Publications

G. Chandrasekhar, E. Srinivasan, P.C. Sekar, S. Venkataramanan, R. Rajasekaran, Molecular simulation probes the potency of resveratrol in regulating the toxic aggregation of mutant V30M TTR fibrils in Transthyretin mediated amyloidosis, Journal of Molecular Graphics and Modelling, 110 (2022).IF-2.5

Vandana, Rajan Pandey, E Srinivasan, Inderjeet Kalia, Agam P Singh, Ajay Saxena, R Rajaekaran, Dinesh Gupta, Kailash C Pandey, Plasmodium falciparum metacaspase-2 capture its natural substrate in a non-canonical way, The Journal of Biochemistry, 170, 5, (2021).IF-1.3

P.C. Sekar, D.M. Paul, E. Srinivasan, R. Rajasekaran, Unravelling the molecular effect of ocellatin-1, F1, K1 and S1, the frog-skin antimicrobial peptides to enhance its therapeutics—quantum and molecular mechanical approaches, Journal of Molecular Modeling, 27 (2021). IF-1.8

G. Chandrasekhar, P. Chandra Sekar, E. Srinivasan, A. Amarnath, H. Pengyong, R. Rajasekaran, Molecular simulation unravels the amyloidogenic misfolding of nascent ApoA1 protein, driven by deleterious point mutations occurring in between 170–178 hotspot region, Journal of Biomolecular Structure and Dynamics, (2021).

E. Srinivasan, G. Chandrasekhar, P. Chandrasekar, K. Anbarasu, A.S. Vickram, R.Karunakaran, R. Rajasekaran, P.S. Srikumar, Alpha-Synuclein Aggregation in Parkinson’s Disease, Frontiers in Medicine, 8 (2021). IF-5.1

E. Srinivasan, G. Chandrasekhar, P. Chandrasekar, K. Anbarasu, A.S. Vickram, I.A.Tayubi, R. Rajasekaran, R. Karunakaran, Decoding Conformational Imprint of Convoluted Molecular Interactions Between Prenylflavonoids and Aggregated Amyloid-Beta42 Peptide Causing Alzheimer’s Disease, Frontiers in Chemistry, 9 (2021). IF-5.0

Sekar, P.C., Paul, D.M., Srinivasan, E., Rajasekaran, R. Unravelling the molecular effect of ocellatin-1, F1, K1 and S1, the frog-skin antimicrobial peptides to enhance its therapeutics—quantum and molecular mechanical approaches. Journal of Molecular Modeling, https://doi.org/10.1007/s00894-020-04652-6 IF-1.3

Srinivasan E, Rajasekaran R. A Systematic and Comprehensive Review on Disease-Causing Genes in Amyotrophic Lateral Sclerosis, Journal of Molecular Neuroscience, https://doi:10.1007/s12031-020-01569-w IF- 2.5

Srinivasan E, Natarajan N, Rajasekaran R. TTRMDB: A database for structural and functional analysis on the impact of SNPs over transthyretin (TTR) using bioinformatic tools, Computational Biology and Chemistry, https://doi:10.1016/j.compbiolchem.2020.107290 IF- 1.5

Srinivasan, E., & Rajasekaran, R. Combating effect of baicalein on human islet amyloid polypeptide aggregates: A quantum chemical and molecular dynamics perspective. Molecular Simulation, https://doi.org/10.1080/08927022.2019.1660778 IF- 1.5

Srinivasan, E., & Rajasekaran, R. Rational design of linear tripeptides against the aggregation of human mutant SOD1 protein causing amyotrophic lateral sclerosis. Journal of the Neurological Sciences, https://doi.org/10.1016/j.jns.2019.116425 IF- 2.6

Srinivasan, E., & Rajasekaran, R. Computational investigation on electrostatic loop mutants instigating destabilization and aggregation on human SOD1 protein causing amyotrophic lateral sclerosis. The Protein Journal, https://doi.org/10.1007/s10930-018-09809-0 IF- 1.5

Srinivasan, E., & Rajasekaran, R. Effect of β-cyclodextrin-EGCG complexion against aggregated a-synuclein through Density Function Theory and Discrete Molecular Dynamics. Chemical Physics Letters, https://doi.org/10.1016/j.cplett.2018.12.042 IF- 1.3

