{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T16:19:58Z","timestamp":1790957998117,"version":"4.1.0"},"reference-count":96,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2020,9,28]],"date-time":"2020-09-28T00:00:00Z","timestamp":1601251200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Molecular targets play important roles in agrochemical discovery. Numerous pesticides target the key proteins in pathogens, insect, or plants. Investigating ligand-binding pockets and\/or active sites in the proteins\u2019 structures is usually the first step in designing new green pesticides. Thus, molecular target structures are extremely important for the discovery and development of such pesticides. In this manuscript, we present a review of the molecular target structures, including those of antiviral, fungicidal, bactericidal, insecticidal, herbicidal, and plant growth-regulator targets, currently used in agrochemical research. The data will be helpful in pesticide design and the discovery of new green pesticides.<\/jats:p>","DOI":"10.3390\/ijms21197144","type":"journal-article","created":{"date-parts":[[2020,9,28]],"date-time":"2020-09-28T08:02:58Z","timestamp":1601280178000},"page":"7144","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":53,"title":["Review on Structures of Pesticide Targets"],"prefix":"10.3390","volume":"21","author":[{"given":"Xiangyang","family":"Li","sequence":"first","affiliation":[{"name":"State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Guiyang 550025, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3919-8013","authenticated-orcid":false,"given":"Xueqing","family":"Yang","sequence":"additional","affiliation":[{"name":"College of Plant Protection, Shenyang Agricultural University, Shenyang 110866, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaodong","family":"Zheng","sequence":"additional","affiliation":[{"name":"College of Horticulture, Qingdao Agricultural University, Qingdao 266109, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miao","family":"Bai","sequence":"additional","affiliation":[{"name":"College of Horticulture, Hunan Agricultural University, Changsha 410128, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deyu","family":"Hu","sequence":"additional","affiliation":[{"name":"State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Guiyang 550025, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,9,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1126\/science.1237227","article-title":"Current challenges and trends in the discovery of agrochemicals","volume":"341","author":"Clemens","year":"2013","journal-title":"Science"},{"key":"ref_2","unstructured":"Turner, J.A. (2015). The Pesticide Manual, British Crop Protection Council. [17th ed.]."},{"key":"ref_3","unstructured":"Fungicide Resistance Action Committee (2020, August 16). Fungal Control Agents Sorted by Cross Resistance Pattern and Mode of Action. Available online: https:\/\/www.frac.info\/."},{"key":"ref_4","unstructured":"IRAC International MoA Working Group (2020, August 16). IRAC Mode of Action Classification Scheme. Available online: https:\/\/irac-online.org\/modes-of-action\/."},{"key":"ref_5","unstructured":"The Global Herbicide Resistance Action Committee (2020, August 16). HRAC Mode of Action Classification. Available online: https:\/\/www.hracglobal.com\/herbicide-resistance."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Li, X., Song, B., Chen, X., Wang, Z., Zeng, M., Yu, D., Hu, D., Chen, Z., Jin, L., and Yang, S. (2013). Crystal structure of a four-layer aggregate of engineered TMV CP implies the importance of terminal residues for oligomer assembly. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0077717"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"7578","DOI":"10.1128\/JVI.74.16.7578-7586.2000","article-title":"The structure of cucumber mosaic virus and comparison to cowpea chlorotic mottle virus","volume":"74","author":"Smith","year":"2000","journal-title":"J. Virol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"eaaw3808","DOI":"10.1126\/sciadv.aaw3808","article-title":"Structural basis for the multitasking nature of the potato virus Y coat protein","volume":"5","author":"Coll","year":"2019","journal-title":"Sci. Adv."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"7565","DOI":"10.1128\/JVI.00118-12","article-title":"Crystal structure of the superfamily 1 helicase from tomato mosaic virus","volume":"86","author":"Nishikiori","year":"2012","journal-title":"J. Virol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1128\/JVI.00826-11","article-title":"Crystallographic analysis reveals octamerization of viroplasm matrix protein P9-1 of rice black streaked Dwarf virus","volume":"86","author":"Akita","year":"2011","journal-title":"J. Virol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.pep.2015.04.003","article-title":"Characterization of the importance of terminal residues for southern rice black-streaked dwarf virus P9-1 viroplasm formations","volume":"111","author":"Li","year":"2015","journal-title":"Protein Expr. Purif."