{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T03:30:25Z","timestamp":1783135825155,"version":"3.54.6"},"reference-count":40,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T00:00:00Z","timestamp":1770681600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2026,3,4]],"date-time":"2026-03-04T00:00:00Z","timestamp":1772582400000},"content-version":"vor","delay-in-days":22,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"name":"A*STAR Joint 1094 Council Office for a Career Development Award\/Fund","award":["222D800029"],"award-info":[{"award-number":["222D800029"]}]},{"DOI":"10.13039\/100010053","name":"Oxford Brookes University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010053","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Mahidol Oxford Translational Innovation Partnership","award":["MoTIP-TSA 2023\/001"],"award-info":[{"award-number":["MoTIP-TSA 2023\/001"]}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"crossref","award":["104926\/Z\/14\/Z"],"award-info":[{"award-number":["104926\/Z\/14\/Z"]}],"id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Ivermectin is lethal to\n                    <jats:italic>Anopheles<\/jats:italic>\n                    mosquitoes making it a possible malaria control intervention. The primary mode of action of ivermectin occurs when it binds to the glutamate-gated chloride channel (GluCl), allowing for continuous flow of chloride leading to flaccid paralysis and death of the mosquito. In\n                    <jats:italic>Caenorhabditis elegans,<\/jats:italic>\n                    ivermectin is thought to open the GluCl channel when the M2-M3 loop forms Van der Waals bonds with the first sugar ring and aglycone structure of ivermectin. Here we investigate in\n                    <jats:italic>Anopheles dirus<\/jats:italic>\n                    and\n                    <jats:italic>Anopheles minimus<\/jats:italic>\n                    the mosquito-lethal effect of ivermectin (both sugar rings), monosaccharide (one sugar ring), and aglycone (no sugar rings) demonstrating full, partial, and no effect, respectively. The\n                    <jats:italic>Anopheles<\/jats:italic>\n                    GluCl protein sequences were determined and used to a create 3-D structural docking models. The docking models identified new binding interactions with a hydrogen bond forming between the second sugar ring hydroxyl group (4\u2033-OH) and THR304 of the\n                    <jats:italic>Anopheles<\/jats:italic>\n                    GluCl M2-M3 loop. This hydrogen bond is possible due to a single substitution in the M2-M3 loop from\n                    <jats:italic>C. elegans<\/jats:italic>\n                    ILE273 to\n                    <jats:italic>Anopheles<\/jats:italic>\n                    THR304. The work presented here improves our understanding of\n                    <jats:italic>Anopheles<\/jats:italic>\n                    GluCl-ivermectin interactions as well as how ivermectin resistance could arise in the future.\n                  <\/jats:p>","DOI":"10.1038\/s41598-026-39698-8","type":"journal-article","created":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T04:19:24Z","timestamp":1770697164000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Lethal effects of ivermectin structures on malaria vectors and in silico analysis of interactions with their glutamate-gated chloride ion channels"],"prefix":"10.1038","volume":"16","author":[{"given":"Minh N.","family":"Nguyen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew