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

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526

Neurotoxicity induces cleavage of p35 to p25 by calpain

Lee, M.-S., Kwon, Y. T., Li, M., Peng, J., Friedlander, R. M., & Tsai, L. (2000) · Nature · doi:10.1038/35012636 · Cited by 1,057

Decreased nuclear β‐catenin, tau hyperphosphorylation and neurodegeneration in GSK‐3β conditional transgenic mice

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Targeted disruption of the cyclin-dependent kinase 5 gene results in abnormal corticogenesis, neuronal pathology and perinatal death.

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Tau phosphorylation in neuronal cell function and dysfunction

Johnson, G. V. W., & Stoothoff, W. H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01558 · Cited by 624

Protein phosphatase 2A regulatory subunits and cancer

Eichhorn, P. J. A., Creyghton, M. P., & Bernards, R. (2009) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2008.05.005 · Cited by 513

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

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

Sontag, E., Nunbhakdi‐Craig, V., Lee, G. S., Bloom, G. S., & Mumby, M. C. (1996) · Neuron · doi:10.1016/s0896-6273(00)80250-0 · Cited by 397

Prominent Axonopathy in the Brain and Spinal Cord of Transgenic Mice Overexpressing Four-Repeat Human tau Protein

Spittaels, K., den Haute, C. V., Dorpe, J. V., Bruynseels, K., Vandezande, K., Laenen, I., Geerts, H., Mercken, M. H., Sciot, R., Lommel, A. V., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65533-2 · Cited by 390

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

Janssens, V., Longin, S., & Goris, J. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.12.004 · Cited by 390

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 502

The importance of tau phosphorylation for neurodegenerative diseases

Noble, W., Hanger, D. P., Miller, C. C. J., & Lovestone, S. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00083 · Cited by 475

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 380

Protein phosphatase 2A dysfunction in Alzheimer’s disease

Sontag, J.-M., & Sontag, E. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00016 · Cited by 304

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

GSK3 and Alzheimer’s disease: facts and fiction…

Kremer, A. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00017 · Cited by 160

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

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

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

Physiologic functions of PP2A: Lessons from genetically modified mice

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

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

Protein Phosphatases and Alzheimer's Disease

Braithwaite, S. P., Stock, J. B., Lombroso, P. J., & Nairn, A. C. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396456-4.00012-2 · Cited by 111

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 108

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 101

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 97

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

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 95

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 86

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 79

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 76

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

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

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 71

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 71

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

Hoffman, A., Taleski, G., & Sontag, E. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.01.005 · Cited by 67

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

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

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

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 48

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 52

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

Verbinnen, I., Vaneynde, P., Reynhout, S., Lenaerts, L., Derua, R., Houge, G., & Janssens, V. (2021) · Biochemical Society Transactions · doi:10.1042/bst20201313 · Cited by 49

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

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

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

Nykänen, N.-P., Kysenius, K., Sakha, P., Tammela, P., & Huttunen, H. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.309385 · Cited by 43

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 44

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

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

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 45

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

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

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

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 35

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

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

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 31

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

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 29

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

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

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 28

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

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

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

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 29

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 32

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

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

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

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

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

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

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

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

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

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

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

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 17

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 13

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

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

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

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

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

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

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

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

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

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

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

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

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

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. P., Arancio, O., & Nicholls, R. E. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-200462 · Cited by 9

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 9

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

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

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

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

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

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

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

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

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

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 6

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

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 4

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 3

NEURONAL FUNCTIONS OF PROTEIN PHOSPHATASE 2A

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

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

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

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

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