Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 283, Issue 44, Pages 29615-29619Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R800019200
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Funding
- National Institutes of Health [AG019070, AG021495]
- NIA [AG032179]
- American Health Assistance Foundation Alzheimer's Disease Research Program and the Alzheimer's Association
- Glenn Foundation for Medical Research
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Intracellular trafficking and proteolytic processing of amyloid precursor protein (APP) have been the focus of numerous investigations over the past two decades. APP is the precursor to the amyloid beta-protein (A beta), the 38-43-amino acid residue peptide that is at the heart of the amyloid cascade hypothesis of Alzheimer disease (AD). Tremendous progress has been made since the initial identification of A beta as the principal component of brain senile plaques of individuals with AD. Specifically, molecular characterization of the secretases involved in A beta production has facilitated cell biological investigations on APP processing and advanced efforts to model AD pathogenesis in animal models. This minireview summarizes salient features of APP trafficking and amyloidogenic processing and discusses the putative biological functions of APP.
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