Targeting phosphatidylinositol 3-kinase signaling in acute myelogenous leukemia.

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article scientifique

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Targeting phosphatidylinositol 3-kinase signaling in acute myelogenous leukemia.

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Targeting phosphatidylinositol 3-kinase signaling in acute myelogenous leukemia.

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Targeting phosphatidylinositol 3-kinase signaling in acute myelogenous leukemia.

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P1476

Targeting phosphatidylinositol 3-kinase signaling in acute myelogenous leukemia.

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P2093

Alberto M Martelli

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Antonino Spartà

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Cecilia Evangelisti

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Daniela Bressanin

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Francesca Chiarini

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Marina Soncin

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P2860

Phosphorylation of the PTEN tail regulates protein stability and function

The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation

Activation of mTORC2 by association with the ribosome

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes

Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway

Two distinct phosphoinositide 3-kinases mediate polypeptide growth factor-stimulated PKB activation.

A pharmacological map of the PI3-K family defines a role for p110alpha in insulin signaling

A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin

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921-936

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scholarly article

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10.1517/14728222.2013.808333

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English

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2013-06-11T00:00:00Z

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23755894

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