Conformational changes in amyloid-beta (12–28) alloforms studied using action-FRET, IMS and molecular dynamics simulations
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Title
Conformational changes in amyloid-beta (12–28) alloforms studied using action-FRET, IMS and molecular dynamics simulations
Authors
Keywords
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Journal
Chemical Science
Volume 6, Issue 8, Pages 5040-5047
Publisher
Royal Society of Chemistry (RSC)
Online
2015-06-18
DOI
10.1039/c5sc01463h
References
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Note: Only part of the references are listed.- Action-FRET: Probing the Molecular Conformation of Mass-Selected Gas-Phase Peptides with Förster Resonance Energy Transfer Detected by Acceptor-Specific Fragmentation
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- Effects of Familial Mutations on the Monomer Structure of Aβ42
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- Formation of Two Different Types of Oligomers in the Early Phase of pH-Induced Aggregation of the Alzheimer Aβ(12-28) Peptide
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- Effects of Different Force Fields and Temperatures on the Structural Character of Abeta (12–28) Peptide in Aqueous Solution
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- Fluorescence Resonance Energy Transfer in Gaseous, Mass-Selected Polyproline Peptides
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- Ion mobility–mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation
- (2010) Christian Bleiholder et al. Nature Chemistry
- Influence of Residue 22 on the Folding, Aggregation Profile, and Toxicity of the Alzheimer's Amyloid β Peptide
- (2009) Alex Perálvarez-Marín et al. BIOPHYSICAL JOURNAL
- Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization
- (2009) Megan M. Murray et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
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- GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
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- Effects of the Arctic (E22→G) Mutation on Amyloid β-Protein Folding: Discrete Molecular Dynamics Study
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