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BACE1 and presenilin: two unusual aspartyl proteases involved in Alzheimer's disease

Author

Bart De Strooper

1950 -

published in: Neurodegenerative Diseases

date of publication: 2004

language: English

main subject: Alzheimer's disease

Bibliographic databases:

Cites articles 73

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Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity
1999-12-01

Targeted gene disruption demonstrates that P-selectin glycoprotein ligand 1 (PSGL-1) is required for P-selectin-mediated but not E-selectin-mediated neutrophil rolling and migration
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Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans
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The gene encoding DRAP (BACE2), a glycosylated transmembrane protein of the aspartic protease family, maps to the down critical region
2000-11-01

ASP1 (BACE2) cleaves the amyloid precursor protein at the beta-secretase site
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BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein
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Expression analysis of BACE2 in brain and peripheral tissues
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A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer's amyloid precursor protein beta-secretase

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Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein
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Presenilins and the intramembrane proteolysis of proteins: facts and fiction
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BACE1 is the major beta-secretase for generation of Abeta peptides by neurons
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BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: implications for Alzheimer's disease therapeutics
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Mice deficient in BACE1, the Alzheimer's beta-secretase, have normal phenotype and abolished beta-amyloid generation
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