Mutation Analysis of the Presenilin 1 N-terminal Domain Reveals a Broad Spectrum of γ-Secretase Activity toward Amyloid Precursor Protein and Other Substrates

The Large Hydrophilic Loop of Presenilin 1 Is Important for Regulating γ-Secretase Complex Assembly and Dictating the Amyloid β Peptide (Aβ) Profile without Affecting Notch Processing

(2010) Johanna Wanngren et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

 -Secretase Composed of PS1/Pen2/Aph1a Can Cleave Notch and Amyloid Precursor Protein in the Absence of Nicastrin

(2010) G. Zhao et al.   JOURNAL OF NEUROSCIENCE

Nicastrin Is Dispensable for γ-Secretase Protease Activity in the Presence of Specific Presenilin Mutations

(2009) Eugene Futai et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Catalytic Core of γ-Secretase: Presenilin Revisited

(2008) Harald Steiner   Current Alzheimer Research

S-Palmitoylation of γ-Secretase Subunits Nicastrin and APH-1

(2008) Haipeng Cheng et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Transmembrane Domain 9 of Presenilin Determines the Dynamic Conformation of the Catalytic Site of γ-Secretase

(2008) Alexandra Tolia et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Amyloid Precursor Protein Trafficking, Processing, and Function

(2008) Gopal Thinakaran et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Building γ-secretase – the bits and pieces

(2008) Dragana Spasic et al.   JOURNAL OF CELL SCIENCE

The C-Terminal PAL Motif and Transmembrane Domain 9 of Presenilin 1 Are Involved in the Formation of the Catalytic Pore of the  -Secretase

(2008) C. Sato et al.   JOURNAL OF NEUROSCIENCE