The phrase "alterations of tau" is correct and usable in written English.
It can be used in contexts discussing changes or modifications related to tau, which may refer to a protein, a mathematical symbol, or other fields depending on the context.
Example: "The study focused on the alterations of tau in neurodegenerative diseases, highlighting their impact on cognitive function."
Alternatives: "changes in tau" or "modifications of tau".
Furthermore, the above described alterations of tau and Aβ42 were highly significant both in AD patients with low and high scores on MMSE at baseline, when compared to the healthy controls (data not shown).
The folding of Tau into a paperclip-like structure, recognized by MC1 antibodies, occurs when the amino acids at residues 7 9 interact with residues 312 342, and is one of the earliest pathological alterations of Tau in Alzheimer disease, preceding the formation of neurofibrillary tangles in AD [48].
Alterations of tau and kinases in the brains of TSE animals during pathogenicity may consist of a complicate network.
Moreover, pathological alterations of tau are most likely not the result of a single post-translational modification, but instead a combination of structural and functional alterations that may ultimately contribute to determine tau pathogenicity.
Understanding the precise molecular mechanisms underlying this pathological alteration of tau is critical to identify novel and effective neurotherapeutics for the treatment of AD and other tauopathies.
The results presented here support a plethora of data that show phosphorylation can affect tau toxicity but demonstrate that alteration of tau phosphorylation state is not required to modify tau toxicity.
Alteration of tau, p-tau (Ser396, Ser404, and Ser202/Thr205), GSK3β and CDK5 were either intermediate or consequent events in TSE pathogenesis and proposed the potential linkage of these bioactive proteins with the pathogenesis of prion diseases.
These results indicate that iAβO-induced spine alteration is independent of tau.
We showed that iAβO-induced spine alteration is independent of tau (Fig 4), but it is unknown if this tau-independence extends to other cellular mechanisms such as intracellular transport.
In our study, however, we did not observe a significant alteration of phosphorylated levels of tau at serine-202 at the 1-week time point.
Since Tau transgenic mice develop an age-dependent Tau neuropathology, alterations of the blood-brain barrier permeability cannot be excluded.
