The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
The roles of amyloid precursor protein (APP) in neurogenesis: Implications to pathogenesis and therapy of Alzheimer disease
Open accessAbstract
The amyloid-beta (Aβ) peptide is the derivative of amyloid precursor protein (APP) generated through sequential proteolytic processing by β- and γ-secretases. Excessive accumulation of Aβ, the main constituent of amyloid plaques, has been implicated in the etiology of Alzheimer's disease (AD). It was found recently that the impairments of neurogenesis in brain were associated with the pathogenesis of AD. Furthermore recent findings implicated that APP could function to influence proliferation of neural progenitor cells (NPC) and might regulate transcriptional activity of various genes. Studies demonstrated that influence of neurogenesis by APP is conferred differently via its two separate domains, soluble secreted APPs (sAPPs, mainly sAPPα) and APP intracellular domain (AICD). The sAPPα was shown to be neuroprotective and important to neurogenesis, whereas AICD was found to negatively modulate neurogenesis. Furthermore, it was demonstrated recently that microRNA could function to regulate APP expression, APP processing, Aβ accumulation and subsequently influence neurotoxicity and neurogenesis related to APP, which was implicated to AD pathogenesis, especially for sporadic AD. Based on data accumulated, secretase balances were proposed. These secretase balances could influence the downstream balance related to regulation of neurogenesis by AICD and sAPPα as well as balance related to influence of neuron viability by Aβ and sAPPα. Disruption of these secretase balances could be culprits to AD onset.
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedThe 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
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
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · cited 2×
“In the brain, β-site APP cleaving enzyme (BACE1) has been found to be the major β-secretase.(38) In the alternative non-amyloidogenic pathway, APP could also be proteolytically processed by a presenilin-containing α-secretase complex, which cleaves at a site within Aβ sequence and consequently abrogates Aβ formation.”
BackgroundKuhn, H., Dickinson-Anson, H., & Gage, F. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-06-02027.1996 · Cited by 3,139
Candidate gene for the chromosome 1 familial Alzheimer’s disease locus
Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821
Nonsteroidal Antiinflammatory Drugs and the Risk of Alzheimer's Disease
in 't Veld, B. A., Ruitenberg, A., Hofman, A., Launer, L. J., van Duijn, C. M., Stijnen, T., Breteler, M. M. B., & Stricker, B. H. C. (2001) · New England Journal of Medicine · doi:10.1056/nejmoa010178 · Cited by 1,196
A microRNA array reveals extensive regulation of microRNAs during brain development
KRICHEVSKY, A. M., KING, K. S., DONAHUE, C. P., KHRAPKO, K., & KOSIK, K. S. (2003) · RNA · doi:10.1261/rna.5980303 · Cited by 1,040
Cited by
Fricker, M., Tolkovsky, A. M., Borutaite, V., Coleman, M., & Brown, G. C. (2018) · Physiological Reviews · doi:10.1152/physrev.00011.2017 · Cited by 1,108
Maarouf, C. L., Kokjohn, T. A., Whiteside, C. M., Macias, M. P., Kalback, W. M., Sabbagh, M. N., Beach, T. G., Vassar, R., & Roher, A. E. (2013) · Biochemistry Insights · doi:10.4137/bci.s13025 · Cited by 60
Zhang, J., Feng, X., Wu, J., Xu, H., Li, G., Zhu, D., Yue, Q., Liu, H., Zhang, Y., Sun, D., et al. (2014) · BioFactors · doi:10.1002/biof.1149 · Cited by 50
Reelin links Apolipoprotein E4, Tau, and Amyloid‐β in Alzheimer’s disease
Yi, L. X., Zeng, L., Wang, Q., Tan, E. K., & Zhou, Z. D. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102339 · Cited by 41
Self-citationChe, H., Sun, L.-H., Guo, F., Niu, H.-F., Su, X.-L., Bao, Y.-N., Fu, Z. D., Liu, H.-L., Hou, X., Yang, B.-F., et al. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356646 · Cited by 35
Metadata
- Authors
- Zhou, Z.-D., Chan, C. H.-S., Ma, Q.-H., Xu, X.-H., Xiao, Z.-C., & Tan, E.-K.
- Venue
- Cell Adhesion & Migration
- Publisher
- Informa UK Limited
- Published
- 2011-07
- Volume
- 5
- Issue
- 4
- Pages
- 280-292
- ISSN
- 1933-6918 (ISSN-L)
- 1933-6926
- OpenAlex
- W1968660802
- Cited by
- 162
- References
- 23
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- gold
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- Zhou, Z.-D., Chan, C. H.-S., Ma, Q.-H., Xu, X.-H., Xiao, Z.-C., & Tan, E.-K. (2011). The roles of amyloid precursor protein (APP) in neurogenesis: Implications to pathogenesis and therapy of Alzheimer disease. Cell Adhesion & Migration. https://doi.org/10.4161/cam.5.4.16986
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
