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

Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,927

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

Yeh, E., Cunningham, M., Arnold, H., Chasse, D., Monteith, T., Ivaldi, G., Hahn, W. C., Stukenberg, P. T., Shenolikar, S., Uchida, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1110 · Cited by 791

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

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

Chen, J., Martin, B. L., & Brautigan, D. L. (1992) · Science · doi:10.1126/science.1325671 · Cited by 601

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

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

Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme

Cho, U. S., & Xu, W. (2007) · Nature · doi:10.1038/nature05351 · Cited by 459

Structure of the Protein Phosphatase 2A Holoenzyme

Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.11.033 · Cited by 450

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

Groves, M. R., Hanlon, N., Turowski, P., Hemmings, B. A., & Barford, D. (1999) · Cell · doi:10.1016/s0092-8674(00)80963-0 · Cited by 442

PP2A: the expected tumor suppressor

Janssens, V., Goris, J., & Van Hoof, C. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.12.004 · Cited by 426

HMGA2 and protein leucine methylation drive pancreatic cancer lineage plasticity

Dobersch, S., Yamamoto, N., Schutter, A., Cavender, S. M., Robertson, T. M., Kartha, N., Samraj, A. N., Doron, B., Poole, L. A., Wladyka, C. L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60129-1 · Cited by 8

The PP2A-B55α phosphatase is a master regulator of mitochondrial degradation and biogenesis

Cianfanelli, V., Nanni, M., Corrà, S., Mauri, S., Sumpton, D. P., Lilla, S., Cegli, R. D., Bordi, M., Milletti, G., Ferraina, C., et al. (2025) · Science Advances · doi:10.1126/sciadv.adw7376 · Cited by 8

Protein phosphatase-2A activation is a critical step for enzastaurin activity in chronic lymphoid leukemia cells

Liffraud, C., Quillet‐Mary, A., Fournié, J., Laurent, G., & Ysebaert, L. (2011) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2011.634041 · Cited by 7

Clinical and molecular characteristics of a novel rare de novo variant in PPP2CA in a patient with a developmental disorder, autism, and epilepsy

Verbinnen, I., Procknow, S. S., Lenaerts, L., Reynhout, S., Mehregan, A., Ulens, C., Janssens, V., & King, K. A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1059938 · Cited by 7

Novel small molecular compound 2JY-OBZ4 alleviates AD pathology in cell models via regulating multiple targets

Guo, Q., Wu, G., Huang, F., Wei, Z. C., Wang, J., Zhang, B., Liu, R., Yang, Y., Wang, X., & Li, H. (2022) · Aging · doi:10.18632/aging.204336 · Cited by 7

C-glycosides analogues of the okadaic acid central fragment exert neuroprotection via restoration of PP2A-phosphatase activity: A rational design of potential drugs for Alzheimer's disease targeting tauopathies

Arribas, R. L., Viejo, L., Bravo, I., Martinez-Castillo, M., Ramos, E., Romero, A., García‐Frutos, E. M., Janssens, V., Montiel, C., & Rı́os, C. D. L. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115245 · Cited by 9

PME-1 sensitizes glioblastoma cells to oxidative stress-induced cell death by attenuating PP2A-B55α-mediated inactivation of MAPKAPK2-RIPK1 signaling

Guffens, L., Derua, R., & Janssens, V. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01572-1 · Cited by 7

The B″ regulatory subunit of protein phosphatase 2A mediates the dephosphorylation of rice retinoblastoma-related protein-1

Ábrahám, E., Yu, P., Farkas, I., Darula, Z., Varga, E., Lukács, N., Ayaydin, F., Medzihradszky, K. F., Dombrádi, V., Dudits, D., et al. (2014) · Plant Molecular Biology · doi:10.1007/s11103-014-0265-y · Cited by 7

The Bait Compatibility Index: Computational Bait Selection for Interaction Proteomics Experiments

Saha, S., Kaur, P., & Ewing, R. M. (2010) · Journal of Proteome Research · doi:10.1021/pr100267t · Cited by 7

Cellular Protein Phosphatase 2A Regulates Cell Survival Mechanisms in Influenza A Virus Infection

