Sensitive kinase assay linked with phosphoproteomics for identifying direct kinase substrates.
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Serine phosphorylation by SYK is critical for nuclear localization and transcription factor function of IkarosStress Granules Modulate SYK to Cause Microglial Cell Dysfunction in Alzheimer's Disease.Inhibition of Spleen Tyrosine Kinase Potentiates Paclitaxel-Induced Cytotoxicity in Ovarian Cancer Cells by Stabilizing Microtubules.Proteogenomic convergence for understanding cancer pathways and networks.Global phosphoproteomics of activated B cells using complementary metal ion functionalized soluble nanopolymers.Current technologies to identify protein kinase substrates in high throughputMethod for identifying phosphorylated substrates of specific cyclin/cyclin-dependent kinase complexes.Syk interacts with and phosphorylates nucleolin to stabilize Bcl-x(L) mRNA and promote cell survival.Tissue phosphoproteomics with PolyMAC identifies potential therapeutic targets in a transgenic mouse model of HER2 positive breast cancer.Identification of nuclear phosphoproteins as novel tobacco markers in mouse lung tissue following short-term exposure to tobacco smoke.Identification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics.Analytical challenges translating mass spectrometry-based phosphoproteomics from discovery to clinical applications.Calling in SYK: SYK's dual role as a tumor promoter and tumor suppressor in cancer.A PREVIOUSLY UNKNOWN UNIQUE CHALLENGE FOR INHIBITORS OF SYK ATP-BINDING SITE: ROLE OF SYK AS A CELL CYCLE CHECKPOINT REGULATORNanomechanical property maps of breast cancer cells as determined by multiharmonic atomic force microscopy reveal Syk-dependent changes in microtubule stability mediated by MAP1B.Salmonella modulation of host cell gene expression promotes its intracellular growthKINATEST-ID: a pipeline to develop phosphorylation-dependent terbium sensitizing kinase assays.NANOG is multiply phosphorylated and directly modified by ERK2 and CDK1 in vitro.Multiplex isotope dimethyl labeling of substrate peptides for high throughput kinase activity assay via quantitative MALDI MS.Specific dephosphorylation of Janus Kinase 2 by protein tyrosine phosphatases.Protein networks and activation of lymphocytes.In-Depth Analyses of B Cell Signaling Through Tandem Mass Spectrometry of Phosphopeptides Enriched by PolyMAC.Syk Is Recruited to Stress Granules and Promotes Their Clearance through Autophagy.Reconstruction and signal propagation analysis of the Syk signaling network in breast cancer cells.Multiplex Substrate Profiling by Mass Spectrometry for Kinases as a Method for Revealing Quantitative Substrate Motifs.A peptide-based biosensor assay to detect intracellular Syk kinase activation and inhibition.Syk inhibits the activity of protein kinase A by phosphorylating tyrosine 330 of the catalytic subunitIs phosphoproteomics ready for clinical research?Quantitative phosphoproteomics identifies SnRK2 protein kinase substrates and reveals the effectors of abscisic acid action.Signal transduction in cerebral arteries after subarachnoid hemorrhage-a phosphoproteomic approach.Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomicsA C-terminal acidic domain regulates degradation of the transcriptional coactivator Bob1.Global screening of CK2 kinase substrates by an integrated phosphoproteomics workflow.An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor.Encephalomyocarditis virus leader is phosphorylated by CK2 and syk as a requirement for subsequent phosphorylation of cellular nucleoporins.RegPhos 2.0: an updated resource to explore protein kinase-substrate phosphorylation networks in mammals.Integration of phosphoproteomic, chemical, and biological strategies for the functional analysis of targeted protein phosphorylation.Proteomic analysis of phosphorylation in cancer.Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform.The role of structural disorder in cell cycle regulation, related clinical proteomics, disease development and drug targeting.
P2860
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P2860
Sensitive kinase assay linked with phosphoproteomics for identifying direct kinase substrates.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Sensitive kinase assay linked ...... ying direct kinase substrates.
@ast
Sensitive kinase assay linked ...... ying direct kinase substrates.
@en
type
label
Sensitive kinase assay linked ...... ying direct kinase substrates.
@ast
Sensitive kinase assay linked ...... ying direct kinase substrates.
@en
prefLabel
Sensitive kinase assay linked ...... ying direct kinase substrates.
@ast
Sensitive kinase assay linked ...... ying direct kinase substrates.
@en
P2093
P2860
P50
P356
P1476
Sensitive kinase assay linked ...... fying direct kinase substrates
@en
P2093
Jacob A Galan
Lianghai Hu
Michael Hans
W Andy Tao
Wen-Horng Wang
P2860
P304
P356
10.1073/PNAS.1119418109
P407
P577
2012-03-26T00:00:00Z