The DOI matches its Crossref record; 80 of the 80 references it cites were found in a registry or an index.
Alzheimer's Disease
Open accessAbstract
Over the last three decades, advances in biochemical pathology and human genetics have illuminated one of the most enigmatic subjects in biomedicine--neurodegeneration. Eponymic diseases of the nervous system such as Alzheimer's, Parkinson's, and Huntington's diseases that were long characterized by mechanistic ignorance have yielded striking progress in our understanding of their molecular underpinnings. A central theme in these and related disorders is the concept that certain normally soluble neuronal proteins can misfold and aggregate into oligomers and amyloid fibrils which can confer profound cytotoxicity. Perhaps the foremost example, both in terms of its societal impact and how far knowledge has moved toward the clinic, is that of Alzheimer's disease (AD). Here, we will review the classical protein lesions of the disorder that have provided a road map to etiology and pathogenesis. We will discuss how elucidating the genotype-to-phenotype relationships of familial forms of Alzheimer's disease has highlighted the importance of the misfolding and altered proteostasis of two otherwise soluble proteins, amyloid β-protein and tau, suggesting mechanism-based therapeutic targets that have led to clinical trials.
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Self-citationImmunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
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Cited by
Astrocyte contribution to dysfunction, risk and progression in neurodegenerative disorders
Brandebura, A. N., Paumier, A., Onur, T. S., & Allen, N. J. (2023) · Nature Reviews Neuroscience · doi:10.1038/s41583-022-00641-1 · Cited by 427
A Human Stem Cell Model of Early Alzheimer’s Disease Pathology in Down Syndrome
Shi, Y., Kirwan, P., Smith, J., MacLean, G., Orkin, S. H., & Livesey, F. J. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003771 · Cited by 310
Mechanisms of secretion and spreading of pathological tau protein
Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304
Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins
Ciryam, P., Tartaglia, G. G., Morimoto, R. I., Dobson, C. M., & Vendruscolo, M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.043 · Cited by 270
Gender, sex steroid hormones, and Alzheimer’s disease
Vest, R. S., & Pike, C. J. (2013) · Hormones and Behavior · doi:10.1016/j.yhbeh.2012.04.006 · Cited by 260
Metadata
- Authors
- Selkoe, D. J.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-05-16
- Volume
- 3
- Issue
- 7
- Pages
- a004457-a004457
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W4231182105
- Cited by
- 363
- References
- 80
- Type
- posted content
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.