ReviewBiochimica et biophysica acta. Proteins and proteomics2019
Imaging individual protein aggregates to follow aggregation and determine the role of aggregates in neurodegenerative disease.
Review in Biochimica et biophysica acta. Proteins and proteomics, 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.
- Molecular Determinants of Protein Pathogenicity at the Single-Aggregate Level.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Oxidative stress induced protein aggregation via GGCT produced pyroglutamic acid in drug resistant glioblastoma.iScience · 2025Article
- Fibrinaloid Microclots and Atrial Fibrillation.Biomedicines · 2024Review
- Developments in Trapped Ion Mobility Mass Spectrometry to Probe the Early Stages of Peptide Aggregation.Journal of the American Society for Mass Spectrometry · 2023Article
- Implementing Complementary Approaches to Shape the Mechanism of α-Synuclein Oligomerization as a Model of Amyloid Aggregation.Molecules (Basel, Switzerland) · 2021Review
- The Diagnostic Potential of Amyloidogenic Proteins.International journal of molecular sciences · 2021Review
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Simultaneous structural and elemental nano-imaging of human brain tissue.Chemical science · 2020Article
- Article
- Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progression.Acta neuropathologica communications · 2019Article
- Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms.Nature communications · 2019Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein aggregates play a key role in the initiation and spreading of neurodegenerative disease but have been difficult to study due to their low abundance and heterogeneity, in both size and structure. Fluorescence based methods capable of detecting and characterising single aggregates have recently been developed and can be used to measure many important aggregate properties, and can be combined with sensitive assays to measure aggregate toxicity. Here we review these methods and discuss recent examples of their application to determine the molecular mechanism of aggregation and the detection of aggregates in cells and cerebrospinal fluid. The further development of these methods and their application to the aggregates present in humans has the potential to solve a major problem in the field and allow the identification of the key toxic species that should be targeted in therapies.
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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.