Tyrosine phosphoproteomics of fibroblast growth factor signaling: a role for insulin receptor substrate-4.
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Phosphoproteomics: new insights into cellular signalingDifferential 14-3-3 affinity capture reveals new downstream targets of phosphatidylinositol 3-kinase signalingQuantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC)Phosphotyrosine interactome of the ErbB-receptor kinase familyNovel binding partners and differentially regulated phosphorylation sites clarify Eps8 as a multi-functional adaptorNovel phosphotyrosine targets of FGFR2IIIb signaling.Potential for sexual conflict assessed via testosterone-mediated transcriptional changes in liver and muscle of a songbirdPICquant: a quantitative platform to measure differential peptide abundance using dual-isotopic labeling with 12C6- and 13C6-phenyl isocyanateEffect of IRS4 levels on PI 3-kinase signalling.Ceramide displaces cholesterol from lipid rafts and decreases the association of the cholesterol binding protein caveolin-1.Quantitative proteomic analysis of protein complexes: concurrent identification of interactors and their state of phosphorylation.Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS.Protein expression signatures for inhibition of epidermal growth factor receptor-mediated signaling.Toward a complete in silico, multi-layered embryonic stem cell regulatory network.SHIP2, a factor associated with diet-induced obesity and insulin sensitivity, attenuates FGF signaling in vivo.Label-free relative quantification of co-eluting isobaric phosphopeptides of insulin receptor substrate-1 by HPLC-ESI-MS/MS.Pan-cancer analysis of somatic copy-number alterations implicates IRS4 and IGF2 in enhancer hijacking.Purification and identification of G protein-coupled receptor protein complexes under native conditions.The localization of FGFR3 mutations causing thanatophoric dysplasia type I differentially affects phosphorylation, processing and ubiquitylation of the receptor.Molecular modulation of the copper and cisplatin transport function of CTR1 and its interaction with IRS-4.Comparison of three quantitative phosphoproteomic strategies to study receptor tyrosine kinase signaling.A proteomic approach to obesity and type 2 diabetes.Variance Component Quantitative Trait Locus Analysis for Body Weight Traits in Purebred Korean Native Chicken.GIT1 utilizes a focal adhesion targeting-homology domain to bind paxillinPhosphoproteomics in analyzing signaling pathways.Melatonin receptors, heterodimerization, signal transduction and binding sites: what's new?Role of insulin and growth hormone/insulin-like growth factor-I signaling in lifespan extension: rodent longevity models for studying aging and calorie restriction.Use of stable isotope labeling by amino acids in cell culture (SILAC) for phosphotyrosine protein identification and quantitationADAM30 Downregulates APP-Linked Defects Through Cathepsin D Activation in Alzheimer's Disease.Evaluation of the variation in sample preparation for comparative proteomics using stable isotope labeling by amino acids in cell cultureChemical and pathway proteomics: powerful tools for oncology drug discovery and personalized health care.Quantitative phosphoproteomics by mass spectrometry: past, present, and futureSystems biology of stem cell fate and cellular reprogramming.Linking the proteins--elucidation of proteome-scale networks using mass spectrometry.The expanding field of SILAC.Role of proteomics in biomarker discovery and psychiatric disorders: current status, potentials, limitations and future challenges.Fibroblast growth factor receptor 2 phosphorylation on serine 779 couples to 14-3-3 and regulates cell survival and proliferation.Differential phosphoproteomics of fibroblast growth factor signaling: identification of Src family kinase-mediated phosphorylation events.Motif decomposition of the phosphotyrosine proteome reveals a new N-terminal binding motif for SHIP2.Quantification of phosphorylation of insulin receptor substrate-1 by HPLC-ESI-MS/MS.
P2860
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P2860
Tyrosine phosphoproteomics of fibroblast growth factor signaling: a role for insulin receptor substrate-4.
description
2004 nî lūn-bûn
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2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
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name
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@ast
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@en
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@nl
type
label
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@ast
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@en
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@nl
prefLabel
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@ast
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@en
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@nl
P2860
P356
P1476
Tyrosine phosphoproteomics of ...... insulin receptor substrate-4.
@en
P2093
Anders M Hinsby
Matthias Mann
P2860
P304
46438-46447
P356
10.1074/JBC.M404537200
P407
P577
2004-08-16T00:00:00Z