Gerlt, V., Mayr, J., Sarto, J. D., Ludwig, S., & Boergeling, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011164 · Cited by 7

CDC6 as a Key Inhibitory Regulator of CDK1 Activation Dynamics and the Timing of Mitotic Entry and Progression

Dika, M. E., Dudka, D., Kloc, M., & Kubiak, J. Z. (2023) · Biology · doi:10.3390/biology12060855 · Cited by 6

White spot syndrome virus hijacks host PP2A-FOXO axes to promote its propagation

Li, C., Zhang, P., Hong, P.-P., Niu, G.-J., Wang, X., Zhao, X., & Wang, J. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128333 · Cited by 6

Folate and Neurological Disease

Bottiglieri, T., & Reynolds, E. H. (2009) · CRC Press eBooks · doi:10.1201/9781420071252-c14 · Cited by 6

Caenorhabditis elegans phosphatase complexes in UniProtKB and Complex Portal

Bye‐A‐Jee, H., Zaru, R., Magrane, M., & Orchard, S. E. (2020) · FEBS Journal · doi:10.1111/febs.15213 · Cited by 7

A Novel Role of PP2A Methylation in the Regulation of Tight Junction Assembly and Integrity

Schuhmacher, D., Sontag, J., & Sontag, E. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.911279 · Cited by 5

Uncoupling of Mitosis and Cytokinesis Upon a Prolonged Arrest in Metaphase Is Influenced by Protein Phosphatases and Mitotic Transcription in Fission Yeast

Chica, N., Portantier, M., Nyquist-Andersen, M., Burriel, S. E., & López‐Avilés, S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.876810 · Cited by 5

Quantum-based modeling implies that bidentate Arg89-substrate binding enhances serine/threonine protein phosphatase-2A(PPP2R5D/PPP2R1A/PPP2CA)-mediated dephosphorylation

Salter, E. A., Wierzbicki, A., Honkanen, R. E., & Swingle, M. R. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1141804 · Cited by 5

Structural characterization of methylation-independent PP2A assembly guides alphafold2Multimer prediction of family-wide PP2A complexes

Wachter, F., Nowak, R. P., Ficarro, S. B., Marto, J. A., & Fischer, E. S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107268 · Cited by 5

Loss of LEUCINE CARBOXYL METHYLTRANSFERASE 1 interferes with metal homeostasis in Arabidopsis and enhances susceptibility to environmental stresses

Creighton, M. T., Nemie-Feyissa, D., Zaman, N., Johansen, S. S., Dysjaland, H., Heidari, B., & Lillo, C. (2022) · Journal of Plant Physiology · doi:10.1016/j.jplph.2022.153843 · Cited by 6

Identification of protein phosphatase interacting proteins from normal and UVA-irradiated HaCaT cell lysates by surface plasmon resonance based binding technique using biotin–microcystin-LR as phosphatase capturing molecule

Bécsi, B., Dedinszki, D., Gyémánt, G., Máthé, C., Vasas, G., Lontay, B., & Erdődi, F. (2014) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2014.06.004 · Cited by 5

p53/FBXL20 axis negatively regulates the protein stability of PR55α, a regulatory subunit of PP2A Ser/Thr phosphatase

Madduri, L. S. V., Brandquist, N. D., Palanivel, C., Talmon, G. A., Baine, M. J., Zhou, S., Enke, C. A., Johnson, K. R., Ouellette, M. M., & Yan, Y. (2021) · Neoplasia · doi:10.1016/j.neo.2021.10.002 · Cited by 5

Apoptosis and Autoimmune Disorders

Halaby, R. (2012) · InTech eBooks · doi:10.5772/48164 · Cited by 5

Supplementary Material and Methods

Rosato, P. C., Anastasiadou, E., Garg, N., Lenze, D., Boccellato, F., Vincenti, S., Severa, M., Coccia, E. M., Bigi, R., Cirone, M., et al. (2012) · Cited by 3

Update on Phosphorylation-Mediated Brassinosteroid Signaling Pathways

Lee, Y., & Kim, S. H. (2012) · Journal of Life Science · doi:10.5352/jls.2012.22.3.428 · Cited by 4

