The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
An interaction of β‐amyloid with aluminium in vitro
Abstract
We have used circular dichroism spectroscopy to confirm that, in a membrane‐mimicking solvent, AβP(1–40) adopts a partially helical conformation and we have demonstrated the loss of this structure in the presence of physiologically relevant concentrations of aluminium. This is the first evidence of a direct biochemical interaction between aluminium and β‐amyloid and may have important implications for the pathogenesis of Alzheimer's disease.
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Protein polypeptides are transformed to secondary structures when aluminium ions interact with them through oxygen-containing amino acids, side chains and protein backbone, leading to ultimate denaturation or conformational or structural alteration as in β-amyloid.
“Protein polypeptides are transformed to secondary structures when Al ions interact with them through oxygen-containing amino acids, side chains and protein backbone leading to ultimate denaturation (Mujika et al., 2018) or conformational or structural alteration (Exley et al., 1993; Zatta et al., 2005; Exley, 2006) as in β-amyloid.”
From Aluminium toxicosis: a review of toxic actions and effects (2019) · cites this paper as Exley et al., 1993
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Cites
Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975
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Research works printed but not linked: 11
- Jope R.S., 1992, Ciba Found. Symp., 169, 254
- 10.1523/JNEUROSCI.12-02-00376.1992 · DOI
- 10.1016/S0022-5193(05)80769-6 · DOI
- 10.1073/pnas.90.2.567 · DOI
- 10.1016/0022-2836(92)90106-T · DOI
- 10.1021/bi00838a031 · DOI
- 10.1021/bi00504a006 · DOI
- Woody R.W., 1974, Peptides, Polypeptides and Proteins, 338
- 10.1016/S0140-6736(86)92319-6 · DOI
- 10.1016/0022-2836(92)90983-Q · DOI
- 10.1038/360065a0 · DOI
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Aluminium toxicosis: a review of toxic actions and effects
Igbokwe, I. O., Igwenagu, E., & Igbokwe, N. A. (2019) · Interdisciplinary Toxicology · doi:10.2478/intox-2019-0007 · Cited by 395
“, 2018) or conformational or structural alteration (Exley et al., 1993; Zatta et al., 2005; Exley, 2006) as in β-amyloid.”
BackgroundHan, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67
Metadata
- Authors
- Exley, C., Price, N. C., Kelly, S. M., & Birchall, J. D.
- Affiliations
- Keele University (GB)
- University of Stirling (GB)
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1993-06-21
- Volume
- 324
- Issue
- 3
- Pages
- 293-295
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1974342751
- Cited by
- 128
- References
- 1
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 5 · 2019: 4 · 2018: 4 · 2017: 6 · 2016: 2 · 2015: 4 · 2014: 2 · 2013: 1 · 2012: 4
- FWCI
- 4.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Aluminum toxicity and tolerance in plants and animals
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta, aluminum, Alzheimer's disease, amyloid conformation, helical conformation, metal-protein interactions, circular dichroism
- MeSH terms
- Aluminum, Circular Dichroism, Humans, Peptides, Amyloid beta-Peptides, Protein Structure, Secondary, In Vitro Techniques
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