Mice lacking phosphatase PP2A subunit PR61/B’δ ( Ppp2r5d ) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3β

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

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Protein phosphatase 2A regulatory subunits and cancer

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PP2A: the expected tumor suppressor

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Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein.

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Regulation of the Phosphorylation State and Microtubule-Binding Activity of Tau by Protein Phosphatase 2A

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

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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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The Roles of Cyclin-dependent Kinase 5 and Glycogen Synthase Kinase 3 in Tau Hyperphosphorylation

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Glycogen Synthase Kinase-3β Phosphorylates Protein Tau and Rescues the Axonopathy in the Central Nervous System of Human Four-repeat Tau Transgenic Mice

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p35, the Neuronal-specific Activator of Cyclin-dependent Kinase 5 (Cdk5) Is Degraded by the Ubiquitin-Proteasome Pathway

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Conformational change as one of the earliest alterations of tau in Alzheimer's disease

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Molecular Interactions among Protein Phosphatase 2A, Tau, and Microtubules

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

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

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p42 map kinase phosphorylation sites in microtubule‐associated protein tau are dephosphorylated by protein phosphatase 2A₁ Implications for Alzheimer's disease

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A novel CDK5‐dependent pathway for regulating GSK3 activity and kinesin‐driven motility in neurons

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Changed Conformation of Mutant Tau-P301L Underlies the Moribund Tauopathy, Absent in Progressive, Nonlethal Axonopathy of Tau-4R/2N Transgenic Mice

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Protein kinase A activates protein phosphatase 2A by phosphorylation of the B56δ subunit

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A phosphatase cascade by which rewarding stimuli control nucleosomal response

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

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Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit Cα

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Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice

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Role for the PP2A/B56δ Phosphatase in Regulating 14-3-3 Release from Cdc25 to Control Mitosis

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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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HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites

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

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Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcmeurin and phosphatase‐2A

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Interplay between Cyclin-Dependent Kinase 5 and Glycogen Synthase Kinase 3β Mediated by Neuregulin Signaling Leads to Differential Effects on Tau Phosphorylation and Amyloid Precursor Protein Processing

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Glycogen Synthase Kinase 3β Phosphorylates Alzheimer's Disease-Specific Ser³⁹⁶ of Microtubule-Associated Protein Tau by a Sequential Mechanism

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PP2AT61ɛ Is an Inhibitor of MAP4K3 in Nutrient Signaling to mTOR

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Cyclin-dependent kinase 5 activity regulates pain signaling

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Purification and properties of polycation-stimulated phosphorylase phosphatases from rabbit skeletal muscle.

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PKA, PKC, and the Protein Phosphatase 2A Influence HAND Factor Function

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Decreased Cyclin-Dependent Kinase 5 (cdk5) Activity Is Accompanied by Redistribution of cdk5 and Cytoskeletal Proteins and Increased Cytoskeletal Protein Phosphorylation in p35 Null Mice

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Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules

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Specificity of the polycation‐stimulated (type‐2A) and ATP, Mg‐dependent (type‐1) protein phosphatases toward substrates phosphorylated by P34cdc2 kinase

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Control of mitotic exit by PP2A regulation of Cdc25C and Cdk1

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Twofold overexpression of human ?-amyloid precursor proteins in transgenic mice does not affect the neuromotor, cognitive, or neurodegenerative sequelae following experimental brain injury

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Animal models reveal role for tau phosphorylation in human disease

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Protein phosphatase 2a and glycogen synthase kinase 3 signaling modulate prepulse inhibition of the acoustic startle response by altering cortical M-type potassium channel activity

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Genomic organisation, chromosomal localisation tissue distribution and developmental regulation of the PR61/B′ regulatory subunits of protein phosphatase 2A in mice

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Functions of B56-containing PP2As in major developmental and cancer signaling pathways

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Neurodegeneration and Neuroinflammation in cdk5/p25-Inducible Mice

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Diversity, developmental regulation and distribution of murine PR55/B subunits of protein phosphatase 2A

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Okadaic Acid-Stimulated Degradation of p35, an Activator of CDK5, by Proteasome in Cultured Neurons

