Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
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Phosphoproteomics: new insights into cellular signalingImmunoaffinity profiling of tyrosine phosphorylation in cancer cellsRegulation of Ack1 localization and activity by the amino-terminal SAM domainCharting the molecular network of the drug target Bcr-AblAnalysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.In silico proteome analysis to facilitate proteomics experiments using mass spectrometryRole of calcium-dependent protein kinases in chronic myeloid leukemia: combined effects of PKC and BCR-ABL signaling on cellular alterations during leukemia developmentCrystal structure of an SH2-kinase construct of c-Abl and effect of the SH2 domain on kinase activityIdentification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell lineTime-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modulesTemporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomicsNSP-CAS Protein Complexes: Emerging Signaling Modules in CancerMass spectrometry-based proteomics turns quantitativePhosphoproteomic profiling of in vivo signaling in liver by the mammalian target of rapamycin complex 1 (mTORC1)A highly scalable peptide-based assay system for proteomicsPeptideDepot: flexible relational database for visual analysis of quantitative proteomic data and integration of existing protein informationProteomic analysis of post-translational modificationsSDF1α-induced interaction of the adapter proteins Nck and HS1 facilitates actin polymerization and migration in T cells.Functional mechanisms and roles of adaptor proteins in abl-regulated cytoskeletal actin dynamics.A key role for the phosphorylation of Ser440 by the cyclic AMP-dependent protein kinase in regulating the activity of the Src homology 2 domain-containing Inositol 5'-phosphatase (SHIP1).Phosphotyrosine proteomic study of interferon alpha signaling pathway using a combination of immunoprecipitation and immobilized metal affinity chromatography.Derivatization of phosphorylated peptides with S- and N-nucleophiles for enhanced ionization efficiency in matrix-assisted laser desorption/ionization mass spectrometry.Enrichment and analysis of peptide subsets using fluorous affinity tags and mass spectrometry.Microarray-based functional protein profiling using peptide nucleic acid-encoded libraries.Identification of mammalian cell lines using MALDI-TOF and LC-ESI-MS/MS mass spectrometry.Using phage display to select antibodies recognizing post-translational modifications independently of sequence context.Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl.Protein kinase substrate identification on functional protein arraysInterplay between kinase domain autophosphorylation and F-actin binding domain in regulating imatinib sensitivity and nuclear import of BCR-ABL.High throughput profiling of serum phosphoproteins/peptides using the SELDI-TOF-MS platformToward quantitative phosphotyrosine profiling in vivo.Tissue phosphoproteomics with PolyMAC identifies potential therapeutic targets in a transgenic mouse model of HER2 positive breast cancer.Quantitative phosphoproteomics reveals SLP-76 dependent regulation of PAG and Src family kinases in T cellsPhosphoproteomics in cancerERK 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) signalingRegulation of ack-family nonreceptor tyrosine kinases.Evolutionary constraints of phosphorylation in eukaryotes, prokaryotes, and mitochondria.Quantitative phosphoproteomic analysis identifies activation of the RET and IGF-1R/IR signaling pathways in neuroblastoma.Identification of Novel Phosphorylation Motifs Through an Integrative Computational and Experimental Analysis of the Human Phosphoproteome
P2860
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P2860
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry
@nl
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
@ast
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
@en
type
label
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry
@nl
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
@ast
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
@en
prefLabel
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry
@nl
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
@ast
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
@en
P2093
P2860
P356
P1476
Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.
@en
P2093
Achim Brinker
Ansgar Brock
Arthur R Salomon
Christer Ericson
David M Horn
Eric C Peters
Karsten Sauer
Laurence M Brill
Peter G Schultz
Qui T Phung
P2860
P304
P356
10.1073/PNAS.2436191100
P407
P577
2003-01-09T00:00:00Z