J
Jatin Sharma
Researcher at Council of Scientific and Industrial Research
Publications - 15
Citations - 803
Jatin Sharma is an academic researcher from Council of Scientific and Industrial Research. The author has contributed to research in topics: Docking (molecular) & Binding site. The author has an hindex of 9, co-authored 15 publications receiving 339 citations.
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Identification of bioactive molecules from tea plant as SARS-CoV-2 main protease inhibitors.
TL;DR: This study showed Oolonghomobisflavan-A as a potential bioactive molecule to act as an inhibitor for the Mpro of SARS-CoV-2.
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An in-silico evaluation of different bioactive molecules of tea for their inhibition potency against non structural protein-15 of SARS-CoV-2.
Jatin Sharma,Vijay Kumar Bhardwaj,Vijay Kumar Bhardwaj,Rahul Singh,Vidya Rajendran,Rituraj Purohit,Rituraj Purohit,Sanjay Kumar +7 more
TL;DR: Barrigenol, Kaempferol, and Myricetin molecules displayed low binding energy during MMPBSA calculations, substantiating their strong association with Nsp15 and the inhibitory potential of these molecules could further be examined by in-vivo and in- vitro investigations to validate their use as inhibitors against Nsp 15 of SARS-CoV2.
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In-silico evaluation of bioactive compounds from tea as potential SARS-CoV-2 nonstructural protein 16 inhibitors.
Rahul Singh,Vijay Kumar Bhardwaj,Vijay Kumar Bhardwaj,Jatin Sharma,Rituraj Purohit,Rituraj Purohit,Sanjay Kumar +6 more
TL;DR: In this article, the authors conducted molecular docking and structural dynamics studies with a set of 65 tea bioactive compounds to illustrate their ability to inhibit NSP16 of SARS-CoV-2.
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Identification of potential plant bioactive as SARS-CoV-2 Spike protein and human ACE2 fusion inhibitors.
TL;DR: In this paper, the Spike receptor binding domain (S-RBD) from SARS-CoV-2, a crucial protein for the entrance of the virus into target cells is known to cause infection by binding to a cell surface protein.
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Structural based study to identify new potential inhibitors for dual specificity tyrosine-phosphorylation- regulated kinase.
TL;DR: Ligand15, Ligand14, and Ligands11 are reported as potent inhibitors of DYRK1A which showed higher ligand efficiency, binding affinity, lipophilic lig and efficiency, and favorable torsion values as compared to 2C3.