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Protein phosphatase 2A (PP2A), a drugable tumor suppressor in Ph1(+) leukemias
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PKR Regulates B56α-mediated BCL2 Phosphatase Activity in Acute Lymphoblastic Leukemia-derived REH Cells
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RAX, the PKR activator, sensitizes cells to inflammatory cytokines, serum withdrawal, chemotherapy, and viral infection
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A point mutation in the RNA-binding domain I results in decrease of PKR activation in acute lymphoblastic leukemia
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Loss of PKR activity in chronic lymphocytic leukemia
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The protein kinase PKR is required for macrophage apoptosis after activation of Toll-like receptor 4
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Mono- and multisite phosphorylation enhances Bcl2's antiapoptotic function and inhibition of cell cycle entry functions
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A novel immunosuppressive agent FTY720 induced Akt dephosphorylation in leukemia cells
Y Matsuoka et al.
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A functional role for nicotine in Bcl2 phosphorylation and suppression of apoptosis
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A functional role for the B56 α-subunit of protein phosphatase 2A in ceramide-mediated regulation of Bcl2 phosphorylation status and function
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RNA-dependent protein kinase PKR is required for activation of NF-κB by IFN-γ in a STAT1-independent pathway
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Phosphorylation of Bcl2 and regulation of apoptosis
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The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin
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The B56α regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKR
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Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR
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