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The Journal of Biological Chemistry|March 7, 1998
The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complexA Capell, J Grünberg, B Pesold, et al.Journal of Neurochemistry|December 31, 1997
Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiationA Capell, R Saffrich, J C Olivo, et al.Journal of Neural Transmission. Supplementum|August 13, 1998
Proteolytic processing of Alzheimer's disease associated proteinsC Haass, J Grünberg, A Capell, et al.Proceedings of the National Academy of Sciences of the United States of America|May 13, 1997
Proteolytic processing of the Alzheimer disease-associated presenilin-1 generates an in vivo substrate for protein kinase CJ Walter, J Grünberg, A Capell, et al.Molecular Medicine (Cambridge, Mass.)|November 1, 1996
The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulumJ Walter, A Capell, J Grünberg, et al.Proceedings of the National Academy of Sciences of the United States of America|March 4, 1997
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) residueT Tomita, K Maruyama, T C Saido, et al.Journal of Neurochemistry|July 2, 1998
Mutant presenilin 2 transgenic mouse: effect on an age-dependent increase of amyloid beta-protein 42 in the brainF Oyama, N Sawamura, K Kobayashi, et al.Pageof 3