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

EMBO Reports

Volumn 2, Issue 9, 2001, Pages 835-841

  Sastre, Magdalena ^a   Steiner, Harald ^a   Fuchs, Klaus ^b   Capell, Anja ^a   Multhaup, Gerd ^c   Condron, Margaret M ^d   Teplow, David B ^d   Haass, Christian ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b BOEHRINGER INGELHEIM PHARMA GMBH AND CO KG   (Germany)

^c UNIVERSITY OF HEIDELBERG   (Germany)

^d MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; ENZYME INHIBITOR; GAMMA SECRETASE; NOTCH RECEPTOR; PRESENILIN 1; PRESENILIN 2; PROTEIN PRECURSOR;

ANIMAL CELL; ARTICLE; BRAIN; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME BINDING; HUMAN; HUMAN CELL; IN VITRO STUDY; KNOCKOUT GENE; MOUSE; MUTATION; NONHUMAN; PREVENTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN SECRETION; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; ASPARTIC ENDOPEPTIDASES; BINDING SITES; BRAIN; CELL LINE; CELLS, CULTURED; DNA, COMPLEMENTARY; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOPEPTIDASES; FIBROBLASTS; GAMMA-AMINOBUTYRIC ACID; HUMANS; MEMBRANE PROTEINS; MICE; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; PRESENILIN-1; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, NOTCH; TIME FACTORS; TRANSFECTION; TRIGLYCERIDES;

EID: 0034774969     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kve180     Document Type: Article

References (21)

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 γ-secretase inhibitors reduce β-amyloid peptide levels in brain
5. Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
6. Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptide
7. Amyloid β-peptide is produced by cultured cells during normal metabolism
8. Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1
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10. A novel γ-secretase assay based on detection of the putative C-terminal fragment-γ of amyloid β protein precursor
11. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
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14. Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
15. Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis
16. Glycine 384 is required for presenilin-1 function and is conserved in polytopic bacterial aspartyl proteases
17. Requirements for presenilin-dependent cleavage of Notch and other transmembrane proteins
18. Aβ-generating enzymes: Recent advances in β- and γ-secretase research
19. Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42
20. The role of presenilins in γ-secretase activity
21. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity