Abstract
New methods for analyzing tau fibrillization have yielded insights into the biochemical transitions involved in the process. Here we review the parallels between the sequential progression of tau fibrillization observed macroscopically in Alzheimer's disease (AD) lesions and the pathway of tau aggregation observed in vitro with purified tau preparations. In addition, pharmacological agents for further dissection of fibrillization mechanism and lesion formation are discussed.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Alzheimer Disease / metabolism*
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Amyloid beta-Peptides / chemistry
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Amyloid beta-Peptides / metabolism
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Brain Chemistry*
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In Vitro Techniques
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Microtubule-Associated Proteins / genetics
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Models, Biological
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Mutation
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Neurofibrillary Tangles / metabolism*
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Phosphorylation
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Protein Isoforms
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Recombinant Proteins
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tau Proteins / drug effects
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tau Proteins / genetics
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tau Proteins / metabolism*
Substances
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Amyloid beta-Peptides
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MAPT protein, human
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Microtubule-Associated Proteins
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Protein Isoforms
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Recombinant Proteins
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tau Proteins