@article { ISI:000315745600001,
	title = {Zoom-in - a targeted database search for identification of glycation modifications analyzed by untargeted tandem mass spectrometry},
	journal = {European Journal of Mass Spectrometry},
	volume = {18},
	number = {6},
	year = {2012},
	month = {JAN},
	pages = {475-481},
	publisher = {IM PUBLICATIONS},
	type = {Article},
	address = {6 CHARLTON MILL, CHARLTON, CHICHESTER,, W SUSSEX PO18 0HY, ENGLAND},
	abstract = {<p>Post-translational modifications (PTMs) are very important to biological function, however their identification and characterization is technically challenging. In this study, we have identified glycation modifications by nano LC-MSE, a data independent acquisition work flow, followed by database search using the Protein Lynx Global Server (PLGS). PLGS search with a complete human protein database hardly identified glycation modifications in a glycated human serum albumin (HSA), which was detected to be glycated by western blotting with advanced glycation end products (AGE) antibody and fluorescence spectroscopy. To overcome this difficulty, {\textquoteleft}{\textquoteleft}Zoom-In{\textquoteright}{\textquoteright} approach, a targeted database search was used to identify glycation modifications in a glycated HSA, which were further manually validated. This approach was useful for identification of glycation modifications from untargeted tandem mass spectrometry workflow such as MSE, but may require the development of a new algorithm or an upgrade of the existing software.</p>},
	keywords = {advanced glycation end products (AGEs), data independent acquisition, Diabetes, post-translational modifications},
	issn = {1469-0667},
	doi = {10.1255/ejms.1203},
	author = {Bhonsle, Hemangi S. and Korwar, Arvind M. and Kesavan, Suresh K. and Bhosale, Santosh D. and Bansode, Sneha B. and Kulkarni, Mahesh J.}
}
@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}
}
