@article { ISI:000226532000006,
	title = {Selective synthesis of N,N-dimethyl aniline derivatives using dimethyl carbonate as a methylating agent and onium salt as a catalyst},
	journal = {Journal of Molecular Catalysis A - Chemical},
	volume = {226},
	number = {1},
	year = {2005},
	month = {FEB},
	pages = {49-56},
	publisher = {ELSEVIER SCIENCE BV},
	type = {Article},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>N-Alkylation of anilines by dimethyl carbonate (DMC) catalyzed by onium salts has been demonstrated. The work presented here shows that a simple catalytic system consisting of onium salts in the presence of a small amount of water is extremely effective in enhancing the DMC mediated N-alkylation of anilines to dialkylated products. The effect of reaction conditions on the synthesis of N,N-dimethyl aniline (NNDMA) from aniline and DMC has been investigated. Under the optimized conditions highest yield of NNDMA obtained was 99.8\%, which is the best reported for liquid phase N-alkylation of aniline using DMC. The role of water in enhancing the yield of NNDMA is explained and a reaction-networking scheme is constructed, which summarizes the chemistry behind liquid phase N-alkylation of anilines by DMC. The catalyst has been shown to recycle up to five times and at the end of fifth recycle almost 98\% of NNDMA yields were obtained. (C) 2004 Elsevier B.V. All rights reserved.</p>},
	keywords = {Aniline, Dimethyl carbonate, methylation, N, N-alkylation, N-dimethyl aniline, onium salts},
	issn = {1381-1169},
	doi = {10.1016/j.molcata.2004.09.025},
	author = {Shivarkar, A. B. and Gupte, S. P. and Chaudhari, Raghunath V.}
}
@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}
}
