Disruption of the interface between the pleckstrin homology (PH) and kinase domains of Akt protein is sufficient for hydrophobic motif site phosphorylation in the absence of mTORC2
about
Interactome of the negative regulator of nuclear import BRCA1-binding protein 2Giant obscurins regulate the PI3K cascade in breast epithelial cells via direct binding to the PI3K/p85 regulatory subunitREDD1 enhances protein phosphatase 2A-mediated dephosphorylation of Akt to repress mTORC1 signaling.A Hot-spot of In-frame Duplications Activates the Oncoprotein AKT1 in Juvenile Granulosa Cell Tumors.Molecular analyses of juvenile granulosa cell tumors bearing AKT1 mutations provide insights into tumor biology and therapeutic leads.Inhibition of triple-negative and Herceptin-resistant breast cancer cell proliferation and migration by Annexin A2 antibodies.Intramembrane binding of VE-cadherin to VEGFR2 and VEGFR3 assembles the endothelial mechanosensory complex.Vav1 Regulates T-Cell Activation through a Feedback Mechanism and Crosstalk between the T-Cell Receptor and CD28.Mammalian target of rapamycin complex 1 (mTORC1) and 2 (mTORC2) control the dendritic arbor morphology of hippocampal neuronsDisruption of PH-kinase domain interactions leads to oncogenic activation of AKT in human cancers.Regulation of insulin receptor substrate-1 by mTORC2 (mammalian target of rapamycin complex 2)Regulation of OSR1 and the sodium, potassium, two chloride cotransporter by convergent signals.Spatiotemporal dynamics of phosphorylation in lipid second messenger signaling.PIM kinase (and Akt) biology and signaling in tumors.A PLC-γ1 Feedback Pathway Regulates Lck Substrate Phosphorylation at the T-Cell Receptor and SLP-76 Complex.SUMOylation regulates AKT1 activity.Novel obscurins mediate cardiomyocyte adhesion and size via the PI3K/AKT/mTOR signaling pathway.Conformational sampling of membranes by Akt controls its activation and inactivation.
P2860
Q24329017-7874E1C9-C551-4B72-BE47-9ADF3E5F4913Q30008900-A46FE82F-0331-4BEA-BBDF-1F92C3028767Q34092837-88C3B2E1-E1B6-444E-AE07-99B604E5BCCEQ34483356-6D4A1F61-DC6E-4A02-95C4-02564EFC4F06Q34493715-FB62BC98-14FB-452A-ABEC-C26D152C6C6FQ34687047-D3B3490D-9A7B-4DCE-A785-ACADFE3E45A1Q35261533-52D56603-DEBB-466E-83A9-5FA0A26F7308Q35811971-40B41DF8-D1D4-430B-8B22-3D9334942FDAQ36216334-9D0069B9-64F9-465B-88B9-CBFD30CE719EQ36436853-F394FEF5-F53E-43C9-AA20-DF058972AD6DQ36939696-4B5893CA-DA5C-40B3-A375-121989D3D940Q37340702-78CFDC2B-F94B-4B29-AAAA-01637E905401Q37388961-90EE495F-446B-4997-AE0B-8DFF1063390FQ38370023-FA2B9D08-53E3-471A-9150-F181E7C68CCFQ38712356-897019BC-C975-49DE-B378-06F079EBB586Q39007397-88B4E5BD-EB72-4F92-B828-2ED02C9D3537Q47136381-CE9441D0-8190-4B0E-8F0C-B344279A8CADQ52327556-58E802FC-8827-45A6-84A2-1E74AA68C898
P2860
Disruption of the interface between the pleckstrin homology (PH) and kinase domains of Akt protein is sufficient for hydrophobic motif site phosphorylation in the absence of mTORC2
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Disruption of the interface be ...... ation in the absence of mTORC2
@ast
Disruption of the interface be ...... ation in the absence of mTORC2
@en
type
label
Disruption of the interface be ...... ation in the absence of mTORC2
@ast
Disruption of the interface be ...... ation in the absence of mTORC2
@en
prefLabel
Disruption of the interface be ...... ation in the absence of mTORC2
@ast
Disruption of the interface be ...... ation in the absence of mTORC2
@en
P2860
P356
P1476
Disruption of the interface be ...... ation in the absence of mTORC2
@en
P2093
Matt Niederst
P2860
P304
39122-39129
P356
10.1074/JBC.M111.278747
P407
P577
2011-09-09T00:00:00Z