Abstract
Amyloid ß protein in Alzheimer’s brain is a cleavage product of the precursor protein (BPP). The sequence analysis of its BPP cDNA showed that BPP resembles a cell-surface receptor (Kang et al., 1987) and that there are three types of BPP mRNA generated by alternative splicing, two of which encode a serine-protease inhibitor (serpin) domain (Kitaguchi et al., 1988, Ponte et al., 1988, Tanzi et al, 1988).
Keywords
- Alternative Splice
- Splice Acceptor Site
- Amyloid Protein Precursor mRNA
- Protease Inhibitor Domain
- Human Genomic Library
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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© 1990 Plenum Press, New York
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Yoshikai, Si., Sasaki, H., Doh-ura, K., Furuya, H., Sakaki, Y. (1990). Molecular Cloning and Structural Analysis of the Human Amyloid ß Protein Precursor Gene. In: Nagatsu, T., Fisher, A., Yoshida, M. (eds) Basic, Clinical, and Therapeutic Aspects of Alzheimer’s and Parkinson’s Diseases. Advances in Behavioral Biology, vol 38A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5844-2_10
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DOI: https://doi.org/10.1007/978-1-4684-5844-2_10
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