Results 201 to 210 of about 35,429 (234)
NAP1 switches from an activator to a limiter of interferon induction by trapping TBK1 in condensates. [PDF]
Nat CommunGlon D +25 more
europepmc +1 more source
HTLV-1 intasome recruits the PP2A-B56 holoenzyme and restricts its phosphatase activity
Minnell JJ +6 more
europepmc +1 more source
Chemogenetic profiling reveals PP2A‐independent cytotoxicity of proposed PP2A activators iHAP1 and DT‐061 [PDF]
EMBO Journal, 2022 Protein phosphatase 2A (PP2A) is an abundant phosphoprotein phosphatase that acts as a tumor suppressor. For this reason, compounds able to activate PP2A are attractive anticancer agents. The compounds iHAP1 and DT-061 have recently been reported to selectively stabilize specific PP2A-B56 complexes to mediate cell killing.
Emil Peter Thrane Hertz +2 more
exaly +7 more sources
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Current Alzheimer Research, 2012
Phosphorylation and, therefore, binding capacity of microtubule-associated protein tau is regulated by specific kinases and phosphatases. Activation of tau kinases plays a crucial role in tau- hyper-phosphorylation in Alzheimer disease (AD) and related tauopathies.
L, Torrent, I, Ferrer
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Phosphorylation and, therefore, binding capacity of microtubule-associated protein tau is regulated by specific kinases and phosphatases. Activation of tau kinases plays a crucial role in tau- hyper-phosphorylation in Alzheimer disease (AD) and related tauopathies.
L, Torrent, I, Ferrer
openaire +2 more sources
Integrator of PP2A and transcription
Nature Reviews Molecular Cell Biology, 2020A dual-activity complex of Integrator and protein phosphatase 2A dephosphorylates RNA polymerase II and suppresses transcription.
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Blood, 2023
Introduction: The dysregulation of phosphorylation-dependent signaling is a hallmark of leukemogenesis. Kinase inhibitors have revolutionized the outcomes of patients with chronic myeloid leukemia. An orthogonal, but less explored way to target phosphorylation pathways is to activate phosphatases, such as the ubiquitously
Franziska Wachter +2 more
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Introduction: The dysregulation of phosphorylation-dependent signaling is a hallmark of leukemogenesis. Kinase inhibitors have revolutionized the outcomes of patients with chronic myeloid leukemia. An orthogonal, but less explored way to target phosphorylation pathways is to activate phosphatases, such as the ubiquitously
Franziska Wachter +2 more
openaire +1 more source
PP2A: the expected tumor suppressor
Current Opinion in Genetics & Development, 2005PP2A is one of the few serine/threonine-specific phosphatases in the cell, and its complex structure and regulation guarantees its many different functions. Some viruses have chosen to target this enzyme system in order to manage the host cell machinery for their own profit and to program cells into a malignant state.
Veerle, Janssens +2 more
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Transgenic and Knockout Models of PP2A
2003Publisher Summary This chapter discusses the transgenic and knockout models of PP2A. Considering the putative role of PP2A in the pathogenesis of human diseases, the development of more transgenic and knockout models of PP2A may provide insight in the regulation of PP2A.
Götz, J, Schild, A
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The structure of the PP2A regulatory subunit B56γ: The remaining piece of the PP2A jigsaw puzzle
Proteins: Structure, Function, and Bioinformatics, 2008AbstractThe PP2A serine/threonine phosphatase regulates a plethora of cellular processes. In the cell the predominant form of the enzyme is a heterotrimer, formed by a core dimer composed of a catalytic and a scaffolding subunit, which assemble together with one of a range of different regulatory B subunits.
Audur, Magnusdottir +7 more
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