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The Impact of Inherited Retinal Diseases in the United States of America (US) and Canada from a Cost-of-Illness Perspective

Clinical ophthalmology (Auckland, N.Z.), 2021-01, Vol.15, p.2855-2866

2021

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Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1

Nature (London), 2000-06, Vol.405 (6787), p.689-694

2000

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Selected non-steroidal anti-inflammatory drugs and their derivatives target gamma-secretase at a novel site. Evidence for an allosteric mechanism

The Journal of biological chemistry, 2004-10, Vol.279 (42), p.43419-43426

2004

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L-685,458, an Aspartyl Protease Transition State Mimic, Is a Potent Inhibitor of Amyloid β-Protein Precursor γ-Secretase Activity

Biochemistry (Easton), 2000-08, Vol.39 (30), p.8698-8704

2000

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Presenilin-Dependent γ-Secretase Activity Modulates Thymocyte Development

Proceedings of the National Academy of Sciences - PNAS, 2001-07, Vol.98 (16), p.9312-9317

2001

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Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated protein complex: implications for schizophrenia and other major neurological disorders

Molecular and cellular neuroscience, 2004-01, Vol.25 (1), p.42-55

2004

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C‐terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation

Journal of neurochemistry, 2006-01, Vol.96 (1), p.218-227

2006

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Quantification of Alzheimer pathology in ageing and dementia: age-related accumulation of amyloid-β(42) peptide in vascular dementia

Neuropathology and applied neurobiology, 2006-04, Vol.32 (2), p.103-118

2006

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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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The toxicity in vitro of beta-amyloid protein

Biochemical journal, 1995-10, Vol.311 ( Pt 1) (1), p.1-16

1995

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Generation of C‐terminally truncated amyloid‐β peptides is dependent on γ‐secretase activity

Journal of neurochemistry, 2002-08, Vol.82 (3), p.563-575

2002

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4-Substituted cyclohexyl sulfones as potent, orally active γ-secretase inhibitors

Bioorganic & medicinal chemistry letters, 2006-01, Vol.16 (2), p.280-284

2006

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Catalytic Site-Directed γ-Secretase Complex Inhibitors Do Not Discriminate Pharmacologically between Notch S3 and β-APP Cleavages

Biochemistry (Easton), 2003-06, Vol.42 (24), p.7580-7586

2003

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Subcellular targeting of DISC1 is dependent on a domain independent from the Nudel binding site

Molecular and cellular neuroscience, 2005-04, Vol.28 (4), p.613-624

2005

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In Vitro Characterization of the Presenilin-Dependent γ-Secretase Complex Using a Novel Affinity Ligand

Biochemistry (Easton), 2003-07, Vol.42 (27), p.8133-8142

2003

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Design and Synthesis of Highly Potent Benzodiazepine γ-Secretase Inhibitors: Preparation of (2S,3R)-3-(3,4- Difluorophenyl)-2-(4-fluorophenyl)-4- hydroxy-N-((3S)-1-methyl-2-oxo-5- phenyl-2,3-dihydro-1H-benzo[e][1,4]- diazepin-3-yl)butyramide by Use of an Asymmetric Ireland−Claisen Rearrangement

Journal of medicinal chemistry, 2003-06, Vol.46 (12), p.2275-2278

2003

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The Intramembrane Cleavage Site of the Amyloid Precursor Protein Depends on the Length of Its Transmembrane Domain

Proceedings of the National Academy of Sciences - PNAS, 2002-02, Vol.99 (3), p.1365-1370

2002

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Two domains within the first putative transmembrane domain of presenilin 1 differentially influence presenilinase and γ‐secretase activity

Journal of neurochemistry, 2005-09, Vol.94 (5), p.1315-1328

2005

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Functional Overexpression of γ-Secretase Reveals Protease-independent Trafficking Functions and a Critical Role of Lipids for Protease Activity

