FT-ICR MS optimization for the analysis of intact proteins
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High resolution time-of-flight mass analysis of the entire range of intact singly-charged proteins.Metalloproteomics as an interdisciplinary area involving proteins and metals.Pressurized pepsin digestion in proteomics: an automatable alternative to trypsin for integrated top-down bottom-up proteomics.Integrated workflow for characterizing intact phosphoproteins from complex mixtures.Transformative effects of higher magnetic field in Fourier transform ion cyclotron resonance mass spectrometryCurrent use of high-resolution mass spectrometry in drug screening relevant to clinical and forensic toxicology and doping control.Mass spectrometry-based proteomics: existing capabilities and future directionsCharacterization and quantification of intact 26S proteasome proteins by real-time measurement of intrinsic fluorescence prior to top-down mass spectrometry.Unit mass baseline resolution for an intact 148 kDa therapeutic monoclonal antibody by Fourier transform ion cyclotron resonance mass spectrometryNano-LC FTICR tandem mass spectrometry for top-down proteomics: routine baseline unit mass resolution of whole cell lysate proteins up to 72 kDaProgress in Top-Down Proteomics and the Analysis of Proteoforms.Mass spectrometry based tools to investigate protein-ligand interactions for drug discovery.The proteomic future: where mass spectrometry should be taking us.Towards analytically useful two-dimensional Fourier transform ion cyclotron resonance mass spectrometry.Binding of an organo-osmium(II) anticancer complex to guanine and cytosine on DNA revealed by electron-based dissociations in high resolution Top-Down FT-ICR mass spectrometry.A novel 9.4 tesla FTICR mass spectrometer with improved sensitivity, mass resolution, and mass range.An improved measurement of isotopic ratios by high resolution mass spectrometry.Foodomics and Food Safety: Where We Are.An integrated top-down and bottom-up proteomic approach to characterize the antigen-binding fragment of antibodies.21 Tesla Fourier Transform Ion Cyclotron Resonance Mass Spectrometer Greatly Expands Mass Spectrometry Toolbox.IR action spectroscopy shows competitive oxazolone and diketopiperazine formation in peptides depends on peptide length and identity of terminal residue in the departing fragment.Quantitative analysis of long chain fatty acids present in a Type I kerogen using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry: compared with BF₃/MeOH methylation/GC-FID.Trapping Radial Electric Field Optimization in Compensated FTICR Cells
P2860
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P2860
FT-ICR MS optimization for the analysis of intact proteins
description
2009 nî lūn-bûn
@nan
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
FT-ICR MS optimization for the analysis of intact proteins
@ast
FT-ICR MS optimization for the analysis of intact proteins
@en
FT-ICR MS optimization for the analysis of intact proteins
@nl
type
label
FT-ICR MS optimization for the analysis of intact proteins
@ast
FT-ICR MS optimization for the analysis of intact proteins
@en
FT-ICR MS optimization for the analysis of intact proteins
@nl
prefLabel
FT-ICR MS optimization for the analysis of intact proteins
@ast
FT-ICR MS optimization for the analysis of intact proteins
@en
FT-ICR MS optimization for the analysis of intact proteins
@nl
P2093
P2860
P1476
FT-ICR MS optimization for the analysis of intact proteins
@en
P2093
Aleksey V Tolmachev
Errol W Robinson
Ljiljana Paša-Tolić
P2860
P356
10.1016/J.IJMS.2008.10.010
P407
P577
2009-10-15T00:00:00Z