The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Rapid induction of Alzheimer A beta amyloid formation by zinc
Abstract
A beta 1-40, a major component of Alzheimer's disease cerebral amyloid, is present in the cerebrospinal fluid and remains relatively soluble at high concentrations (less than or equal to 3.7 mM). Thus, physiological factors which induce A beta amyloid formation could provide clues to the pathogenesis of the disease. It has been shown that human A beta specifically and saturably binds zinc. Here, concentrations of zinc above 300 nM rapidly destabilized human A beta 1-40 solutions, inducing tinctorial amyloid formation. However, rat A beta 1-40 binds zinc less avidly and is immune to these effects, perhaps explaining the scarcity with which these animals form cerebral A beta amyloid. These data suggest a role for cerebral zinc metabolism in the neuropathogenesis of Alzheimer's disease.
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In the citing paper
“For example, it was shown that that metal ions promote Aβ aggregation,16,17 as well as formation of reactive oxygen species (ROS) and lead to oxidative stress.18–20”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [16]
In the citing paper
“Several studies showed that Zn2+ promotes formation of nonfibrillar aggregates,16,29–31 yet conflicting results have been reported for the Cu2+-mediated Aβ aggregation.”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [16]
In the citing paper
“These metal ions have been shown to affect Aβ aggregation, as well as lead to the formation of reactive oxygen species (ROS).12−16”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [12]
Citations
Cites
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Self-citationJarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Amyloid Deposits and Amyloidosis
Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,780
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
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Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type
Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,399
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The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Oxidative stress, aging, and diseases
Liguori, I., Russo, G., Curcio, F., Bulli, G., Aran, L., Della-Morte, D., Gargiulo, G., Testa, G., Cacciatore, F., Bonaduce, D., et al. (2018) · Clinical Interventions in Aging · doi:10.2147/cia.s158513 · Cited by 3,979
Copper, iron and zinc in Alzheimer's disease senile plaques
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Metals in Neurobiology: Probing Their Chemistry and Biology with Molecular Imaging
Que, E. L., Domaille, D. W., & Chang, C. J. (2008) · Chemical Reviews · doi:10.1021/cr078203u · Cited by 2,077
The neurobiology of zinc in health and disease
Frederickson, C. J., Koh, J., & Bush, A. I. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1671 · Cited by 1,841
Self-citation
Metadata
- Authors
- Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R.
- Affiliations
- Harvard University (US)
- Heidelberg University (DE)
- Mental Health Research Institute (AU)
- Venue
- Science
- Published
- 1994-09-02
- Volume
- 265
- Issue
- 5177
- Pages
- 1464-1467
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2094808560
- Cited by
- 1,522
- References
- 31
- Citations by year
- 2026: 20 · 2025: 24 · 2024: 28 · 2023: 46 · 2022: 36 · 2021: 52 · 2020: 68 · 2019: 56 · 2018: 58 · 2017: 78 · 2016: 64 · 2015: 60 · 2014: 74 · 2013: 64 · 2012: 80
- FWCI
- 21.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ag011899-03, 5r01ns030428-07)
- National Institute on Aging (R01 AG11899-01)
- National Institute of Neurological Disorders and Stroke (R01 NS30428-03)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- Alzheimer's disease, Aβ40, zinc binding, amyloid fibril formation, zinc metabolism, cerebrospinal fluid, neuropathogenesis
- MeSH terms
- Alzheimer Disease, Animals, Brain, Edetic Acid, Humans, Kinetics, Peptide Fragments, Solubility, Zinc, Amyloid beta-Peptides, Mice, Rats
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