Alzheimer's Disease and Transmissible Virus Dementia (Creutzfeldt‐Jakob Disease)
Open accessAbstract
Ample justification exists on clinical, pathologic, and biologic grounds for considering a similar pathogenesis for AD and the spongiform virus encephalopathies. However, the crux of the comparison rests squarely on results of attempts to transmit AD to experimental animals, and these results have not as yet validated a common etiology. Investigations of the biologic similarities between AD and the spongiform virus encephalopathies proceed in several laboratories, and our own observation of inoculated animals will be continued in the hope that incubation periods for AD may be even longer than those of CJD.
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Pathologic similarities with prion disease suggest that the formation and spread of proteinaceous lesions might involve a common molecular mechanism, corruptive protein templating.
“Pathologic similarities with prion disease suggest that the formation and spread of these proteinaceous lesions might involve a common molecular mechanism – corruptive protein templating.”
From Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders (2011) · cites this paper as [1]
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Flagged first, then by citations
Research works printed but not linked: 2
- PERRY, E.K., P. H. GOBSON, G . BLESSED, R.H. PERRY k B.E TOMLINSON. 1977. 17496632, 1982, 1, · DOI
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Cited by
Sorted by citations
Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622 · see citing works
“Several lines of evidence49-52 collectively argue that aggregated Aβ in the brain extract is critical for in vivo seeding: (1) The extract is able to seed only if it contains aggregated, human-sequence Aβ; (2) Immunoneutralization/depletion of Aβ in the extract by anti-Aβ antibodies impedes seeding; (3) Seeding of Aβ…”
BackgroundThe Alzheimer’s Disease Mitochondrial Cascade Hypothesis
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100339 · Cited by 562 · see citing works
“Tau, prion, and environmental causes have all been proposed to initiate AD and mediate progression [11,12,13].”
Background
- Authors
- BROWN, P., SALAZAR, A. M., GIBBS, C. J., & GAJDUSEK, D. C.
- Affiliations
- National Institutes of Health (US)
- ORCID
- BROWN, PAUL
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 1982-10
- Volume
- 396
- Issue
- 1
- Pages
- 131-143
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- OpenAlex
- W2049526380
- Cited by
- 43
- References
- 36
- Citations by year
- 2024: 1 · 2019: 1 · 2016: 1 · 2015: 3 · 2013: 2 · 2012: 1
- FWCI
- 1.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Annals of the New York Academy of Sciences (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, Creutzfeldt-Jakob disease, prion disease, prion transmission, pathogenesis, incubation period, etiology
- MeSH terms
- Adult, Aged, Alzheimer Disease, Animals, Autopsy, Biopsy, Brain, Dementia, Female, Humans, Creutzfeldt-Jakob Syndrome, Male, Middle Aged, Primates, Scrapie, Sheep
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