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Li, X., Chen, Z., Jin, L., Hu, D., and Yang, S. (2016). New strategies and methods to study interactions between tobacco mosaic virus coat protein and its inhibitors. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17030252"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"82446","DOI":"10.18632\/oncotarget.19401","article-title":"Ningnanmycin inhibits tobacco mosaic virus virulence by binding directly to its coat protein discs","volume":"8","author":"Li","year":"2017","journal-title":"Oncotarget"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.1016\/j.bmc.2015.04.008","article-title":"Studies of binding interactions between Dufulin and southern rice black-streaked dwarf virus P9-1","volume":"23","author":"Li","year":"2015","journal-title":"Bioorganic Med. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"11380","DOI":"10.1021\/acs.jafc.9b05793","article-title":"Dufulin intervenes the viroplasmic proteins as the mechanism of action against Southern rice black-streaked Dwarf virus","volume":"67","author":"Wang","year":"2019","journal-title":"J. Agric. Food Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/j.ijbiomac.2017.05.059","article-title":"Interaction research on an antiviral molecule that targets the coat protein of southern rice black-streaked dwarf virus","volume":"103","author":"Ran","year":"2017","journal-title":"Int. J. Boil. Macromol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"18952","DOI":"10.1039\/C8RA01466C","article-title":"Binding studies between cytosinpeptidemycin and the superfamily 1 helicase protein of tobacco mosaic virus","volume":"8","author":"Li","year":"2018","journal-title":"RSC Adv."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"104449","DOI":"10.1016\/j.pestbp.2019.07.017","article-title":"Screening anti-TMV agents targeting tobacco mosaic virus helicase protein","volume":"166","author":"Wang","year":"2020","journal-title":"Pestic. Biochem. Physiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.pestbp.2018.06.002","article-title":"Baseline sensitivity of Bipolaris maydis to the novel succinate dehydrogenase inhibitor benzovindiflupyr and its efficacy","volume":"149","author":"Hou","year":"2018","journal-title":"Pestic. Biochem. Physiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"5965","DOI":"10.1074\/jbc.M511270200","article-title":"3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme","volume":"281","author":"Huang","year":"2005","journal-title":"J. Boil. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/j.chembiol.2017.05.016","article-title":"Triazolopyrimidines are microtubule-stabilizing agents that bind the Vinca inhibitor site of tubulin","volume":"24","author":"Sharma","year":"2017","journal-title":"Cell Chem. Boil."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"11692","DOI":"10.1021\/bi026252p","article-title":"The crystal structure of mitochondrial cytochromebc1in complex with famoxadone: The role of aromatic\u2212aromatic interaction in inhibition","volume":"41","author":"Gao","year":"2002","journal-title":"Biochemistry"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"25019","DOI":"10.1074\/jbc.M116.744391","article-title":"Hydrogen bonding to the substrate is not required for Rieske iron-sulfur protein docking to the quinol oxidation site of complex III","volume":"291","author":"Esser","year":"2016","journal-title":"J. Boil. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"12007","DOI":"10.1074\/jbc.RA119.008381","article-title":"Crystal structure of bacterial cytochrome bc1 in complex with azoxystrobin reveals a conformational switch of the Rieske iron\u2013sulfur protein subunit","volume":"294","author":"Esser","year":"2019","journal-title":"J. Boil. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1021\/ja905756c","article-title":"Subnanomolar inhibitor of cytochromebc1complex designed by optimizing interaction with conformationally flexible residues","volume":"132","author":"Zhao","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"8927","DOI":"10.1021\/acs.jafc.6b03464","article-title":"Design, synthesis, fungicidal activity, and unexpected docking model of the first chiral boscalid analogues containing oxazolines","volume":"64","author":"Li","year":"2016","journal-title":"J. Agric. Food Chem."