K.","family":"Jones","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Hotwagner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pattarapon","family":"Khemrattrakool","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thitipong","family":"Hongsuwong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Borimas","family":"Hanboonkunupakarn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Podjanee","family":"Jittamala","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patchara","family":"Sriwichai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joel","family":"Tarning","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin C.","family":"Kobylinski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,2,10]]},"reference":[{"key":"39698_CR1","doi-asserted-by":"publisher","first-page":"3","DOI":"10.4269\/ajtmh.19-0620","volume":"102","author":"P Billingsley","year":"2020","unstructured":"Billingsley, P. et al. A Roadmap for the Development of Ivermectin as a Complementary Malaria Vector Control Tool. Am. J. Trop. Med. Hyg. 102, 3\u201324. https:\/\/doi.org\/10.4269\/ajtmh.19-0620 (2020).","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"39698_CR2","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1038\/nature10139","volume":"474","author":"R Hibbs","year":"2011","unstructured":"Hibbs, R. & Gouaux, E. Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 474, 54\u201360. https:\/\/doi.org\/10.1038\/nature10139 (2011).","journal-title":"Nature"},{"key":"39698_CR3","doi-asserted-by":"publisher","first-page":"707","DOI":"10.1038\/371707a0","volume":"371","author":"D Cully","year":"1994","unstructured":"Cully, D. et al. Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans. Nature 371, 707\u2013711. https:\/\/doi.org\/10.1038\/371707a0 (1994).","journal-title":"Nature"},{"key":"39698_CR4","doi-asserted-by":"publisher","first-page":"20187","DOI":"10.1074\/jbc.271.33.20187","volume":"271","author":"D Cully","year":"1996","unstructured":"Cully, D., Paress, P., Liu, K., Schaeffer, J. & Arena, J. Identification of a Drosophila melanogaster glutamate-gated chloride channel sensitive to the antiparasitic agent avermectin. J. Biol. Chem. 271, 20187\u201320191. https:\/\/doi.org\/10.1074\/jbc.271.33.20187 (1996).","journal-title":"J. Biol. Chem."},{"key":"39698_CR5","doi-asserted-by":"publisher","first-page":"13949","DOI":"10.1073\/pnas.240464697","volume":"97","author":"N Kane","year":"2000","unstructured":"Kane, N. et al. Drug-resistant Drosophila indicate glutamate-gated chloride channels are targets for the antiparasitics nodulisporic acid and ivermectin. Proc. Natl. Acad. Sci. USA 97, 13949\u201313954. https:\/\/doi.org\/10.1073\/pnas.240464697 (2000).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"39698_CR6","doi-asserted-by":"publisher","first-page":"40232","DOI":"10.1074\/jbc.R112.406280","volume":"287","author":"A Wolstenholme","year":"2012","unstructured":"Wolstenholme, A. Glutamate-gated chloride channels. J. Biol. Chem. 287, 40232\u201340238. https:\/\/doi.org\/10.1074\/jbc.R112.406280 (2012).","journal-title":"J. Biol. Chem."},{"key":"39698_CR7","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1038\/nature13669","volume":"512","author":"T Althoff","year":"2014","unstructured":"Althoff, T., Hibbs, R., Banerjee, S. & Gouaux, E. X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors. Nature 512, 333\u2013337. https:\/\/doi.org\/10.1038\/nature13669 (2014).","journal-title":"Nature"},{"key":"39698_CR8","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.cois.2018.07.016","volume":"30","author":"A Jones","year":"2018","unstructured":"Jones, A. Genomics, cys-loop ligand-gated ion channels and new targets for the control of insect pests and vectors. Curr. Opin. Insect Sci. 30, 1\u20137. https:\/\/doi.org\/10.1016\/j.cois.2018.07.016 (2018).","journal-title":"Curr. Opin. Insect Sci."