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Saposin proteins: structure, function, and role in human lysosomal storage disorders
Abstract
Saposins are sphingolipid activator proteins, four of which are derived from a single precursor, prosaposin, by proteolytic processing. These small heat‐stable glycoproteins (12–14 kDa) are required for the lysosomal hydrolysis of a variety of sphingolipids. Characterization of these four activator proteins, two of which were recently discovered, and their importance in human health and disease are reviewed in this article.—O'Brien, J. S.; Kishimoto, Y. Saposin proteins: structure, function, and role in human lysosomal storage disorders. FASEB J. 5 : 301–308; 1991.
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Simões, I., & Faro, C. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04136.x · Cited by 298
The lysosomal function of progranulin, a guardian against neurodegeneration
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Lysosomal multienzyme complex: Biochemistry, genetics, and molecular pathophysiology
Pshezhetsky, A. V., & Ashmarina, M. (2001) · Progress in Nucleic Acid Research and Molecular Biology · doi:10.1016/s0079-6603(01)69045-7 · Cited by 131
Hiraiwa, M., Martin, B. M., Kishimoto, Y., Conner, G. E., Tsuji, S., & O'Brien, J. S. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9958 · Cited by 120
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Metadata
- Authors
- O'Brien, J. S., & Kishimoto, Y.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1991-03
- Volume
- 5
- Issue
- 3
- Pages
- 301-308
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2116966882
- Cited by
- 326
- References
- 0
- FWCI
- 10.53
- Type
- journal article
- Language
- en
- Open access
- closed
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- O'Brien, J. S., & Kishimoto, Y. (1991). Saposin proteins: structure, function, and role in human lysosomal storage disorders. The FASEB Journal. https://doi.org/10.1096/fasebj.5.3.2001789
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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.