ReviewComputational and structural biotechnology journal2021
Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches.
Review in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- DNA Origami and Their Application in Biosensors.Biosensors · 2026Review
- Covalent ferrocene conjugation as an intramolecular strategy for photostability in fluorescein.Scientific reports · 2026Article
- The Catalyzing Effect of Aggregates on the Fibrillation Pathway of Human Insulin: A Spectroscopic Investigation During the Lag Phase.International journal of molecular sciences · 2025Article
- Recent Advances in Amyloids Structural Studies and Thin Film Applications.Molecules (Basel, Switzerland) · 2025Review
- Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins.The Biochemical journal · 2025Article
- Advancements in Single-Molecule Fluorescence Detection Techniques and Their Expansive Applications in Drug Discovery and Neuroscience.Biosensors · 2025Review
- Fluorescent probes in autoimmune disease research: current status and future prospects.Journal of translational medicine · 2025Review
- FLIM-Phasor Analysis (FLIM-ϕ) of Aβ-Induced Membrane Order Alterations: Towards a Cell-Based Biosensor for Early Alzheimer's Disease Diagnosis.Micromachines · 2025Article
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- Comparative Study of the Solid-Liquid Interfacial Adsorption of Proteins in Their Native and Amyloid Forms.International journal of molecular sciences · 2022Article
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aggregation of proteins into insoluble filamentous amyloid fibrils is a pathological hallmark of neurodegenerative diseases that include Parkinson's disease and Alzheimer's disease. Since the identification of amyloid fibrils and their association with disease, there has been much work to describe the process by which fibrils form and interact with other proteins. However, due to the dynamic nature of fibril formation and the transient and heterogeneous nature of the intermediates produced, it can be challenging to examine these processes using techniques that rely on traditional ensemble-based measurements. Single-molecule approaches overcome these limitations as rare and short-lived species within a population can be individually studied. Fluorescence-based single-molecule methods have proven to be particularly useful for the study of amyloid fibril formation. In this review, we discuss the use of different experimental single-molecule fluorescence microscopy approaches to study amyloid fibrils and their interaction with other proteins, in particular molecular chaperones. We highlight the mechanistic insights these single-molecule techniques have already provided in our understanding of how fibrils form, and comment on their potential future use in studying amyloid fibrils and their intermediates.
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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.