Identification of potent inhibitors targeting Tribolium castaneum GSTe2 via structure-based screening and molecular dynamics simulation
Author:
Affiliation:
1. Jiangsu Key Laboratory for Biodiversity and Biotechnology, College of Life Sciences, Nanjing Normal University, Nanjing, China
2. Department of Life Science, University of Science, Pyongyang, Democratic People’s Republic of Korea
Funder
National Natural Science Foundation of China
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2024.2306499
Reference50 articles.
1. Biotransformation of Methyl Parathion by Glutathione S-Transferases
2. Baker, E. N. (2001). Hydrogen bonding in biological macromolecules. In M. G. Rossmann & E. Arnold (Eds.), International Tables for Crystallography Volume F: Crystallography of biological macromolecules. (pp. 546–552). Springer Netherlands.
3. In vitro and in silico enzyme inhibition effects of some metal ions and compounds on glutathione S-transferase enzyme purified from Vaccinium arctostapylous L.
4. Tribolium castaneum: A Model Insect for Fundamental and Applied Research
5. Homology modeling, docking, molecular dynamics and in vitro studies to identify Rhipicephalus microplus acetylcholinesterase inhibitors
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