title: Presenilins are required for gamma-secretase cleavage of beta-APP and transmembrane cleavage of Notch-1.
authors.affiliation: Department of Neurology, Harvard Medical School and Division of Neuroscience, Children's Hospital, Boston, MA 02115, USA.
authors.forename: Z
authors.initials: Z
authors.lastname: Zhang
authors.forename: P
authors.initials: P
authors.lastname: Nadeau
authors.forename: W
authors.initials: W
authors.lastname: Song
authors.forename: D
authors.initials: D
authors.lastname: Donoviel
authors.forename: M
authors.initials: M
authors.lastname: Yuan
authors.forename: A
authors.initials: A
authors.lastname: Bernstein
authors.forename: B A
authors.initials: BA
authors.lastname: Yankner
mesh_terms: D053829:Amyloid Precursor Protein Secretases; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism; D016564:Amyloid beta-Protein Precursor / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002478:Cells, Cultured; D010450:Endopeptidases / Q000378:metabolism*; D017353:Gene Deletion; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D018345:Mice, Knockout; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D053764:Presenilin-1; D053766:Presenilin-2; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D051881:Receptor, Notch1; D011956:Receptors, Cell Surface; D014157:Transcription Factors; D014162:Transfection
chemical_list: D016229:Amyloid beta-Peptides; D016564:Amyloid beta-Protein Precursor; D008565:Membrane Proteins; C497762:Notch1 protein, mouse; D010446:Peptide Fragments; D053764:Presenilin-1; D053766:Presenilin-2; D051881:Receptor, Notch1; D011956:Receptors, Cell Surface; D014157:Transcription Factors; D053829:Amyloid Precursor Protein Secretases; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C509282:Bace1 protein, mouse