Role of protein phosphatases in genitourinary cancers

Igawa, T. (2016) · International Journal of Urology · doi:10.1111/iju.13197 · Cited by 4

Dysregulated protein kinase/phosphatase networks in SLE T cells

Suárez‐Rojas, G., & Crispín, J. C. (2022) · Clinical Immunology · doi:10.1016/j.clim.2022.108952 · Cited by 4

Germline Determination: Don't Mind the P Granules

Marcello, M. R., & Singson, A. W. (2011) · Current Biology · doi:10.1016/j.cub.2011.01.029 · Cited by 4

Regulation of Striatal Signaling by Protein Phosphatases

Girault, J., Greengard, P., & Nairn, A. C. (2016) · Handbook of behavioral neuroscience · doi:10.1016/b978-0-12-802206-1.00029-5 · Cited by 5

Alpha4‐overexpressing HL7702 cells can counteract microcystin‐LR effects on cytoskeletal structure

Huang, P., Wang, S., Weng, D., & Xu, L. (2018) · Environmental Toxicology · doi:10.1002/tox.22585 · Cited by 4

Emerging Dynamics of Brassinosteroids Research

Sharma, I., Kaur, N., Saini, S., & Pati, P. K. (2013) · Springer eBooks · doi:10.1007/978-81-322-1683-4_1 · Cited by 4

Analysis of the potential role of fission yeast PP2A in spindle assembly checkpoint inactivation

Deng, D., Wang, X., Yue, K., Wang, Y., & Jin, Q. (2022) · The FASEB Journal · doi:10.1096/fj.202101884r · Cited by 2

A disease-associated PPP2R3C-MAP3K1 phospho-regulatory module controls centrosome function

Ganga, A. K., Sweeney, L. K., Rubio-Ramos, A., Wrinn, C. M., Bishop, C. S., Hamel, V., Guichard, P., & Breslow, D. K. (2024) · Current Biology · doi:10.1016/j.cub.2024.08.058 · Cited by 3

Aurora Kinase A Regulation by Cysteine Oxidative Modification

Lee, I., & Lee, B. (2023) · Antioxidants · doi:10.3390/antiox12020531 · Cited by 4

NEURONAL FUNCTIONS OF PROTEIN PHOSPHATASE 2A

Leung, H. (2013) · Neuroscience International · doi:10.3844/amjnsp.2013.46.55 · Cited by 3

Protein Phosphatase 2A Has Positive and Negative Roles in Autophagy

Kabi, A., & McDonald, C. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405529-2.00015-9 · Cited by 4

Ser/Thr Phosphatases: The New Frontier for Myeloid Leukemia Therapy?

Amanda, M., Kathryn, G., & Nicole, M. (2011) · InTech eBooks · doi:10.5772/26425 · Cited by 3

Protein Phosphatases and DNA Replication Initiation

Stark, M. J. R., Hiraga, S., & Donaldson, A. D. (2016) · Springer eBooks · doi:10.1007/978-3-319-24696-3_23 · Cited by 3

Post‐Translational Modifications in Pancreatic Cancer: Mechanisms to Clinical Applications

Zhang, G., Zhu, W., Zhao, Y., Cheng, Y., & Zhou, W. (2026) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.70441 · Cited by 2

Protein Phosphatase Methylesterase 1: A potential therapeutic target and companion diagnostic marker for cancer

(2014) · Cancer Cell & Microenvironment · doi:10.14800/ccm.299 · Cited by 2

Research progress on the relationship between the TOR signaling pathway regulator, epigenetics, and tumor development

Sun, J., Yang, M., Zhao, W., Wang, F., Yang, L., Tan, C., Hu, T., Zhu, H., & Zhao, G. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.1006936 · Cited by 2

Structural and functional studies of proteins in cell signaling and cancer

Dovega, R. (2014) · Figshare · Cited by 2

Functional analysis of STRIPAK complex components in the filamentous ascomycete Sordaria macrospora

Reschka, E. J. (2018) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7002 · Cited by 2

Relevance of acquired T cell molecular defects in the immunopathogenesis of SLE

Rosetti, F., Madera-Salcedo, I. K., & Crispín, J. C. (2024) · Clinical Immunology · doi:10.1016/j.clim.2024.110225 · Cited by 1

