A frequent kinase domain mutation that changes the interaction between PI3K and the membrane
about
Gain of interaction with IRS1 by p110α-helical domain mutants is crucial for their oncogenic functionsPhosphoinositide 3-kinase δ gene mutation predisposes to respiratory infection and airway damageMosaic overgrowth with fibroadipose hyperplasia is caused by somatic activating mutations in PIK3CAPhosphoinositides: tiny lipids with giant impact on cell regulationThe Key Role of Calmodulin in KRAS-Driven AdenocarcinomasInvestigating the structure and dynamics of the PIK3CA wild-type and H1047R oncogenic mutantThe p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitorsStructural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 proteinStructure of the iSH2 domain of human phosphatidylinositol 3-kinase p85β subunit reveals conformational plasticity in the interhelical turn regionStructure of Lipid Kinase p110β/p85β Elucidates an Unusual SH2-Domain-Mediated Inhibitory MechanismRegulation of lipid binding underlies the activation mechanism of class IA PI3-kinasesAutoinhibition and Phosphorylation-Induced Activation of Phospholipase C-γ IsozymesCrystal Structures of PI3Kα Complexed with PI103 and Its Derivatives: New Directions for Inhibitors DesignEngineering of an isolated p110α subunit of PI3Kα permits crystallization and provides a platform for structure-based drug designKDM1 class flavin-dependent protein lysine demethylasesIdentification of novel piperazinylquinoxaline derivatives as potent phosphoinositide 3-kinase (PI3K) inhibitorsAnticancer compound plumbagin and its molecular targets: a structural insight into the inhibitory mechanisms using computational approachesAssembly and Molecular Architecture of the Phosphoinositide 3-Kinase p85α Homodimer.The next generation of metastatic melanoma: uncovering the genetic variants for anti-BRAF therapy responseActivating mutations in TOR are in similar structures as oncogenic mutations in PI3KCalpha.Dynamic steps in receptor tyrosine kinase mediated activation of class IA phosphoinositide 3-kinases (PI3K) captured by H/D exchange (HDX-MS).Molecular determinants of PI3Kγ-mediated activation downstream of G-protein-coupled receptors (GPCRs)Somatic mutations in PI3Kalpha: structural basis for enzyme activation and drug designHot-spot mutations in p110alpha of phosphatidylinositol 3-kinase (pI3K): differential interactions with the regulatory subunit p85 and with RAS.Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH).Small-molecule inhibitors of the PI3K signaling network(+)-2-(1-Hydroxyl-4-oxocyclohexyl) ethyl caffeate suppresses solar UV-induced skin carcinogenesis by targeting PI3K, ERK1/2, and p38.Functional and genomic analyses of alpha-solenoid proteins.Eradication of metastatic mouse cancers resistant to immune checkpoint blockade by suppression of myeloid-derived cells.Cancer-derived mutations in the regulatory subunit p85alpha of phosphoinositide 3-kinase function through the catalytic subunit p110alphaA human immunodeficiency caused by mutations in the PIK3R1 gene.PI3K: from the bench to the clinic and back.Structural basis of nSH2 regulation and lipid binding in PI3Kα.A biochemical mechanism for the oncogenic potential of the p110beta catalytic subunit of phosphoinositide 3-kinase.Dominant-activating germline mutations in the gene encoding the PI(3)K catalytic subunit p110δ result in T cell senescence and human immunodeficiencyPI3Kα inhibitors that inhibit metastasis.The landscape of somatic mutations in infant MLL-rearranged acute lymphoblastic leukemiasGain-of-function mutations and immunodeficiency: at a loss for proper tuning of lymphocyte signaling.Autophosphorylation of serine 608 in the p85 regulatory subunit of wild type or cancer-associated mutants of phosphoinositide 3-kinase does not affect its lipid kinase activityRole of E542 and E545 missense mutations of PIK3CA in breast cancer: a comparative computational approach.
P2860
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P2860
A frequent kinase domain mutation that changes the interaction between PI3K and the membrane
description
2009 nî lūn-bûn
@nan
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
A frequent kinase domain mutat ...... between PI3K and the membrane
@ast
A frequent kinase domain mutat ...... between PI3K and the membrane
@en
A frequent kinase domain mutat ...... between PI3K and the membrane
@nl
type
label
A frequent kinase domain mutat ...... between PI3K and the membrane
@ast
A frequent kinase domain mutat ...... between PI3K and the membrane
@en
A frequent kinase domain mutat ...... between PI3K and the membrane
@nl
prefLabel
A frequent kinase domain mutat ...... between PI3K and the membrane
@ast
A frequent kinase domain mutat ...... between PI3K and the membrane
@en
A frequent kinase domain mutat ...... between PI3K and the membrane
@nl
P2093
P2860
P50
P356
P1476
A frequent kinase domain mutat ...... between PI3K and the membrane
@en
P2093
Diana Mandelker
Ian Cheong
Jiuxiang Zhu
Oleg Schmidt-Kittler
P2860
P304
16996-7001
P356
10.1073/PNAS.0908444106
P407
P577
2009-10-06T00:00:00Z