The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
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PTEN function: how normal cells control it and tumour cells lose itInositol phosphatase SHIP1 is a primary target of miR-155Inpp5f is a polyphosphoinositide phosphatase that regulates cardiac hypertrophic responsivenessSHIP2 multiple functions: a balance between a negative control of PtdIns(3,4,5)P₃ level, a positive control of PtdIns(3,4)P₂ production, and intrinsic docking properties.A key role for the phosphorylation of Ser440 by the cyclic AMP-dependent protein kinase in regulating the activity of the Src homology 2 domain-containing Inositol 5'-phosphatase (SHIP1).Insulin hypersensitivity and resistance to streptozotocin-induced diabetes in mice lacking PTEN in adipose tissuePhosphoinositide phosphatases in cell biology and disease.SHIP2, a factor associated with diet-induced obesity and insulin sensitivity, attenuates FGF signaling in vivo.Distinguishing modes of eukaryotic gradient sensing.A screen for novel phosphoinositide 3-kinase effector proteins.Phosphoinositide phosphatases and disease.Down-regulation of microRNA-155 attenuates retinal neovascularization via the PI3K/Akt pathway.Mutations in phosphoinositide metabolizing enzymes and human disease.Phosphoinositide 3-kinase/Akt signaling pathway and its therapeutical implications for human acute myeloid leukemia.SHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core proteinMiR-155-regulated molecular network orchestrates cell fate in the innate and adaptive immune response to Mycobacterium tuberculosis.Phosphoinositide 3-kinase p110δ promotes lumen formation through the enhancement of apico-basal polarity and basal membrane organization.SHIP2 and its involvement in various diseases.Biochemistry and structure of phosphoinositide phosphatases.Coupling an EML4-ALK-centric interactome with RNA interference identifies sensitizers to ALK inhibitors.Kinases as Novel Therapeutic Targets in Asthma and Chronic Obstructive Pulmonary Disease.INPPL1 gene mutations in opsismodysplasiaThe control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2, SHIP2.Evidence of SHIP2 Ser132 phosphorylation, its nuclear localization and stability.Novel compound heterozygous mutations in inositol polyphosphate phosphatase-like 1 in a family with severe opsismodysplasia.Identification of cyclin A2 as the downstream effector of the nuclear phosphatidylinositol 4,5-bisphosphate signaling network.Endogenous SHIP2 does not localize in lipid rafts in 3T3-L1 adipocytes.Suppression of SHIP2 contributes to tumorigenesis and proliferation of gastric cancer cells via activation of Akt.Underexpression of INPPL1 is associated with aggressive clinicopathologic characteristics in papillary thyroid carcinoma
P2860
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P2860
The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
@ast
The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
@en
type
label
The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
@ast
The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
@en
prefLabel
The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
@ast
The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
@en
P2093
P1476
The termination of PI3K signalling by SHIP1 and SHIP2 inositol 5-phosphatases.
@en
P2093
Christophe Erneux
Daniel Blero
Jing Zhang
Katrien Backers
Nathalie Paternotte
P356
10.1016/S0065-2571(02)00043-2
P577
2003-01-01T00:00:00Z