ArticlePrion
Assessing the causes and consequences of co-polymerization in amyloid formation.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
29 citing papers in PubMed.
- Amyloid Cross-Interactions through the Lens of Simulations: The Case of Aβ-IAPP.The journal of physical chemistry. B · 2025Article
- Understanding the structural dynamics of human islet amyloid polypeptide: Advancements in and applications of ion-mobility mass spectrometry.Biophysical chemistry · 2024Review
- A Perspective on How Fibrinaloid Microclots and Platelet Pathology May be Applied in Clinical Investigations.Seminars in thrombosis and hemostasis · 2024Review
- Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids.eLife · 2022Article
- Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation.Chemical science · 2022Article
- Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Quantitative interrogation of protein co-aggregation using multi-color fluorogenic protein aggregation sensors.Chemical science · 2021Article
- Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.Nature structural & molecular biology · 2020Article
- Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson's Disease.Journal of Parkinson's disease · 2020Review
- Looking Beyond the Core: The Role of Flanking Regions in the Aggregation of Amyloidogenic Peptides and Proteins.Frontiers in neuroscience · 2020Review
- Molecular insights into the surface-catalyzed secondary nucleation of amyloid-βScience advances · 2019Article
- Molecular and Clinical Aspects of Protein Aggregation Assays in Neurodegenerative Diseases.Molecular neurobiology · 2018Review
- Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in aThe Journal of biological chemistry · 2018Article
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein.Journal of molecular biology · 2018Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Article
- Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils.PloS one · 2018Article
- Functional Amyloids and their Possible Influence on Alzheimer Disease.Discoveries (Craiova, Romania) · 2017Review
- Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Chemical science · 2017Article
Corrections and comments
- Comment on
Authors and funding
3 authors.
Funding
Abstract
How, and why, different proteins form amyloid fibrils is most often studied in vitro using a single purified protein sequence. However, many amyloid diseases involve co-aggregation of different protein species, including proteins with/without post-translational modifications (e.g., different strains of PrP), proteins of different length (e.g., β₂-microglobulin and ΔN6, Aβ40, and Aβ42), sequence variants (e.g., Aβ and Aβ(ARC)), and proteins from different organisms (e.g., bovine PrP and human PrP). The consequences of co-aggregation of different proteins upon the structure, stability, species transmission and toxicity of the resulting amyloid aggregates is discussed here, including the role of co-aggregation in expanding the repertoire of oligomeric and fibrillar structures and how this can affect their biological and biophysical properties.
Indexed as
Identifiers
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.