ReviewBrain pathology (Zurich, Switzerland)2013
From soluble aβ to progressive aβ aggregation: could prion-like templated misfolding play a role?
Review in Brain pathology (Zurich, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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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
22 citing papers in PubMed, 37 citations in OpenAlex.
- Amyloid-β, Tau Protein, α-Synuclein, TDP-43, and FUS in Mixed Pathology: And Intrinsic Disorder to Rule Them All.International journal of molecular sciences · 2026Review
- Longitudinal MRI Characterization of TNMR in biomedicine · 2026Article
- The amino acid substitutions A30W, K28A, and M35C alter amyloid-β peptide toxicity in cell culture and in anFrontiers in aging neuroscience · 2026Article
- Microglia and Astrocytes in Alzheimer's Disease: Significance and Summary of Recent Advances.Aging and disease · 2024Review
- Isotope-labeled amyloid-β does not transmit to the brain in a prion-like manner after peripheral administration.EMBO reports · 2022Article
- Resolution exchange with tunneling for enhanced sampling of protein landscapes.Physical review. E · 2022Article
- The effect of Aβ seeding is dependent on the presence of knock-in genes in theFrontiers in dementia · 2022Article
- Genetic Dissection of Alzheimer's Disease UsingInternational journal of molecular sciences · 2020Review
- Brain-Gut-Microbiota Axis in Alzheimer's Disease.Journal of neurogastroenterology and motility · 2019Review
- Amyloid fibril polymorphism: a challenge for molecular imaging and therapy.Journal of internal medicine · 2018Review
- Expression and function of Abcg4 in the mouse blood-brain barrier: role in restricting the brain entry of amyloid-β peptide.Scientific reports · 2017Article
- Seed-induced acceleration of amyloid-β mediated neurotoxicity in vivo.Nature communications · 2017Article
- Protein/Peptide Aggregation and Amyloidosis on Biointerfaces.Materials (Basel, Switzerland) · 2016Review
- In Vivo Detection of Amyloid Plaques by Gadolinium-Stained MRI Can Be Used to Demonstrate the Efficacy of an Anti-amyloid Immunotherapy.Frontiers in aging neuroscience · 2016Article
- Targeting protein aggregation for the treatment of degenerative diseases.Nature reviews. Drug discovery · 2015Review
- Article
- pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.PloS one · 2015Article
- Effects of several quinones on insulin aggregation.Scientific reports · 2014Article
- Tau acts as a mediator for Alzheimer's disease-related synaptic deficits.The European journal of neuroscience · 2014Review
- Gain-of-function mutations in the ALS8 causative gene VAPB have detrimental effects on neurons and muscles.Biology open · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Accumulation, aggregation and deposition of Aβ peptides are pathological hallmarks in the brains of individuals affected by Alzheimer's disease (AD) or by cerebral β-amyloid angiopathy (Aβ-CAA). While Aβ is a peptide of yet largely unknown function, it is constantly produced in the human brain where it normally remains in a soluble state. However, Aβ peptides are aggregation prone by their intrinsic ability to adopt alternative conformations rich in β-sheet structure that aggregate into oligomeric as well as fibrillar formations. This transition from soluble to aggregated state has been hypothesized to initiate the pathological cascade and is therefore subject to intensive research. Mounting evidence suggests prion-like templated misfolding as the biochemical phenomenon responsible for promoting progressive Aβ aggregation. Here, we review studies in vitro and in vivo that suggest that cerebral Aβ aggregation may indeed progress via prion-like templated misfolding. The implications of these findings are discussed with respect to understanding initiation and progression of the disease and to developing therapeutics.
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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.