ArticleNano letters2018
Reversible Cation-Selective Attachment and Self-Assembly of Human Tau on Supported Brain Lipid Membranes.
Article in Nano letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- Tau protein in Parkinson's disease: advances in phosphoproteomics and molecular dynamics simulations.Frontiers in aging neuroscience · 2026Review
- Biochemical and Biophysical Characterization of Tau and α-Linolenic Acid Vesicles In Vitro.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Single-molecule imaging reveals Tau trapping at nanometer-sized dynamic hot spots near the plasma membrane that persists after microtubule perturbation and cholesterol depletion.The EMBO journal · 2022Article
- Associations Between Plasma Metals and Cognitive Function in People Aged 60 and Above.Biological trace element research · 2022Article
- Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates.The EMBO journal · 2022Article
- Transcription Elongation Factor A (SII)-Like (TCEAL) Gene Family Member-TCEAL2: A Novel Prognostic Marker in Pan-Cancer.Cancer informatics · 2022Article
- Genetically engineered MAPT 10+16 mutation causes pathophysiological excitability of human iPSC-derived neurons related to 4R tau-induced dementia.Cell death & disease · 2021Article
- Interaction of Tau construct K18 with model lipid membranes.Nanoscale advances · 2021Article
- Tau and Membranes: Interactions That Promote Folding and Condensation.Frontiers in cell and developmental biology · 2021Review
- Role of the Lipid Membrane and Membrane Proteins in Tau Pathology.Frontiers in cell and developmental biology · 2021Review
- Cholesterol-rich naked mole-rat brain lipid membranes are susceptible to amyloid beta-induced damageAging · 2020Article
- Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein.Scientific reports · 2020Article
- Mechanisms of secretion and spreading of pathological tau protein.Cellular and molecular life sciences : CMLS · 2020Review
- Mechanisms of Pathogenic Tau and Aβ Protein Spreading in Alzheimer's Disease.Frontiers in aging neuroscience · 2020Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Misfolding and aggregation of the neuronal, microtubule-associated protein tau is involved in the pathogenesis of Alzheimer's disease and tauopathies. It has been proposed that neuronal membranes could play a role in tau release, internalization, and aggregation and that tau aggregates could exert toxicity via membrane permeabilization. Whether and how tau interacts with lipid membranes remains a matter of discussion. Here, we characterize the interaction of full-length human tau (htau40) with supported lipid membranes (SLMs) made from brain total lipid extract by time-lapse high-resolution atomic force microscopy (AFM). We observe that tau attaches to brain lipid membranes where it self-assembles in a cation-dependent manner. Sodium triggers the attachment, self-assembly, and growth, whereas potassium inhibits these processes. Moreover, tau assemblies are stable in the presence of sodium and lithium but disassemble in the presence of potassium and rubidium. Whereas the pseudorepeat domains (R1-R4) of htau40 promote the sodium-dependent attachment to the membrane and stabilize the tau assemblies, the N-terminal region promotes tau self-assembly and growth.
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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.