AR
AMUTHA RAMASWAMY
Bioinformatics Centre Pondicherry, Katholieke Universiteit Leuven, Central Leather Research Institute CSIR, Madras Christian College, University of Tokyo, Manonmaniam Sundaranar University
0000-0002-4677-2263
Employment
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Bioinformatics Centre Pondicherry Assistant Professor2009 - Present
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Katholieke Universiteit Leuven Postdoctoral Fellow2008 - 2009
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University of Tokyo Postdoctoral Fellow2005 - 2006
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Ohio State University Postdoctoral Fellow2003 - 2004
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University of Pittsburgh Postdoctoral Fellow2002 - 2003
Education
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Central Leather Research Institute CSIR Ph. D1999 - 2002
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Madras Christian College M. Phil.1996 - 1997
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Manonmaniam Sundaranar University B.Ed1995 - 1996
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Manonmaniam Sundaranar University MSc1993 - 1995
Projects & Funding
Projects & funding information is unavailable.
Publications (38)
- Designing a multi-epitope vaccine candidate against pandemic influenza a virus: an immunoinformatics and structural vaccinology approach Save
- Structural dynamics of the RNA dependent RNA polymerase of H1N1 strain affecting humans: a bioinformatics approach Save
- Structure-based virtual screening of natural compounds against wild and mutant (R1155K, A1156T and D1168A) NS3-4A protease of Hepatitis C virus Save
- Influence of Cataract Causing Mutations on αA-Crystallin: A Computational Approach Save
- Molecular dynamics of interaction of Sesamin and related compounds with the cancer marker β-catenin: an in silico study Save
- Effects of Peutz-Jeghers syndrome (PJS) causing missense mutations L67P, L182P, G242V and R297S on the structural dynamics of LKB1 (Liver kinase B1) protein Save
- Identification of inhibitor against H. pylori HtrA protease using structure-based virtual screening and molecular dynamics simulations approaches Save
- Structural dynamics of wild type and mutated forms of human L1 endonuclease and insights into its sequence specific nucleic acid binding mechanism: A molecular dynamics study Save
- Molecular Dynamics of double stranded Xylo Nucleic Acid (XyloNA) Save
- The proteinopathy of D169G and K263E mutants at the RNA Recognition Motif (RRM) domain of tar DNA-binding protein (tdp43) causing neurological disorders: A computational study Save