Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein.
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Summary
Results suggest that memapsin 2 fits all of the criteria of beta-secretase, which catalyzes the rate-limiting step of the in vivo production of the beta-amyloid (Abeta) peptide leading to the progression of Alzheimer's disease.
- Type
- article
- Published
- 2000-02-15
- Cited by
- 771
- References
- 14
- Access
- Open access
- OpenAlex
- https://openalex.org/W2026053103
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:27126290
Keywords
Amyloid precursor protein, Biochemistry, Transmembrane domain, Protease, Biology
References
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- Relationships of human immunodeficiency virus protease with eukaryotic aspartic proteases.
- Evolution in the structure and function of aspartic proteases
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- Cellular mechanisms of beta-amyloid production and secretion.
- A locus for familial early–onset Alzhelmer's disease on the long arm of chromosome 14, proximal to the α1–antichymotrypsin gene
- Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo.
- Generation of amyloid beta protein from its precursor is sequence specific.
- Enhanced Release of Amyloid -Protein from Codon 670/671 Swedish Mutant -Amyloid Precursor Protein Occurs in Both Secretory and Endocytic Pathways (*)
- Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue.
- Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE.
- Phosphorylation, Subcellular Localization, and Membrane Orientation of the Alzheimer's Disease-associated Presenilins*
Cited by
- A two decade contribution of molecular cell biology to the centennial of Alzheimer's disease: are we progressing toward therapy?
- Functional Characterization of the Presenilin Homologue SPE-4
- Presenilin, Notch, and the genesis and treatment of Alzheimer's disease
- Linear Non-competitive Inhibition of Solubilized Human γ-Secretase by Pepstatin A Methylester, L685458, Sulfonamides, and Benzodiazepines*
- Solution studies and structural model of the extracellular domain of the human amyloid precursor protein.
- BACE1 and Presenilin: Two Unusual Aspartyl Proteases Involved in Alzheimer’s Disease
- GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide
- Receptor tyrosine kinases positively regulate BACE activity and Amyloid-β production through enhancing BACE internalization
- Therapeutic options in Alzheimer’s disease
- Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations.
- Structure-based design of β-site APP cleaving enzyme 1 (BACE1) inhibitors for the treatment of Alzheimer's disease.
- Assessing the contribution of antiretroviral therapy to neuronal damage and death as a mediator of cognitive decline in HIV-associated neurocognitive disorders
- The Resveratrol Trimer Miyabenol C Inhibits β-Secretase Activity and β-Amyloid Generation
- Studies on the use of glycosaminoglycans for the treatment of Alzheimer's Disease
- Rôle des ADAM dans le processus physiopathologique de la maladie d'Alzheimer
- Comparable dimerization found in wildtype and familial Alzheimer's disease amyloid precursor protein mutants.
- Disease-Modifying Approach to the Treatment of Alzheimer’s Disease
- Efecto del resveratrol en modelos murinos de envejecimiento y enfermedad de Alzheimer
- Notch signaling : From receptor cleavage to chromatin remodeling
- Serotonergic Signaling Pathways that Suppress Amyloid Beta in Mouse Models of AD
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