The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Membrane Disruption by Alzheimer β-Amyloid Peptides Mediated through Specific Binding to Either Phospholipids or Gangliosides
Open accessAbstract
Increasing evidence implicates Abeta peptides as neurotoxic agents in Alzheimer's disease. We investigated one possible mechanism of neurotoxicity, namely Abeta-membrane lipid interactions. We find that Abeta disrupts membranes containing acidic phospholipids. This disruption is greater at slightly acidic pH (characteristic of endosomes) than at neutral pH (characteristic of the extracellular space). This pH dependence suggests that Abeta has the capacity to disrupt endosomal and plasma membranes, and this disruption could account, at least in part, for the observed neurotoxic effects of the peptide. We also find that gangliosides induce Abeta to adopt a novel alpha/beta conformation at neutral pH.
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Cites
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
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Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
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Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
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Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
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Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain
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Cited by
TREM2 Lipid Sensing Sustains the Microglial Response in an Alzheimer’s Disease Model
Wang, Y., Cella, M., Mallinson, K., Ulrich, J. D., Young, K. L., Robinette, M. L., Gilfillan, S., Krishnan, G. M., Sudhakar, S., Zinselmeyer, B. H., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.049 · Cited by 1,736
Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954
Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559
Chong, Z. Z., Li, F., & Maiese, K. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.02.004 · Cited by 536
Abramov, A. Y., Canevari, L., & Duchen, M. R. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-12-05088.2003 · Cited by 337
Metadata
- Authors
- McLaurin, J., & Chakrabartty, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-10
- Volume
- 271
- Issue
- 43
- Pages
- 26482-26489
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1989269014
- Cited by
- 335
- References
- 8
- FWCI
- 7.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Membrane Disruption by Alzheimer β-Amyloid Peptides Mediated through Specific Binding to Either Phospholipids or Gangliosides. https://app.cochat.ai/papers/10.1074/jbc.271.43.26482
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- McLaurin, J., & Chakrabartty, A. (1996). Membrane Disruption by Alzheimer β-Amyloid Peptides Mediated through Specific Binding to Either Phospholipids or Gangliosides. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.271.43.26482
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
