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The Disintegrin ADAM9 Indirectly Contributes to the Physiological Processing of Cellular Prion by Modulating ADAM10 Activity

The Journal of biological chemistry, 2005-12, Vol.280 (49), p.40624-40631

2005

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Long-term tolerance of preservative-free eye drops containing macrogol hydroxystearate as an excipient

Journal francais d'ophtalmologie, 2016-02, Vol.39 (2), p.156-163

2016

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APPε, the ε-secretase-derived N-terminal product of the β-amyloid precursor protein, behaves as a type I protein and undergoes α-, β-, and γ-secretase cleavages

Journal of neurochemistry, 2006-05, Vol.97 (3), p.807-817

2006

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BACE1- and BACE2-expressing human cells: characterization of beta-amyloid precursor protein-derived catabolites, design of a novel fluorimetric assay, and identification of new in vitro inhibitors

The Journal of biological chemistry, 2003-07, Vol.278 (28), p.25859-25866

2003

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Design and characterization of a new cell‐permeant inhibitor of the β‐secretase BACE1

British journal of pharmacology, 2005-05, Vol.145 (2), p.228-235

2005

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The epsilon-secretase-derived N-terminal product of the Beta-amyloid precursor protein behaves as a membrane-bound protein and undergoes alpha-, beta-, and gamma-secretase cleavages

Journal of neurochemistry, 2006, Vol.97, p.807-817

2006

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Design and characterization of a new cell permanent inhibitor of the beta-secretase BACE1

British journal of pharmacology, 2005, Vol.145, p.228-235

2005

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BACE1- and BACE2-expressing Human Cells

The Journal of biological chemistry, 2003-07, Vol.278 (28), p.25859-25866

2003

Volltextzugriff (PDF)

The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity

The Journal of biological chemistry, 2013-08, Vol.288 (32), p.23433-23433

2013

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APP[epsilon], the [epsilon]-secretase-derived N-terminal product of the [beta]-amyloid precursor protein, behaves as a type I protein and undergoes [alpha]-, [beta]-, and [gamma]-secretase cleavages

Journal of neurochemistry, 2006-05, Vol.97 (3), p.807

2006

Volltextzugriff (PDF)

APPepsilon, the epsilon-secretase-derived N-terminal product of the beta-amyloid precursor protein, behaves as a type I protein and undergoes alpha-, beta-, and gamma-secretase cleavages

Journal of neurochemistry, 2006-05, Vol.97 (3), p.807

2006

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APPε, the ε-secretase-derived Ν-terminal product of the β-amyloid precursor protein, behaves as a type Ι protein and undergoes α-, β-, and γ-secretase cleavages

Journal of neurochemistry, 2006, Vol.97 (3), p.807-817

2006

Volltextzugriff (PDF)

The Disintegrin ADAM9 Indirectly Contributes to the Physiological Processing of Cellular Prion by Modulating ADAM10 Activity

The Journal of biological chemistry, 2005-12, Vol.280 (49), p.40624-40631

2005

Volltextzugriff (PDF)

Design and characterization of a new cell-permeant inhibitor of the [beta]-secretase BACE1

British journal of pharmacology, 2005-05, Vol.145 (2), p.228

2005

Volltextzugriff (PDF)

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The Disintegrin ADAM9 Indirectly Contributes to the Physiological Processing of Cellular Prion by Modulating ADAM10 Activity

Long-term tolerance of preservative-free eye drops containing macrogol hydroxystearate as an excipient

APPε, the ε-secretase-derived N-terminal product of the β-amyloid precursor protein, behaves as a type I protein and undergoes α-, β-, and γ-secretase cleavages

BACE1- and BACE2-expressing human cells: characterization of beta-amyloid precursor protein-derived catabolites, design of a novel fluorimetric assay, and identification of new in vitro inhibitors

Design and characterization of a new cell‐permeant inhibitor of the β‐secretase BACE1

The epsilon-secretase-derived N-terminal product of the Beta-amyloid precursor protein behaves as a membrane-bound protein and undergoes alpha-, beta-, and gamma-secretase cleavages

Design and characterization of a new cell permanent inhibitor of the beta-secretase BACE1

JLK inhibitors: isocoumarin compounds as putative probes to selectively target the gamma-secretase pathway

BACE1- and BACE2-expressing Human Cells

The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity

APP[epsilon], the [epsilon]-secretase-derived N-terminal product of the [beta]-amyloid precursor protein, behaves as a type I protein and undergoes [alpha]-, [beta]-, and [gamma]-secretase cleavages

APPepsilon, the epsilon-secretase-derived N-terminal product of the beta-amyloid precursor protein, behaves as a type I protein and undergoes alpha-, beta-, and gamma-secretase cleavages

APPε, the ε-secretase-derived Ν-terminal product of the β-amyloid precursor protein, behaves as a type Ι protein and undergoes α-, β-, and γ-secretase cleavages

The Disintegrin ADAM9 Indirectly Contributes to the Physiological Processing of Cellular Prion by Modulating ADAM10 Activity

Design and characterization of a new cell-permeant inhibitor of the [beta]-secretase BACE1

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