A guide to selecting high-performing antibodies for Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PPP2R5D) for use in Western Blot, immunoprecipitation and immunofluorescence

Ayoubi, R., Fotouhi, M., Alende, C., Southern, K., Laflamme, C., & NeuroSGC/YCharOS/EDDU collaborative group (2024) · F1000Research · doi:10.12688/f1000research.145146.2 · Cited by 1

PP2Acα regulates sleep amount and sleep homeostasis in mice

Zhou, S., Shi, B., Chen, L., Yin, X., Liu, M., Wu, C., Wang, H., Wang, X., Li, B., Wang, F., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08437-6 · Cited by 1

Interplay Between Protein Phosphatase 2A (PP2A) and SE Translocation (SET) as Macromolecular Target of Anticancer Compounds: A Combined Computational and Experimental Study

Ribaudo, G., Pagano, M. A., Anyanwu, M., Giannangeli, M., Vezzoli, M., Visentin, A., Frezzato, F., Trentin, L., Brunati, A. M., & Gianoncelli, A. (2025) · Macromol—A Journal of Macromolecular Research · doi:10.3390/macromol5030043 · Cited by 1

PP2A methylesterase, PME‐1, and PP2A methyltransferase, LCMT‐1, control sensitivity to impairments caused by injury‐related oligomeric tau

Sundaresh, S. N., Vogel, E. W., Hue, C. D., Zhang, H., Staniszewski, A., Berman, H. L., Gill, Z., Asam, K. R., Liang, S., Shen, L., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70947 · Cited by 1

Advanced Optical Microscopy: Unveiling Functional Insights Regarding a Novel PPP2R1A Variant and Its Unreported Phenotype

Roldán, M., Nolasco, G. A., Armengol, L., Frías, M., Morell, M., García‐Aragonés, M., Epifani, F., Muchart, J., Ramírez-Almaraz, M. L., Martorell, L., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813699 · Cited by 1

TIPRL, a Potential Double-edge Molecule to be Targeted and Re-targeted Toward Cancer

Gao, J., You, T., Liu, J., Yang, L., Liu, Y., & Wang, Y. (2024) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-024-01334-5 · Cited by 1

Complex regulation of Forkhead Box O transcription factors

van den Berg, M. C. W. (2013) · Utrecht University Repository (Utrecht University) · Cited by 1

New pathophysiological function of protein phosphatase 2A?

Neumann, J. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn204 · Cited by 1

Cytoplasmic zinc regulates IL-1β production by monocytes/macrophages via mTORC1-induced glycolysis in rheumatoid arthritis (RA)Preprint

Kim, B., Kim, H. Y., Yoon, B. R., Yeo, J., Yu, K., Kim, H. C., Park, J. K., Kang, S. W., & Lee, W. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.16.437150 · Cited by 1

Mechanisms for Calorie Restriction Effects on Insulin-stimulated Glucose Uptake by Rat Skeletal Muscle.

Sequea, D. A. (2014) · Deep Blue (University of Michigan)

Worming to Complete the Insulin/IGF-1 Signaling Cascade: A Dissertation

Padmanabhan, S. (2009) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/40am-yf26

Protein Phosphatases Drive Mitotic Exit

Chircop, M. (2012) · InTech eBooks · doi:10.5772/38477

Protein Phosphatases in Trypanosome Growth and Development

Szöőr, B., & Matthews, K. R. (2013) · Wiley eBooks · doi:10.1002/9783527675401.ch08

Regulation of protein phosphatase 2A by proteasomal degradation

Oberg, E. A. (2012) · doi:10.17077/etd.i2uanvgl

Kinases and phosphatases: the lifes yin yan

Fernández, R. A. H. (2012) · Revista Habanera de Ciencias Médicas

Protein Phosphatase 4 ist ein neuer Regulator der circadianen Uhr in Säugern

Mathematisch-naturwissenschaftlichen Fakultät, I. (2014)

IDENTIFICATION AND CHARACTERIZATION OF CIP2A AS A NOVEL ONCOGENIC INHIBITOR OF PP2A

Niemelä, M. (2012) · UTUPub (University of Turku)

REGULATIONOF CELL POLARITYAND SELF-RENEWALIN DROSOPHILA NEURAL STEM CELLS

Chabu, C. Y. (2008)

Acetaldehyde and Epithelial Junctions: Role of Pp2A and Occludin Phosphorylation

Dunagan, M. (2012) · doi:10.21007/etd.cghs.2012.0075

Cloning and characterization of a serine/threonine protein phosphatase2A-encoding gene IbPP2A1 from Ipomoea batatas (L.) Lam.

