Author

S. Kalyaanamoorthy

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:drug response / drug discovery· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1 Assay:structural biology· 1 Organism:virus· 1

Frequent Co-Authors

A. Ganesan· 2 shared M. McLeod· 1 shared N. Dingelstad· 1 shared N. Tran· 1 shared S. Barwell· 1 shared S. Dasari· 1 shared S. R. Naik· 1 shared T. Holyoak· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 21 mutual co-author links

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2 shared papersBiochemistry

A. Ganesan

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Author profile →

2 papers

Recent·Most cited

BiochemistrybioRxivPreprintDec 16, 2022

The H163A Mutation Unravels an Oxidized Conformation of the SARS-CoV-2 Main Protease and Opens a New Avenue for Anti-Viral Therapeutic Design

N. Tran, S. Dasari, S. Barwell…·A. Ganesan

This study identifies an oxidized conformation of SARS-CoV-2 Mpro through a point mutation and suggests it could inform new antiviral strategies.

DOI 10.1101/2022.12.16.520794

virusstructural biology

𝕏 PostBluesky

BiophysicsbioRxivOct 31, 2020

Molecular dynamics and in silico mutagenesis on the reversible inhibitor-bound SARS-CoV-2 Main Protease complexes reveal the role of lateral pocket in enhancing the ligand affinity

Y. L. Weng, S. R. Naik, N. Dingelstad…·A. Ganesan

This study uses molecular dynamics simulations and in silico mutagenesis to analyze ligand binding in SARS-CoV-2 Mpro, identifying key residues and a lateral pocket critical for enhancing ligand affinity.

DOI 10.1038/s41598-021-86471-0

humanprotein structure

𝕏 PostBluesky