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Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.
TLDR
A substantially enriched preparation of Alzheimer paired helical filaments has been used as a starting point for biochemical studies and sequence analysis of these peptides was used to design oligonucleotide probes for cloning a cognate cDNA, which leads to its identification as human microtubule-associated tau protein.
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Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau.
TLDR
The proof that at least part of tau protein forms a component of the paired helical filament core opens the way to understanding the mode of formation of paired helicals filaments and thus, ultimately, the pathogenesis of Alzheimer disease.
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Structural characterization of the core of the paired helical filament of Alzheimer disease.
TLDR
The paired helical filament, the principal constituent of the neurofibrillary tangles characteristic of Alzheimer disease, is shown to consist of two structurally distinct parts, and the mass per unit length measurements imply that the three-domain structural subunit of the core has a molecular mass of approximately equal to 100 kDa.
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Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51.
TLDR
It is concluded that 423 reactivity also requires a modification(s) occurring within an approximately 90-residue segment that are not present in tau proteins so far described in the human brain.
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Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament.
TLDR
MAb 423 labels isolated PHFs prior to Pronase digestion and intracellular granular and neurofibrillary degeneration in Alzheimer's disease tissues, and is described as the minimal protease resistant tau unit of the core PHF.
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Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies
TLDR
It is concluded that answering key questions on the relationship between Aβ and tau pathology should lead to a better understanding of the nature of secondary tauopathies, especially AD, and open new therapeutic targets and strategies.
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Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines.
TLDR
It is shown that a similar proteolytically stable complex can be generated in vitro following the self-aggregation of tau protein through a high-affinity binding site in the repeat domain and that biologically selective pharmaceutical agents could be developed to facilitate the proteolytic degradation of tAU aggregates and prevent the further propagation of t Tau capture in AD.
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Tau aggregation inhibitor therapy: an exploratory phase 2 study in mild or moderate Alzheimer's disease.
TLDR
The minimum safe and effective daily MT dose is 138 mg and suggests that further study of MT is warranted in AD, and the delivery of the highest dose was impaired due to dose-dependent dissolution and absorption limitations.
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Association between Alzheimer's disease and the NOS3 gene
TLDR
A highly significant enrichment for Glu/Glu homozygotes in LOAD compared with controls appears to be independent of ApoE status, and NOS3 may be a new genetic risk factor for LOAD.
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Alzheimer's Disease-like Paired Helical Filament Assembly from Truncated Tau Protein Is Independent of Disulfide Crosslinking.
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