Xu, P., Yong, B., Shao, H., Jia-Bin, S. H. E. N., He, B., Ma, Q.-Q., Yuan, X., & Wang, Y. (2017) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-1604-94

Serine/Threonine-Protein Phosphatase 2A

Janssens, V. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101865-1

Protein Phosphatase 2a Interactions In Islet And Human Skeletal Muscle In Diabetes

Damacharla, D. (2017) · Human Biology

Calcium-binding proteins that are type B″ regulatory subunits of phosphatase 2A in Giardia intestinalis

Alvarado, M. E., Rubiano, C. C., Sánchez, W., Díaz, A., & Wasserman, M. M. (2018) · Parasitology Research · doi:10.1007/s00436-018-6019-z

Fibronectin receptor integrin α5β1 regulates assembly of PP2A complexes through PDE4D: modulation of vascular inflammation and atherosclerosisPreprint

Yun, S., Hu, R., Schwaemmle, M. E., Scherer, A. N., Zhuang, Z., Koleske, A. J., Pallas, D. C., & Schwartz, M. A. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/680728

Regulation of PP2Ac stability – discovery of a novel α4 monoubiquitination-dependent mechanism that is altered in Alzheimer’s disease

Watkins, G. R. (2012)

The Key Role of the Phosphatase PP2A in the Development of Acute Myeloid Leukemia

Marco, J., Peris, I., Vicente, C., & Arriazu, E. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.94380

Transient Structure, Flexibility, and Function Relationships in Intrinsically Unstructured Protein Regulators of Protein Phosphatase 1

Dancheck, B. (2009) · doi:10.7301/z0xg9pfs

Identification and characterization of acid and alkaline phosphatases and protein phosphatases in L. catesbeianus tail during metamorphosis

Gonçalves, A. M., Santana, C. C., dos Santos, L. F. J., Colósio, R. R., Balbuena, T. S., & Pizauro, J. M. (2021) · Biologia · doi:10.1007/s11756-021-00877-9

Cross-talk between brassinosteroids and other phytohormones

Gupta, A., Singh, M. P., Singh, D., & Laxmi, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-813227-2.00013-8

Phosphorylation Status of B Beta Subunit Controls PP2A activity in Ethylene-mediated Root Growth InhibitionPreprint

Shao, Z., Zhao, B., Kotla, P., Burns, J. G., Tran, J., Ke, M., Chen, X., Browning, K. S., & Qiao, H. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.11.491551

Serine/Threonine-Protein Phosphatase 2A

Janssens, V. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101865

Supplementary Methods, Figure Legends 1-4, Tables 1-5, References from Cell Surface Tetraspanin Tspan8 Contributes to Molecular Pathways of Exosome-Induced Endothelial Cell Activation

Nazarenko, I. A., Rana, S., Baumann, A., McAlear, J., Hellwig, A., Trendelenburg, M. F., Lochnit, G., Preissner, K. T., & Zöller, M. (2023) · doi:10.1158/0008-5472.22384311

Supplementary Methods, Figure Legends 1-4, Tables 1-5, References from Cell Surface Tetraspanin Tspan8 Contributes to Molecular Pathways of Exosome-Induced Endothelial Cell Activation

Nazarenko, I. A., Rana, S., Baumann, A., McAlear, J., Hellwig, A., Trendelenburg, M. F., Lochnit, G., Preissner, K. T., & Zöller, M. (2023) · doi:10.1158/0008-5472.22384311.v1

Data from 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. (2023) · doi:10.1158/0008-5472.c.6499386.v1

Supplementary Tables 1-3, Figures 1-6 from 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. (2023) · doi:10.1158/0008-5472.22379901

