ArticleBiophysical journal2008
Protofibril assemblies of the arctic, Dutch, and Flemish mutants of the Alzheimer's Abeta1-40 peptide.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Key considerations for ELISA-based quantification of diverse amyloid beta forms in murine brain homogenates.Frontiers in neuroscience · 2025Article
- Rosemarinic Acid-Induced Destabilization of Aβ Peptides: Insights from Molecular Dynamics Simulations.Foods (Basel, Switzerland) · 2024Article
- Differential effects of familial Alzheimer's disease-causing mutations on amyloid precursor protein (APP) trafficking, proteolytic conversion, and synaptogenic activity.Acta neuropathologica communications · 2023Article
- Moving the Needle on Alzheimer's Disease with an Anti-Oligomer Antibody.The New England journal of medicine · 2023Article
- Interaction of amyloid beta with humanin and acetylcholinesterase is modulated by ATP.FEBS open bio · 2020Article
- Humanin Blocks the Aggregation of Amyloid-β Induced by Acetylcholinesterase, an Effect Abolished in the Presence of IGFBP-3.Biochemistry · 2020Article
- Novel Phosphorylation-State Specific Antibodies Reveal Differential Deposition of Ser26 Phosphorylated Aβ Species in a Mouse Model of Alzheimer's Disease.Frontiers in molecular neuroscience · 2020Article
- Thermodynamics of Amyloid-β Fibril Elongation: Atomistic Details of the Transition State.ACS chemical neuroscience · 2018Article
- Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.International journal of molecular sciences · 2018Review
- Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline.Biochemical and biophysical research communications · 2017Article
- Familial Alzheimer's Disease Mutations within the Amyloid Precursor Protein Alter the Aggregation and Conformation of the Amyloid-β Peptide.The Journal of biological chemistry · 2017Article
- Phosphorylation of the amyloid β-peptide at Ser26 stabilizes oligomeric assembly and increases neurotoxicity.Acta neuropathologica · 2016Article
- Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Biophysical journal · 2015Article
- Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations.PloS one · 2014Article
- Effect of alanine replacement of l17 and f19 on the aggregation and neurotoxicity of arctic-type aβ40.PloS one · 2013Article
- Side-chain hydrophobicity and the stability of Aβ₁₆₋₂₂ aggregates.Protein science : a publication of the Protein Society · 2012Article
- Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFM.Journal of structural biology · 2012Article
- Controlling the aggregation and rate of release in order to improve insulin formulation: molecular dynamics study of full-length insulin amyloid oligomer models.Journal of molecular modeling · 2012Article
- Structure and dynamics of amyloid-β segmental polymorphisms.PloS one · 2012Article
- Structural dynamics of the ΔE22 (Osaka) familial Alzheimer's disease-linked amyloid β-protein.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2011Article
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Abstract
Using a coarse-grained model of the Abeta peptide, we analyze the Arctic (E22G), Dutch (E22Q), and Flemish (A21G) familial Alzheimer's disease (FAD) mutants for any changes in the stability of amyloid assemblies with respect to the wild-type (WT) sequence. Based on a structural reference state of two protofilaments aligned to create the "agitated" protofibril as determined by solid-state NMR, we determine free energy trends for Abeta assemblies for the WT and FAD familial sequences. We find that the structural characteristics and oligomer size of the critical nucleus vary dramatically among the hereditary mutants. The Arctic mutant's disorder in the turn region introduces new stabilizing interactions that better align the two protofilaments, yielding a well-defined protofibril axis at relatively small oligomer sizes with respect to WT. By contrast, the critical nucleus for the Flemish mutant is beyond the 20 chains characterized in this study, thereby showing a strong shift in the equilibrium toward monomers with respect to larger protofibril assemblies. The Dutch mutant forms more ordered protofilaments than WT, but exhibits greater disorder in protofibril structure that includes an alternative polymorph of the WT fibril. An important conclusion of this work is that the Dutch mutant does not support the agitated protofibril assembly. We discuss the implications of the structural ensembles and free energy profiles for the FAD mutants in regards to interpretation of the kinetics of fibril assembly using chromatography and dye-binding experiments.
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