A
Amit Sonkar
Researcher at North Eastern Hill University
Publications - 18
Citations - 404
Amit Sonkar is an academic researcher from North Eastern Hill University. The author has contributed to research in topics: Isocitrate lyase & Glyoxylate cycle. The author has an hindex of 9, co-authored 17 publications receiving 320 citations. Previous affiliations of Amit Sonkar include Central Drug Research Institute.
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Journal ArticleDOI
Structure-based screening and molecular dynamics simulations offer novel natural compounds as potential inhibitors of Mycobacterium tuberculosis isocitrate lyase.
TL;DR: It is concluded that ZINC2111081 has a great potential to inhibit MtbICL and would add to the drug discovery process against tuberculosis.
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Distant Phe345 mutation compromises the stability and activity of Mycobacterium tuberculosis isocitrate lyase by modulating its structural flexibility.
TL;DR: The conformational flexibility of MtbICL is studied to better understand its stability and catalytic activity and reveals internal dynamics of the enzyme structure and suggests that regions other than the active site should be exploited for targeting MtbicL inhibition and development of novel anti-tuberculosis compounds.
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Identification of potential inhibitors of Fasciola gigantica thioredoxin1: computational screening, molecular dynamics simulation, and binding free energy studies.
Rohit Shukla,Harish Shukla,Parismita Kalita,Amit Sonkar,Tripti Pandey,Dev Bukhsh Singh,Awanish Kumar,Timir Tripathi +7 more
TL;DR: A structure-based virtual screening of natural compounds from the ZINC database against the FgTrx1 structure found two compounds that could be potential drug candidates to fight against F. gigantica parasites.
Journal ArticleDOI
Alterations in conformational topology and interaction dynamics caused by L418A mutation leads to activity loss of Mycobacterium tuberculosis isocitrate lyase.
TL;DR: The docking results suggest that L418A mutation influenced the binding interactions of the substrate with several residues in the active site of MtbICL, highlighting the importance of residue level interactions in the protein.
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Identification of novel natural inhibitors of Opisthorchis felineus cytochrome P450 using structure-based screening and molecular dynamic simulation.
Rohit Shukla,Purna B Chetri,Amit Sonkar,Maria Y. Pakharukova,Viatcheslav A. Mordvinov,Timir Tripathi +5 more
TL;DR: A structure-based virtual screening of natural compounds from the ZINC database against the OfCYP450 concluded that Zinc8790946, ZINC70707116, and ZINC85878789 have excellent potential to inhibit OfCyp450.