The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Soluble Amyloid Oligomers Increase Bilayer Conductance by Altering Dielectric Structure
Open accessAbstract
The amyloid hypothesis of Alzheimer's toxicity has undergone a resurgence with increasing evidence that it is not amyloid fibrils but a smaller oligomeric species that produces the deleterious results. In this paper we address the mechanism of this toxicity. Only oligomers increase the conductance of lipid bilayers and patch-clamped mammalian cells, producing almost identical current–voltage curves in both preparations. Oligomers increase the conductance of the bare bilayer, the cation conductance induced by nonactin, and the anion conductance induced by tetraphenyl borate. Negative charge reduces the sensitivity of the membrane to amyloid, but cholesterol has little effect. In contrast, the area compressibility of the lipid has a very large effect. Membranes with a large area compressibility modulus are almost insensitive to amyloid oligomers, but membranes formed from soft, highly compressible lipids are highly susceptible to amyloid oligomer-induced conductance changes. Furthermore, membranes formed using the solvent decane (instead of squalane) are completely insensitive to the presence of oligomers. One simple explanation for these effects on bilayer conductance is that amyloid oligomers increase the area per molecule of the membrane-forming lipids, thus thinning the membrane, lowering the dielectric barrier, and increasing the conductance of any mechanism sensitive to the dielectric barrier.
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Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
PARSEGIAN, A. (1969) · Nature · doi:10.1038/221844a0 · Cited by 854
Cited by
Alzheimer's Disease and the Amyloid-β Peptide
Murphy, M. P., & LeVine, H. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-1221 · Cited by 1,750
Alzheimer's Disease: From Pathology to Therapeutic Approaches
Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802808 · Cited by 626
Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5
Renner, M., Lacor, P. N., Velasco, P. T., Xu, J., Contractor, A., Klein, W. L., & Triller, A. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.029 · Cited by 468
Oligomeric amyloid-β peptide disrupts phosphatidylinositol-4,5-bisphosphate metabolism
Berman, D. E., Dall'Armi, C., Voronov, S. V., McIntire, L. B. J., Zhang, H., Moore, A. Z., Staniszewski, A., Arancio, O., Kim, T.-W., & Di Paolo, G. (2008) · Nature Neuroscience · doi:10.1038/nn.2100 · Cited by 199
Tau Oligomers Impair Artificial Membrane Integrity and Cellular Viability
Flach, K., Hilbrich, I., Schiffmann, A., Gärtner, U., Krüger, M., Leonhardt, M., Waschipky, H., Wick, L., Arendt, T., & Holzer, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.396176 · Cited by 188
Metadata
- Authors
- Sokolov, Y., Kozak, J. A., Kayed, R., Chanturiya, A., Glabe, C., & Hall, J. E.
- Venue
- The Journal of General Physiology
- Publisher
- Rockefeller University Press
- Published
- 2006-11-13
- Volume
- 128
- Issue
- 6
- Pages
- 637-647
- ISSN
- 0022-1295 (ISSN-L)
- 1540-7748
- OpenAlex
- W2096336861
- Cited by
- 228
- References
- 3
- FWCI
- 8.04
- Type
- journal article
- Language
- en
- Open access
- green
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- Sokolov, Y., Kozak, J. A., Kayed, R., Chanturiya, A., Glabe, C., & Hall, J. E. (2006). Soluble Amyloid Oligomers Increase Bilayer Conductance by Altering Dielectric Structure. The Journal of General Physiology. https://doi.org/10.1085/jgp.200609533
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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