Hypothesis: amyloid beta-peptides truncated at the N-terminus contribute to the pathogenesis of Alzheimer's disease
- PMID: 10466895
- DOI: 10.1016/s0197-4580(99)00014-7
Hypothesis: amyloid beta-peptides truncated at the N-terminus contribute to the pathogenesis of Alzheimer's disease
Abstract
Fragments of amyloid beta-peptide truncated at the N-terminus are present in AD brain early in the course of Alzheimer's disease. It is proposed that these species contribute to the pathogenesis of AD, possibly through destabilization of elements of the neuronal cytoskeleton by small fibrillar deposits.
Comment in
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Truncating the amyloid cascade hypothesis: the role of C-terminal Abeta peptides in Alzheimer's disease.Neurobiol Aging. 1999 Jan-Feb;20(1):71-3; discussion 87. doi: 10.1016/s0197-4580(99)00013-5. Neurobiol Aging. 1999. PMID: 10466896 No abstract available.
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N-terminus truncated beta-amyloid peptides and C-terminus truncated secreted forms of amyloid precursor protein: distinct roles in the pathogenesis of Alzheimer's disease.Neurobiol Aging. 1999 Jan-Feb;20(1):75-9; discussion 87. doi: 10.1016/s0197-4580(99)00012-3. Neurobiol Aging. 1999. PMID: 10466897 No abstract available.
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Familial Alzheimer disease: changes in Abeta production may indicate a disturbance in protein transport or function caused by pleiotropic effects of FAD mutations.Neurobiol Aging. 1999 Jan-Feb;20(1):81-3; discussion 87. doi: 10.1016/s0197-4580(99)00011-1. Neurobiol Aging. 1999. PMID: 10466898 No abstract available.
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The shorter amyloid cascade hypothesis.Neurobiol Aging. 1999 Jan-Feb;20(1):85; discussion 87. Neurobiol Aging. 1999. PMID: 10466899 No abstract available.
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