The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Normal and Abnormal Biology of the beta-Amyloid Precursor Protein
Abstract
Few macromolecules have become the object of more intense chemical and biological scrutiny in recent years than has the l3-amyloid precursor protein. This highly conserved and widely expressed integral membrane protein is the focus of a rapidly growing number of studies aimed at its characterization by protein chemical, molecular biological , cell biological , and neuroanatomical methods. The principal reason for this attention is clear. The early promise that a 39-43 residue fragment of I3APP, the amyloid l3-protein (AI3), might play a central role in the pathogenesis of Alzheimer's disease has increasingly been borne out. Although there is still substantial debate about exactly when AI3 becomes involved in Alzheimer's disease and how attractive a therapeutic target it represents , accumulating evidence now points to an early and sometimes causative role in the pathogenetic cascade. I3APP has become a compelling example of the phenomenon of research that begins with a strictly disease-oriented focus giving rise to novel insights about the normal biology of a whole family of macromolecules, in this case about the processing of certain cell surface, single membrane-spanning polypeptides. Here, I review recent information about the normal structure and function of I3APP and how its AI3 fragment contributes to Alzheimer's disease. Such
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Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Self-citationBrain interleukin 1 and S-100 immunoreactivity are elevated in Down syndrome and Alzheimer disease.
Griffin, W. S., Stanley, L. C., Ling, C., White, L., MacLeod, V, Perrot, L. J., White, C. L., & Araoz, C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.19.7611 · Cited by 1,777
Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus
Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611
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., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,381
Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity
Kitaguchi, N., Takahashi, Y., Tokushima, Y., Shiojiri, S., & Ito, H. (1988) · Nature · doi:10.1038/331530a0 · Cited by 1,086
A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
Ponte, P., DeWhitt, P. G., Schilling, J., Miller, J., Hsu, D., Greenberg, B., Davis, K., Wallace, W., Lieberburg, I., Fuller, F., et al. (1988) · Nature · doi:10.1038/331525a0 · Cited by 1,052
Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease
KIDD, M. (1963) · Nature · doi:10.1038/197192b0 · Cited by 1,012
Genetic Linkage Evidence for a Familial Alzheimer's Disease Locus on Chromosome 14
Schellenberg, G. D., Bird, T. D., Wijsman, E. M., Orr, H. T., Anderson, L., Nemens, E., White, J. A., Bonnycastle, L., Weber, J. L., Alonso, M. E., et al. (1992) · Science · doi:10.1126/science.1411576 · Cited by 946
Cited by
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
Inflammation as a central mechanism in Alzheimer's disease
Kinney, J. W., Bemiller, S. M., Murtishaw, A. S., Leisgang, A. M., Salazar, A. M., & Lamb, B. T. (2018) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.06.014 · Cited by 2,253
“Ab pathology arises from the improper cleavage of the amyloid precursor protein (APP) resulting in Ab monomers that aggregate forming oligomeric Ab and eventually aggregating into Ab fibrils and plaques [4].”
BackgroundInflammation in obesity, diabetes, and related disorders
Rohm, T. V., Meier, D. T., Olefsky, J. M., & Donath, M. Y. (2022) · Immunity · doi:10.1016/j.immuni.2021.12.013 · Cited by 2,066
Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
Yu, G., Nishimura, M., Arawaka, S., Levitan, D., Zhang, L., Tandon, A., Song, Y.-Q., Rogaeva, E., Chen, F., Kawarai, T., et al. (2000) · Nature · doi:10.1038/35024009 · Cited by 911
Metadata
- Authors
- Selkoe, D. J.
- Venue
- Annual Review of Neuroscience
- Publisher
- Annual Reviews
- Published
- 1994-03
- Volume
- 17
- Issue
- 1
- Pages
- 489-517
- ISSN
- 0147-006X (ISSN-L)
- 1545-4126
- OpenAlex
- W2162059739
- Cited by
- 818
- References
- 49
- FWCI
- 43.12
- Type
- journal article
- Language
- en
- Open access
- closed
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- Selkoe, D. J. (1994). Normal and Abnormal Biology of the beta-Amyloid Precursor Protein. Annual Review of Neuroscience. https://doi.org/10.1146/annurev.ne.17.030194.002421
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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.
