ReviewTrends in biochemical sciences2015
Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease?
Review in Trends in biochemical sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
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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.
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Who cites it
49 citing papers in PubMed.
- Amyloid-beta fibrils as active contributors to synaptic dysfunction in Alzheimer's disease.Acta pharmacologica Sinica · 2026Article
- Current Understanding of Protein Aggregation in Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- Proteostasis and Its Role in Disease Development.Cell biochemistry and biophysics · 2025Review
- Impact of Sinapic Acid on Bovine Serum Albumin Thermal Stability.International journal of molecular sciences · 2024Article
- BFACS applied bio materials · 2023Article
- The Double-Layered Structure of Amyloid-β Assemblage on GM1-Containing Membranes Catalytically Promotes Fibrillization.ACS chemical neuroscience · 2023Article
- New Evidence on a Distinction between Aβ40 and Aβ42 Amyloids: Thioflavin T Binding Modes, Clustering Tendency, Degradation Resistance, and Cross-Seeding.International journal of molecular sciences · 2022Article
- Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies.Communications biology · 2021Article
- Noncanonical protein kinase A activation by oligomerization of regulatory subunits as revealed by inherited Carney complex mutations.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Defining the Neuropathological Aggresome acrossThe journal of physical chemistry. B · 2021Review
- AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils.Nature communications · 2021Article
- An Expanded Polyproline Domain Maintains Mutant Huntingtin SolubleFrontiers in molecular neuroscience · 2021Article
- Activate or Inhibit? Implications of Autophagy Modulation as a Therapeutic Strategy for Alzheimer's Disease.International journal of molecular sciences · 2020Review
- The protein-surfactant stoichiometry governs the conformational switching and amyloid nucleation kinetics of tau K18.European biophysics journal : EBJ · 2020Article
- Disruption of the CD Loop by Enzymatic Cleavage Promotes the Formation of Toxic Transthyretin Oligomers through a Common Transthyretin Misfolding Pathway.Biochemistry · 2020Article
- A KLVFFAE-Derived Peptide Probe for Detection of Alpha-Synuclein Fibrils.Applied biochemistry and biotechnology · 2020Article
- Structure and Aggregation Mechanisms in Amyloids.Molecules (Basel, Switzerland) · 2020Review
- Mitochondrial lipid droplet formation as a detoxification mechanism to sequester and degrade excessive urothelial membranes.Molecular biology of the cell · 2019Article
- The proteostasis network and its decline in ageing.Nature reviews. Molecular cell biology · 2019Review
- Transthyretin Aggregation Pathway toward the Formation of Distinct Cytotoxic Oligomers.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The formation of amyloid fibres is a hallmark of amyloid disorders. Nevertheless, the lack of correlation between fibre load and disease as observed, for example, in Alzheimer's disease, means that fibres are considered secondary contributors to the onset of cellular dysfunction. Instead, soluble intermediates of amyloid assembly are often described as the agents of toxicity. Here, we discuss recent experimental discoveries which suggest that amyloid fibres should be considered as disease-relevant species that can mediate a range of pathological processes. These include disruption of biological membranes, secondary nucleation, amyloid aggregate transmission, and the disruption of protein homeostasis (proteostasis). Thus, a greater understanding of amyloid fibre biology could enhance prospects of developing therapeutic interventions against this devastating class of protein-misfolding disorders.
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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.