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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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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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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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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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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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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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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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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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γ-Secretase Exists on the Plasma Membrane as an Intact Complex That Accepts Substrates and Effects Intramembrane Cleavage

The Journal of biological chemistry, 2005-02, Vol.280 (6), p.4383-4392

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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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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γ-Secretase Activity Is Associated with a Conformational Change of Nicastrin

The Journal of biological chemistry, 2003-05, Vol.278 (19), p.16474-16477

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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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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γ-Secretase Complex Assembly within the Early Secretory Pathway

The Journal of biological chemistry, 2005-02, Vol.280 (8), p.6471-6478

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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Overexpression of calsenilin enhances γ-secretase activity

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

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

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

A Nine-transmembrane Domain Topology for Presenilin 1

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

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

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

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

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

γ-Secretase Exists on the Plasma Membrane as an Intact Complex That Accepts Substrates and Effects Intramembrane Cleavage

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

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

γ-Secretase Activity Is Associated with a Conformational Change of Nicastrin

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

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

γ-Secretase Complex Assembly within the Early Secretory Pathway

Identity and function of γ-secretase

Overexpression of calsenilin enhances γ-secretase activity

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

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

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

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