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Activation of the ERK and JNK signaling pathways caused by neuron-specific inhibition of PP2A in transgenic mice

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Overexpression of the catalytic subunit of protein phosphatase 2A impairs cardiac function

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

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Physiologic functions of PP2A: Lessons from genetically modified mice

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

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

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Tau acts as a mediator for<scp>A</scp>lzheimer's disease‐related synaptic deficits

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Tau-directed approaches for the treatment of Alzheimer’s disease: focus on leuco-methylthioninium

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

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Impaired development of the Harderian gland in mutant protein phosphatase 2A transgenic mice

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Targeting PP2A in cancer: an underrated option

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Hyperphosphorylation of retinoblastoma protein and p53 by okadaic acid, a tumor promoter.

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Concentration-Dependent Effects of Protein Phosphatase (PP) Inhibitors Implicate PP1 and PP2A in Different Stages of Memory Formation

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An Anti-okadaic Acid-Anti-idiotypic Antibody Bearing An Internal Image of Okadaic Acid Inhibits Protein Phosphatase PP1 and PP2A Catalytic Activity

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Carcinogenic Aspects of Protein Phosphatase 1 and 2A Inhibitors

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Serine/Threonine Protein Phosphatase 2A Regulates the Transport of Axonal Mitochondria

Heo, K., Basu, H., Gutnick, A., Wei, W., Shlevkov, E., & Schwarz, T. L. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.852245 · Cited by 7 · see citing works