The DOI matches its Crossref record; 198 of the 198 references it cites were found in a registry or an index.
Insights into the physiological function of the β‐amyloid precursor protein: beyond Alzheimer's disease
Open accessAbstract
The β‐amyloid precursor protein (APP) has been extensively studied for its role as the precursor of the β‐amyloid protein (Aβ) of Alzheimer's disease. However, the normal function of APP remains largely unknown. This article reviews studies on the structure, expression and post‐translational processing of APP, as well as studies on the effects of APP in vitro and in vivo. We conclude that the published data provide strong evidence that APP has a trophic function. APP is likely to be involved in neural stem cell development, neuronal survival, neurite outgrowth and neurorepair. However, the mechanisms by which APP exerts its actions remain to be elucidated. The available evidence suggests that APP interacts both intracellularly and extracellularly to regulate various signal transduction mechanisms. image This article reviews studies on the structure, expression and post‐translational processing of β‐amyloid precursor protein (APP), as well as studies on the effects of APP in vitro and in vivo. We conclude that the published data provide strong evidence that APP has a trophic function. APP is likely to be involved in neural stem cell development, neuronal survival, neurite outgrowth and neurorepair. However, the mechanisms by which APP exerts its actions remain to be elucidated. The available evidence suggests that APP interacts both intracellularly and extracellularly to regulate various signal transduction mechanisms.
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1 retracted
RETRACTED ARTICLE: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
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RetractedCell Signaling by Receptor Tyrosine Kinases
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“The b-secretase has been identified as a type 1 transmembrane aspartyl protease termed the b-site APP-cleaving enzyme 1 (BACE 1) (Hussain et al. 1999; Sinha et al. 1999; Vassar et al. 1999; Yan et al. 1999; Lin et al. 2000).”
BackgroundA presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
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Cited by
Clearance systems in the brain—implications for Alzheimer disease
Tarasoff-Conway, J. M., Carare, R. O., Osorio, R. S., Glodzik, L., Butler, T., Fieremans, E., Axel, L., Rusinek, H., Nicholson, C., Zlokovic, B. V., et al. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.119 · Cited by 1,678
Not just amyloid: physiological functions of the amyloid precursor protein family
Müller, U. C., Deller, T., & Korte, M. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.29 · Cited by 634
Neuroprotective Effects of Quercetin in Alzheimer’s Disease
Khan, H., Ullah, H., Aschner, M., Cheang, W. S., & Akkol, E. K. (2019) · Biomolecules · doi:10.3390/biom10010059 · Cited by 537
Practical considerations for choosing a mouse model of Alzheimer’s disease
Jankowsky, J. L., & Zheng, H. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0231-7 · Cited by 449
Dementia in Down syndrome: unique insights for Alzheimer disease research
Lott, I. T., & Head, E. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0132-6 · Cited by 383
Metadata
- Authors
- Dawkins, E., & Small, D. H.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2014-03-07
- Volume
- 129
- Issue
- 5
- Pages
- 756-769
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2001445086
- Cited by
- 279
- References
- 198
- FWCI
- 14.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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