ArticleThe Journal of biological chemistry2013
Binding of apolipoprotein E inhibits the oligomer growth of amyloid-β peptide in solution as determined by fluorescence cross-correlation spectroscopy.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Article
- The HDL-Mimetic Peptide 4F Mitigates Vascular and Cortical Amyloid Pathology and Associated Neuroinflammation in a Transgenic Mouse Model of Cerebral Amyloid Angiopathy and Alzheimer's Disease.Molecular neurobiology · 2025Article
- Evidence that Alzheimer's Disease Is a Disease of Competitive Synaptic Plasticity Gone Awry.Journal of Alzheimer's disease : JAD · 2024Review
- Four-color fluorescence cross-correlation spectroscopy with one laser and one camera.Biomedical optics express · 2023Article
- Four-color fluorescence cross-correlation spectroscopy with one laser and one camera.bioRxiv : the preprint server for biology · 2023Article
- Endogenous Human Proteins Interfering with Amyloid Formation.Biomolecules · 2022Review
- Review
- Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches.Computational and structural biotechnology journal · 2021Review
- Influence of FRET and fluorescent protein maturation on the quantification of binding affinity with dual-channel fluorescence cross-correlation spectroscopy.Biomedical optics express · 2020Article
- High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease.Chemical communications (Cambridge, England) · 2020Review
- Reduced Influence of apoE on Aβ43 Aggregation and Reduced Vascular Aβ43 Toxicity as Compared with Aβ40 and Aβ42.Molecular neurobiology · 2020Article
- Apolipoprotein E Interferes with IAPP Aggregation and Protects Pericytes from IAPP-Induced Toxicity.Biomolecules · 2020Article
- Morphological analysis of Apolipoprotein E binding to Aβ Amyloid using a combination of Surface Plasmon Resonance, Immunogold Labeling and Scanning Electron Microscopy.BMC biotechnology · 2019Article
- Amyloid-β and tau complexity - towards improved biomarkers and targeted therapies.Nature reviews. Neurology · 2018Review
- Study of Exosomes Shed New Light on Physiology of Amyloidogenesis.Cellular and molecular neurobiology · 2016Review
- Clusterin Binds to Aβ1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation.The Journal of biological chemistry · 2016Article
- Neuronal response in Alzheimer's and Parkinson's disease: the effect of toxic proteins on intracellular pathways.BMC neuroscience · 2015Review
- ApoE: the role of conserved residues in defining function.Protein science : a publication of the Protein Society · 2015Article
- Article
- Amyloid-β pathology and APOE genotype modulate retinoid X receptor agonist activity in vivo.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
One of the primary neuropathological hallmarks of Alzheimer disease is the presence of extracellular amyloid plaques resulting from the aggregation of amyloid-β (Aβ) peptides. The intrinsic disorder of the Aβ peptide drives self-association and progressive reordering of the conformation in solution, and this dynamic distribution of Aβ complicates biophysical studies. This property poses a challenge for understanding the interaction of Aβ with apolipoprotein E (apoE). ApoE plays a pivotal role in the aggregation and clearance of Aβ peptides in the brain, and the ε4 allele of APOE is the most significant known genetic modulator of Alzheimer risk. Understanding the interaction between apoE and Aβ will provide insight into the mechanism by which different apoE isoforms determine Alzheimer disease risk. Here we applied alternating laser excitation fluorescence cross-correlation spectroscopy to observe the single molecule interaction of Aβ with apoE in the hydrated state. The diffusion time of freely diffusing Aβ in the absence of apoE shows significant self-aggregation, whereas in the presence of apoE, binding of the protein results in a more stable complex. These results show that apoE slows down the oligomerization of Aβ in solution and provide direct insight into the process by which apoE influences the deposition and clearance of Aβ peptides in the brain. Furthermore, by developing an approach to remove signals arising from very large Aβ aggregates, we show that real-time single particle observations provide access to information regarding the fraction of apoE bound and the stoichiometry of apoE and Aβ in the complex.
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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 Socratic graph.