The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation
Open accessAbstract
β-amyloid protein (Aβ) formation was reconstituted in permeabilized neuroblastoma cells expressing human Alzheimer β-amyloid precursor protein (βAPP) harboring the Swedish double mutation associated with familial early-onset Alzheimer disease. Permeabilized cells were prepared following metabolic labeling and incubation at 20°C, a temperature that allows βAPP to accumulate in the trans-Golgi network (TGN) without concomitant Aβ formation. Subsequent incubation at 37°C led to the generation of Aβ. Aβ production in the TGN persisted even under conditions in which formation of nascent post-TGN vesicles was inhibited by addition of guanosine 5′- O -(3-thiotriphosphate), a nonhydrolyzable GTP analogue, or by omission of cytosol. These and other results indicate that vesicle budding and trafficking may not be required for proteolytic metabolism of βAPP to Aβ, a process that includes “γ-secretase” cleavage within the βAPP transmembrane domain.
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Cites
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
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
Haass, C., Lemere, C. A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L., & Selkoe, D. J. (1995) · Nature Medicine · doi:10.1038/nm1295-1291 · Cited by 592
Metabolism of the “Swedish” Amyloid Precursor Protein Variant in Neuro2a (N2a) Cells
Thinakaran, G., Teplow, D. B., Siman, R., Greenberg, B., & Sisodia, S. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9390 · Cited by 317
Self-citation
Cited by
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991
Self-citationAPP processing in Alzheimer’s disease.
Zhang, Y.-W., Thompson, R., Zhang, H., & Xu, H. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-3 · Cited by 983
Self-citationStamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885
Cataldo, A. M., Peterhoff, C. M., Troncoso, J. C., Gomez-Isla, T., Hyman, B. T., & Nixon, R. A. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64538-5 · Cited by 776
Kamal, A., Almenar-Queralt, A., LeBlanc, J. F., Roberts, E. A., & Goldstein, L. S. B. (2001) · Nature · doi:10.1038/414643a · Cited by 583
Metadata
- Authors
- Xu, H., Sweeney, D., Wang, R., Thinakaran, G., Lo, A. C. Y., Sisodia, S. S., Greengard, P., & Gandy, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-04-15
- Volume
- 94
- Issue
- 8
- Pages
- 3748-3752
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2074438246
- Cited by
- 282
- References
- 5
- FWCI
- 7.85
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Xu, H., Sweeney, D., Wang, R., Thinakaran, G., Lo, A. C. Y., Sisodia, S. S., Greengard, P., & Gandy, S. (1997). Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.8.3748
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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.
