PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
about
Voltage-Controlled Enzymes: The New JanusBifronsMyotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphateThe human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complexPhosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusionDeficiency of PTEN in Jurkat T cells causes constitutive localization of Itk to the plasma membrane and hyperresponsiveness to CD3 stimulationNegative regulation of PI 3-kinase by Ruk, a novel adaptor proteinTherapeutic Implications of Targeting AKT Signaling in MelanomaRetroviral expression of a kinase-defective IGF-I receptor suppresses growth and causes apoptosis of CHO and U87 cells in-vivo.Role of APC and DNA mismatch repair genes in the development of colorectal cancers.Medical treatment for gastro-entero-pancreatic neuroendocrine tumours'Micro-managers' of hepatic lipid metabolism and NAFLDPI3K-AKT-mTOR-signaling and beyond: the complex network in gastroenteropancreatic neuroendocrine neoplasmsPhosphoinositides: tiny lipids with giant impact on cell regulationTurning off AKT: PHLPP as a drug targetThe role of phosphoinositide-regulated actin reorganization in chemotaxis and cell migrationThe structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutationsA glutamate switch controls voltage-sensitive phosphatase functionEngineering of an isolated p110α subunit of PI3Kα permits crystallization and provides a platform for structure-based drug designA Subset of Autism-Associated Genes Regulate the Structural Stability of Neurons.Discovery of Rare Mutations in Autism: Elucidating Neurodevelopmental MechanismsThe Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cellsPTEN regulates tumor cell adhesion of colon carcinoma cells under dynamic conditions of fluid flowMultimerization of the protein-tyrosine phosphatase (PTP)-like insulin-dependent diabetes mellitus autoantigens IA-2 and IA-2beta with receptor PTPs (RPTPs). Inhibition of RPTPalpha enzymatic activityPleiotrophin signaling through anaplastic lymphoma kinase is rate-limiting for glioblastoma growthRequirement of phosphoinositide 3-kinase and Akt for interferon-beta-mediated induction of the beta-R1 (SCYB11) geneTargeting mutants of PTEN reveal distinct subsets of tumour suppressor functionsThe future role of personalized medicine in the treatment of glioblastoma multiformeOverexpression of Akt1 enhances adipogenesis and leads to lipoma formation in zebrafishPIK3IP1, a negative regulator of PI3K, suppresses the development of hepatocellular carcinomaPTEN is recruited to the postsynaptic terminal for NMDA receptor-dependent long-term depressionInositol trisphosphate 3-kinase B (InsP3KB) as a physiological modulator of myelopoiesisEthanol impairs insulin-stimulated neuronal survival in the developing brain: role of PTEN phosphatase.The complement of protein phosphatase catalytic subunits encoded in the genome of ArabidopsisThe mechanism involved in the regulation of phospholipase Cgamma1 activity in cell migration.Use of double-stranded RNA interference in Drosophila cell lines to dissect signal transduction pathways.PTEN blocks tumor necrosis factor-induced NF-kappa B-dependent transcription by inhibiting the transactivation potential of the p65 subunit.PTEN knockdown alters dendritic spine/protrusion morphology, not densityPTEN can inhibit in vitro organotypic and in vivo orthotopic invasion of human bladder cancer cells even in the absence of its lipid phosphatase activity.Akt-mediated activation of HIF-1 in pulmonary vascular endothelial cells by S-nitrosoglutathioneTumor suppressor PTEN is a physiologic suppressor of chemoattractant-mediated neutrophil functions
P2860
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P2860
PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
@ast
PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
@en
type
label
PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
@ast
PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
@en
prefLabel
PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
@ast
PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
@en
P1476
PTEN: a tumour suppressor that functions as a phospholipid phosphatase.
@en
P2093
P304
P356
10.1016/S0962-8924(99)01519-6
P577
1999-04-01T00:00:00Z