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PI-3-kinases


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'PI-3-kinases' can also refer to...

PI-3-kinases

Molecular targeting: PI3 kinase pathway

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Myricetin inhibits UVB-induced angiogenesis by regulating PI-3 kinase in vivo

Functional studies of the PI(3)‐kinase signalling pathway employing synthetic and expressed siRNA

PI 3-kinase, protein kinase C, and protein kinase A are involved in the trigger phase of β1-adrenergic preconditioning

73PEXPRESSION OF PHOSPHORYLATED PROTEINS FROM PI3-KINASE AND MAP-KINASE SIGNALING PATHWAYS IN INFILTRATING BREAST CANCER: RELATION WITH HISTOPATHOLOGIC AND MOLECULAR SUBTYPES

Infarct size limitation by adrenomedullin: protein kinase A but not PI3-kinase is linked to mitochondrial KCa channels

Reduced PTEN expression in breast cancer cells confers susceptibility to inhibitors of the PI3 kinase/Akt pathway

Physiological concentrations of insulin induce endothelin-mediated vasoconstriction during inhibition of NOS or PI3-kinase in skeletal muscle arterioles

Ischemic postconditioning protects remodeled myocardium via the PI3K–PKB/Akt reperfusion injury salvage kinase pathway

Erythropoietin promotes endothelial progenitor cell proliferative and adhesive properties in a PI 3-kinase-dependent manner

The acute phase protein α2-macroglobulin induces rat ventricular cardiomyocyte hypertrophy via ERK1,2 and PI3-kinase/Akt pathways*

IL-6 induces PI 3-kinase and nitric oxide-dependent protection and preserves mitochondrial function in cardiomyocytes

Biphasic effect of p21Cip1 on smooth muscle cell proliferation: Role of PI 3-kinase and Skp2-mediated degradation

 

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A family of kinases (phosphatidylinositol-3-kinases, PI kinases) that phosphorylate phosphatidylinositol phosphate on the 3 position. They are involved in signalling cascades downstream of many growth factor receptors, particularly receptor tyrosine kinases (RTKs). The classical form (class I) has a p110 enzymatic subunit which is regulated by p85 (p85α, p85β, p55γ, and splicing variants). p110 is recruited to the membrane and activated via the interaction of SH2 domains on the regulatory subunit which bind phosphotyrosine motifs on the stimulated RTK. An increasing family is being identified, including the PI3Kγ isoform which is activated by receptor-stimulated G proteins and recruited to the membrane by p101. Others are regulated by calcium. Most, but not all, are inhibited by wortmannin. See Akt.

Subjects: Medicine and Health.


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