},{"key":"39698_CR9","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1007\/s10158-008-0068-4","volume":"8","author":"A Jones","year":"2008","unstructured":"Jones, A. & Sattelle, D. The cys-loop ligand-gated ion channel gene superfamily of the nematode. Caenorhabditis elegans. Invert. Neurosci. 8, 41\u201347. https:\/\/doi.org\/10.1007\/s10158-008-0068-4 (2008).","journal-title":"Caenorhabditis elegans. Invert. Neurosci."},{"key":"39698_CR10","doi-asserted-by":"publisher","first-page":"1478","DOI":"10.1242\/jeb.118570","volume":"218","author":"J Meyers","year":"2015","unstructured":"Meyers, J. et al. Characterization of the target of ivermectin, the glutamate-gated chloride channel, from Anopheles gambiae. J. Exp. Biol. 218, 1478\u20131486. https:\/\/doi.org\/10.1242\/jeb.118570 (2015).","journal-title":"J. Exp. Biol."},{"key":"39698_CR11","doi-asserted-by":"publisher","first-page":"8131","DOI":"10.1038\/s41598-023-34719-2","volume":"13","author":"K Kobylinski","year":"2023","unstructured":"Kobylinski, K. et al. Ivermectin metabolites reduce Anopheles survival. Sci. Rep. 13, 8131. https:\/\/doi.org\/10.1038\/s41598-023-34719-2 (2023).","journal-title":"Sci. Rep."},{"key":"39698_CR12","doi-asserted-by":"publisher","DOI":"10.1186\/s12936-023-04624-0","volume":"22","author":"C Kern","year":"2023","unstructured":"Kern, C. et al. Pharmacokinetics of ivermectin metabolites and their activity against Anopheles stephensi mosquitoes. Malar. J. 22, e194. https:\/\/doi.org\/10.1186\/s12936-023-04624-0 (2023).","journal-title":"Malar. J."},{"key":"39698_CR13","doi-asserted-by":"publisher","DOI":"10.1002\/prp2.712","volume":"9","author":"P Tipthara","year":"2021","unstructured":"Tipthara, P. et al. Identification of the metabolites of ivermectin in humans. Pharmacol. Res. Perspect. 9, e00712. https:\/\/doi.org\/10.1002\/prp2.712 (2021).","journal-title":"Pharmacol. Res. Perspect."},{"key":"39698_CR14","doi-asserted-by":"publisher","first-page":"692","DOI":"10.1645\/0022-3395(2001)087[0692:Coidsa]2.0.Co;2","volume":"87","author":"B Michael","year":"2001","unstructured":"Michael, B., Meinke, P. & Shoop, W. Comparison of ivermectin, doramectin, selamectin, and eleven intermediates in a nematode larval development assay. J. Parasitol. 87, 692\u2013696. https:\/\/doi.org\/10.1645\/0022-3395(2001)087[0692:Coidsa]2.0.Co;2 (2001).","journal-title":"J. Parasitol."},{"key":"39698_CR15","doi-asserted-by":"publisher","first-page":"1750","DOI":"10.1021\/acs.jmedchem.0c00033","volume":"63","author":"L Singh","year":"2020","unstructured":"Singh, L. et al. Molecular Design and Synthesis of Ivermectin Hybrids Targeting Hepatic and Erythrocytic Stages of Plasmodium Parasites. J. Med. Chem. 63, 1750\u20131762. https:\/\/doi.org\/10.1021\/acs.jmedchem.0c00033 (2020).","journal-title":"J. Med. Chem."},{"key":"39698_CR16","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1007570","volume":"15","author":"M Atif","year":"2019","unstructured":"Atif, M. et al. GluClR-mediated inhibitory postsynaptic currents reveal targets for ivermectin and potential mechanisms of ivermectin resistance. PLoS Pathog. 15, e1007570. https:\/\/doi.org\/10.1371\/journal.ppat.1007570 (2019).","journal-title":"PLoS Pathog."},{"key":"39698_CR17","doi-asserted-by":"publisher","first-page":"43913","DOI":"10.1074\/jbc.M111.262634","volume":"286","author":"T Lynagh","year":"2011","unstructured":"Lynagh, T., Webb, T., Dixon, C., Cromer, B. & Lynch, J. Molecular determinants of ivermectin sensitivity at the glycine receptor chloride channel. J. Biol. Chem. 286, 43913\u201343924. https:\/\/doi.org\/10.1074\/jbc.M111.262634 (2011).","journal-title":"J. Biol. Chem."},{"key":"39698_CR18","doi-asserted-by":"publisher","first-page":"546","DOI":"10.1124\/mol.117.109413","volume":"92","author":"Y Nakata","year":"2017","unstructured":"Nakata, Y. et al. A Single Amino Acid Substitution in the Third Transmembrane Region Has Opposite Impacts on the Selectivity of the Parasiticides Fluralaner and Ivermectin for Ligand-Gated Chloride Channels. Mol. Pharmacol. 