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The presenilin 2 mutation (N141I) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue.
Tomita T, Maruyama K, Saido TC, Kume H, Shinozaki K, Tokuhiro S, Capell A, Walter J, Grünberg J, Haass C, Iwatsubo T, Obata K. Tomita T, et al. Among authors: haass c. Proc Natl Acad Sci U S A. 1997 Mar 4;94(5):2025-30. doi: 10.1073/pnas.94.5.2025. Proc Natl Acad Sci U S A. 1997. PMID: 9050898 Free PMC article.
Presenilins are processed by caspase-type proteases.
Loetscher H, Deuschle U, Brockhaus M, Reinhardt D, Nelboeck P, Mous J, Grünberg J, Haass C, Jacobsen H. Loetscher H, et al. Among authors: haass c. J Biol Chem. 1997 Aug 15;272(33):20655-9. doi: 10.1074/jbc.272.33.20655. J Biol Chem. 1997. PMID: 9252383 Free article.
The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex.
Capell A, Grünberg J, Pesold B, Diehlmann A, Citron M, Nixon R, Beyreuther K, Selkoe DJ, Haass C. Capell A, et al. Among authors: haass c. J Biol Chem. 1998 Feb 6;273(6):3205-11. doi: 10.1074/jbc.273.6.3205. J Biol Chem. 1998. PMID: 9452432 Free article.
PS-1 proteins are proteolytically processed by an unknown protease to two stable fragments of approximately 30 kDa (N-terminal fragment (NTF)) and approximately 20 kDa (C-terminal fragment (CTF)) (Thinakaran, G., Borchelt, D. R., Lee, M. K., Slunt, H. H., Spitzer, L., Kim, …
PS-1 proteins are proteolytically processed by an unknown protease to two stable fragments of approximately 30 kDa (N-terminal fragment (NTF …
470 results