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The Protein Phosphatase 2A Regulatory Subunits B′β and B′δ Mediate Sustained TrkA Neurotrophin Receptor Autophosphorylation and Neuronal Differentiation

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Altered phosphorylation of cytoskeletal proteins in mutant protein phosphatase 2A transgenic mice

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A Specific Immunoprecipitation Assay for the Protein Kinase FA/Glycogen Synthase Kinase 3

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Regulation of Protein Phosphatase Inhibitor-1 by Cyclin-dependent Kinase 5

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Influence of phosphorylation of p35, an activator of cyclin-dependent kinase 5 (cdk5), on the proteolysis of p35

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Protein phosphatase 2A carboxymethylation and regulatory B subunits differentially regulate mast cell degranulation

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Untitled work

(1997) · doi:10.1002/(sici)1097-4547(19970415)48:2

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

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The importance of tau phosphorylation for neurodegenerative diseases

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PP2A as a master regulator of the cell cycle

Wlodarchak, N., & Xing, Y. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2016.1143913 · Cited by 366 · see citing works

Protein phosphatase 2A dysfunction in Alzheimer’s disease

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

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GSK3 and Alzheimer’s disease: facts and fiction…

Kremer, A. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00017 · Cited by 155 · see citing works

The broken “Off” switch in cancer signaling: PP2A as a regulator of tumorigenesis, drug resistance, and immune surveillance

Ruvolo, P. P. (2016) · BBA Clinical · doi:10.1016/j.bbacli.2016.08.002 · Cited by 143 · see citing works

Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

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Modulation of Phosphoprotein Activity by Phosphorylation Targeting Chimeras (PhosTACs)

Chen, P.-H., Hu, Z., An, E., Okeke, I., Zheng, S., Luo, X., Gong, A., Jaime-Figueroa, S., & Crews, C. M. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00693 · Cited by 130 · see citing works

Physiologic functions of PP2A: Lessons from genetically modified mice

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

Houge, G., Haesen, D., Vissers, L. E. L. M., Mehta, S., Parker, M. J., Wright, M., Vogt, J., McKee, S., Tolmie, J. L., Cordeiro, N., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci79860 · Cited by 124 · see citing works

Protein Phosphatases and Alzheimer's Disease

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Untangling Tau and Iron: Exploring the Interaction Between Iron and Tau in Neurodegeneration

Rao, S. S., & Adlard, P. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00276 · Cited by 105 · see citing works

Axonal Degeneration in AD: The Contribution of Aβ and Tau

Salvadores, N., Gerónimo‐Olvera, C., & Court, F. A. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.581767 · Cited by 97 · see citing works

APC/C-Cdh1 coordinates neurogenesis and cortical size during development

Delgado‐Esteban, M., García-Higuera, I., Maestre, C., Moreno, S., & Almeida, Á. (2013) · Nature Communications · doi:10.1038/ncomms3879 · Cited by 94 · see citing works

MicroRNA-9 regulates steroid-resistant airway hyperresponsiveness by reducing protein phosphatase 2A activity

Li, J. J., Tay, H. L., Maltby, S., Xiang, Y., Eyers, F., Hatchwell, L., Zhou, H., Toop, H. D., Morris, J. C., Nair, P. K., et al. (2015) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2014.11.044 · Cited by 94 · see citing works

The Role and Therapeutic Potential of Ser/Thr Phosphatase PP2A in Apoptotic Signalling Networks in Human Cancer Cells

Janssens, V., & Rebollo, A. (2012) · Current Molecular Medicine · doi:10.2174/156652412799218930 · Cited by 93 · see citing works

De novo missense variants in PPP2R5D are associated with intellectual disability, macrocephaly, hypotonia, and autism

Shang, L., Henderson, L. B., Cho, M. T., Petrey, D. S., Fong, C.-T., Haude, K. M., Shur, N. E., Lundberg, J., Hauser, N., Carmichael, J., et al. (2015) · Neurogenetics · doi:10.1007/s10048-015-0466-9 · Cited by 83 · see citing works

Sigma-1 receptor regulates Tau phosphorylation and axon extension by shaping p35 turnover via myristic acid

Tsai, S., Pokrass, M. J., Klauer, N. R., Nohara, H., & Su, T. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422001112 · Cited by 77 · see citing works

