Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization - Wikidata - wikimedia - TriplyDB

Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization

Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization

http://www.wikidata.org/entity/Q35456689

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Mass spectrometry-based methods to study protein architecture and dynamics Epitope characterization of an anti-PD-L1 antibody using orthogonal approaches Analytical Aspects of Hydrogen Exchange Mass Spectrometry Biophysical analysis of apolipoprotein E3 variants linked with development of type III hyperlipoproteinemia Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis.A novel mechanism for regulating the activity of proliferating cell nuclear antigen by a small protein Swapping the N- and C-terminal domains of human apolipoprotein E3 and AI reveals insights into their structure/activity relationship ApoE: In Vitro Studies of a Small Molecule Effector.Emerging mass spectrometry-based approaches to probe protein-receptor interactions: focus on overcoming physiological barriers ApoE4-specific Misfolded Intermediate Identified by Molecular Dynamics Simulations.Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease.Thermodynamic and structural destabilization of apoE3 by hereditary mutations associated with the development of lipoprotein glomerulopathy Age, APOE and sex: Triad of risk of Alzheimer's disease.Pulsed hydrogen-deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation.Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis.A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation The impact of mass spectrometry on the study of intact antibodies: from post-translational modifications to structural analysis.Higher order structure characterization of protein therapeutics by hydrogen/deuterium exchange mass spectrometry.Analysis of phosphoinositide 3-kinase inhibitors by bottom-up electron-transfer dissociation hydrogen/deuterium exchange mass spectrometry.Regio-Selective Intramolecular Hydrogen/Deuterium Exchange in Gas-Phase Electron Transfer Dissociation.Determination of Equine Cytochrome c Backbone Amide Hydrogen/Deuterium Exchange Rates by Mass Spectrometry Using a Wider Time Window and Isotope Envelope.Concerning the structure of apoE Functional dynamics of hexameric helicase probed by hydrogen exchange and simulation.Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4.ApoE: the role of conserved residues in defining function Helical structure, stability, and dynamics in human apolipoprotein E3 and E4 by hydrogen exchange and mass spectrometry.Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment.Lysine residues in the N-terminal huntingtin amphipathic α-helix play a key role in peptide aggregation.The Role of Electron Transfer Dissociation in Modern Proteomics.Atomistic Insights into Structural Differences between E3 and E4 Isoforms of Apolipoprotein E.Peptide-Level Interactions between Proteins and Small-Molecule Drug Candidates by Two Hydrogen-Deuterium Exchange MS-Based Methods: The Example of Apolipoprotein E3.Hydrogen/deuterium exchange mass spectrometry and computational modeling reveal a discontinuous epitope of an antibody/TL1A Interaction.Lipidated apolipoprotein E4 structure and its receptor binding mechanism determined by a combined cross-linking coupled to mass spectrometry and molecular dynamics approach

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Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization

http://www.wikidata.org/entity/Q35456689

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2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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Hydrogen/deuterium exchange an ...... olipoprotein E oligomerization

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Carl Frieden

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Kanchan Garai

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Michael L Gross

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P2860

Behavior of human apolipoprotein E in aqueous solutions and at interfaces

Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

Interaction of the N-terminal domain of apolipoprotein E4 with heparin

Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E

Topology of human apolipoprotein E3 uniquely regulates its diverse biological functions

Apolipoprotein E: far more than a lipid transport protein

Intramolecular migration of amide hydrogens in protonated peptides upon collisional activation

Collisional activation by MALDI tandem time-of-flight mass spectrometry induces intramolecular migration of amide hydrogens in protonated peptides

Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution

Factors affecting gas-phase deuterium scrambling in peptide ions and their implications for protein structure determination.

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43

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50

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Richard Y-C Huang

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