SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides.
about
Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniquesProtein Phosphorylation and Redox Modification in Stomatal Guard CellsRecent findings and technological advances in phosphoproteomics for cells and tissuesProteomics-based discovery of biomarkers for paediatric acute lymphoblastic leukaemia: challenges and opportunitiesEnrichment techniques employed in phosphoproteomicsMass spectrometry-based detection and assignment of protein posttranslational modificationsIntegrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapyLow-bias phosphopeptide enrichment from scarce samples using plastic antibodiesc-Jun N-terminal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cellsPlasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasionQuantitative proteomic analysis of histone modificationsPhosphoproteomics--more than meets the eye.The coming of age of phosphoproteomics--from large data sets to inference of protein functionsLarge-scale label-free phosphoproteomics: from technology to data interpretation.Enhanced detection and identification of multiply phosphorylated peptides using TiO2 enrichment in combination with MALDI TOF/TOF MS.Recent advances in capillary and microfluidic platforms with MS detection for the analysis of phosphoproteins.Optimization of immobilized gallium (III) ion affinity chromatography for selective binding and recovery of phosphopeptides from protein digests.Enrichment and analysis of phosphopeptides under different experimental conditions using titanium dioxide affinity chromatography and mass spectrometry.Global Cell Proteome Profiling, Phospho-signaling and Quantitative Proteomics for Identification of New Biomarkers in Acute Myeloid Leukemia PatientsStrategies for quantitation of phosphoproteomic data.In-depth analyses of kinase-dependent tyrosine phosphoproteomes based on metal ion-functionalized soluble nanopolymersLarge scale phosphoprotein profiling to explore Drosophila cold acclimation regulatory mechanisms.Nanodiamond-based two-step sampling of multiply and singly phosphorylated peptides for MALDI-TOF mass spectrometry analysis.Highly specific capture and direct MALDI-MS analysis of phosphorylated peptides using novel multifunctional chitosan-GMA-IDA-Fe (III) nanosphere.Bifunctional polymer brushes for low-bias enrichment of mono- and multi-phosphorylated peptides prior to mass spectrometry analysis.Preparation of proteins and peptides for mass spectrometry analysis in a bottom-up proteomics workflow.Phosphorylation site localization in peptides by MALDI MS/MS and the Mascot Delta Score.Plasma membrane proteomics and its application in clinical cancer biomarker discovery.Proteomics: challenges, techniques and possibilities to overcome biological sample complexityHighly efficient precipitation of phosphoproteins using trivalent europium, terbium, and erbium ions.Sequential enrichment with titania-coated magnetic mesoporous hollow silica microspheres and zirconium arsenate-modified magnetic nanoparticles for the study of phosphoproteome of HL60 cellsA novel strategy for phosphopeptide enrichment using lanthanide phosphate co-precipitation.Discontinuous pH gradient-mediated separation of TiO2-enriched phosphopeptides.Phosphoproteomics characterization of novel phosphorylated sites of lens proteins from normal and cataractous human eye lensesMapping of p140Cap phosphorylation sites: the EPLYA and EGLYA motifs have a key role in tyrosine phosphorylation and Csk binding, and are substrates of the Abl kinase.Robust phosphoproteome enrichment using monodisperse microsphere-based immobilized titanium (IV) ion affinity chromatography.Protein analysis by shotgun/bottom-up proteomicsAnalytical challenges translating mass spectrometry-based phosphoproteomics from discovery to clinical applications.Highly selective recovery of phosphopeptides using trypsin-assisted digestion of precipitated lanthanide-phosphoprotein complexes.Mass spectrometric analysis of mono- and multi-phosphopeptides by selective binding with NiZnFe₂O₄ magnetic nanoparticles.
P2860
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P2860
SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides.
description
2007 nî lūn-bûn
@nan
2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
name
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@ast
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@en
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@nl
type
label
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@ast
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@en
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@nl
prefLabel
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@ast
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@en
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@nl
P2860
P50
P1476
SIMAC (sequential elution from ...... tiply phosphorylated peptides.
@en
P2860
P304
P356
10.1074/MCP.M700362-MCP200
P577
2007-11-26T00:00:00Z