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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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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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Presenilins Mutated at Asp-257 or Asp-385 Restore Pen-2 Expression and Nicastrin Glycosylation but Remain Catalytically Inactive in the Absence of Wild Type Presenilin

The Journal of biological chemistry, 2003-10, Vol.278 (44), p.43430-43436

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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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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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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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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Expression profiles of two human APH-1 genes and their roles in formation of presenilin complexes

Biochemical and biophysical research communications, 2005-02, Vol.327 (1), p.18-22

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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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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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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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

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

Presenilins Mutated at Asp-257 or Asp-385 Restore Pen-2 Expression and Nicastrin Glycosylation but Remain Catalytically Inactive in the Absence of Wild Type Presenilin

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

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

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

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

Expression profiles of two human APH-1 genes and their roles in formation of presenilin complexes

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

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

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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