Protein phosphatase 2A – structure, function and role in neurodevelopmental disorders

Sandal, P., Jong, C. J., Merrill, R. A., Song, J., & Strack, S. (2021) · Journal of Cell Science · doi:10.1242/jcs.248187 · Cited by 72 · see citing works

Cacnb4 directly couples electrical activity to gene expression, a process defective in juvenile epilepsy

Tadmouri, A., Kiyonaka, S., Barbado, M., Rousset, M., Fablet, K., Sawamura, S., Bahembera, E., Pernet‐Gallay, K., Arnoult, C., Miki, T., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.226 · Cited by 74 · see citing works

The basic biology of PP2A in hematologic cells and malignancies

Haesen, D., Sents, W., Lemaire, K., Hoorne, Y., & Janssens, V. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00347 · Cited by 73 · see citing works

Protein phosphatase 2A and tau: an orchestrated ‘Pas de Deux’

Taleski, G., & Sontag, E. (2017) · FEBS Letters · doi:10.1002/1873-3468.12907 · Cited by 70 · see citing works

Molecular Implication of PP2A and Pin1 in the Alzheimer's Disease Specific Hyperphosphorylation of Tau

Landrieu, I., Smet‐Nocca, C., Amniai, L., Louis, J. V., Wieruszeski, J., Goris, J., Janssens, V., & Lippens, G. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021521 · Cited by 68 · see citing works

The protein serine/threonine phosphatases PP2A, PP1 and calcineurin: A triple threat in the regulation of the neuronal cytoskeleton

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FKBP51 inhibits GSK3β and augments the effects of distinct psychotropic medications

Gassen, N. C., Hartmann, J., Zannas, A. S., Kretzschmar, A., Zschocke, J., Maccarrone, G., Hafner, K., Zellner, A., Kollmannsberger, L. K., Wagner, K. V., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2015.38 · Cited by 62 · see citing works

Early‐Onset Parkinsonism Is a Manifestation of the PPP2R5D p. E200K Mutation

Kim, C., Wirth, T., Hubsch, C. A., Nemeth, A. H., Okur, V., Anheim, M., Drouot, N., Tranchant, C., Rudolf, G., Chelly, J., et al. (2020) · Annals of Neurology · doi:10.1002/ana.25863 · Cited by 55 · see citing works

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

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PPP2R5D-Related Intellectual Disability and Neurodevelopmental Delay: A Review of the Current Understanding of the Genetics and Biochemical Basis of the Disorder

Biswas, D., Cary, W., & Nolta, J. A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041286 · Cited by 49 · see citing works

The broad phenotypic spectrum of PPP2R1A-related neurodevelopmental disorders correlates with the degree of biochemical dysfunction

Lenaerts, L., Reynhout, S., Verbinnen, I., Laumonnier, F., Toutain, A., Bonnet‐Brilhault, F., Hoorne, Y., Joss, S. K., Chassevent, A., Smith‐Hicks, C. L., et al. (2020) · Genetics in Medicine · doi:10.1038/s41436-020-00981-2 · Cited by 50 · see citing works

Protein Phosphatase 2A (PP2A) mutations in brain function, development, and neurologic disease

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Altered Cerebrospinal Fluid Exosomal microRNA Levels in Young-Onset Alzheimer’s Disease and Frontotemporal Dementia

Tan, Y. J., Wong, B. Y. X., Vaidyanathan, R., Sreejith, S., Chia, S. Y., Kandiah, N., Ng, A. S. L., & Zeng, L. (2021) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-210311 · Cited by 48 · see citing works

PPP2R5C couples hepatic glucose and lipid homeostasis

Cheng, Y.-S., Seibert, O., Klöting, N., Dietrich, A., Straßburger, K., Fernández-Veledo, S., Vendrell, J. J., Zorzano, A., Blüher, M., Herzig, S., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005561 · Cited by 43 · see citing works

γ-Aminobutyric Acid Type A (GABAA) Receptor Activation Modulates Tau Phosphorylation

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Protein Phosphatase 2A: a Double-Faced Phosphatase of Cellular System and Its Role in Neurodegenerative Disorders

