Biotech Values

[Kadaicher1]

Dew, I doubt that tau theory for a few reasons. Firstly it appears that tau is used to transport metals to the edge of the cells for removal, and lack of tau appears to cause buildup of iron in the SN leading to Parkinsons. Secondly is that prions, first suspected back in the 80's have recently been identified in the process and may be the infectious component.
http://www.pnas.org/content/109/5/1737
[Aß neurotoxicity depends on interactions between copper ions, prion protein, and N-methyl-d-aspartate receptors
Haitao Youa,1, Shigeki Tsutsuib,1, Shahid Hameeda, Thomas J. Kannanayakalb, Lina Chena, Peng Xiac, Jordan D. T. Engbersa, Stuart A. Liptonc, Peter K. Stysb,2, and Gerald W. Zamponia,2
+ Author Affiliations

aDepartment of Physiology and Pharmacology and
bDepartment of Clinical Neurosciences, Hotchkiss Brain Institute, University of Calgary, Calgary, AB, Canada, T2N 4N1; and
cDel E. Webb Center for Neuroscience, Aging, and Stem Cell Research, Sanford-Burnham Medical Research Institute, La Jolla, CA 92037
Edited* by Stanley B. Prusiner, University of California, San Francisco, CA, and approved December 21, 2011 (received for review July 5, 2011)

Abstract
N-methyl-d-aspartate receptors (NMDARs) mediate critical CNS functions, whereas excessive activity contributes to neuronal damage. At physiological glycine concentrations, NMDAR currents recorded from cultured rodent hippocampal neurons exhibited strong desensitization in the continued presence of NMDA, thus protecting neurons from calcium overload. Reducing copper availability by specific chelators (bathocuproine disulfonate, cuprizone) induced nondesensitizing NMDAR currents even at physiologically low glycine concentrations. This effect was mimicked by, and was not additive with, genetic ablation of cellular prion protein (PrPC), a key copper-binding protein in the CNS. Acute ablation of PrPC by enzymatically cleaving its cell-surface GPI anchor yielded similar effects. Biochemical studies and electrophysiological measurements revealed that PrPC interacts with the NMDAR complex in a copper-dependent manner to allosterically reduce glycine affinity for the receptor. Synthetic human Aß1–42 (10 nM–5 µM) produced an identical effect that could be mitigated by addition of excess copper ions or NMDAR blockers. Taken together, Aß1–42, copper chelators, or PrPC inactivation all enhance the activity of glycine at the NMDAR, giving rise to pathologically large nondesensitizing steady-state NMDAR currents and neurotoxicity. We propose a physiological role for PrPC, one that limits excessive NMDAR activity that might otherwise promote neuronal damage. In addition, we provide a unifying molecular mechanism whereby toxic species of Aß1–42 might mediate neuronal and synaptic injury, at least in part, by disrupting the normal copper-mediated, PrPC-dependent inhibition of excessive activity of this highly calcium-permeable glutamate receptor.]

Note that abstract has been edited by Stanley Prusiner. who won the Nobel for his prion discovery work.
My lay opinion is that part of the answer will be about protecting tau, rather than stopping it.