The Journal of biological chemistry, 2005-04, Vol.280 (13), p.12523-12535

2005

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Quantitation of amyloid-β peptides in biological milieu using a novel homogeneous time-resolved fluorescence (HTRF) assay

Journal of neuroscience methods, 2000-10, Vol.102 (1), p.61-68

2000

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Determination of guinea-pig cortical γ-secretase activity ex vivo following the systemic administration of a γ-secretase inhibitor

Neuropharmacology, 2005-06, Vol.48 (7), p.1002-1011

2005

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A novel series of potent γ-secretase inhibitors based on a benzobicyclo[4.2.1]nonane core

Bioorganic & medicinal chemistry letters, 2005-01, Vol.15 (2), p.373-378

2005

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Fatty acids increase presenilin-1 levels and γ-secretase activity in PSwt-1 cells

Journal of lipid research, 2004-12, Vol.45 (12), p.2368-2376

2004

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gamma-Secretase cleavage site specificity differs for intracellular and secretory amyloid beta

The Journal of biological chemistry, 2003-04, Vol.278 (15), p.13077-13085

2003

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Modulation of ion channel activity: a key function of the protein kinase C enzyme family

Pharmacological reviews, 1989-06, Vol.41 (2), p.211

1989

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The Impact of Inherited Retinal Diseases in the United States of America (US) and Canada from a Cost-of-Illness Perspective

Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1

Selected non-steroidal anti-inflammatory drugs and their derivatives target gamma-secretase at a novel site. Evidence for an allosteric mechanism

L-685,458, an Aspartyl Protease Transition State Mimic, Is a Potent Inhibitor of Amyloid β-Protein Precursor γ-Secretase Activity

Presenilin-Dependent γ-Secretase Activity Modulates Thymocyte Development

Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated protein complex: implications for schizophrenia and other major neurological disorders

C‐terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation

Quantification of Alzheimer pathology in ageing and dementia: age-related accumulation of amyloid-β(42) peptide in vascular dementia

γ-Secretase Complex Assembly within the Early Secretory Pathway

The toxicity in vitro of beta-amyloid protein

Generation of C‐terminally truncated amyloid‐β peptides is dependent on γ‐secretase activity

4-Substituted cyclohexyl sulfones as potent, orally active γ-secretase inhibitors

Catalytic Site-Directed γ-Secretase Complex Inhibitors Do Not Discriminate Pharmacologically between Notch S3 and β-APP Cleavages

Subcellular targeting of DISC1 is dependent on a domain independent from the Nudel binding site

In Vitro Characterization of the Presenilin-Dependent γ-Secretase Complex Using a Novel Affinity Ligand

Design and Synthesis of Highly Potent Benzodiazepine γ-Secretase Inhibitors: Preparation of (2S,3R)-3-(3,4- Difluorophenyl)-2-(4-fluorophenyl)-4- hydroxy-N-((3S)-1-methyl-2-oxo-5- phenyl-2,3-dihydro-1H-benzo[e][1,4]- diazepin-3-yl)butyramide by Use of an Asymmetric Ireland−Claisen Rearrangement

The Intramembrane Cleavage Site of the Amyloid Precursor Protein Depends on the Length of Its Transmembrane Domain

Two domains within the first putative transmembrane domain of presenilin 1 differentially influence presenilinase and γ‐secretase activity

Functional Overexpression of γ-Secretase Reveals Protease-independent Trafficking Functions and a Critical Role of Lipids for Protease Activity

Quantitation of amyloid-β peptides in biological milieu using a novel homogeneous time-resolved fluorescence (HTRF) assay

Determination of guinea-pig cortical γ-secretase activity ex vivo following the systemic administration of a γ-secretase inhibitor

A novel series of potent γ-secretase inhibitors based on a benzobicyclo[4.2.1]nonane core

Fatty acids increase presenilin-1 levels and γ-secretase activity in PSwt-1 cells

gamma-Secretase cleavage site specificity differs for intracellular and secretory amyloid beta

Modulation of ion channel activity: a key function of the protein kinase C enzyme family

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