Nematullah, M., Hoda, M. N., & Khan, F. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0444-3 · 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

B′-protein phosphatase 2A is a functional binding partner of delta-retroviral integrase

Maertens, G. N. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1347 · Cited by 38 · see citing works

Rescue of impaired late–phase long-term depression in a tau transgenic mouse model

Ahmed, T., Blum, D. L., Burnouf, S., Demeyer, D., Buée‐Scherrer, V., D’Hooge, R., Buée, L., & Balschun, D. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.09.015 · Cited by 38 · see citing works

Glycogen synthase kinase‐3β regulates leucine‐309 demethylation of protein phosphatase‐2A via PPMT1 and PME‐1

Yao, X., Li, X., Zhang, X., Yin, Y., Liu, B., Luo, D., Wang, Q., Wang, J., & Liu, G. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.06.018 · Cited by 37 · see citing works

Regulatory B Subunits of Protein Phosphatase 2A Are Involved in Site-specific Regulation of Tau Protein Phosphorylation

Yu, U.-Y., Yoo, B. C., & Ahn, J. (2014) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2014.18.2.155 · Cited by 35 · see citing works

The protein phosphatase 2A B56γ regulatory subunit is required for heart development

Varadkar, P., Despres, D., Kraman, M., Lozier, J., Phadke, A., Nagaraju, K., & Mccright, B. (2014) · Developmental Dynamics · doi:10.1002/dvdy.24111 · Cited by 34 · see citing works

GSK-3β is Dephosphorylated by PP2A in a Leu309 Methylation-Independent Manner

Chu, D., Tan, J., Xie, S.-T., Jin, N., Yin, X., Gong, C., Iqbal, K., & Liu, F. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150497 · Cited by 34 · see citing works

Atypical Protein Phosphatase 2A Gene Families Do Not Expand via Paleopolyploidization

Booker, M. A., & DeLong, A. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.16.01768 · Cited by 34 · see citing works

PP2A–AMPKα–HSF1 axis regulates the metal-inducible expression of HSPs and ROS clearance

Zhu, X., Chen, L., Bai, Q., Ma, L., Li, D., Zhang, J.-M., Gao, C., Lei, Z., Zhang, Z., Xing, X., et al. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.01.002 · Cited by 33 · see citing works

Clinical, neuroimaging and molecular characteristics of PPP2R5D-related neurodevelopmental disorders: an expanded series with functional characterisation and genotype–phenotype analysis

Oyama, N., Vaneynde, P., Reynhout, S., Pao, E., Timms, A. E., Fan, X., Foss, K., Derua, R., Janssens, V., Chung, W. K., et al. (2022) · Journal of Medical Genetics · doi:10.1136/jmg-2022-108713 · Cited by 33 · see citing works

Partial Inhibition of Mitochondrial Complex I Reduces Tau Pathology and Improves Energy Homeostasis and Synaptic Function in 3xTg-AD Mice

Stojakovic, A., Chang, S.-Y., Nesbitt, J. J., Pichurin, N. P., Ostroot, M., Aikawa, T., Kanekiyo, T., & Trushina, E. V. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201015 · Cited by 31 · see citing works

Early-onset parkinsonism in PPP2R5D-related neurodevelopmental disorder

Hetzelt, K. L. M. L., Kerling, F., Kraus, C. S., Rauch, C., Thiel, C. T., Winterholler, M., Reis, A., & Zweier, C. (2020) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2020.104123 · Cited by 30 · see citing works

Protein phosphatase 2ACα gene knock-out results in cortical atrophy through activating hippo cascade in neuronal progenitor cells

Liu, B., Sun, L.-H., Huang, Y.-F., Guo, L.-J., & Luo, L.-S. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.12.015 · Cited by 29 · see citing works

PHD2 Targeting Overcomes Breast Cancer Cell Death upon Glucose Starvation in a PP2A/B55α-Mediated Manner

Conza, G. D., Cafarello, S. T., Zheng, X., Zhang, Q. H., & Mazzone, M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.081 · Cited by 29 · see citing works

Ppp2r2a Knockout Mice Reveal That Protein Phosphatase 2A Regulatory Subunit, PP2A-B55α, Is an Essential Regulator of Neuronal and Epidermal Embryonic Development

