{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["20(10)"],"submitter":["Reyes-Espinosa F"],"pubmed_abstract":["An in silico analysis of the interaction between the complex-ligands of nine acetylcholinesterase (AChE) structures of Lepidopteran organisms and 43 organophosphorus (OPs) pesticides with previous resistance reports was carried out. To predict the potential resistance by structural modifications in Lepidoptera insects, due to proposed point mutations in AChE, a broad analysis was performed using computational tools, such as homology modeling and molecular docking. Two relevant findings were revealed: (1) Docking results give a configuration of the most probable spatial orientation of two interacting molecules (AChE enzyme and OP pesticide) and (2) a predicted ΔGb. The mutations evaluated in the form 1 acetylcholinesterase (AChE-1) and form 2 acetylcholinesterase (AChE-2) structures of enzy"],"journal":["International journal of molecular sciences"],"pagination":["E2404"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6566587"],"repository":["biostudies-literature"],"pubmed_title":["In Silico Study of the Resistance to Organophosphorus Pesticides Associated with Point Mutations in Acetylcholinesterase of Lepidoptera: B. mandarina, B. mori, C. auricilius, C. suppressalis, C. pomonella, H. armigera, P. xylostella, S. frugiperda, and S. litura."],"pmcid":["PMC6566587"],"pubmed_authors":["Herrera-Mayorga V","Rivera G","Reyes-Espinosa F","Mendez-Alvarez D","Perez-Rodriguez MA","Cruz-Hernandez MA","Juarez-Saldivar A"],"additional_accession":[]},"is_claimable":false,"name":"In Silico Study of the Resistance to Organophosphorus Pesticides Associated with Point Mutations in Acetylcholinesterase of Lepidoptera: B. mandarina, B. mori, C. auricilius, C. suppressalis, C. pomonella, H. armigera, P. xylostella, S. frugiperda, and S. litura.","description":"An in silico analysis of the interaction between the complex-ligands of nine acetylcholinesterase (AChE) structures of Lepidopteran organisms and 43 organophosphorus (OPs) pesticides with previous resistance reports was carried out. To predict the potential resistance by structural modifications in Lepidoptera insects, due to proposed point mutations in AChE, a broad analysis was performed using computational tools, such as homology modeling and molecular docking. Two relevant findings were revealed: (1) Docking results give a configuration of the most probable spatial orientation of two interacting molecules (AChE enzyme and OP pesticide) and (2) a predicted ΔGb. The mutations evaluated in the form 1 acetylcholinesterase (AChE-1) and form 2 acetylcholinesterase (AChE-2) structures of enzy","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 May","modification":"2025-04-05T10:22:17.758Z","creation":"2019-07-24T07:17:52Z"},"accession":"S-EPMC6566587","cross_references":{"pubmed":["31096579"],"doi":["10.3390/ijms20102404"]}}