Intermolecular interactions of the p85alpha regulatory subunit of phosphatidylinositol 3-kinase.
about
The p85 regulatory subunit of phosphoinositide 3-kinase down-regulates IRS-1 signaling via the formation of a sequestration complexNegative regulation of PI 3-kinase by Ruk, a novel adaptor proteinThe BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAPAssembly and Molecular Architecture of the Phosphoinositide 3-Kinase p85α Homodimer.Regulation of the PI3K pathway through a p85α monomer-homodimer equilibriumIntermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase.Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells.Phosphoinositide-3 kinase binds to a proline-rich motif in the Na+, K+-ATPase alpha subunit and regulates its trafficking.High frequency of PIK3R1 and PIK3R2 mutations in endometrial cancer elucidates a novel mechanism for regulation of PTEN protein stabilityRegulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo.Ether-linked diglycerides inhibit vascular smooth muscle cell growth via decreased MAPK and PI3K/Akt signaling.Multiple roles for the p85α isoform in the regulation and function of PI3K signalling and receptor trafficking.Targeting therapeutic liabilities engendered by PIK3R1 mutations for cancer treatment.Cell activation-induced phosphoinositide 3-kinase alpha/beta dimerization regulates PTEN activity.Neomorphic mutations create therapeutic challenges in cancer.Positive and negative regulation of phosphoinositide 3-kinase-dependent signaling pathways by three different gene products of the p85alpha regulatory subunit.Tyrosine phosphorylation of p85 relieves its inhibitory activity on phosphatidylinositol 3-kinase.Uncovering the PI3Ksome: phosphoinositide 3-kinases and counteracting PTEN form a signaling complex with intrinsic regulatory properties.Computational models of tandem SRC homology 2 domain interactions and application to phosphoinositide 3-kinase.Patient-derived mutations within the N-terminal domains of p85α impact PTEN or Rab5 binding and regulation.
P2860
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P2860
Intermolecular interactions of the p85alpha regulatory subunit of phosphatidylinositol 3-kinase.
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
Intermolecular interactions of ...... phosphatidylinositol 3-kinase.
@ast
Intermolecular interactions of ...... phosphatidylinositol 3-kinase.
@en
type
label
Intermolecular interactions of ...... phosphatidylinositol 3-kinase.
@ast
Intermolecular interactions of ...... phosphatidylinositol 3-kinase.
@en
prefLabel
Intermolecular interactions of ...... phosphatidylinositol 3-kinase.
@ast
Intermolecular interactions of ...... phosphatidylinositol 3-kinase.
@en
P2093
P2860
P356
P1476
Intermolecular interactions of ...... phosphatidylinositol 3-kinase
@en
P2093
A G Harpur
G Panayotou
M D Waterfield
M J Bottomley
M J Layton
P2860
P304
12323-12332
P356
10.1074/JBC.274.18.12323
P407
P577
1999-04-01T00:00:00Z