Panicker, N., Coutman, M., Lawlor-O’Neill, C., Kahl, R. G. S., Roselli, S., & Verrills, N. M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00358 · Cited by 27 · see citing works

Nuclear life of the voltage-gated Cacnb4 subunit and its role in gene transcription regulation

Ronjat, M., Kiyonaka, S., Barbado, M., WAARD, M. M. D., & Mori, Y. (2013) · Channels · doi:10.4161/chan.23895 · Cited by 29 · see citing works

Eicosanoyl-5-hydroxytryptamide (EHT) prevents Alzheimer’s disease-related cognitive and electrophysiological impairments in mice exposed to elevated concentrations of oligomeric beta-amyloid

Asam, K. R., Staniszewski, A., Zhang, H., Melideo, S. L., Mazzeo, A., Voronkov, M. V., Huber, K. L., Pérez, E., Stock, M. B., Stock, J. B., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189413 · Cited by 28 · see citing works

Cyclin‐Dependent kinase 5 targeting prevents β‐Amyloid aggregation involving glycogen synthase kinase 3β and phosphatases

Castro-Álvarez, J. F., Uribe‐Arias, A., & Cardona‐Gómez, G. P. (2015) · Journal of Neuroscience Research · doi:10.1002/jnr.23576 · Cited by 26 · see citing works

Validity of the MPTP-Treated Mouse as a Model for Parkinson’s Disease

Klemann, C. J. H. M., Martens, G. J. M., Poelmans, G., & Visser, J. E. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9103-8 · Cited by 26 · see citing works

Amyloid-like aggregating proteins cause lysosomal defects in neurons via gain-of-function toxicity

Riera-Tur, I., Schäfer, T., Hornburg, D., Mishra, A., Padilha, M. D. S., Fernández-Mosquera, L., Feigenbutz, D., Auer, P., Mann, M., Baumeister, W. P., et al. (2021) · Life Science Alliance · doi:10.26508/lsa.202101185 · Cited by 29 · see citing works

Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease

Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23 · see citing works

β-Adrenergic regulation of cardiac type 2A protein phosphatase through phosphorylation of regulatory subunit B56δ at S573

Ranieri, A., Kemp, E., Burgoyne, J. R., & Avkiran, M. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.12.016 · Cited by 23 · see citing works

PP2A Ligand ITH12246 Protects against Memory Impairment and Focal Cerebral Ischemia in Mice

Lorrio, S., Romero, A., González‐Lafuente, L., Lajarín-Cuesta, R., Martínez-Sanz, F. J., Estrada, M., Samadi, A., Marco, J. L., Rodrı́guez-Franco, M. I., Villarroya, M., et al. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn400050p · Cited by 23 · see citing works

Modulating Protein Phosphatase 2A Rescues Disease Phenotype in Neurodegenerative Tauopathies

McKenzie-Nickson, S., Chan, J., Perez, K. A., Hung, L. W., Cheng, L., Sedjahtera, A., Gunawan, L., Adlard, P. A., Hayne, D. J., McInnes, L. E., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00161 · Cited by 22 · see citing works

The tumor suppressor phosphatase PP2A-B56α regulates stemness and promotes the initiation of malignancies in a novel murine model

Janghorban, M., Langer, E. M., Wang, X., Zachman, D., Daniel, C. J., Hooper, J., Fleming, W. H., Agarwal, A., & Sears, R. C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0188910 · Cited by 19 · see citing works

S-Adenosylmethionine Rescues Cognitive Deficits in the rTg4510 Animal Model by Stabilizing Protein Phosphatase 2A and Reducing Phosphorylated Tau

Beauchamp, L. C., Liu, X. M., Sedjahtera, A., Bogeski, M., Vella, L. J., Bush, A. I., Adlard, P. A., & Barnham, K. J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200756 · Cited by 19 · see citing works

Microcystin-Leucine-Arginine Induces Tau Pathology Through Bα Degradation via Protein Phosphatase 2A Demethylation and Associated Glycogen Synthase Kinase-3β Phosphorylation

