Identification of the major sites of autophosphorylation of the murine protein-tyrosine kinase Syk
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The protein-tyrosine kinase Syk interacts with the C-terminal region of tensin2Molecular basis for a direct interaction between the Syk protein-tyrosine kinase and phosphoinositide 3-kinaseThe kinase Syk as an adaptor controlling sustained calcium signalling and B-cell developmentA novel histidine tyrosine phosphatase, TULA-2, associates with Syk and negatively regulates GPVI signaling in plateletsProfiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.3D structure of Syk kinase determined by single-particle electron microscopyFunctional roles of Syk in macrophage-mediated inflammatory responsesThe Syk kinase SmTK4 of Schistosoma mansoni is involved in the regulation of spermatogenesis and oogenesisBiochemical interactions integrating Itk with the T cell receptor-initiated signaling cascadeCbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130Phosphorylation of Tyr342 in the linker region of Syk is critical for Fc epsilon RI signaling in mast cellsPhospholipase D2 acts as an essential adaptor protein in the activation of Syk in antigen-stimulated mast cellsPhosphorylation of Syk activation loop tyrosines is essential for Syk function. An in vivo study using a specific anti-Syk activation loop phosphotyrosine antibodyThe Syk family of protein tyrosine kinases in T-cell activation and developmentTULA-2 Protein Phosphatase Suppresses Activation of Syk through the GPVI Platelet Receptor for Collagen by Dephosphorylating Tyr(P)346, a Regulatory Site of SykEnhancement of B-cell receptor signaling by a point mutation of adaptor protein 3BP2 identified in human inherited disease cherubism.Tyrosine phosphorylation of 3BP2 regulates B cell receptor-mediated activation of NFATAdaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains of Lyn protein-tyrosine kinase.Conformational rearrangements upon Syk auto-phosphorylation.The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70.Reactive oxygen species play a critical role in collagen-induced platelet activation via SHP-2 oxidation.A unique insert in the linker domain of Syk is necessary for its function in immunoreceptor signalling.Phosphorylation of Tyr319 in ZAP-70 is required for T-cell antigen receptor-dependent phospholipase C-gamma1 and Ras activation.Tyrosines in the carboxyl terminus regulate Syk kinase activity and functionMast cell signaling: the role of protein tyrosine kinase Syk, its activation and screening methods for new pathway participantsRegulation of Syk by phosphorylation on serine in the linker insertProgress towards the development of SH2 domain inhibitors.Regulation and function of syk tyrosine kinase in mast cell signaling and beyond.Peroxiredoxin II is an antioxidant enzyme that negatively regulates collagen-stimulated platelet functionOnce phosphorylated, tyrosines in carboxyl terminus of protein-tyrosine kinase Syk interact with signaling proteins, including TULA-2, a negative regulator of mast cell degranulationThe TREM2-DAP12 signaling pathway in Nasu-Hakola disease: a molecular genetics perspective.Spleen Tyrosine Kinase Is Involved in the CD38 Signal Transduction Pathway in Chronic Lymphocytic Leukemia.Spleen tyrosine kinase (Syk) as a novel target for allergic asthma and rhinitis.The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor-mediated signal transduction.Multiplexed quantitation of protein expression and phosphorylation based on functionalized soluble nanopolymers.The SYK tyrosine kinase: a crucial player in diverse biological functions.Syk inhibits the activity of protein kinase A by phosphorylating tyrosine 330 of the catalytic subunitTyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling.Syk and pTyr'd: Signaling through the B cell antigen receptor
P2860
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P2860
Identification of the major sites of autophosphorylation of the murine protein-tyrosine kinase Syk
description
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1997
@ast
im Februar 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/02/04)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/02/04)
@nl
наукова стаття, опублікована в лютому 1997
@uk
مقالة علمية (نشرت في 4-2-1997)
@ar
name
Identification of the major si ...... ne protein-tyrosine kinase Syk
@ast
Identification of the major si ...... ne protein-tyrosine kinase Syk
@en
Identification of the major si ...... ne protein-tyrosine kinase Syk
@nl
type
label
Identification of the major si ...... ne protein-tyrosine kinase Syk
@ast
Identification of the major si ...... ne protein-tyrosine kinase Syk
@en
Identification of the major si ...... ne protein-tyrosine kinase Syk
@nl
prefLabel
Identification of the major si ...... ne protein-tyrosine kinase Syk
@ast
Identification of the major si ...... ne protein-tyrosine kinase Syk
@en
Identification of the major si ...... ne protein-tyrosine kinase Syk
@nl
P2093
P3181
P1476
Identification of the major si ...... ne protein-tyrosine kinase Syk
@en
P2093
A M Mahrenholz
C L Ashendel
M L Harrison
M T Furlong
P304
P3181
P356
10.1016/S0167-4889(96)00131-0
P407
P577
1997-02-01T00:00:00Z