ArticleCommunications biology2019
Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid.
Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Clinically relevant stereochemistry reprograms amyloid proteome for aggregation cross-talk-conferred neuroprotection.Science advances · 2026Article
- Allosteric Modulation of Pathological Ataxin-3 Aggregation: A Path to Spinocerebellar Ataxia Type-3 Therapies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Discovery of NIRF theranostic probes targeting amyloid-β and cholinesterases in Alzheimer's disease models.Nature communications · 2026Article
- Chemically Fueled, Active Droplets Prevent the Aging of Peptides into Amyloid-Like Fibers.Journal of the American Chemical Society · 2025Article
- Molecular architectures of glycosylated dendronized bottle brushes in action: Biocompatibility and anti-amyloidogenic activity of pseudo-glycodendrimers.Materials today. Bio · 2025Article
- Potential Mechanisms of Tunneling Nanotube Formation and Their Role in Pathology Spread in Alzheimer's Disease and Other Proteinopathies.International journal of molecular sciences · 2024Review
- α-Synuclein oligomers form by secondary nucleation.Nature communications · 2024Article
- Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces.ACS chemical neuroscience · 2024Article
- The thermodynamics of neurodegenerative disease.Biophysics reviews · 2024Review
- Molecular Mechanisms of Amyloid-β Self-Assembly Seeded by In Vivo-Derived Fibrils and Inhibitory Effects of the BRICHOS Chaperone.ACS chemical neuroscience · 2023Article
- The Major Components of Cerebrospinal Fluid Dictate the Characteristics of Inhibitors against Amyloid-Beta Aggregation.International journal of molecular sciences · 2023Article
- Simple, Reliable Protocol for High-Yield Solubilization of Seedless Amyloid-β Monomer.ACS chemical neuroscience · 2023Article
- Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary Nucleation.ACS chemical neuroscience · 2022Article
- Uncovering the universality of self-replication in protein aggregation and its link to disease.Science advances · 2022Article
- Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids.eLife · 2022Article
- Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation.Chemical science · 2022Article
- Influence of denaturants on amyloid β42 aggregation kinetics.Frontiers in neuroscience · 2022Article
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
- Mechanistic Models of Protein Aggregation Across Length-Scales and Time-Scales: From the Test Tube to Neurodegenerative Disease.Frontiers in neuroscience · 2022Review
- Autoxidation Enhances Anti-Amyloid Potential of Flavone Derivatives.Antioxidants (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alzheimer's disease is linked to amyloid β (Aβ) peptide aggregation in the brain, and a detailed understanding of the molecular mechanism of Aβ aggregation may lead to improved diagnostics and therapeutics. While previous studies have been performed in pure buffer, we approach the mechanism in vivo using cerebrospinal fluid (CSF). We investigated the aggregation mechanism of Aβ42 in human CSF through kinetic experiments at several Aβ42 monomer concentrations (0.8-10 µM). The data were subjected to global kinetic analysis and found consistent with an aggregation mechanism involving secondary nucleation of monomers on the fibril surface. A mechanism only including primary nucleation was ruled out. We find that the aggregation process is composed of the same microscopic steps in CSF as in pure buffer, but the rate constant of secondary nucleation is decreased. Most importantly, the autocatalytic amplification of aggregate number through catalysis on the fibril surface is prevalent also in CSF.
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