Zhang, Y., Zhang, J., Wang, E., Qian, W., Fan, Y., Feng, Y., Yin, H., Li, Y., Wang, Y., & Yuan, T. (2017) · Toxicological Sciences · doi:10.1093/toxsci/kfx271 · Cited by 19 · see citing works

PPM1G forms a PPP‐type phosphatase holoenzyme with B56δ that maintains adherens junction integrity

Kumar, P., Tathe, P., Chaudhary, N., & Maddika, S. (2019) · EMBO Reports · doi:10.15252/embr.201846965 · Cited by 18 · see citing works

A Newborn with Severe Ventriculomegaly: Expanding the PPP2R1A Gene Mutation Phenotype

Wallace, A., Caruso, P. A., & Karaa, A. (2019) · Journal of Pediatric Genetics · doi:10.1055/s-0039-1692414 · Cited by 16 · see citing works

Post-translational modifications and stress adaptation: the paradigm of FKBP51

Rein, T. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190332 · Cited by 15 · see citing works

A novel function of Ataxin-1 in the modulation of PP2A activity is dysregulated in the spinocerebellar ataxia type 1

Sánchez, I., Piñol‐Jurado, P., Corral‐Juan, M., Pandolfo, M., & Matilla‐Dueñas, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt197 · Cited by 16 · see citing works

Growth arrest of PPP2R5C and PPP2R5D double knockout mice indicates a genetic interaction and conserved function for these PP2A B subunits

Dyson, J. J., Abbasi, F., Varadkar, P. A., & McCright, B. (2021) · FASEB BioAdvances · doi:10.1096/fba.2021-00130 · Cited by 15 · see citing works

Aerobic Exercise Training-Induced Changes on DNA Methylation in Mild Cognitively Impaired Elderly African Americans: Gene, Exercise, and Memory Study - GEMS-I

Ngwa, J. S., Nwulia, E. A., Ntekim, O. E., Bedada, F. B., Kwabi‐Addo, B., Nadarajah, S., Johnson, S. P., Southerland, W. M., Kwagyan, J., & Obisesan, T. O. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.752403 · Cited by 15 · see citing works

Prenatal bisphenol A exposure contributes to Tau pathology: Potential roles of CDK5/GSK3β/PP2A axis in BPA-induced neurotoxicity

Xue, J., Zhang, L., Xie, X., Gao, Y., Jiang, L., Wang, J., Wang, Y., Gao, R., Yu, J., & Xiao, H. (2020) · Toxicology · doi:10.1016/j.tox.2020.152442 · Cited by 14 · see citing works

Cloning and Characterization of TaPP2AbB"-α, a Member of the PP2A Regulatory Subunit in Wheat

Liu, D., Li, A., Mao, X., & Jing, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094430 · Cited by 14 · see citing works

The prognostic value of Cyclin-Dependent Kinase 5 and Protein Phosphatase 2A in Gastric Cancer

Lin, J.-X., Xie, X., Weng, X., Zheng, C., Xie, J., Wang, J.-B., Lu, J., Chen, Q., Cao, L., Lin, M., et al. (2018) · Journal of Cancer · doi:10.7150/jca.27015 · Cited by 13 · see citing works

The Anti-Tumor Agent Sodium Selenate Decreases Methylated PP2A, Increases GSK3βY216 Phosphorylation, Including Tau Disease Epitopes and Reduces Neuronal Excitability in SHSY-5Y Neurons

Habbab, W., Aoudé, I., Palangi, F., Abdulla, S., & Ahmed, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040844 · Cited by 12 · see citing works

Terminal hypothermic T au. P 301 L mice have increased Tau phosphorylation independently of glycogen synthase kinase 3α/β

Maurin, H., Lechat, B., Borghgraef, P., Devijver, H., Jaworski, T., & LEUVEN, F. V. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12595 · Cited by 11 · see citing works

Rare Missense Variants in The Ppp2r5dgene Associated with Parkinson's Disease in the Han Chinese Population

Ning, P., Li, K., Ren, H. J., Yang, H., Xu, Y., & Yang, X. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2022.136564 · Cited by 10 · see citing works

The Deficits of Insulin Signal in Alzheimer’s Disease and the Mechanisms of Vanadium Compounds in Curing AD

Yao, J., He, Z., You, G., Liu, Q., & Li, N. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45080402 · Cited by 9 · see citing works

