@article {46383,
	title = {Engineering of the tat pathway and chaperons},
	journal = {Acta Crystallographica A-Foundation and Advances},
	volume = {70},
	year = {2014},
	month = {APR},
	pages = {C273},
	type = {Meeting Abstract},
	keywords = {Protein transport, Signal sequence, Tat Pathway},
	issn = {2053-2733},
	author = {Ghosh, Deepanjan and Ramasamy, Sureshkumar}
}
@article { ISI:000362499200027,
	title = {Engineering proteins for thermostability with iRDP web server},
	journal = {Plos One},
	volume = {10},
	number = {10},
	year = {2015},
	month = {OCT},
	pages = {e0139486},
	publisher = {PUBLIC LIBRARY SCIENCE},
	address = {1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA},
	abstract = {<p>Engineering protein molecules with desired structure and biological functions has been an elusive goal. Development of industrially viable proteins with improved properties such as stability, catalytic activity and altered specificity by modifying the structure of an existing protein has widely been targeted through rational protein engineering. Although a range of factors contributing to thermal stability have been identified and widely researched, the in silico implementation of these as strategies directed towards enhancement of protein stability has not yet been explored extensively. A wide range of structural analysis tools is currently available for in silico protein engineering. However these tools concentrate on only a limited number of factors or individual protein structures, resulting in cumbersome and time-consuming analysis. The iRDP web server presented here provides a unified platform comprising of iCAPS, iStability and iMutants modules. Each module addresses different facets of effective rational engineering of proteins aiming towards enhanced stability. While iCAPS aids in selection of target protein based on factors contributing to structural stability, iStability uniquely offers in silico implementation of known thermostabilization strategies in proteins for identification and stability prediction of potential stabilizing mutation sites. iMutants aims to assess mutants based on changes in local interaction network and degree of residue conservation at the mutation sites. Each module was validated using an extensively diverse dataset. The server is freely accessible at http://irdp.ncl.res.in and has no login requirements.</p>},
	issn = {1932-6203},
	doi = {10.1371/journal.pone.0139486},
	author = {Panigrahi, Priyabrata and Sule, Manas and Ghanate, Avinash and Ramasamy, Sureshkumar and Suresh, C. G.}
}
@article {46768,
	title = {EGCG impedes human Tau aggregation and interacts with Tau},
	journal = {Scientific Reports},
	volume = {10},
	year = {2020},
	month = {JUL},
	pages = {12579},
	type = {Article},
	abstract = {<p>Tau aggregation and accumulation is a key event in the pathogenesis of Alzheimer{\textquoteright}s disease. Inhibition of Tau aggregation is therefore a potential therapeutic strategy to ameliorate the disease. Phytochemicals are being highlighted as potential aggregation inhibitors. Epigallocatechin-3-gallate (EGCG) is an active phytochemical of green tea that has shown its potency against various diseases including aggregation inhibition of repeat Tau. The potency of EGCG in altering the PHF assembly of full-length human Tau has not been fully explored. By various biophysical and biochemical analyses like ThS fluorescence assay, MALDI-TOF analysis and Isothermal Titration Calorimetry, we demonstrate dual effect of EGCG on aggregation inhibition and disassembly of full-length Tau and their binding affinity. The IC50 for Tau aggregation by EGCG was found to be 64.2 mu M.</p>
},
	issn = {2045-2322},
	doi = {10.1038/s41598-020-69429-6},
	author = {Sonawane, Shweta Kishor and Chidambaram, Hariharakrishnan and Boral, Debjyoti and Gorantla, Nalini Vijay and Balmik, Abhishek Ankur and Dangi, Abha and Ramasamy, Sureshkumar and Marelli, Udaya Kiran and Chinnathambi, Subashchandrabose}
}
