Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4.
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The Use of Advanced Mass Spectrometry to Dissect the Life-Cycle of Photosystem IIBiophysical analysis of apolipoprotein E3 variants linked with development of type III hyperlipoproteinemiaImproved identification and relative quantification of sites of peptide and protein oxidation for hydroxyl radical footprinting.Resolution of protein structure by mass spectrometry.Hydroxyl Radical Dosimetry for High Flux Hydroxyl Radical Protein Footprinting Applications Using a Simple Optical Detection Method.Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.Fast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstarQuantitative Protein Topography Measurements by High Resolution Hydroxyl Radical Protein Footprinting Enable Accurate Molecular Model SelectionHydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerizationStructural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease.Isotope-Encoded Carboxyl Group Footprinting for Mass Spectrometry-Based Protein Conformational StudiesThermodynamic and structural destabilization of apoE3 by hereditary mutations associated with the development of lipoprotein glomerulopathyAge, APOE and sex: Triad of risk of Alzheimer's disease.Incorporation of a Reporter Peptide in FPOP Compensates for Adventitious Scavengers and Permits Time-Dependent Measurements.Relative Quantification of Sites of Peptide and Protein Modification Using Size Exclusion Chromatography Coupled with Electron Transfer Dissociation.Modelling proteins' hidden conformations to predict antibiotic resistance.Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4.ApoE: the role of conserved residues in defining functionHelical structure, stability, and dynamics in human apolipoprotein E3 and E4 by hydrogen exchange and mass spectrometry.Ligand migration in the gaseous insulin-CB7 complex--a cautionary tale about the use of ECD-MS for ligand binding site determination.Orthogonal Mass Spectrometry-Based Footprinting for Epitope Mapping and Structural Characterization: The IL-6 Receptor upon Binding of Protein Therapeutics.Mass Spectrometry-Based Fast Photochemical Oxidation of Proteins (FPOP) for Higher Order Structure Characterization.Modifications generated by fast photochemical oxidation of proteins reflect the native conformations of proteins.
P2860
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P2860
Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4.
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Mass spectrometry-based protei ...... apolipoprotein E2, E3, and E4.
@ast
Mass spectrometry-based protei ...... apolipoprotein E2, E3, and E4.
@en
type
label
Mass spectrometry-based protei ...... apolipoprotein E2, E3, and E4.
@ast
Mass spectrometry-based protei ...... apolipoprotein E2, E3, and E4.
@en
prefLabel
Mass spectrometry-based protei ...... apolipoprotein E2, E3, and E4.
@ast
Mass spectrometry-based protei ...... apolipoprotein E2, E3, and E4.
@en
P2093
P2860
P356
P1433
P1476
Mass spectrometry-based protei ...... apolipoprotein E2, E3, and E4.
@en
P2093
Carl Frieden
Kanchan Garai
Michael L Gross
P2860
P304
P356
10.1021/BI200911C
P407
P577
2011-09-02T00:00:00Z