Structural Insight into an Alzheimer’s Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR
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Summary
Electron microscopy and immunological analyses using ASPD-specific “conformational” antibodies established synthetic ASPD for the 42-residue Aβ as an excellent structural/morphological analogue of native ASPD extracted from AD patients, the level of which correlates with the severity of AD.
- Type
- article
- Published
- 2015-05-04
- Cited by
- 56
- References
- 31
- Access
- Open access
- OpenAlex
- https://openalex.org/W219891006
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:16374051
Keywords
Chemistry, Amyloid (mycology), Solid-state nuclear magnetic resonance, Neurotoxin, Conformational isomerism
References
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- 13C–1H dipolar-driven 13C–13C recoupling without 13C rf irradiation in nuclear magnetic resonance of rotating solids
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- Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models
- Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate
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- Toxic fibrillar oligomers of amyloid-β have cross-β structure
- Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
- Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils
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- Resolution of Oligomeric Species during the Aggregation of Aβ1-40 Using 19F NMR
- Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomers.
- Formation Kinetics and Structural Features of Beta‐Amyloid Aggregates by Sedimented Solute NMR
- A specific amyloid-β protein assembly in the brain impairs memory
- Structural and Morphological Characterization of Aggregated Species of α-Synuclein Induced by Docosahexaenoic Acid
- The Alzheimer’s Amyloid-β(1–42) Peptide Forms Off-Pathway Oligomers and Fibrils that are Distinguished Structurally by Intermolecular Organization
Cited by
- Major Reaction Coordinates Linking Transient Amyloid-β Oligomers to Fibrils Measured at Atomic Level.
- Na, K-ATPase α3 is a death target of Alzheimer patient amyloid-β assembly
- Protein structural and surface water rearrangement constitute major events in the earliest aggregation stages of tau
- An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations
- L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment
- Phosphorylation modifies the molecular stability of β-amyloid deposits
- Evidence for Inhibition of Lysozyme Amyloid Fibrillization by Peptide Fragments from Human Lysozyme: A Combined Spectroscopy, Microscopy, and Docking Study.
- Successive stages of amyloid-β self-assembly characterized by solid state nuclear magnetic resonance with dynamic nuclear polarization
- Structural Polymorphism of Alzheimer’s β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study
- Molecular Structure of Aggregated Amyloid-β: Insights from Solid State Nuclear Magnetic Resonance
- Solid-State NMR Studies Reveal Native-like β-sheet Structures in Transthyretin amyloid
- Combined Solution- and Magic Angle Spinning NMR Reveals Regions of Distinct Dynamics in Amyloid β Protofibrils
- Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
- Nano-assembly of amyloid β peptide: role of the hairpin fold
- Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication
- Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity.
- Pathogenic Mutations Induce Partial Structural Changes in Native β-Sheet Structure of Transthyretin and Accelerate Aggregation
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions
- A long-lived Aβ oligomer resistant to fibrillization
- Depletion of amyloid‐β peptides from solution by sequestration within fibril‐seeded hydrogels
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