ArticleChemical science2019
Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
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.
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Who cites it
12 citing papers in PubMed.
- Zooming into Disease at the Nanoscale: High-Speed Atomic Force Microscopy in Biomedical Discovery.ACS nano · 2026Review
- Article
- Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics.ACS nano · 2023Article
- Controllable membrane damage by tunable peptide aggregation with albumin.AIChE journal. American Institute of Chemical Engineers · 2022Article
- Hampering the early aggregation of PrP-E200K protein by charge-based inhibitors: a computational study.Journal of computer-aided molecular design · 2021Article
- Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Identification of on- and off-pathway oligomers in amyloid fibril formation.Chemical science · 2020Article
- Kinetic diversity of amyloid oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Real-Time BODIPY-Binding Assay To Screen Inhibitors of the Early Oligomerization Process of Aβ1-42 Peptide.Chembiochem : a European journal of chemical biology · 2020Article
- Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019Review
- Cytoskeleton-dependent clustering of membrane-bound prion protein on the cell surface.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The aggregation of the prion protein (PrP) plays a key role in the development of prion diseases. In the past decade, a similar process has been associated with other proteins, such as Aβ, tau, and α-synuclein, which participate in other neurodegenerative diseases. It is increasingly recognized that the small oligomeric species of aggregates can play an important role in the development of prion diseases. However, determining the nature of the oligomers formed during the aggregation process has been experimentally difficult due to the lack of suitable methods capable of the detection and characterization of the low level of oligomers that may form. To address this problem, we have utilized single-aggregate methods to study the early events associated with aggregation of recombinant murine PrP
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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.