ArticleBiochemistry2012
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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
48 citing papers in PubMed, 106 citations in OpenAlex.
- An edge β-strand mutation turns ubiquitin into a pore-forming amyloid.Protein science : a publication of the Protein Society · 2026Article
- Differential effects of ganglioside lipids on the conformation and aggregation of islet amyloid polypeptide.Protein science : a publication of the Protein Society · 2024Article
- Possible Role of Fibrinaloid Microclots in Postural Orthostatic Tachycardia Syndrome (POTS): Focus on Long COVID.Journal of personalized medicine · 2024Article
- Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism.Chemical science · 2023Article
- Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage.BBA advances · 2023Article
- Amyloids on Membrane Interfaces: Implications for Neurodegeneration.The Journal of membrane biology · 2022Review
- Semax, a Synthetic Regulatory Peptide, Affects Copper-Induced Abeta Aggregation and Amyloid Formation in Artificial Membrane Models.ACS chemical neuroscience · 2022Article
- Peptide backbone modifications of amyloid β (1-40) impact fibrillation behavior and neuronal toxicity.Scientific reports · 2021Article
- Lipidomic Profiling Identifies Signatures of Poor Cardiovascular Health.Metabolites · 2021Article
- Development and Application of High-Throughput Single Cell Lipid Profiling: A Study ofiScience · 2020Article
- Amyloidogenic Intrinsically Disordered Proteins: New Insights into Their Self-Assembly and Their Interaction with Membranes.Life (Basel, Switzerland) · 2020Review
- Fibrillization of 40-Residue β-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms.Biomolecules · 2020Article
- Imaging Flow Cytometry Illuminates New Dimensions of Amyloid Peptide-Membrane Interactions.Biophysical journal · 2020Article
- The role of phosphatidylserine recognition receptors in multiple biological functions.Cellular & molecular biology letters · 2020Review
- Unpacking the aggregation-oligomerization-fibrillization process of naturally-occurring hIAPP amyloid oligomers isolated directly from sera of children with obesity or diabetes mellitus.Scientific reports · 2019Article
- Zinc boosts EGCG's hIAPP amyloid Inhibition both in solution and membrane.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Article
- Membranes as modulators of amyloid protein misfolding and target of toxicity.Biochimica et biophysica acta. Biomembranes · 2018Review
- Impact of membrane curvature on amyloid aggregation.Biochimica et biophysica acta. Biomembranes · 2018Review
- Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity.Cells · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The toxicity of amyloid-forming peptides has been hypothesized to reside in the ability of protein oligomers to interact with and disrupt the cell membrane. Much of the evidence for this hypothesis comes from in vitro experiments using model membranes. However, the accuracy of this approach depends on the ability of the model membrane to accurately mimic the cell membrane. The effect of membrane composition has been overlooked in many studies of amyloid toxicity in model systems. By combining measurements of membrane binding, membrane permeabilization, and fiber formation, we show that lipids with the phosphatidylethanolamine (PE) headgroup strongly modulate the membrane disruption induced by IAPP (islet amyloid polypeptide protein), an amyloidogenic protein involved in type II diabetes. Our results suggest that PE lipids hamper the interaction of prefibrillar IAPP with membranes but enhance the membrane disruption correlated with the growth of fibers on the membrane surface via a detergent-like mechanism. These findings provide insights into the mechanism of membrane disruption induced by IAPP, suggesting a possible role of PE and other amyloids involved in other pathologies.
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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.