ArticleBiophysical journal2007
Time-dependent DNA condensation induced by amyloid beta-peptide.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- Virus-Like Cytosolic and Cell-Free Oxidatively Damaged Nucleic Acids Likely Drive Inflammation, Synapse Degeneration, and Neuron Death in Alzheimer's Disease.Journal of Alzheimer's disease reports · 2023Review
- Identification and characterization of the Hfq bacterial amyloid region DNA interactions.BBA advances · 2021Article
- Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy.Archives of virology · 2020Review
- Functional Reciprocity of Amyloids and Antimicrobial Peptides: Rethinking the Role of Supramolecular Assembly in Host Defense, Immune Activation, and Inflammation.Frontiers in immunology · 2020Review
- Propidium iodide staining underestimates viability of adherent bacterial cells.Scientific reports · 2019Article
- A Comprehensive Biophysical Analysis of the Effect of DNA Binding Drugs on Protamine-induced DNA Condensation.Scientific reports · 2019Article
- Mining Clinical Case Reports to Identify New Lines of Investigation in Alzheimer's Disease: The Curious Case of DNase I.Journal of Alzheimer's disease reports · 2019Article
- Revised role for Hfq bacterial regulator on DNA topology.Scientific reports · 2018Article
- Ascovirus P64 Homologs: A Novel Family of Large Cationic Proteins That Condense Viral Genomic DNA for Encapsidation.Biology · 2018Article
- Prion Protein PRNP: A New Player in Innate Immunity? The Aβ Connection.Journal of Alzheimer's disease reports · 2017Article
- The "Jekyll and Hyde" Actions of Nucleic Acids on the Prion-like Aggregation of Proteins.The Journal of biological chemistry · 2016Review
- Extracellular DNA facilitates the formation of functional amyloids in Staphylococcus aureus biofilms.Molecular microbiology · 2016Article
- Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases.Biophysical reviews · 2014Review
- Structure-activity relationships of αs-casein peptides with multifunctional biological activities.Molecular and cellular biochemistry · 2013Article
- Binding with nucleic acids or glycosaminoglycans converts soluble protein oligomers to amyloid.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major protein component of the amyloid deposition in Alzheimer's disease is a 39-43 residue peptide, amyloid beta (Abeta). Abeta is toxic to neurons, although the mechanism of neurodegeneration is uncertain. Evidence exists for non-B DNA conformation in the hippocampus of Alzheimer's disease brains, and Abeta was reportedly able to transform DNA conformation in vitro. In this study, we found that DNA conformation was altered in the presence of Abeta, and Abeta induced DNA condensation in a time-dependent manner. Furthermore, Abeta sheets, serving as condensation nuclei, were crucial for DNA condensation, and Cu(2+) and Zn(2+) ions inhibited Abeta sheet-induced DNA condensation. Our results suggest DNA condensation as a mechanism of Abeta toxicity.
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Registered trials
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