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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Neurotoxicity induces cleavage of p35 to p25 by calpain

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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

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Protein phosphatase 2A regulatory subunits and cancer

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PP2A: the expected tumor suppressor

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

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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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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

Götz, J., Probst, A., Ehler, E., Hemmings, B., & Kues, W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12370 · Cited by 220

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

Kins, S., Crameri, A., Evans, D. R. H., Hemmings, B. A., Nitsch, R. M., & Götz, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102621200 · Cited by 203

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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Brain protein phosphatase 2A: Developmental regulation and distinct cellular and subcellular localization by B subunits

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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

Tian, Q., & Wang, J. (2002) · Neurosignals · doi:10.1159/000067425 · Cited by 156

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

Wen, Y., Planel, E., Herman, M., Figueroa, H. Y., Wang, L., Liu, L., Lau, L.-F., Yu, W. H., & Duff, K. E. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.5245-07.2008 · Cited by 145

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

Li, T., & Paudel, H. K. (2006) · Biochemistry · doi:10.1021/bi051634r · Cited by 140

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

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

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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

Hallows, J. L., Chen, K., DePinho, R. A., & Vincent, I. J. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-33-10633.2003 · Cited by 112

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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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

Kapfhamer, D., Berger, K. H., Hopf, F. W., Seif, T., Kharazia, V., Bonci, A., & Heberlein, U. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1292-10.2010 · Cited by 71

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

Martens, E., Stevens, I., Janssens, V., Vermeesch, J., Götz, J., Goris, J., & Van Hoof, C. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.12.047 · Cited by 57

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

Yang, J., & Phiel, C. J. (2010) · Life Sciences · doi:10.1016/j.lfs.2010.10.003 · Cited by 56

Neurodegeneration and Neuroinflammation in cdk5/p25-Inducible Mice

Muyllaert, D., Terwel, D., Kremer, A., Sennvik, K., Borghgraef, P., Devijver, H., Dewachter, I., & LEUVEN, F. V. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070693 · Cited by 55

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

Schmidt, K., Kins, S., Schild, A., Nitsch, R. M., Hemmings, B. A., & Götz, J. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.02274.x · Cited by 54

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

Kanegan, M. J. V., & Strack, S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01242-08 · Cited by 42

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

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

Schild, A., Ittner, L. M., & Götz, J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.066 · Cited by 38

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

Lint, J. V., Khandelwal, R. L., Merlevede, W. J., & Vandenheede, J. R. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1018 · Cited by 31

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

Nguyen, C. T. N., Nishi, A., Kansy, J. W., Fernandez, J., Hayashi, K., Gillardon, F., Hemmings, H. C., Nairn, A. C., & Bibb, J. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701046200 · Cited by 27

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

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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

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