The DOI matches its Crossref record; 234 of the 234 references it cites were found in a registry or an index.
The role of metallobiology and amyloid-β peptides in Alzheimer's disease
Abstract
The biggest risk factor for Alzheimer's disease is the process of ageing, but the mechanisms that lead to the manifestation of the disease remain to be elucidated. Why age triggers the disease is unclear but an emerging theme is the inability for a cell to efficiently maintain many key processes such as energy production, repair, and regenerative mechanisms. Metal ions are essential to the metabolic function of every cell. This review will explore the role and reported changes in metal ions in Alzheimer disease, particularly the brain, blood and cerebral spinal fluid, emphasizing how iron, copper and zinc may be involved through the interactions with amyloid precursor protein, the proteolytically cleaved peptide amyloid-beta (Aβ), and other related metalloproteins. Finally, we explore the monomeric makeup of possible Aβ dimers, what a dimeric Aβ species from Alzheimer's disease brain tissue is likely to be composed of, and discuss how metals may influence Aβ production and toxicity via a copper catalyzed dityrosine cross-link.
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In the citing paper
“High concentrations of zinc, copper, and iron are present in the insoluble amyloid plaques and neurofibrillary tangles characteristic of Alzheimer’s disease.”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [75]
In the citing paper
“Focal accumulation of zinc, copper, and iron might deprive other brain tissues of these essential metals, leading to aberrant neuronal function.75”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [75]
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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RetractedThe precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
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Self-citationAmyloid plaque core protein in Alzheimer disease and Down syndrome.
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“b-APP-site cleaving enzyme (BACE) is a membrane anchored aspartyl protease (Sinha et al. 1999; Vassar et al. 1999; Yan et al. 1999; Cai et al. 2001; Luo et al. 2001) that is able to bind Cu through C-terminal cysteines.”
BackgroundShankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Plasma Homocysteine as a Risk Factor for Dementia and Alzheimer's Disease
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Copper, iron and zinc in Alzheimer's disease senile plaques
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Aβ Oligomers – a decade of discovery
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Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database
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Research works printed but not linked: 1
- Weir D. G., 1999, Cobalamin: Nutrition in Health and Disease
Cited by
Sorted by citations
The role of iron in brain ageing and neurodegenerative disorders
Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723
The application of Ferroptosis in diseases
Qiu, Y., Cao, Y., Cao, W., Jia, Y., & Lu, N. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104919 · Cited by 415
SOD2 in mitochondrial dysfunction and neurodegeneration
Flynn, J. M., & Melov, S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.027 · Cited by 390
Management of oxidative stress and other pathologies in Alzheimer’s disease
Simunkova, M., Alwasel, S. H., Alhazza, I. M., Jomova, K., Kollar, V., Rusko, M., & Valko, M. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02538-y · Cited by 303
Metadata
- Authors
- Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., & Duce, J. A.
- Affiliations
- Mental Health Research Institute (AU)
- Corresponding author
- Duce, James A.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2011-11-28
- Volume
- 120
- Issue
- s1
- Pages
- 149-166
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1784444703
- Cited by
- 266
- References
- 234
- Citations by year
- 2026: 5 · 2025: 1 · 2024: 18 · 2023: 11 · 2022: 13 · 2021: 17 · 2020: 14 · 2019: 25 · 2018: 16 · 2017: 21 · 2016: 24 · 2015: 22 · 2014: 29 · 2013: 31 · 2012: 19
- FWCI
- 2.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion)
- Funders
- State Government of Victoria
- Australian Research Council
- National Health and Medical Research Council
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, metal ions, amyloid-beta, amyloid precursor protein, iron, copper, zinc, metalloproteins, amyloid-beta dimers, cerebrospinal fluid, aging, metal homeostasis
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Brain Chemistry, Copper, Humans, Iron, Metalloproteins, Molecular Sequence Data, Protein Binding, Zinc, Amyloid beta-Peptides
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