R
R. Rajasekaran
Researcher at VIT University
Publications - 71
Citations - 931
R. Rajasekaran is an academic researcher from VIT University. The author has contributed to research in topics: Mutant & Single-nucleotide polymorphism. The author has an hindex of 15, co-authored 69 publications receiving 758 citations. Previous affiliations of R. Rajasekaran include Department of Biotechnology.
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Quantum chemical and molecular mechanics studies on the assessment of interactions between resveratrol and mutant SOD1 (G93A) protein.
E. Srinivasan,R. Rajasekaran +1 more
TL;DR: The combined biophysical and quantum chemical studies in this study supported the results of previous experimental studies, thereby stipulating an action of resveratrol on mutant SOD1 and paving a way for the design of highly potent effective inhibitors against fALS affecting the mankind.
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Spectroscopic, Computational, Antimicrobial, DNA Interaction, In Vitro Anticancer and Molecular Docking Properties of Biochemically Active Cu(II) and Zn(II) Complexes of Pyrimidine-Ligand
Murugesan Sankarganesh,Jeyaraj Dhaveethu Raja,Paul Raj Adwin Jose,Gujuluva Gangatharan Vinoth Kumar,Jegathalaprathaban Rajesh,R. Rajasekaran +5 more
TL;DR: In vitro anticancer activities of L, complexes 1 and 2 against selected cancer and normal (NHDF) cell lines were assessed by MTT assay and results suggest, the compounds are interacted with DNA may be electrostatic binding.
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Bio-active mixed ligand Cu(II) and Zn(II) complexes of pyrimidine derivative Schiff base: DFT calculation, antimicrobial, antioxidant, DNA binding, anticancer and molecular docking studies
Nagaraj Revathi,Murugesan Sankarganesh,Jeyaraj Dhaveethu Raja,Gujuluva Gangatharan Vinoth Kumar,A. Sakthivel,R. Rajasekaran +5 more
TL;DR: In vitro cytotoxicity of the Schiff base (HL) and complexes 1–4 shows that complex 1 shows better ability to inhibit the growth of cancer cells and may be an appreciated material in cancer chemotherapy mediators in imminent years.
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Exploring the cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis.
E. Srinivasan,R. Rajasekaran +1 more
TL;DR: The theoretical mechanism to unravel the mutational effects of cofactor dependent protein, G85R, is revealed, indicating the reduced Zn binding affinity in the mutant as compared to that of the wild type.
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Phenytoin-Bovine Serum Albumin interactions - modeling plasma protein - drug binding: A multi-spectroscopy and in silico-based correlation.
TL;DR: In vitro interactions of Phenytoin with BSA corroborate the tryptophan-based spectral shifts and the fluorescence quenching data and provides a basis for screening other hydrophobic drugs in its class.