title: Sorting Out Presenilins in Alzheimer's Disease.
abstract: Mutations in the presenilins that cause familial Alzheimer's disease alter the activity of these proteases to increase generation of an aggregation-prone isoform of the amyloid β-peptide (Aβ). How these mutations do so has been unclear. Sannerud et al. now show that regulation of subcellular localization plays a central role, advancing our understanding of the cell biology of Alzheimer's disease.
authors.affiliation: Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital, Boston, MA 02115, USA. Electronic address: mswolfe@partners.org.
authors.forename: Michael S
authors.initials: MS
authors.lastname: Wolfe
authors.affiliation: Department of Genetics, Harvard Medical School, Boston, MA 02115, USA. Electronic address: bruce_yankner@hms.harvard.edu.
authors.forename: Bruce A
authors.initials: BA
authors.lastname: Yankner
mesh_terms: D000544:Alzheimer Disease / Q000235:genetics*; D053829:Amyloid Precursor Protein Secretases / Q000235:genetics; D016229:Amyloid beta-Peptides / Q000235:genetics; D016564:Amyloid beta-Protein Precursor / Q000235:genetics; D006801:Humans; D053763:Presenilins / Q000235:genetics*; D021381:Protein Transport
chemical_list: D016229:Amyloid beta-Peptides; D016564:Amyloid beta-Protein Precursor; D053763:Presenilins; D053829:Amyloid Precursor Protein Secretases