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Take five-BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation

The EMBO journal, 2004-02, Vol.23 (3), p.483-488

Haass, Christian

2004

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A Nine-transmembrane Domain Topology for Presenilin 1

The Journal of biological chemistry, 2005-10, Vol.280 (42), p.35352-35360

2005

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Transmembrane Protein 147 (TMEM147) Is a Novel Component of the Nicalin-NOMO Protein Complex

The Journal of biological chemistry, 2010-08, Vol.285 (34), p.26174-26181

2010

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Assembly of the γ-Secretase Complex Involves Early Formation of an Intermediate Subcomplex of Aph-1 and Nicastrin

The Journal of biological chemistry, 2003-09, Vol.278 (39), p.37213-37222

2003

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Requirement of PEN-2 for Stabilization of the Presenilin N-/C-terminal Fragment Heterodimer within the γ-Secretase Complex

The Journal of biological chemistry, 2004-05, Vol.279 (22), p.23255-23261

2004

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Pen-2 Is Sequestered in the Endoplasmic Reticulum and Subjected to Ubiquitylation and Proteasome-mediated Degradation in the Absence of Presenilin

The Journal of biological chemistry, 2004-04, Vol.279 (16), p.16744-16753

2004

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Aph-1 Contributes to the Stabilization and Trafficking of the γ-Secretase Complex through Mechanisms Involving Intermolecular and Intramolecular Interactions

The Journal of biological chemistry, 2005-04, Vol.280 (13), p.12967-12975

2005

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Down-regulation of Endogenous Amyloid Precursor Protein Processing due to Cellular Aging

The Journal of biological chemistry, 2006-02, Vol.281 (5), p.2405-2413

2006

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Evidence That the “NF” Motif in Transmembrane Domain 4 of Presenilin 1 Is Critical for Binding with PEN-2

The Journal of biological chemistry, 2005-12, Vol.280 (51), p.41953-41966

2005

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Identity and function of γ-secretase

Journal of neuroscience research, 2003-11, Vol.74 (3), p.353-360

2003

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A Sequence within the First Transmembrane Domain of PEN-2 Is Critical for PEN-2-mediated Endoproteolysis of Presenilin 1

The Journal of biological chemistry, 2005-01, Vol.280 (3), p.1992-2001

2005

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Membrane Topology of γ-Secretase Component PEN-2

The Journal of biological chemistry, 2003-05, Vol.278 (22), p.20117-20123

2003

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Conserved “PAL” sequence in presenilins is essential for γ-secretase activity, but not required for formation or stabilization of γ-secretase complexes

Neurobiology of disease, 2004-04, Vol.15 (3), p.654-666

2004

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Presenilin endoproteolysis mediated by an aspartyl protease activity pharmacologically distinct from γ‐secretase

Journal of neurochemistry, 2003-06, Vol.85 (6), p.1563-1574

2003

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Co-expression of Nicastrin and Presenilin Rescues a Loss of Function Mutant of APH-1

The Journal of biological chemistry, 2004-09, Vol.279 (36), p.37311-37315

2004

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APP processing enzymes (secretases) as therapeutic targets: insights from the use of transgenics (Tgs) and transfected cells

Neurochemical research, 2003-07, Vol.28 (7), p.1049-1062

2003

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Take five-BACE and the γ-secretase quartet conduct Alzheimer's amyloid β-peptide generation

A Nine-transmembrane Domain Topology for Presenilin 1

Transmembrane Protein 147 (TMEM147) Is a Novel Component of the Nicalin-NOMO Protein Complex

Assembly of the γ-Secretase Complex Involves Early Formation of an Intermediate Subcomplex of Aph-1 and Nicastrin

Requirement of PEN-2 for Stabilization of the Presenilin N-/C-terminal Fragment Heterodimer within the γ-Secretase Complex

Pen-2 Is Sequestered in the Endoplasmic Reticulum and Subjected to Ubiquitylation and Proteasome-mediated Degradation in the Absence of Presenilin

Aph-1 Contributes to the Stabilization and Trafficking of the γ-Secretase Complex through Mechanisms Involving Intermolecular and Intramolecular Interactions

Down-regulation of Endogenous Amyloid Precursor Protein Processing due to Cellular Aging

Evidence That the “NF” Motif in Transmembrane Domain 4 of Presenilin 1 Is Critical for Binding with PEN-2

Identity and function of γ-secretase

A Sequence within the First Transmembrane Domain of PEN-2 Is Critical for PEN-2-mediated Endoproteolysis of Presenilin 1

Membrane Topology of γ-Secretase Component PEN-2

Conserved “PAL” sequence in presenilins is essential for γ-secretase activity, but not required for formation or stabilization of γ-secretase complexes

Presenilin endoproteolysis mediated by an aspartyl protease activity pharmacologically distinct from γ‐secretase

Co-expression of Nicastrin and Presenilin Rescues a Loss of Function Mutant of APH-1

APP processing enzymes (secretases) as therapeutic targets: insights from the use of transgenics (Tgs) and transfected cells

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