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On one hand, tau deficiency is largely protective against Aβ toxicity, suggesting that in AD tau may gain a toxic function [ 55, 117].
Disease toxicity in HD is thought to reflect a gain of toxic function that accompanies conformational changes in the mutant protein.
On a basic level, it is known that HD is caused by a mutation in huntingtin that causes it to gain a new toxic function and harm the cell.
Indeed, it is possible that only taurine and GABA prevent neurons from damage with anticarbonylation toxic function besides inhibiting neuron superexcitation [40].
There are multiple cellular changes through which the toxic function of mHtt may manifest and produce the HD pathology.
It is thought that the disease is not caused by inadequate production of Htt, but by a gain of toxic function of mHtt.
Other views suggest gain of toxic function by PrPSc due to sequestration of PrPC-associated metals within the aggregates, resulting in the generation of redox-active PrPSc complexes.
Mutant Htt protein (mHtt) perturbs many cellular processes by both gain of toxic function and loss of normal function.
This component may participate to the pathogenic process together with a gain of toxic function due to amyloidosis.
It may also result in a gain of toxic function of the protein and therefore contribute to neuronal injury and degeneration [10] [13].
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Collectively TAU-phosphorylation comprises a gain-of-toxic function driving AD pathogenesis.
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