A new approach for quantitative phosphoproteomic dissection of signaling pathways applied to T cell receptor activation.
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Phosphoproteomic profiling of in vivo signaling in liver by the mammalian target of rapamycin complex 1 (mTORC1)Phosphorylation site dynamics of early T-cell receptor signalingProteomic approaches to understanding the role of the cytoskeleton in host-defense mechanismsKinome analysis of receptor-induced phosphorylation in human natural killer cellsPeptideDepot: flexible relational database for visual analysis of quantitative proteomic data and integration of existing protein informationDramatic reduction of dimensionality in large biochemical networks owing to strong pair correlationsThe coming of age of phosphoproteomics--from large data sets to inference of protein functionsA proteomic view at T cell costimulationStrategies for quantitation of phosphoproteomic data.In-depth analyses of kinase-dependent tyrosine phosphoproteomes based on metal ion-functionalized soluble nanopolymersProteomic analysis of laser capture microdissected focal lesions in a rat model of progenitor marker-positive hepatocellular carcinoma.Quantitative phosphoproteomics reveals SLP-76 dependent regulation of PAG and Src family kinases in T cellsPhosphoproteome profiling of the macrophage response to different toll-like receptor ligands identifies differences in global phosphorylation dynamics.Phosphoproteomics in cancerQuantitative measurement of phosphoproteome response to osmotic stress in arabidopsis based on Library-Assisted eXtracted Ion Chromatogram (LAXIC)ERK positive feedback regulates a widespread network of tyrosine phosphorylation sites across canonical T cell signaling and actin cytoskeletal proteins in Jurkat T cells.SRC homology 2 domain-containing leukocyte phosphoprotein of 76 kDa (SLP-76) N-terminal tyrosine residues regulate a dynamic signaling equilibrium involving feedback of proximal T-cell receptor (TCR) signalingPhosphoproteomic analysis reveals an intrinsic pathway for the regulation of histone deacetylase 7 that controls the function of cytotoxic T lymphocytes.Quantitative phosphoproteomic analysis identifies activation of the RET and IGF-1R/IR signaling pathways in neuroblastoma.Protein networks and activation of lymphocytes.Wide-scale quantitative phosphoproteomic analysis reveals that cold treatment of T cells closely mimics soluble antibody stimulation.The catalytic activity of the kinase ZAP-70 mediates basal signaling and negative feedback of the T cell receptor pathway.Adaptation of HepG2 cells to a steady-state reduction in the content of protein phosphatase 6 (PP6) catalytic subunitVav1 Regulates T-Cell Activation through a Feedback Mechanism and Crosstalk between the T-Cell Receptor and CD28.Quantitative phosphoproteomic analysis reveals a role for serine and threonine kinases in the cytoskeletal reorganization in early T cell receptor activation in human primary T cells.TSLP signaling network revealed by SILAC-based phosphoproteomicsAnalysis of Phosphorylation-dependent Protein Interactions of Adhesion and Degranulation Promoting Adaptor Protein (ADAP) Reveals Novel Interaction Partners Required for Chemokine-directed T cell Migration.Proteomic responses to elevated ocean temperature in ovaries of the ascidian Ciona intestinalis.Phosphoproteomic analysis of liver homogenates.Quantitative phosphoproteomic analysis of T cell receptor signaling in diabetes prone and resistant miceRegPhos 2.0: an updated resource to explore protein kinase-substrate phosphorylation networks in mammals.Quantitative analysis of phosphorylation-based protein signaling networks in the immune system by mass spectrometry.The coordination of T-cell function by serine/threonine kinases.Mammalian plasma membrane proteins as potential biomarkers and drug targets.Phosphoproteomic analysis: an emerging role in deciphering cellular signaling in human embryonic stem cells and their differentiated derivatives.From global phosphoproteomics to individual proteins: the case of translation elongation factor eEF1A.Holistic systems biology approaches to molecular mechanisms of human helper T cell differentiation to functionally distinct subsets.Exploring intercellular signaling by proteomic approaches.Lighting Up T Lymphocyte Signaling with Quantitative Phosphoproteomics.A PLC-γ1 Feedback Pathway Regulates Lck Substrate Phosphorylation at the T-Cell Receptor and SLP-76 Complex.
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P2860
A new approach for quantitative phosphoproteomic dissection of signaling pathways applied to T cell receptor activation.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 14 July 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
A new approach for quantitativ ...... to T cell receptor activation.
@en
A new approach for quantitativ ...... to T cell receptor activation.
@nl
type
label
A new approach for quantitativ ...... to T cell receptor activation.
@en
A new approach for quantitativ ...... to T cell receptor activation.
@nl
prefLabel
A new approach for quantitativ ...... to T cell receptor activation.
@en
A new approach for quantitativ ...... to T cell receptor activation.
@nl
P2093
P2860
P1476
A new approach for quantitativ ...... to T cell receptor activation.
@en
P2093
Arthur R Salomon
Benjamin J Raphael
David H Laidlaw
Jonathan T Lin
Norris Hung
Radu Jianu
Samuel P Ulin
Vinh Nguyen
P2860
P304
P356
10.1074/MCP.M800307-MCP200
P577
2009-07-14T00:00:00Z