Mechanistic insight of cyclin-dependent kinase 5 in modulating lung cancer growth

Lin, H., Chen, M., Prince, G. M. S. H., & Yang, T. (2019) · The Chinese Journal of Physiology · doi:10.4103/cjp.cjp_67_19 · Cited by 10 · see citing works

The role of serine/threonine phosphatases in human development: Evidence from congenital disorders

Vaneynde, P., Verbinnen, I., & Janssens, V. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1030119 · Cited by 9 · see citing works

Protein Phosphatase 2A Regulates Phenotypic and Metabolic Alteration of Microglia Cells in HFD-Associated Vascular Dementia Mice via TNF-α/Arg-1 Axis

Nematullah, M., Rashid, F., Nimker, S., & Khan, F. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03324-9 · Cited by 9 · see citing works

Protein Biomarkers for the Diagnosis of Alzheimer’s Disease at Different Stages of Neurodegeneration

Pérez, M., Hernández, F., & Ávila, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186749 · Cited by 9 · 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 & Clinical Cancer Research · doi:10.1186/s13046-025-03560-y · Cited by 8 · see citing works

Leucine Carboxyl Methyltransferase 1 Overexpression Protects Against Cognitive and Electrophysiological Impairments in Tg2576 APP Transgenic Mice

Gnanaprakash, M., Staniszewski, A., Zhang, H., Pitstick, R., Kavanaugh, M., Arancio, O., & Nicholls, R. E. (2021) · Journal of Alzheimer's Disease · doi:10.3233/jad-200462 · Cited by 7 · see citing works

Role of proline‐rich tyrosine kinase 2 (Pyk2) in the pathogenesis of Alzheimer's disease

Kumar, R. K., Tiwari, V., & Dey, S. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15569 · Cited by 8 · see citing works

Anesthesia promotes acute expression of genes related to Alzheimer’s disease and latent tau aggregation in transgenic mouse models of tauopathy

Eun, J. D., Jimenez, H. T., Adrien, L. R., Wolin, A., Marambaud, P., Davies, P., & Koppel, J. L. (2022) · Molecular Medicine · doi:10.1186/s10020-022-00506-4 · Cited by 7 · see citing works

Saturated fatty acids stimulate cytokine production in tanycytes via the PP2Ac-dependent signaling pathway

Liu, D., Wang, T., Zhao, X., Chen, J., Yang, T., Shen, Y., & Zhou, Y. (2023) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x231219115 · Cited by 7 · see citing works

Refractory Epilepsy in a Toddler With PPP2R1A Gene Mutation and Congenital Hydrocephalus

Ruxmohan, S., Quinonez, J., Yadav, R. S., Shrestha, S., Poudel, S., & Stein, J. D. (2021) · Cureus · doi:10.7759/cureus.19988 · Cited by 7 · see citing works

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 7 · see citing works

Reduced Expression of the PP2A Methylesterase, PME-1, or the PP2A Methyltransferase, LCMT-1, Alters Sensitivity to Beta-Amyloid-Induced Cognitive and Electrophysiological Impairments in Mice

Staniszewski, A., Zhang, H., Asam, K. R., Pitstick, R., Kavanaugh, M. P., Arancio, O., & Nicholls, R. E. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2983-19.2020 · Cited by 7 · see citing works

Differential Proteomic Analysis of Hepatocellular Carcinomas from Ppp2r5d Knockout Mice and Normal (Knockout) Livers

Lambrecht, C., Ferreira, G. B., Omella, J. D., Libbrecht, L. J., Vos, R. D., Derua, R., Mathieu, C., Overbergh, L., Waelkens, E., & Janssens, V. (2020) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20222 · Cited by 7 · see citing works

Pathogenic de novo variants in PPP2R5C cause a neurodevelopmental disorder within the Houge-Janssens syndrome spectrum

Verbinnen, I., Douzgou, S., Hsieh, T., Lesmann, H., Kirchhoff, A., Geneviève, D., Brimble, E., Lenaerts, L., Haesen, D., Levy, R. J., et al. (2025) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2025.01.021 · Cited by 6 · see citing works

