The DOI matches its Crossref record; 90 of the 90 references it cites were found in a registry or an index.
Physiological Roles of Amyloid-?? and Implications for its Removal in Alzheimer???s Disease
Abstract
The underlying pathological cause of Alzheimer's disease has been postulated to be an excess of amyloid-beta (Abeta) which aggregates into toxic fibrillar deposits within the extracellular space of the brain, thereby disrupting neuronal and synaptic function and eventually leading to neuronal degeneration and dementia. As a result, therapeutic strategies have been developed that are designed to remove Abeta from the brain. Caution needs to be exercised concerning such strategies because, in addition to its presence in neuritic plaques, Abeta has a widespread distribution through the brain and body, even in cognitively normal individuals. Evidence indicates that instead of being a toxic peptide, soluble Abeta serves a variety of physiological functions, including modulation of synaptic function, facilitation of neuronal growth and survival, protection against oxidative stress, and surveillance against neuroactive compounds, toxins and pathogens. These physiological functions must be taken into account when strategies are developed to reduce Abeta load in Alzheimer's disease. Ideally, such strategies should target forms of Abeta that are not bioavailable, such as fibrillar Abeta, or forms that are regarded to be overexpressed in Alzheimer's disease (such as oligomers) while leaving normal soluble Abeta1-40 and Abeta1-42 intact. At present none of the available therapeutic strategies appears to have such selectivity. Until these technical limitations and the uncertainties regarding the effect of depletion of Abeta from the brain are resolved, it would not be prudent to begin further clinical trials.
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“The report revealed no change in primary or secondary outcome measures [56].”
From Clinical trials of new drugs for Alzheimer disease (2020) · cites this paper as [56]
In the citing paper
“The NILVAD trial, which took place in 2013, examined the effectiveness of nilvadipine in people with AD. ADAS-Cog was the main outcome measure, but there was no difference in the primary or secondary end point measures according to a published report (Bishop et al., 2004).”
From An update on the novel and approved drugs for Alzheimer disease (2022) · cites this paper as Bishop et al., 2004
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Cites
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
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
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
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
The molecular pathology of Alzheimer's disease
Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012
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
Oxidative Damage Is the Earliest Event in Alzheimer Disease
Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885
Research works printed but not linked: 3
- Li, 1998, Lab Invest, 78, 461
- Mileusnic, 2000, Eur J Neurosci, 12, 4487, 10.1046/j.1460-9568.2000.01344.x · DOI
- Koudinov, 2003, Neurobiol Lipids, 1, 45
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Sorted by citations
A critical appraisal of amyloid-β-targeting therapies for Alzheimer disease
Panza, F., Lozupone, M., Logroscino, G., & Imbimbo, B. P. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0116-6 · Cited by 965
Clinical trials of new drugs for Alzheimer disease
Huang, L.-K., Chao, S.-P., & Hu, C.-J. (2020) · Journal of Biomedical Science · doi:10.1186/s12929-019-0609-7 · Cited by 702
“The report revealed no change in primary or secondary outcome measures [56].”
BackgroundThe Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease
Brothers, H. M., Gosztyla, M. L., & Robinson, S. R. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00118 · Cited by 314
Self-citationDrachman, D. A. (2014) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2013.11.003 · Cited by 224
Roy, R. G., Mandal, P. K., & Maroon, J. C. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00486 · Cited by 194
Metadata
- Authors
- Bishop, G. M., & Robinson, S. R.
- Affiliations
- Monash University (AU)
- Corresponding author
- Robinson, Stephen R
- Venue
- Drugs & Aging
- Published
- 2004
- Volume
- 21
- Issue
- 10
- Pages
- 621-630
- ISSN
- 1170-229X (ISSN-L)
- OpenAlex
- W2083481304
- Cited by
- 94
- References
- 90
- Citations by year
- 2026: 4 · 2025: 12 · 2024: 11 · 2023: 6 · 2022: 10 · 2021: 3 · 2020: 2 · 2019: 6 · 2018: 6 · 2017: 6 · 2016: 4 · 2015: 1 · 2014: 5 · 2013: 1 · 2012: 3
- FWCI
- 0.31
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Drugs & Aging (publishedVersion)
- PubMed (publishedVersion)
- 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
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, Alzheimer's disease, amyloid-beta oligomers, fibrillar amyloid-beta, soluble amyloid-beta, synaptic function, oxidative stress, neuroprotection, anti-amyloid therapy, clinical trial safety
- MeSH terms
- Alzheimer Disease, Animals, Brain, Humans, Amyloid beta-Peptides, Drug-Related Side Effects and Adverse Reactions
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- Bishop, G. M., & Robinson, S. R. (2004). Physiological Roles of Amyloid-?? and Implications for its Removal in Alzheimer???s Disease. Drugs & Aging. https://doi.org/10.2165/00002512-200421100-00001