92, 546\u2013555. https:\/\/doi.org\/10.1124\/mol.117.109413 (2017).","journal-title":"Mol. Pharmacol."},{"key":"39698_CR19","doi-asserted-by":"publisher","first-page":"432","DOI":"10.1016\/j.tips.2012.05.002","volume":"33","author":"T Lynagh","year":"2012","unstructured":"Lynagh, T. & Lynch, J. Ivermectin binding sites in human and invertebrate Cys-loop receptors. Trends Pharmacol. Sci. 33, 432\u2013441. https:\/\/doi.org\/10.1016\/j.tips.2012.05.002 (2012).","journal-title":"Trends Pharmacol. Sci."},{"key":"39698_CR20","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1016\/j.ibmb.2016.08.005","volume":"77","author":"T Fuse","year":"2016","unstructured":"Fuse, T., Kita, T., Nakata, Y., Ozoe, F. & Ozoe, Y. Electrophysiological characterization of ivermectin triple actions on Musca chloride channels gated by l-glutamic acid and \u03b3-aminobutyric acid. Insect Biochem. Mol. Biol. 77, 78\u201386. https:\/\/doi.org\/10.1016\/j.ibmb.2016.08.005 (2016).","journal-title":"Insect Biochem. Mol. Biol."},{"key":"39698_CR21","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1111\/bph.14855","volume":"177","author":"M Atif","year":"2020","unstructured":"Atif, M., Lynch, J. & Keramidas, A. The effects of insecticides on two splice variants of the glutamate-gated chloride channel receptor of the major malaria vector. Anopheles gambiae. Br. J. Pharmacol. 177, 175\u2013187. https:\/\/doi.org\/10.1111\/bph.14855 (2020).","journal-title":"Anopheles gambiae. Br. J. Pharmacol."},{"key":"39698_CR22","doi-asserted-by":"publisher","first-page":"686","DOI":"10.1124\/mol.114.095869","volume":"86","author":"S Furutani","year":"2014","unstructured":"Furutani, S. et al. Exon 3 splicing and mutagenesis identify residues influencing cell surface density of heterologously expressed silkworm (Bombyx mori) glutamate-gated chloride channels. Mol. Pharmacol. 86, 686\u2013695. https:\/\/doi.org\/10.1124\/mol.114.095869 (2014).","journal-title":"Mol. Pharmacol."},{"key":"39698_CR23","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/j.pestbp.2014.10.010","volume":"117","author":"F Jiang","year":"2015","unstructured":"Jiang, F. et al. Identification of polymorphisms in Cyrtorhinus lividipennis RDL subunit contributing to fipronil sensitivity. Pestic. Biochem. Physiol. 117, 62\u201367. https:\/\/doi.org\/10.1016\/j.pestbp.2014.10.010 (2015).","journal-title":"Pestic. Biochem. Physiol."},{"key":"39698_CR24","doi-asserted-by":"publisher","first-page":"2114","DOI":"10.1002\/ps.8610","volume":"81","author":"S Wang","year":"2025","unstructured":"Wang, S. et al. Overexpression and alternative splicing of the glutamate-gated chloride channel are associated with emamectin benzoate resistance in the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Crambidae). Pest Manag. Sci. 81, 2114\u20132125. https:\/\/doi.org\/10.1002\/ps.8610 (2025).","journal-title":"Pest Manag. Sci."},{"key":"39698_CR25","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1046\/j.1471-4159.1999.0720066.x","volume":"72","author":"E Semenov","year":"1999","unstructured":"Semenov, E. & Pak, W. Diversification of Drosophila chloride channel gene by multiple posttranscriptional mRNA modifications. J. Neurochem. 72, 66\u201372. https:\/\/doi.org\/10.1046\/j.1471-4159.1999.0720066.x (1999).","journal-title":"J. Neurochem."},{"key":"39698_CR26","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.adi9101","volume":"10","author":"H Zak","year":"2024","unstructured":"Zak, H. et al. A highly conserved A-to-I RNA editing event within the glutamate-gated chloride channel GluCl\u03b1 is necessary for olfactory-based behaviors in Drosophila. Sci. Adv. 10, e9101. https:\/\/doi.org\/10.1126\/sciadv.adi9101 (2024).","journal-title":"Sci. Adv."