Global ETD Search

1	Structural studies of protein phosphatase 2A, simian virus 40 small t antigen, and the PhoQ sensor domain / Cho, Uhn-Soo. January 2007 (has links) Thesis (Ph. D.)--University of Washington, 2007. / Includes bibliographical references (leaves 124-143).
2	TARGETED DEGRADATION OF THE MYC ONCOGENE USING PP2AB56ALPHASELECTIVE SMALL MOLECULE MODULATORS OF PROTEINPHOSPHATASE 2A AS A THERAPEUTIC STRATEGY FOR TREATING MYCDRIVENCANCERS Farrington, Caroline Cain 29 May 2020 (has links) No description available. Biomedical Research Pharmacology Burkitt Lymphoma non-small cell lung cancer small molecule activator of PP2A SMAP anticancer drug Myc c-Myc breast cancer protein phosphatase 2 PP2A protein degradation oncogene small molecule
3	Biguanide metformin acts on tau phosphorylation via mTOR/protein phosphatase 2A (PP2A) signaling Kickstein, E., Krauss, S., Thornhill, P., Rutschow, D., Zeller, R., Sharkey, J., Williamson, Ritchie, Fuchs, M., Kohler, A., Glossmann, H., Schneider, R., Sutherland, C., Schweiger, S. January 2010 (has links) No / Hyperphosphorylated tau plays an important role in the formation of neurofibrillary tangles in brains of patients with Alzheimer's disease (AD) and related tauopathies and is a crucial factor in the pathogenesis of these disorders. Though diverse kinases have been implicated in tau phosphorylation, protein phosphatase 2A (PP2A) seems to be the major tau phosphatase. Using murine primary neurons from wild-type and human tau transgenic mice, we show that the antidiabetic drug metformin induces PP2A activity and reduces tau phosphorylation at PP2A-dependent epitopes in vitro and in vivo. This tau dephosphorylating potency can be blocked entirely by the PP2A inhibitors okadaic acid and fostriecin, confirming that PP2A is an important mediator of the observed effects. Surprisingly, metformin effects on PP2A activity and tau phosphorylation seem to be independent of AMPK activation, because in our experiments (i) metformin induces PP2A activity before and at lower levels than AMPK activity and (ii) the AMPK activator AICAR does not influence the phosphorylation of tau at the sites analyzed. Affinity chromatography and immunoprecipitation experiments together with PP2A activity assays indicate that metformin interferes with the association of the catalytic subunit of PP2A (PP2Ac) to the so-called MID1-alpha4 protein complex, which regulates the degradation of PP2Ac and thereby influences PP2A activity. In summary, our data suggest a potential beneficial role of biguanides such as metformin in the prophylaxis and/or therapy of AD. Adenylate Kinase Metabolism Alzheimer Disease Pathology Physiopathology Animals Cells Cultured Enzyme Inhibitors Pharmacology Epitopes HeLa cells Humans Hypoglycemic agents Metformin Mice Transgenic Multiprotein complexes Neurofibrillary Tangles Neurons Cytology Okadaic acid Phosphorylation Protein Phosphatase 2 Proteins Signal Transduction Drug effects TOR Serine-Threonine Kinases Tau Proteins REF 2014

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