ReviewBiophysical chemistry2021
Visualizing and trapping transient oligomers in amyloid assembly pathways.
Review in Biophysical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
48 citing papers in PubMed.
- Targeting soluble misfolded oligomers in anti-amyloid research.Nature reviews. Chemistry · 2026Review
- Mass Spectrometric Characterization of Native Insulin Hexamers and Non-Native Heptamers: Formation and Stability Across Insulin Analogs.Journal of mass spectrometry : JMS · 2026Article
- Transient Interactions of α-Synuclein N- and C-Termini.ACS chemical neuroscience · 2026Article
- Multiscale simulations of folded and intrinsically disordered region-containing protein condensates.Biophysical journal · 2026Article
- A genetically encoded selection for amyloid-β oligomer binders.Nature chemical biology · 2025Article
- The role of hydrophobic collapse in cytotoxic and functional amyloid oligomerization.Biophysical journal · 2025Article
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- Rapid discovery of cyclic peptide protein aggregation inhibitors by continuous selection.Nature chemical biology · 2025Article
- Biophysical and spectroscopical insights into structural modulation of species in the aggregation pathway of superoxide dismutase 1.Communications chemistry · 2025Article
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- Characterizing Prion-Like Protein Aggregation: Emerging Nanopore-Based Approaches.Small methods · 2024Review
- Unraveling the Structure and Dynamics of Ac-PHF6-NHACS chemical neuroscience · 2024Article
- MAPT mutations associated with familial tauopathies lead to formation of conformationally distinct oligomers that have cross-seeding ability.Protein science : a publication of the Protein Society · 2024Article
- Understanding the mechanisms of green tea EGCG against amyloid β oligomer neurotoxicity through computational studies.RSC advances · 2024Article
- Fibrinaloid Microclots and Atrial Fibrillation.Biomedicines · 2024Review
- PACT - Prediction of amyloid cross-interaction by threading.Scientific reports · 2023Article
- Advances in mass spectrometry to unravel the structure and function of protein condensates.Nature protocols · 2023Review
- Interfacial Dynamics and Growth Modes of βJournal of chemical information and modeling · 2023Article
- Decoding the Roles of Amyloid-β (1-42)'s Key Oligomerization Domains toward Designing Epitope-Specific Aggregation Inhibitors.JACS Au · 2023Article
- Alleviating the unwanted effects of oxidative stress on Aβ clearance: a review of related concepts and strategies for the development of computational modelling.Translational neurodegeneration · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Oligomers which form during amyloid fibril assembly are considered to be key contributors towards amyloid disease. However, understanding how such intermediates form, their structure, and mechanisms of toxicity presents significant challenges due to their transient and heterogeneous nature. Here, we discuss two different strategies for addressing these challenges: use of (1) methods capable of detecting lowly-populated species within complex mixtures, such as NMR, single particle methods (including fluorescence and force spectroscopy), and mass spectrometry; and (2) chemical and biological tools to bias the amyloid energy landscape towards specific oligomeric states. While the former methods are well suited to following the kinetics of amyloid assembly and obtaining low-resolution structural information, the latter are capable of producing oligomer samples for high-resolution structural studies and inferring structure-toxicity relationships. Together, these different approaches should enable a clearer picture to be gained of the nature and role of oligomeric intermediates in amyloid formation and disease.
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What OpenQuestion holds
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.