},{"key":"39698_CR27","doi-asserted-by":"publisher","first-page":"4173","DOI":"10.1002\/ps.7035","volume":"78","author":"Q Wang","year":"2022","unstructured":"Wang, Q. et al. Functional analysis reveals ionotropic GABA receptor subunit RDL is a target site of ivermectin and fluralaner in the yellow fever mosquito. Aedes aegypti. Pest Manag. Sci. 78, 4173\u20134182. https:\/\/doi.org\/10.1002\/ps.7035 (2022).","journal-title":"Aedes aegypti. Pest Manag. Sci."},{"key":"39698_CR28","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ibmb.2017.12.001","volume":"93","author":"J Taylor-Wells","year":"2018","unstructured":"Taylor-Wells, J., Senan, A., Bermudez, I. & Jones, A. Species specific RNA A-to-I editing of mosquito RDL modulates GABA potency and influences agonistic, potentiating and antagonistic actions of ivermectin. Insect Biochem. Mol. Biol. 93, 1\u201311. https:\/\/doi.org\/10.1016\/j.ibmb.2017.12.001 (2018).","journal-title":"Insect Biochem. Mol. Biol."},{"key":"39698_CR29","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0097468","volume":"9","author":"K Lees","year":"2014","unstructured":"Lees, K. et al. Actions of agonists, fipronil and ivermectin on the predominant in vivo splice and edit variant (RDLbd, I\/V) of the Drosophila GABA receptor expressed in Xenopus laevis oocytes. PLoS ONE 9, e97468. https:\/\/doi.org\/10.1371\/journal.pone.0097468 (2014).","journal-title":"PLoS ONE"},{"key":"39698_CR30","doi-asserted-by":"publisher","first-page":"117954331880478","DOI":"10.1177\/1179543318804782","volume":"10","author":"AK Jones","year":"2018","unstructured":"Jones, A. K. How Complex Can Resistance to Dieldrin, the Insect \u03b3-Aminobutyric Acid Receptor, Get?. Int. J. Insect Sci. 10, 1179543318804782. https:\/\/doi.org\/10.1177\/1179543318804782 (2018).","journal-title":"Int. J. Insect Sci."},{"key":"39698_CR31","doi-asserted-by":"publisher","DOI":"10.1186\/s13071-021-04675-9","volume":"14","author":"P Nicolas","year":"2021","unstructured":"Nicolas, P. et al. Potential metabolic resistance mechanisms to ivermectin in Anopheles gambiae: a synergist bioassay study. Parasit. Vectors. 14, e172. https:\/\/doi.org\/10.1186\/s13071-021-04675-9 (2021).","journal-title":"Parasit. Vectors."},{"key":"39698_CR32","doi-asserted-by":"publisher","DOI":"10.1186\/s13071-024-06294-6","volume":"17","author":"P Khemrattrakool","year":"2024","unstructured":"Khemrattrakool, P. et al. Impact of ivermectin components on Anopheles dirus and Anopheles minimus mosquito survival. Parasit. Vectors. 17, e224. https:\/\/doi.org\/10.1186\/s13071-024-06294-6 (2024).","journal-title":"Parasit. Vectors."},{"key":"39698_CR33","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1016\/s0022-2836(05)80360-2","volume":"215","author":"S Altschul","year":"1990","unstructured":"Altschul, S., Gish, W., Miller, W., Myers, E. & Lipman, D. Basic local alignment search tool. J. Mol. Biol. 215, 403\u2013410. https:\/\/doi.org\/10.1016\/s0022-2836(05)80360-2 (1990).","journal-title":"J. Mol. Biol."},{"key":"39698_CR34","doi-asserted-by":"publisher","first-page":"4876","DOI":"10.1093\/nar\/25.24.4876","volume":"25","author":"J Thompson","year":"1997","unstructured":"Thompson, J., Gibson, T., Plewniak, F., Jeanmougin, F. & Higgins, D. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876\u20134882. https:\/\/doi.org\/10.1093\/nar\/25.24.4876 (1997).","journal-title":"Nucleic Acids Res."},{"key":"39698_CR35","doi-asserted-by":"publisher","first-page":"W24","DOI":"10.1093\/nar\/gkr393","volume":"39","author":"M Nguyen","year":"2011","unstructured":"Nguyen, M., Tan, K. & Madhusudhan, M. CLICK\u2013topology-independent comparison of biomolecular 3D structures. Nucleic Acids Res. 39, W24-28. https:\/\/doi.org\/10.1093\/nar\/gkr393 (2011).","journal-title":"Nucleic Acids Res."