@article {46401,
	title = {Allostery mapping in enterococcus faecalis Bile Salt Hydrolase (BSH)},
	journal = {Acta Crystallographica A-Foundation and Advances},
	volume = {70},
	year = {2014},
	month = {MAY},
	pages = {C274},
	type = {Meeting Abstract},
	keywords = {Allostery, Bile salt hydrolase, MD Simulation},
	issn = {2053-2733},
	author = {Yadav, Yashpal and Ramasamy, Sureshkumar}
}
@article {44349,
	title = {Analysis of Kunitz inhibitors from plants for comprehensive structural and functional insights},
	journal = {International Journal of Biological Macromolecules},
	volume = {113},
	year = {2018},
	month = {JUL},
	pages = {933-943},
	type = {Article},
	abstract = {Legume Kunitz type trypsin inhibitor (KTI) family is one of the most versatile families of proteins. A typical KTI features a single peptide folded in beta-trefoil manner, with the molecular weight about 20-22 kDa and two disulphide bonds. The members are known to inhibit a wide range of serpins proteases at the same time many of them possess unique features. Copaifera langsdoiffii Trypsin inhibitor (CTI) has a beta-trefoil fold made up of two non-covalently bound polypeptide chains with only a single disulfide bridge. Delonix regia Trypsin inhibitor (DrTI) has one amino acid insertion between P1 and P2 of the reactive site distorting its conformation. Bauhinia bauhinioides Cruzipain inhibitor (BbCI) has a conservative beta-trefoil fold but lacks disulfide bonds. Such subtle differences in structures make Kunitz inhibitors different from other inhibitor families. Most of the studies on these inhibitors are focused towards their proposed role in defense from insect pests and wounding but their exact physiological role in nature is still uncharted. Thus, it would be very interesting to closely analyze the structural details of these inhibitors in order to ascertain their biological role and other fascinating applications. (C) 2018 Elsevier B.V. All rights reserved.},
	doi = {10.1016/j.ijbiomac.2018.02.148},
	author = {Bendre, Ameya D. and Ramasamy, Sureshkumar and Suresh, C. G.}
}
@article {44422,
	title = {Analysis of tail-anchored protein translocation pathway in plants},
	journal = {Biochemistry and Biophysics Reports },
	volume = {14},
	year = {2018},
	month = {JUL},
	pages = {161-167},
	abstract = {Tail-anchored (TA) proteins are a special class of membrane proteins that carry out vital functions in all living cells. Targeting mechanisms of TA proteins are investigated as the best example for post-translational protein targeting in yeast. Of the several mechanisms, Guided Entry of Tail-anchored protein (GET) pathway plays a major role in TA protein targeting. Many in silico and in vivo analyses are geared to identify TA proteins and their targeting mechanisms in different systems including Arabidopsis thaliana. Yet, crop plants that grow in specific and/or different conditions are not investigated for the presence of TA proteins and GET pathway. This study majorly investigates GET pathway in two crop plants, Oryza sativa subsp. Indica and Solanum tuberosum, through detailed in silico analysis. 508 and 912 TA proteins are identified in Oryza sativa subsp. Indica and Solanum tuberosum respectively and their localization with respect to endoplasmic reticulum (ER), mitochondria, and chloroplast has been delineated. Similarly, the associated GET proteins are identified (Get1, Get3 and Get4) and their structural inferences are elucidated using homology modelling. Get3 models are based on yeast Get3. The cytoplasmic Get3 from O. sativa is identified to be very similar to yeast Get3 with conserved P-loop and TA binding groove. Three cytoplasmic Get3s are identified for S. tuberosum. Taken together, this is the first study to identify TA proteins and GET components in Oryza sativa subsp. Indica and Solanum tuberosum, forming the basis for any further experimental characterization of TA targeting and GET pathway mechanisms in crop plants.

},
	doi = {10.1016/j.bbrep.2018.05.001},
	author = {Manu, M. S. and Ghosh, Deepanjan and Chaudhari, Bhushan P. and Ramasamy, Sureshkumar}
}
@article {47018,
	title = {Archeal Di-O-geranylgeranyl glyceryl phosphate synthase of a UbiA superfamily member provides insight into the multiple human diseases},
	journal = {Protein and Peptide Letters},
	volume = {27},
	year = {2020},
	month = {JAN},
	pages = {568-573},
	type = {Review},
	abstract = {<p>One of the unique characteristic features of the domain archaea, are the lipids that form the hydrophobic core of their cell membrane. These membrane lipids are characterized by distinctive isoprenoid biochemistry and the building blocks are two core lipid structures, sn-2,3-diphytanyl glycerol diether (archaeol) and sn-2,3-dibiphytanyl diglycerol tetraether (caldarchaeol). Archaeol has two phytanyl chains (C-20 in a bilayer structure connected to the glycerol moiety by an ether bond. The enzyme involved in this bilayer formation is Di-O-Geranylgeranyl Glyceryl Phosphate Synthase (DGGGPS), which is a member of a very versatile superfamily of enzymes known as UbiA superfamily. Multiple sequence analysis of the typical members of the UbiA superfamily indicates that the majority of conserved residues are located around the central cavity of these enzymes. Interestingly few of these conserved residues in the human homologs are centrally implicated in several human diseases, on basis of the major mutations reported against these diseases in the earlier clinical studies. It remains to he investigated about the role of these conserved residues in the biochemistiy of these enzymes. The binding and active site of these enzymes found to be similar architecture but have different substrate affinities ranging from aromatic to linear compounds. So further investigation of UbiA superfamily may be translated to novel therapeutic and diagnostic application of these proteins in human disease management.</p>
},
	keywords = {Archeal lipids, biA superfamily, DGGGPS, genetic diseases, lipid synthesis, membrane protein},
	issn = {0929-8665},
	doi = {10.2174/0929866526666191209143948},
	author = {Boral, Debjyoti and Rao, Vamkudoth Koteswara and Ramasamy, Sureshkumar}
}
