Structural insights into Alzheimer filament assembly pathways based on site-directed mutagenesis and S-glutathionylation of three-repeat neuronal Tau protein

Although Tau and MAP2 readily assemble into straight filaments (SFs), Tau's unique ability to form paired‐helical filaments (PHFs) may offer clues as to why Tau's microtubule‐binding region (MTBR) is the exclusive building block of the neurofibrillary tangles that accumulate during Alzheim...

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Veröffentlicht in:	Microscopy research and technique 2005-07, Vol.67 (3-4), p.156-163
Hauptverfasser:	Dinoto, Luca, Deture, Michael A., Purich, Daniel L.
Format:	Artikel
Sprache:	eng
Schlagworte:	aberrant protein polymerization Alzheimer Disease - genetics Alzheimer Disease - metabolism Alzheimer Disease - pathology Amino Acid Sequence cyto-skeletal protein glutathione Humans MAP2 microtubule-associated proteins Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Microtubule-Associated Proteins - ultrastructure Microtubules - metabolism Microtubules - ultrastructure Molecular Sequence Data Mutagenesis, Site-Directed Neurofibrillary Tangles - metabolism Neurofibrillary Tangles - ultrastructure oxidative stress Phosphorylation Protein Binding tau Proteins - genetics tau Proteins - metabolism tau Proteins - ultrastructure
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