ArticleChemical science2018
Origin of metastable oligomers and their effects on amyloid fibril self-assembly.
Article in Chemical science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
50 citing papers in PubMed.
- Liquid-liquid phase-separated tau colocalizes with and stabilizes Aβ oligomers.Communications chemistry · 2026Article
- Shrinking of Extracellular Space During Metabolic Stress Accelerates Amyloid-β Aggregation.Biomolecules · 2026Article
- Self-Assembly of Amyloid Fibrils into Fibrillar Superstructure Monitored with Thioflavin T.Biomolecules · 2026Article
- Cosolute effects reveal the nature of weak forces governing GLP-1 oligomer stability.The Journal of biological chemistry · 2026Article
- The Basis of Anti-Aβ Antibody Therapy: The Toxicity of Aβ Aggregates and the Mechanism of Action of Anti-Aβ Antibodies.Internal medicine (Tokyo, Japan) · 2026Review
- A tunable affinity fusion tag for protein self-assembly.bioRxiv : the preprint server for biology · 2025Article
- A sticky situation - simple method for rapid poissonian encapsulation of highly aggregation-prone microbeads in polydisperse emulsions.Frontiers in bioengineering and biotechnology · 2025Article
- Detecting and Tracking β-Amyloid Oligomeric Forms and Dynamics In Vitro by a High-Sensitivity Fluorescent-Based Assay.ACS chemical neuroscience · 2024Article
- Characterizing Prion-Like Protein Aggregation: Emerging Nanopore-Based Approaches.Small methods · 2024Review
- Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide.Communications biology · 2024Article
- Crystal Violet Selectively Detects Aβ Oligomers but Not Fibrils In Vitro and in Alzheimer's Disease Brain Tissue.Biomolecules · 2024Article
- The thermodynamics of neurodegenerative disease.Biophysics reviews · 2024Review
- Conformation of Pyroglutamated Amyloid β (3-40) and (11-40) Fibrils - Extended or Hairpin?The journal of physical chemistry. B · 2024Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Glucagon-like peptide 1 aggregates into low-molecular-weight oligomers off-pathway to fibrillation.Biophysical journal · 2023Article
- Probing differences among Aβ oligomers with two triangular trimers derived from Aβ.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering.Nature communications · 2023Article
- Cascade autohydrolysis of Alzheimer's Aβ peptides.Chemical science · 2023Article
- Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils.Frontiers in molecular biosciences · 2023Review
- Effects of zinc and carnosine on aggregation kinetics of Amyloid-β40 peptide.Biochemistry and biophysics reports · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors.
Funding
Abstract
Assembly of rigid amyloid fibrils with their characteristic cross-β sheet structure is a molecular signature of numerous neurodegenerative and non-neuropathic disorders. Frequently large populations of small globular amyloid oligomers (gOs) and curvilinear fibrils (CFs) precede the formation of late-stage rigid fibrils (RFs), and have been implicated in amyloid toxicity. Yet our understanding of the origin of these metastable oligomers, their role as on-pathway precursors or off-pathway competitors, and their effects on the self-assembly of amyloid fibrils remains incomplete. Using two unrelated amyloid proteins, amyloid-β and lysozyme, we find that gO/CF formation, analogous to micelle formation by surfactants, is delineated by a "critical oligomer concentration" (COC). Below this COC, fibril assembly replicates the sigmoidal kinetics of nucleated polymerization. Upon crossing the COC, assembly kinetics becomes biphasic with gO/CF formation responsible for the lag-free initial phase, followed by a second upswing dominated by RF nucleation and growth. RF lag periods below the COC, as expected, decrease as a power law in monomer concentration. Surprisingly, the build-up of gO/CFs above the COC causes a progressive increase in RF lag periods. Our results suggest that metastable gO/CFs are off-pathway from RF formation, confined by a condition-dependent COC that is distinct from RF solubility, underlie a transition from sigmoidal to biphasic assembly kinetics and, most importantly, not only compete with RFs for the shared monomeric growth substrate but actively inhibit their nucleation and growth.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.