ArticlePloS one2010
Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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
26 citing papers in PubMed.
- Direct Observation of Secondary Nucleation in Huntingtin Amyloid Formation by High-Speed Atomic Force Microscopy.Journal of the American Chemical Society · 2025Article
- Morphometric and Nanomechanical Screening of Peripheral Blood Cells with Atomic Force Microscopy for Label-Free Assessment of Alzheimer's Disease, Parkinson's Disease, and Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2023Review
- Reg-1α, a New Substrate of Calpain-2 Depending on Its Glycosylation Status.International journal of molecular sciences · 2022Article
- Spatial organization of protein aggregates on red blood cells as physical biomarkers of Alzheimer's disease pathology.Science advances · 2021Article
- Elongation rate and average length of amyloid fibrils in solution using isotope-labelled small-angle neutron scattering.RSC chemical biology · 2021Article
- Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics.Biomacromolecules · 2020Article
- Caught in the Act: Mechanistic Insight into Supramolecular Polymerization-Driven Self-Replication from Real-Time Visualization.Journal of the American Chemical Society · 2020Article
- High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-β and Amylin Aggregation Pathways.International journal of molecular sciences · 2020Review
- Atomic Force Microscopy Visualizes Mobility of Photosynthetic Proteins in Grana Thylakoid Membranes.Biophysical journal · 2020Article
- Reg-1α Promotes Differentiation of Cortical Progenitors via Its N-Terminal Active Domain.Frontiers in cell and developmental biology · 2020Article
- Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide.Nano letters · 2019Article
- A cationic polymethacrylate-copolymer acts as an agonist for β-amyloid and an antagonist for amylin fibrillation.Chemical science · 2019Article
- Atomic force microscopy for single molecule characterisation of protein aggregation.Archives of biochemistry and biophysics · 2019Review
- Sequence-dependent catalytic regulation of the SpoIIIE motor activity ensures directionality of DNA translocation.Scientific reports · 2018Article
- Directly watching biomolecules in action by high-speed atomic force microscopy.Biophysical reviews · 2017Review
- Harnessing the damping properties of materials for high-speed atomic force microscopy.Nature nanotechnology · 2016Article
- Article
- Ultrafast propagation of β-amyloid fibrils in oligomeric cloud.Scientific reports · 2014Article
- Filming biomolecular processes by high-speed atomic force microscopy.Chemical reviews · 2014Review
- Structure and DNA-binding properties of the Bacillus subtilis SpoIIIE DNA translocase revealed by single-molecule and electron microscopies.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of fibrillar structures of proteins that deposit into aggregates has been suggested to play a key role in various neurodegenerative diseases. However mechanisms and dynamics of fibrillization remains to be elucidated. We have previously established that lithostathine, a protein overexpressed in the pre-clinical stages of Alzheimer's disease and present in the pathognomonic lesions associated with this disease, form fibrillar aggregates after its N-terminal truncation. In this paper we visualized, using high-speed atomic force microscopy (HS-AFM), growth and assembly of lithostathine protofibrils under physiological conditions with a time resolution of one image/s. Real-time imaging highlighted a very high velocity of elongation. Formation of fibrils via protofibril lateral association and stacking was also monitored revealing a zipper-like mechanism of association. We also demonstrate that, like other amyloid ß peptides, two lithostathine protofibrils can associate to form helical fibrils. Another striking finding is the propensity of the end of a growing protofibril or fibril to associate with the edge of a second fibril, forming false branching point. Taken together this study provides new clues about fibrillization mechanism of amyloid proteins.
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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.