Proteome analysis using selective incorporation of isotopically labeled amino acids
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Amino acid residue specific stable isotope labeling for quantitative proteomicsMass spectrometry-based proteomics turns quantitativeBioinformatics meets proteomics--bridging the gap between mass spectrometry data analysis and cell biology.Stable isotope labelling in vivo as an aid to protein identification in peptide mass fingerprintingQuantitative proteomics by metabolic labeling of model organisms.Comparative proteomics based on stable isotope labeling and affinity selection.Viable Staphylococcus aureus quantitation using ¹⁵N metabolically labeled bacteriophage amplification coupled with a multiple reaction monitoring proteomic workflow.Proteomic profiling of pancreatic cancer for biomarker discovery.Metabolic labeling of proteins for proteomics.High-throughput proteomics using Fourier transform ion cyclotron resonance mass spectrometry.Mass spectrometry-based quantitative proteomics.Total kinetic analysis reveals how combinatorial methylation patterns are established on lysines 27 and 36 of histone H3A quantitative results-driven approach to analyzing multisite protein phosphorylation: the phosphate-dependent phosphorylation profile of the transcription factor Pho4.Issues and applications in label-free quantitative mass spectrometry.Analytical strategies for the global quantification of intact proteins.Quantitative proteomics using SILAC: Principles, applications, and developments.A timeline of stable isotopes and mass spectrometry in the life sciences.Top-Down Mass Spectrometry: Proteomics to Proteoforms.Using ion purity scores for enhancing quantitative accuracy and precision in complex proteomics samples.Comparison of stable-isotope labeling with amino acids in cell culture and spectral counting for relative quantification of protein expression.Quantitative top-down proteomics of SILAC labeled human embryonic stem cells.Measurement of acetylation turnover at distinct lysines in human histones identifies long-lived acetylation sites.Selective incorporation of isotopically labeled amino acids for identification of intact proteins on a proteome-wide level.In vivo labeling: a glimpse of the dynamic proteome and additional constraints for protein identification.Proteome analysis of intact proteins in complex mixtures.HysTag--a novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain.Top-down quantitation and characterization of SILAC-labeled proteins.A method for calculating 16O/18O peptide ion ratios for the relative quantification of proteomes.Controlled ion fragmentation in a 2-D quadrupole ion trap for external ion accumulation in ESI FTICR mass spectrometry.A dynamic ion cooling technique for FTICR mass spectrometry.Electrospray ionization-Fourier transform ion cyclotron mass spectrometry using ion preselection and external accumulation for ultrahigh sensitivity.
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P2860
Proteome analysis using selective incorporation of isotopically labeled amino acids
description
article
@en
im Januar 2000 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в січні 2000
@uk
name
Proteome analysis using selective incorporation of isotopically labeled amino acids
@en
Proteome analysis using selective incorporation of isotopically labeled amino acids
@nl
type
label
Proteome analysis using selective incorporation of isotopically labeled amino acids
@en
Proteome analysis using selective incorporation of isotopically labeled amino acids
@nl
prefLabel
Proteome analysis using selective incorporation of isotopically labeled amino acids
@en
Proteome analysis using selective incorporation of isotopically labeled amino acids
@nl
P2093
P2860
P1476
Proteome analysis using selective incorporation of isotopically labeled amino acids
@en
P2093
G A Anderson
L Pasa-Tolić
S Martinović
T D Veenstra
P2860
P356
10.1016/S1044-0305(99)00120-8
P577
2000-01-01T00:00:00Z
P6179
1003136388