@article {46759,
	title = {Transition metal nickel prevents Tau aggregation in Alzheimer{\textquoteright}s disease},
	journal = {International Journal of Biological Macromolecules},
	volume = {156},
	year = {2020},
	month = {AUG },
	pages = {1359-1365},
	type = {Article},
	abstract = {<p>Alzheimer{\textquoteright}s disease is the leading cause of dementia, effecting majority of aged people worldwide. The multifaceted effectors of Alzheimer{\textquoteright}s disease primarily include Tau, amyloid-beta along with hyper activation of kinases, oxidative stress and mutations etc., makes it challenging to design therapeutics. Tau is a microtubule-associating protein, which is subjected to cellular stress resulting in the formation of neurofibrillary tangles, leading to loss of affinity for microtubules. This causes loss of microtubule stability and in turn alters axonal integrity. In the present work, emphasis towards understanding interaction of nickel with Tau was made. Metals such as iron, zinc, copper and lead etc., are known to modulate Tau conformation and enhance its aggregation. Our results showed the deliverance of Tau aggregation by nickel and its synthetic morpholine conjugate. Nickel prevents aggregation by inducing degradation of Tau as evidenced by SDS-PAGE and TEM. Nickel and the synthetic conjugate being non toxic to neuro2a cells and prevent Tau aggregation, might direct these complexes to overcome AD. (C) 2019 Published by Elsevier B.V.</p>
},
	keywords = {Aggregation, Alzheimer{\textquoteright}s disease, metals, Morpholine, Nickel chloride, Tau},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2019.11.176},
	author = {Gorantla, Nalini Vijay and Das, Rashmi and Balaraman, Ekambaram and Chinnathambi, Subashchandrabose}
}
@article {47364,
	title = {Methylation as a key regulator of Tau aggregation and neuronal health in Alzheimer{\textquoteright}s disease},
	journal = {Cell Communication and Signaling},
	volume = {19},
	year = {2021},
	month = {MAY },
	pages = {51},
	type = {Review},
	abstract = {<p>Neurodegenerative diseases like Alzheimer{\textquoteright}s, Parkinson{\textquoteright}s and Huntington{\textquoteright}s disease involves abnormal aggregation and accumulation of toxic proteins aggregates. Post-translational modifications (PTMs) of the causative proteins play an important role in the etiology of disease as they could either slow down or accelerate the disease progression. Alzheimer disease is associated with the aggregation and accumulation of two major protein aggregates-intracellular neurofibrillary tangles made up of microtubule-associated protein Tau and extracellular Amyloid-beta plaques. Post-translational modifications are important for the regulation of Tau{\textquoteleft}s function but an imbalance in PTMs may lead to abnormal Tau function and aggregation. Tau methylation is one of the important PTM of Tau in its physiological state. However, the methylation signature on Tau lysine changes once it acquires pathological aggregated form. Tau methylation can compete with other PTMs such as acetylation and ubiquitination. The state of PTM at these sites determines the fate of Tau protein in terms of its function and stability. The global methylation in neurons, microglia and astrocytes are involved in multiple cellular functions involving their role in epigenetic regulation of gene expression via DNA methylation. Here, we have discussed the effect of methylation on Tau function in a site-specific manner and their cross-talk with other lysine modifications. We have also elaborated the role of methylation in epigenetic aspects and neurodegenerative conditions associated with the imbalance in methylation metabolism affecting global methylation state of cells.</p>},
	keywords = {Aggregation, Epigenetics, methylation, Methyltransferases, post-translational modifications, Tau},
	doi = {10.1186/s12964-021-00732-z},
	author = {Balmik, Abhishek Ankur and Chinnathambi, Subashchandrabose}
}