A Systematic Review of Dietary Supplements in Alzheimer’s Disease

Chimakurthy, A., Lingam, S., Pasya, S. K. R., & Copeland, B. J. (2023) · Cureus · doi:10.7759/cureus.33982 · Cited by 7 · see citing works

Amyloid-like aggregates cause lysosomal defects in neurons via gain-of-function toxicityPreprint

Riera-Tur, I., Schäfer, T., Hornburg, D., Mishra, A., Fernández-Mosquera, L., Feigenbutz, D., Auer, P., Mann, M., Baumeister, W. P., Klein, R., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2019.12.16.877431 · Cited by 6 · see citing works

A Novel Mouse Model of Combined Hepatocellular-Cholangiocarcinoma Induced by Diethylnitrosamine and Loss of Ppp2r5d

Omella, J. D., Cortesi, E. E., Verbinnen, I., Remmerie, M., Wu, H., Cubero, F. J., Roskams, T., & Janssens, V. (2023) · Cancers · doi:10.3390/cancers15164193 · Cited by 5 · see citing works

Determining Structural Changes for Ligand Recognition between Human and Rat Phosphorylated BACE1 in Silico and Its Phosphorylation by GSK3β at Thr252 by in Vitro Studies

Toledano, J. V., Bello, M., Correa‐Basurto, J., González, I. G., Pacheco‐Yépez, J., & Rosales‐Hernández, M. C. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00669 · Cited by 5 · see citing works

FK-binding protein 5: Possible relevance to the pathogenesis of metabolic dysfunction and alcohol-associated liver disease

Ma, J., Yang, Z., Gao, H., Huda, N., Jiang, Y., & Liangpunsakul, S. (2023) · Journal of Investigative Medicine · doi:10.1177/10815589231207793 · Cited by 3 · see citing works

The B56α subunit of PP2A is necessary for mesenchymal stem cell commitment to adipocyte

Hanse, E. A., Pan, M., Liu, W., Yang, Y., Gabra, M. B. I., Tran, T. Q., Lowman, X. H., Ruiz, B. I., Wang, Q. A., & Kong, M. (2021) · EMBO Reports · doi:10.15252/embr.202051910 · Cited by 4 · see citing works

NEURONAL FUNCTIONS OF PROTEIN PHOSPHATASE 2A

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

Houge-Janssens syndrome

Houge, G., Douzgou, S., Hsieh, T., Verbinnen, I., & Janssens, V. (2025) · European Journal of Human Genetics · doi:10.1038/s41431-025-01901-1 · Cited by 3 · see citing works

Functional Roles of a Putative B' Delta Regulatory Subunit and a Catalytic Subunit of Protein Phosphatase 2A in the Cereal Pathogen Fusarium graminearum

Kim, H.-K., & Yun, S. (2012) · The Plant Pathology Journal · doi:10.5423/ppj.oa.05.2012.0059 · Cited by 3 · see citing works

Tau hyperphosphorylation and sensorimotor impairment in mice lacking the PP2A regulatory subunit PR61/B’delta

Lambrecht, C., Louis, J. V., Sents, W., Borghgraef, P., Derua, R., Waelkens, E., Leuven, F. V., Goris, J., & Janssens, V. (2009)

Genetic inactivation of a specific PP2A subunit, PR61/B'delta, in a mouse model generates tauopathy through an indirect mechanism

Louis, J. V., Martens, E., Borghgraef, P., Longin, S., Zwaenepoel, K., Lambrecht, C., Pijnenborg, R., Landrieu, I., Lippens, G. M., Ledermann, B., et al. (2010)

Regulatory B Subunits of Protein Phosphatase 2A Are Involved in Site-specific Regulation of Tau Protein Phosphorylation

Yu, U.-Y., Yoo, B. C., & Ahn, J. (2014) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2014.18.2.155 · Cited by 35 · see citing works

Protein phosphatase 2A in Alzheimer's disease pathogenesis, memory and development

Schild, A. (2005) · Zurich Open Repository and Archive (University of Zurich) · doi:10.5167/uzh-49456

Substrate-specific reduction of PP2A activity exaggerates tau pathology

Deters, N., Ittner, L. M., & Götz, J. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.140 · Cited by 39 · see citing works