Presenilin‐dependent γ‐secretase processing of β‐amyloid precursor protein at a site corresponding to the S3 cleavage of Notch-Reference-Cited by-同舟云学术

Presenilin‐dependent γ‐secretase processing of β‐amyloid precursor protein at a site corresponding to the S3 cleavage of Notch

Published:2001-09 Issue:9 Volume:2 Page:835-841
ISSN:1469-221X
Container-title:EMBO reports
language:en
Short-container-title:EMBO Rep

Author:

Sastre Magdalena¹,Steiner Harald¹,Fuchs Klaus²,Capell Anja¹,Multhaup Gerd³,Condron Margaret M⁴,Teplow David B⁴,Haass Christian¹

Affiliation:

1. Adolf Butenandt‐Institute, Department of Biochemistry, Laboratory for Alzheimer's and Parkinson's Disease Research, Ludwig‐Maximilians‐University Schillerstrasse 44 80336 Munich Germany

2. Boehringer Ingelheim Pharma KG, Chemical Research 55216 Ingelheim Germany

3. Center for Molecular Biology Heidelberg Im Neuenheimer Feld 282 69120 Heidelberg Germany

4. Department of Neurology, Harvard Medical School, and Center for Neurologic Diseases, Brigham and Women's Hospital Boston MA 02115 USA

Publisher

EMBO

Subject

Genetics,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1093/embo-reports/kve180

Reference21 articles.

1. Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

2. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein

3. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain

4. Functional gamma-secretase inhibitors reduce beta-amyloid peptide levels in brain

5. Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1

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