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Diwakar Kumar

Researcher at Assam University

Publications -  12
Citations -  189

Diwakar Kumar is an academic researcher from Assam University. The author has contributed to research in topics: Docking (molecular) & Binding site. The author has an hindex of 5, co-authored 12 publications receiving 99 citations.

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Identification of potential inhibitors against SARS-CoV-2 by targeting proteins responsible for envelope formation and virion assembly using docking based virtual screening, and pharmacokinetics approaches.

TL;DR: Rutin, a bioflavonoid and the antibiotic, doxycycline, is identified as the most potent inhibitor of SARS-CoV-2 envelope protein, which is a essential role in the assembly and formation of the infectious virion particles.
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Evaluation of Flavonoids as 2019-nCoV Cell Entry Inhibitor Through Molecular Docking and Pharmacological Analysis

TL;DR: In this article, the authors aimed at the receipt binding domain of S protein and ACE-2 receptor as promising drug targets against SARS-CoV-2 Flavonoids with anti-viral properties were taken as ligand for molecular docking Selected flavonoids showed extremely good pharmacokinetics properties with good absorption, solubility, metabolism, excretion, distribution, bioavailability and minimal toxicity.
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Linking gut microbiota with the human diseases.

TL;DR: A review of known data for the correction of dysbiosis (imbalance in microbe population) towards improved human health is reported.
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Discovering Potential RNA Dependent RNA Polymerase Inhibitors as Prospective Drugs Against COVID-19: An in silico Approach

TL;DR: In this paper, a unique collection of 248 plant compounds were selected based on their antiviral activity published in previous literature and were subjected to molecular docking analysis against the catalytic sub-unit of RdRp.
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Evaluation of potential drugs against leishmaniasis targeting catalytic subunit of Leishmania donovani nuclear DNA primase using ligand based virtual screening, docking and molecular dynamics approaches.

TL;DR: This study aimed Ld-PriS for the first time as a prospective target for the application of drug against Leishmania parasite and showed very poor binding affinity toward the catalytic subunit of human primase indicating their safety toward the host normal replication mechanism.