PPM1G dephosphorylates eIF4E to reduce selective mRNA translation.Preprint

Sonenberg, N., Wang, P., Li, Z., Kim, S., Huang, H., Choi, J., Xu, H., yang, C., Snape, A., Bermudez, S., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2847028/v1

Role of protein phosphatase 2A in inflammation and proliferation of fibroblast-like synoviocytes in rheumatoid arthritisPreprint

Guo, X., Bao, G., Zhang, D., & Rui, Y. (2023) · Research Square · doi:10.21203/rs.3.rs-3321951/v1

A PP4 foszfatáz és a Centrobin kapcsolata a DNS hibajavítás késői szakaszaiban

Réthi‐Nagy, Z. (2023) · SZTE Repository of Dissertations (University of Szeged) · doi:10.14232/phd.11931

The Multifaceted Roles of PP2A-B56 in Tumor Progression

Kim, L. W. (2025) · International Journal of Applied Science and Technology · doi:10.30845/ijast.v14p7

Neurocognitive and Neurological Effects of Coffee and Caffeine: A Narrative Review

Pergolizzi, J. V., Tenenbaum, J. T., Pergolizzi, C. S., & LeQuang, J. A. (2025) · Cureus · doi:10.7759/cureus.94742

Converging Pathways in the Regulation of Longevity and Metabolism in Caenorhabditis Elegans: A Dissertation

Narasimhan, S. D. (2010) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/fhpk-6423

Regulation of the M-phase of cell cycle by CDK1, PP2A and CDC6

Dika, M. E. (2013) · doi:10.70675/55071395zf6b6z48d0zaae5z659fb6a2e630 · Cited by 1

Conséquences fonctionnelles et pathologiques de la phosphorylation de la protéine neuronale Tau impliquée dans la maladie d’Alzheimer

Amniai, L. (2010) · theses.fr (ABES) · doi:10.70675/8a5d8b6czffdez46dbzbb29z8c12935243d0

Contrôle de l’entrée en division méiotique par les enzymes PKA et PP2A, et leur substrat Arpp19

Lemonnier, T. (2019) · theses.fr (ABES) · doi:10.70675/b9fe4b33z7306z4ab0z8e98z0bd27780c3a6

Research Progress on Regulatory Mechanisms of Conical Cell Morphogenesis in Arabidopsis thaliana

Li, X. W., Lin, D., & Zhu, L. (2026) · Plants · doi:10.3390/plants15132069

BindingDB Entry 50016393: Small molecule therapeutics for tauopathy in Alzheimer's disease: Walking on the path of most resistance.

BindingDB (2023) · UC San Diego · doi:10.7270/q2cv4nqf

Regulation and Pharmacological Manipulation of the Type 5 Metabotropic Glutamate (mGlu5) Receptor

Bradley, S. J. (2011) · Leicester Research Archive (University of Leicester)

Phosphatase regulation in cardiovascular physiology and disease

DeGrande, S. T. (2012) · doi:10.17077/etd.or34zt15

Structural Genetics to Understand Holoenzyme Assembly and Substrate Selection of Diverse Multimeric Serine-threonine Phosphatases

Huang, W., Veis, J., Day, A., Cui, S., Leonard, D., Narla, G., Ogris, E., & Taylor, D. J. (2024) · Microscopy and Microanalysis · doi:10.1093/mam/ozae044.354

Determinants for Substrate Specificity of Protein Phosphatase 2A

Slupe, A. M., Merrill, R. A., & Strack, S. (2011) · Enzyme Research · doi:10.4061/2011/398751 · Cited by 91

Recent insights into Protein Phosphatase 2A structure and regulation: the reasons why PP2A is no longer considered as a lazy passive housekeeping enzyme

Martin, M., Kettmann, R., & Dequiedt, S. (2010) · Open Repository and Bibliography (University of Liège) · Cited by 10

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

Sents, W., Ivanova, E., Lambrecht, C., Haesen, D., & Janssens, V. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08579.x · Cited by 204

Assembly and structure of protein phosphatase 2A

Shi, Y. (2009) · Science in China Series C Life Sciences · doi:10.1007/s11427-009-0018-3 · Cited by 56