Pages that link to "Q54325610"

The following pages link to Conformer-specific hydrogen exchange analysis of Aβ(1-42) oligomers by top-down electron capture dissociation mass spectrometry. (Q54325610):

Displaying 26 items.

• Structural Basis of β‐Amyloid‐Dependent Synaptic Dysfunctions (Q30318220) (← links)
• Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers (Q30365652) (← links)
• Diethylpyrocarbonate Labeling for the Structural Analysis of Proteins: Label Scrambling in Solution and How to Avoid It (Q30413314) (← links)
• Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis (Q30427725) (← links)
• Enhancing the quality of H/D exchange measurements with mass spectrometry detection in disulfide-rich proteins using electron capture dissociation (Q33732576) (← links)
• Approach to characterization of the higher order structure of disulfide-containing proteins using hydrogen/deuterium exchange and top-down mass spectrometry (Q34089233) (← links)
• Mass spectrometry: come of age for structural and dynamical biology. (Q35347233) (← links)
• Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization (Q35456689) (← links)
• Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes (Q35696876) (← links)
• Pulsed hydrogen-deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation (Q37157432) (← links)
• Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis (Q37236489) (← links)
• A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation (Q37240962) (← links)
• Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry. (Q37395119) (← links)
• Kinetic intermediates of amyloid fibrillation studied by hydrogen exchange methods with nuclear magnetic resonance (Q38033934) (← links)
• Higher order structure characterization of protein therapeutics by hydrogen/deuterium exchange mass spectrometry. (Q38221786) (← links)
• Beta Amyloid Hallmarks: From Intrinsically Disordered Proteins to Alzheimer's Disease (Q38589816) (← links)
• Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment (Q42392279) (← links)
• A folding transition underlies the emergence of membrane affinity in amyloid-β. (Q44009111) (← links)
• Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR. (Q44590637) (← links)
• Lysine residues in the N-terminal huntingtin amphipathic α-helix play a key role in peptide aggregation (Q45008320) (← links)
• Understanding Curli Amyloid-Protein Aggregation by Hydrogen-Deuterium Exchange and Mass Spectrometry (Q46278075) (← links)
• Amyloid-β dimers in the absence of plaque pathology impair learning and synaptic plasticity. (Q46625235) (← links)
• Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation (Q51838104) (← links)
• Biosensors for the Determination of Amyloid-Beta Peptides and their Aggregates with Application to Alzheimer's Disease (Q58129350) (← links)
• Structural Interrogation of Electrosprayed Peptide Ions by Gas-Phase H/D Exchange and Electron Capture Dissociation Mass Spectrometry (Q82741274) (← links)
• Tracking Higher Order Protein Structure by Hydrogen-Deuterium Exchange Mass Spectrometry (Q90446257) (← links)