Ding, Y. (2013) · Gastroenterology Research and Practice · doi:10.1155/2013/675429 · Cited by 57 · see citing works