ArticleJournal of bioenergetics and biomembranes2013
AβP1-42 incorporation and channel formation in planar lipid membranes: the role of cholesterol and its oxidation products.
Article in Journal of bioenergetics and biomembranes, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- An edge β-strand mutation turns ubiquitin into a pore-forming amyloid.Protein science : a publication of the Protein Society · 2026Article
- Aggregation Behavior of Amyloid Beta Peptide Depends Upon the Membrane Lipid Composition.The Journal of membrane biology · 2024Review
- Real-time monitoring of the amyloid βPNAS nexus · 2024Article
- The Effect of Calcium Ions on hIAPP Channel Activity: Possible Implications in T2DM.Membranes · 2023Article
- Dendrimers in Alzheimer's Disease: Recent Approaches in Multi-Targeting Strategies.Pharmaceutics · 2023Review
- AmyP53 Prevents the Formation of Neurotoxic β-Amyloid Oligomers through an Unprecedent Mechanism of Interaction with Gangliosides: Insights for Alzheimer's Disease Therapy.International journal of molecular sciences · 2023Article
- Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer's disease.Frontiers in molecular neuroscience · 2022Review
- Accumulation of Amyloid Beta (Aβ) Peptide on Blood Vessel Walls in the Damaged Brain after Transient Middle Cerebral Artery Occlusion.Biomolecules · 2019Article
- Concentration-dependent effects of mercury and lead on Aβ42: possible implications for Alzheimer's disease.European biophysics journal : EBJ · 2019Article
- Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts.ACS chemical neuroscience · 2017Article
- Ion Channel Formation by Amyloid-β42 Oligomers but Not Amyloid-β40 in Cellular Membranes.The Journal of biological chemistry · 2017Article
- Comparative modeling of hypothetical amyloid pores based on cylindrin.Journal of molecular modeling · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid beta peptide (AβP) is a natural peptide, normally released into the cerebrospinal fluid (CSF), that plays a key role in Alzheimer's disease. The conversion of the peptide from a native soluble form to a non-native and often insoluble form, such as small and large aggregates, protofibrils and fibrils of AβP appears to be implicated in the pathogenesis of AD. Although the molecular mechanisms of AβP neurotoxicity are not fully understood, a large body of data suggests that the primary target of amyloid peptides is the cell membrane of neurons, that may modulate the structural and functional conversion of AβP into assemblies involved in pathological processes. In our study, we provide a systematic investigation of AβP1-42's ability to incorporate and form channel-like events in membranes of different lipid composition and focus on cholesterol and its oxidation products. We propose that cholesterol and its oxidation products can be considered neuroprotective factors because a) by favouring AβP1-42 insertion into membranes, the fibrillation/clearance balance shifts toward clearance; b) by shifting channel selectivity toward anions, the membrane potential is moved far from the threshold of membrane excitability, thus decreasing the influx of calcium into the cell.
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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.