Srinivasan, E., & Rajasekaran, R. Molecular binding response of naringin and naringenin to H46R mutant SOD1 protein in combating protein aggregation using density functional theory and discrete molecular dynamics. Progress in Biophysics and Molecular Biology, https://doi.org/10.1016/j.pbiomolbio.2018.12.003 IF-3.4

Srinivasan, E., & Rajasekaran, R. Quantum chemical and molecular mechanics studies on the assessment of interactions between Resveratrol and mutant SOD1 (G93A) protein. Journal of Computer aided Molecular Design, https://doi.org/10.1007/s10822-018-0175-1 IF-2.4

E. Srinivasan, R. Rajasekaran: Comparative binding of Kaempferol and Kaempferide on inhibiting the aggregate formation of mutant (G85R) SOD1 protein in familial amyotrophic lateral sclerosis - A quantum chemical and molecular mechanics study. BioFactors, https://doi.org/10.1002/biof.1441 IF-3.2

Srinivasan, E., & Rajasekaran, R. Deciphering the loss of metal binding due to mutation D83G of human SOD1 protein causing FALS disease. International Journal of Biological Macromolecules, 107(PartA), 521–529. https://doi.org/10.1016/j.ijbiomac.2017.09.019 IF-3.9

Srinivasan, E Rajasekaran, R. Cysteine to Serine Conversion at 111th Position Renders the Disaggregation and Retains the Stabilization of Detrimental SOD1 A4V Mutant Against Amyotrophic Lateral Sclerosis in Human—A Discrete Molecular Dynamics Study. Cell Biochemistry and Biophysics. https://doi.org/10.1007/s12013-017-0830-5 IF-1.3

Senthilkumar, B., Meshach Paul, D., Srinivasan, E., & Rajasekaran, R. Structural Stability Among Hybrid Antimicrobial Peptide Cecropin A(1–8)–Magainin 2(1–12) and Its Analogues: A Computational Approach. Journal of Cluster Science, 28(5), 2549–2563. https://doi.org/10.1007/s10876-017-1240-y IF-1.7

Srinivasan E, Rajasekaran R: Computational investigation on human SOD1 mutant (Cys146Arg) that directs familial amyotrophic lateral sclerosis. Molecular BioSystems, https://doi.org/10.1039/C7MB00106A IF-2.8

E. Srinivasan, R. Rajasekaran: Probing the inhibitory activity of Epigallocatechin-gallate on toxic aggregates of mutant (L84F) SOD1 protein through geometry based sampling and steered molecular dynamics. Journal of molecular graphics & modeling. https://doi.org/10.1016/j.jmgm.2017.04.019 IF-1.7

E. Srinivasan, Rao Sethumadhavan, R. Rajasekaran: A theoretical study on Zn binding loop mutants instigating destabilization and metal binding loss in human SOD1 protein. Journal of Molecular Modeling, 23(4). https://doi.org/10.1007/s00894-017-3286-z IF-1.4

E. Srinivasan, R. Rajasekaran: Exploring the cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering Amyotrophic lateral sclerosis: In silico study on SOD1 mutant G85R. Proteins Structure Function and Bioinformatics, https://doi.org/10.1002/prot.25288 IF-2.4

E. Srinivasan & R. Rajasekaran. Computational simulation analysis on human SOD1 mutant (H80R) exposes the structural destabilization and the deviation of Zn binding that directs familial amyotrophic lateral sclerosis, Journal of Biomolecular Structure and Dynamics, 35:12, 2645-2653, https://doi.org/10.1080/07391102.2016.1227723 IF-3.2

E. Srinivasan, R. Rajasekaran: Computational investigation of curcumin, a natural polyphenol that inhibits the destabilization and the aggregation of human SOD1 mutant (Ala4Val). RSC Advances, 6(104):102744-102753., https://doi.org/10.1039/C6RA21927F IF-3.2

V Bala Vignesh E Srinivasan: Molecular docking study ON NS5B polymerase of hepatitis c virus by screening of volatile compounds from Acacia concinna and ADMET prediction. International Journal of pharmacy and life sciences, 43(4), ISSN: 0976-7126.