2001•Unpublished venueRequires access
Characterization of Alzheimer's β‐Secretase Protein BACE: Processing and Other Post‐translational Modifications
Mitsuru Haniu, Brian D. Bennett, Paul Denis, Yunjen Young, Elizabeth A. Mendiaz, Janis Fuller, John O. Hui, Steven E. Kahn, Safura Babu‐Khan, Sandra L. Ross, Teresa L. Burgess, Viswanatham Katta, Margery Nicolson, Jonathan Lull, Shue‐Yuan Wang, Gary N. Rogers, Robert Vassar, Martin Citron
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Abstract
Beta-amyloid, the main component of the hallmark of amyloid plaques of Alzheimer's disease is generated by proteolytic cleavage of the large amyloid precursor protein. Two distinct proteoyltic activities, termed β-secretase and γ-secretase, cleave to release the amino- and carboxy-termini, respectively, of the 39–42 amino acid Beta-amyloid peptide from its precursor protein. According to the amyloid cascade hypothesis, Beta-amyloid plays an early and critical role in Alzheimer's disease. Consequently, inhibition of Beta-amyloid appear as the most tractable targets in the Beta-amyloid formation pathway.