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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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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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Presenilin-1, Nicastrin, Amyloid Precursor Protein, and γ-Secretase Activity Are Co-localized in the Lysosomal Membrane

The Journal of biological chemistry, 2003-07, Vol.278 (29), p.26687-26694

2003

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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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Nicastrin Is Critical for Stability and Trafficking but Not Association of Other Presenilin/γ-Secretase Components

The Journal of biological chemistry, 2005-04, Vol.280 (17), p.17020-17026

2005

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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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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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Functional γ-secretase complex assembly in Golgi/ trans-Golgi network: interactions among presenilin, nicastrin, Aph1, Pen-2, and γ-secretase substrates

Neurobiology of disease, 2003-11, Vol.14 (2), p.194-204

2003

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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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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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Amyloid precursor protein (APP) and the biology of proteolytic processing: relevance to Alzheimer’s disease

International Journal of Biochemistry and Cell Biology, 2003-11, Vol.35 (11), p.1505-1535

2003

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The Transmembrane Domain Region of Nicastrin Mediates Direct Interactions with APH-1 and the γ-Secretase Complex

The Journal of biological chemistry, 2003-10, Vol.278 (44), p.43284-43291

2003

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A Conserved GXXXG Motif in APH-1 Is Critical for Assembly and Activity of the γ-Secretase Complex

The Journal of biological chemistry, 2004-02, Vol.279 (6), p.4144-4152

2004

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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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Presenilins and γ-Secretase Inhibitors Affect Intracellular Trafficking and Cell Surface Localization of the γ-Secretase Complex Components

The Journal of biological chemistry, 2004-09, Vol.279 (39), p.40560-40566

2004

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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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Nicastrin Interacts with γ-Secretase Complex Components via the N-terminal Part of Its Transmembrane Domain

The Journal of biological chemistry, 2003-12, Vol.278 (52), p.52519-52523

2003

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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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Overexpression of calsenilin enhances γ-secretase activity

Neuroscience letters, 2005-04, Vol.378 (1), p.59-64

2005

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Localization of presenilin–nicastrin complexes and γ‐secretase activity to the trans‐Golgi network

Journal of neurochemistry, 2003-03, Vol.84 (5), p.1143-1153

2003

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Gamma-secretase subunit composition and distribution in the presenilin wild-type and mutant mouse brain

Neuroscience, 2004, Vol.129 (3), p.615-628

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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Characterization of presenilin complexes from mouse and human brain using Blue Native gel electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with pathogenic presenilin mutations

European journal of biochemistry, 2004-01, Vol.271 (2), p.375-385

2004

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

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

Presenilin-1, Nicastrin, Amyloid Precursor Protein, and γ-Secretase Activity Are Co-localized in the Lysosomal Membrane

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

Nicastrin Is Critical for Stability and Trafficking but Not Association of Other Presenilin/γ-Secretase Components

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

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

Functional γ-secretase complex assembly in Golgi/ trans-Golgi network: interactions among presenilin, nicastrin, Aph1, Pen-2, and γ-secretase substrates

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

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

Amyloid precursor protein (APP) and the biology of proteolytic processing: relevance to Alzheimer’s disease

The Transmembrane Domain Region of Nicastrin Mediates Direct Interactions with APH-1 and the γ-Secretase Complex

A Conserved GXXXG Motif in APH-1 Is Critical for Assembly and Activity of the γ-Secretase Complex

Membrane Topology of γ-Secretase Component PEN-2

Presenilins and γ-Secretase Inhibitors Affect Intracellular Trafficking and Cell Surface Localization of the γ-Secretase Complex Components

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

Nicastrin Interacts with γ-Secretase Complex Components via the N-terminal Part of Its Transmembrane Domain

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

Overexpression of calsenilin enhances γ-secretase activity

Localization of presenilin–nicastrin complexes and γ‐secretase activity to the trans‐Golgi network

Gamma-secretase subunit composition and distribution in the presenilin wild-type and mutant mouse brain

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

Characterization of presenilin complexes from mouse and human brain using Blue Native gel electrophoresis reveals high expression in embryonic brain and minimal change in complex mobility with pathogenic presenilin mutations

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