ArticleBiophysical journal2009
Cholesterol modulates the interaction of beta-amyloid peptide with lipid bilayers.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 52 citations in OpenAlex.
- Polyallylamine Binds to Aβ Amyloid and Inhibits Antibody Recognition.International journal of molecular sciences · 2024Article
- A Hairpin Motif in the Amyloid-β Peptide Is Important for Formation of Disease-Related Oligomers.Journal of the American Chemical Society · 2023Article
- Study on the Association of Dietary Fatty Acid Intake and Serum Lipid Profiles With Cognition in Aged Subjects With Type 2 Diabetes Mellitus.Frontiers in aging neuroscience · 2022Article
- Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer's disease.Frontiers in molecular neuroscience · 2022Review
- Interaction of Amyloidogenic Proteins with Membranes and Molecular Mechanism for the Development of Alzheimer's disease.Alzheimer's research & therapy open access · 2019Article
- Toward common mechanisms for risk factors in Alzheimer's syndrome.Alzheimer's & dementia (New York, N. Y.) · 2017Review
- Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Interface focus · 2017Review
- Article
- Effects of Charged Cholesterol Derivatives on Aβ40 Amyloid Formation.The journal of physical chemistry. B · 2016Article
- Characterization of 3D Voronoi tessellation nearest neighbor lipid shells provides atomistic lipid disruption profile of protein containing lipid membranes.Biophysical chemistry · 2015Article
- The role of cholesterol metabolism in Alzheimer's disease.Molecular neurobiology · 2015Review
- Scaling and alpha-helix regulation of protein relaxation in a lipid bilayer.The Journal of chemical physics · 2014Article
- Monitoring of single vesicle cytochrome-c release illuminates BAK as a novel target of Aβ oligomers.Biophysical journal · 2014Article
- Bexarotene blocks calcium-permeable ion channels formed by neurotoxic Alzheimer's β-amyloid peptides.ACS chemical neuroscience · 2014Article
- Latest developments in experimental and computational approaches to characterize protein-lipid interactions.Proteomics · 2012Review
- Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Cold Spring Harbor perspectives in medicine · 2012Review
- Cholesterol superlattice modulates CA4P release from liposomes and CA4P cytotoxicity on mammary cancer cells.Biophysical journal · 2012Article
- Fluorescent analysis of the cell-selective Alzheimer's disease aβ Peptide surface membrane binding: influence of membrane components.International journal of Alzheimer's disease · 2011Article
- Lipid Rafts: Linking Alzheimer's Amyloid-β Production, Aggregation, and Toxicity at Neuronal Membranes.International journal of Alzheimer's disease · 2010Article
- Effect of membrane structure on the action of polyenes: I. Nystatin action in cholesterol- and ergosterol-containing membranes.The Journal of membrane biology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction of an amphiphilic, 40-amino acid beta-amyloid (Abeta) peptide with liposomal membranes as a function of sterol mole fraction (X(sterol)) was studied based on the fluorescence anisotropy of a site-specific membrane sterol probe, dehydroergosterol (DHE), and fluorescence resonance energy transfer (FRET) from the native Tyr-10 residue of Abeta to DHE. Without Abeta, peaks or kinks in the DHE anisotropy versus X(sterol) plot were detected at X(sterol) approximately 0.25, 0.33, and 0.53. Monomeric Abeta preserved these peaks/kinks, but oligomeric Abeta suppressed them and created a new DHE anisotropy peak at X(sterol) approximately 0.38. The above critical X(sterol) values coincide favorably with the superlattice compositions predicted by the cholesterol superlattice model, suggesting that membrane cholesterol tends to adopt a regular lateral arrangement, or domain formation, in the lipid bilayers. For FRET, a peak was also detected at X(sterol) approximately 0.38 for both monomeric and oligomeric Abeta, implying increased penetration of Abeta into the lipid bilayer at this sterol mole fraction. We conclude that the interaction of Abeta with membranes is affected by the lateral organization of cholesterol, and hypothesize that the formation of an oligomeric Abeta/cholesterol domain complex may be linked to the toxicity of Abeta in neuronal membranes.
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.