},{"key":"39698_CR36","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkr348","volume":"39","author":"M Nguyen","year":"2011","unstructured":"Nguyen, M. & Madhusudhan, M. Biological insights from topology independent comparison of protein 3D structures. Nucleic Acids Res. 39, e94. https:\/\/doi.org\/10.1093\/nar\/gkr348 (2011).","journal-title":"Nucleic Acids Res."},{"key":"39698_CR37","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkw819","volume":"45","author":"M Nguyen","year":"2017","unstructured":"Nguyen, M., Sim, A., Wan, Y., Madhusudhan, M. & Verma, C. Topology independent comparison of RNA 3D structures using the CLICK algorithm. Nucleic Acids Res. 45, e5. https:\/\/doi.org\/10.1093\/nar\/gkw819 (2017).","journal-title":"Nucleic Acids Res."},{"key":"39698_CR38","doi-asserted-by":"publisher","first-page":"1529","DOI":"10.1021\/acs.jcim.8b00762","volume":"59","author":"M Nguyen","year":"2019","unstructured":"Nguyen, M. et al. Discovering Putative Protein Targets of Small Molecules: A Study of the p53 Activator Nutlin. J. Chem. Inf. Model. 59, 1529\u20131546. https:\/\/doi.org\/10.1021\/acs.jcim.8b00762 (2019).","journal-title":"J. Chem. Inf. Model."},{"key":"39698_CR39","doi-asserted-by":"publisher","first-page":"W482","DOI":"10.1093\/nar\/gkz358","volume":"47","author":"M Nguyen","year":"2019","unstructured":"Nguyen, M., Verma, C. & Zhong, P. AppA: a web server for analysis, comparison, and visualization of contact residues and interfacial waters of antibody-antigen structures and models. Nucleic Acids Res. 47, W482\u2013W489. https:\/\/doi.org\/10.1093\/nar\/gkz358 (2019).","journal-title":"Nucleic Acids Res."},{"key":"39698_CR40","doi-asserted-by":"publisher","first-page":"W36","DOI":"10.1093\/nar\/gkac446","volume":"50","author":"M Nguyen","year":"2022","unstructured":"Nguyen, M. et al. AllerCatPro 2.0: a web server for predicting protein allergenicity potential. Nucleic Acids Res. 50, W36-43. https:\/\/doi.org\/10.1093\/nar\/gkac446 (2022).","journal-title":"Nucleic Acids Res."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-39698-8","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-39698-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-39698-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,16]],"date-time":"2026-06-16T17:59:32Z","timestamp":1781632772000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-026-39698-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,10]]},"references-count":40,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["39698"],"URL":"https:\/\/doi.org\/10.1038\/s41598-026-39698-8","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,10]]},"assertion":[{"value":"25 August 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"6 February 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"10 February 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}},{"value":"The human study protocol was approved by the ethics committees of the Faculty of Tropical Medicine, Mahidol University (MUTM 2021\u2013077) and the Oxford University Tropical Research Ethics Committee (OXTREC 28\u201321). The animal study protocol was approved by the Animal Care and Use Committee of the Faculty of Tropical Medicine, Mahidol University (007\u20132023). All experiments were performed in accordance with the relevant guidelines and regulations of the above listed institutions. Each blood donor volunteer was provided with an explanation of the study and signed a written informed consent before study entry.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics declaration"}}],"article-number":"8141"}}