Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells
about
Cell adhesion regulates the interaction between the docking protein p130(Cas) and the 14-3-3 proteinsDYRK1A autophosphorylation on serine residue 520 modulates its kinase activity via 14-3-3 bindingKank regulates RhoA-dependent formation of actin stress fibers and cell migration via 14-3-3 in PI3K-Akt signalingSerine phosphorylation of Cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T cells via a novel serine-rich 14-3-3-binding motifProtein binding and signaling properties of RIN1 suggest a unique effector functionActivation-modulated association of 14-3-3 proteins with Cbl in T cells14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit G proteins14-3-3zeta interacts with the alpha-chain of human interleukin 9 receptorPhosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteinsThe 4.1/ezrin/radixin/moesin domain of the DAL-1/Protein 4.1B tumour suppressor interacts with 14-3-3 proteinsIdentification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zetaIntegration of calcium and cyclic AMP signaling pathways by 14-3-3Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and functionCrystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic grooveProtein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activityIdentification of a novel interaction between integrin beta1 and 14-3-3betaBinding of 14-3-3beta regulates the kinase activity and subcellular localization of testicular protein kinase 114-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent mannerCoordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinasesAssociation of the TLX-2 homeodomain and 14-3-3eta signaling proteinsFAM65B controls the proliferation of transformed and primary T cells.The cytoplasmic domain of the platelet glycoprotein Ibalpha is phosphorylated at serine 609.Study of therapy resistance in cancer cells with functional proteome analysis.Inhibition of calcium/calmodulin-dependent protein kinase kinase by protein 14-3-3.Raf-1 kinase and exoenzyme S interact with 14-3-3zeta through a common site involving lysine 49.The chaperone protein 14-3-3 interacts with 3BP2/SH3BP2 and regulates its adapter function.Serine 257 phosphorylation regulates association of polyomavirus middle T antigen with 14-3-3 proteinsThe zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different alpha2-adrenergic receptor subtypes.14-3-3tau associates with a translational control factor FKBP12-rapamycin-associated protein in T-cells after stimulation by pervanadate.Dynamic aspects of platelet adhesion under flow.14-3-3 proteins: key regulators of cell division, signalling and apoptosis.14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction.Dynamic multiprotein assemblies shape the spatial structure of cell signalingCaveolin-1 maintains activated Akt in prostate cancer cells through scaffolding domain binding site interactions with and inhibition of serine/threonine protein phosphatases PP1 and PP2A.14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthasecDNA cloning, expression pattern, and chromosomal localization of Mlf1, murine homologue of a gene involved in myelodysplasia and acute myeloid leukemia14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor.A novel pathway down-modulating T cell activation involves HPK-1-dependent recruitment of 14-3-3 proteins on SLP-76.
P2860
Q22008792-D5EA82A3-CC61-41B5-A122-D490BE369E77Q24293338-F89B4354-949B-4426-A004-D3E24A0B1638Q24310007-F5B930C4-3EBD-490B-9AA7-54121F323DD0Q24311683-3090E8CE-B3E2-49D4-8919-EC641BA59DC7Q24319548-84111B1B-1D32-46F6-9C9B-CCC816F541B6Q24321362-6616DBBF-31D3-4284-869C-E37FE49DC40DQ24339259-EC4FD28A-F604-4C92-B1BC-EBA8FB0FCFF0Q24531933-DBFC9101-57F1-4CC3-9EEB-908869DC42F4Q24533191-3064A440-81FD-4BE3-8B63-BD5AE4D4F34EQ24534317-BF5B2AA4-6C57-4DCA-B129-22CC9BC44A46Q24534993-35987A07-7533-461E-966B-315B9D07A2AEQ24554335-3283FB89-C50A-4E3D-A9DC-4764DE74D567Q24648178-EFD08E39-A1AB-4B6F-BF04-9F2235E27972Q27734201-20BEF3D4-58AD-4214-83DB-39DC91BFE53FQ27758986-4F2BC21F-BD7A-4D34-9B8F-D061EF29F640Q28139665-3AB85CE8-4902-4A38-939D-3574F8FEE351Q28180815-53DE25CF-B30C-48BF-8FAB-869C744A6F44Q28213843-E258FB5B-41E5-40E3-859D-77A3FD0F8B46Q28216136-94D64DF3-581F-44F9-A708-C38D62FA4253Q28235588-5488108C-12F0-415A-9029-19CCDE6C4C30Q28267092-766A6E61-CE9D-4824-980A-8BBD92D12144Q28282466-1FB46602-71FC-44EC-9F5F-C4863A5977D0Q29465807-48D556F4-991B-495C-AA4F-9F2E6214BA88Q30811815-A779BDDE-80F9-4578-BCFF-BEAB47CEDFE6Q31053524-54A78AB2-AECD-462E-AC84-F8AB5B4BC2FDQ33288845-10B801D5-C7E9-4207-8013-1FD0C4DCA2BBQ33292522-FB10123D-E597-48FE-A29F-2F0B7F042BFCQ33292565-81E34DD1-D82F-4A24-B4F4-E82EAFBEEB6FQ33782069-390914D7-4174-4F62-8543-2E8F387D4A77Q33860370-0B4BF24A-333E-472E-8272-A3DAAE3FCF34Q33889159-F948C6EC-6B57-419A-A1E2-4E1147F33532Q34266326-9E85C5F5-0E98-4B7C-A67C-9A8E7EE251E7Q34400246-87249017-16F4-41CA-A712-9DD3BF200528Q34445338-36BA7D1C-C6B5-47DC-ABD3-C2F8B679B3DCQ34602367-BADF8C22-BC33-4C5E-9189-EAB56DF19FE4Q34986770-90B04F04-60AA-46C8-9D2B-552F21376C43Q35062365-6DE802D3-C9CB-44A8-A989-A24D430A78B1Q35787253-A5E8C9B3-7C2D-4B81-B767-EEF3A3A9BEBDQ36236699-13856DA1-2BFD-4012-8F10-9A3EB45DEC3AQ36267208-1C261139-54AE-49C4-A934-6778CEAD37CC
P2860
Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@ast
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@en
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@nl
type
label
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@ast
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@en
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@nl
prefLabel
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@ast
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@en
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@nl
P2093
P2860
P356
P1476
Inhibition of phosphatidylinos ...... ith 14-3-3 proteins in T cells
@en
P2093
K Ishizaka
M von Willebrand
N Bonnefoy-Bérard
T Mustelin
P2860
P304
10142-10146
P356
10.1073/PNAS.92.22.10142
P407
P50
P577
1995-10-01T00:00:00Z