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Tyndall, J.D.A., Sabherwal, M., Sagatova, A.A., Keniya, M.V., Negroni, J., Wilson, R.K., Woods, M.A., Tietjen, K., and Monk, B.C. (2016). Structural and functional elucidation of yeast lanosterol 14\u03b1-demethylase in complex with agrochemical antifungals. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0167485"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"6728","DOI":"10.1074\/jbc.M117.778308","article-title":"Structural analyses of Candida albicanssterol 14\u03b1-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis","volume":"292","author":"Hargrove","year":"2017","journal-title":"J. Boil. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1038\/nature03923","article-title":"Structural mechanism for sterol sensing and transport by OSBP-related proteins","volume":"437","author":"Im","year":"2005","journal-title":"Nature"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/j.str.2017.02.010","article-title":"Structure of yeast OSBP-related protein Osh1 reveals key determinants for lipid transport and protein targeting at the nucleus-vacuole junction","volume":"25","author":"Manik","year":"2017","journal-title":"Structure"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1038\/s41467-019-08791-0","article-title":"Allosteric enhancement of ORP1-mediated cholesterol transport by PI(4,5)P2\/PI(3,4)P2","volume":"10","author":"Dong","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.1021\/acs.jafc.8b06054","article-title":"Discovery of novel piperidinylthiazole derivatives as broad-spectrum fungicidal candidates","volume":"67","author":"Wu","year":"2019","journal-title":"J. Agric. Food Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"8248","DOI":"10.1038\/srep08248","article-title":"Whole-genome sequencing reveals that mutations in myosin-5 confer resistance to the fungicide phenamacril in Fusarium graminearum","volume":"5","author":"Zheng","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Zhou, Y., Zhou, X.E., Gong, Y., Zhu, Y., Cao, X., Brunzelle, J.S., Xu, H.E., Zhou, M., Melcher, K., and Zhang, F. (2020). Structural basis of Fusarium myosin I inhibition by phenamacril. PLOS Pathog., 16.","DOI":"10.1371\/journal.ppat.1008323"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/S0969-2126(98)00021-5","article-title":"The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate","volume":"6","author":"Jurica","year":"1998","journal-title":"Structure"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"12439","DOI":"10.1021\/acs.jafc.8b03797","article-title":"Discovery of pyruvate kinase as a novel target of new fungicide candidate 3-(4-Methyl-1,2,3-thiadiazolyl)-6-trichloromethyl-[1,2,4]-triazolo-[3,4-b][1,3,4]-thiadizole","volume":"66","author":"Zhao","year":"2018","journal-title":"J. Agric. Food Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"6962","DOI":"10.1021\/acs.jafc.9b02059","article-title":"Sulfone-based probes unraveled dihydrolipoamide S-Succinyltransferase as an unprecedented target in phytopathogens","volume":"67","author":"Chen","year":"2019","journal-title":"J. Agric. Food Chem."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Li, H., Zhang, X., Bi, L., He, J., and Jiang, T. (2011). Determination of the crystal structure and active residues of FabV, the Enoyl-ACP reductase from xanthomonas oryzae. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0026743"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1021\/tx400055p","article-title":"New GABA\/glutamate receptor target for [3H] isoxazoline insecticide","volume":"26","author":"Zhao","year":"2013","journal-title":"Chem. Res. Toxicol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"7865","DOI":"10.1021\/acs.jafc.7b02924","article-title":"Flupyrimin: A novel insecticide acting at the nicotinic acetylcholine receptors","volume":"65","author":"Onozaki","year":"2017","journal-title":"J. Agric. Food Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3277","DOI":"10.1021\/acs.jafc.7b05984","article-title":"Radioligand recognition of insecticide targets","volume":"66","author":"Casida","year":"2018","journal-title":"J. Agric. Food Chem."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Liu1, G., Wu, Y., Gao, Y., Ju, X.-L., and Ozoe, Y. (2020). Potential of competitive antagonists of insect ionotropic \u03b3-aminobutyric acid receptors as insecticides. J. Agric. Food Chem., 68, 4760\u20134768.","DOI":"10.1021\/acs.jafc.9b08189"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1021\/tx500520w","article-title":"Golden age of RyR and GABA-R diamide and isoxazoline insecticides: Common genesis, serendipity, surprises, selectivity, and safety","volume":"28","author":"Casida","year":"2015","journal-title":"Chem. Res. Toxicol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"4127","DOI":"10.1016\/j.bmc.2009.01.018","article-title":"New and selective ryanodine receptor activators for insect control","volume":"17","author":"George","year":"2009","journal-title":"Bioorg. Med. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Xu, T., and Yuchi, Z. (2019). Crystal structure of diamondback moth ryanodine receptor Repeat34 domain reveals insect-specific phosphorylation sites. BMC Boil., 17.","DOI":"10.1186\/s12915-019-0698-5"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.ibmb.2017.11.009","article-title":"Crystal structure of ryanodine receptor N-terminal domain from Plutella xylostella reveals two potential species-specific insecticide-targeting sites","volume":"92","author":"Lin","year":"2018","journal-title":"Insect Biochem. Mol. Boil."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1021\/acs.jafc.9b08151","article-title":"Crystal structure of the ryanodine receptor SPRY2 domain from the diamondback moth provides insights into the development of novel insecticides","volume":"68","author":"Zhou","year":"2020","journal-title":"J. Agric. Food Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"4528","DOI":"10.1021\/acs.jafc.0c01063","article-title":"Discovery of potential species-specific green insecticides targeting the lepidopteran ryanodine receptor","volume":"68","author":"Samurkas","year":"2020","journal-title":"J. Agric. Food Chem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.ibmb.2017.03.005","article-title":"Afidopyropen: New and potent modulator of insect transient receptor potential channels","volume":"84","author":"Kandasamy","year":"2017","journal-title":"Insect Biochem. Mol. Boil."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"4049","DOI":"10.1074\/jbc.M110.184796","article-title":"Structural determinants of an insect beta-N-Acetyl-D-hexosaminidase specialized as a chitinolytic enzyme","volume":"286","author":"Liu","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1042\/BJ20110390","article-title":"Active-pocket size differentiating insectile from bacterial chitinolytic \u03b2-N-acetyl-D-hexosaminidases","volume":"438","author":"Liu","year":"2011","journal-title":"Biochem. J."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"15429","DOI":"10.1074\/jbc.RA118.004351","article-title":"Glycoside hydrolase family 18 and 20 enzymes are novel targets of the traditional medicine berberine","volume":"293","author":"Duan","year":"2018","journal-title":"J. Boil. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"9358","DOI":"10.1074\/jbc.RA119.007812","article-title":"Structural dissection reveals a general mechanistic principle for group II chitinase (ChtII) inhibition","volume":"294","author":"Chen","year":"2019","journal-title":"J. Boil. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"4559","DOI":"10.1021\/acs.jafc.0c00888","article-title":"Development of novel pesticides targeting insect chitinases: A minireview and perspective","volume":"68","author":"Chen","year":"2020","journal-title":"J. Agric. Food Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1111\/j.1742-4658.2009.06863.x","article-title":"Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase","volume":"276","author":"Wang","year":"2009","journal-title":"FEBS J."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"4845","DOI":"10.1021\/acs.jafc.6b00720","article-title":"Triazolopyrimidines as a new herbicidal lead for combating weed resistance associated with acetohydroxyacid synthase mutation","volume":"64","author":"Liu","year":"2016","journal-title":"J. Agric. Food Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.jsb.2009.11.012","article-title":"Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis","volume":"170","author":"Qin","year":"2010","journal-title":"J. Struct. Boil."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1096\/fj.10-170811","article-title":"Structural insight into human variegate porphyria disease","volume":"25","author":"Qin","year":"2010","journal-title":"FASEB J."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"5581","DOI":"10.1021\/acs.jafc.7b01557","article-title":"Computational discovery of potent and bioselective protoporphyrinogen IX oxidase inhibitor via fragment deconstruction analysis","volume":"65","author":"Hao","year":"2017","journal-title":"J. Agric. Food Chem."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Hao, G.-F., Tan, Y., Yang, S.-G., Wang, Z.-F., Zhan, C.-G., Xi, Z., and Yang, G.-F. (2013). Computational and experimental insights into the mechanism of substrate recognition and feedback inhibition of protoporphyrinogen oxidase. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0069198"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"961","DOI":"10.2533\/chimia.2011.961","article-title":"Protoporphyrinogen oxidase inhibitor: An ideal target for herbicide discovery","volume":"65","author":"Hao","year":"2011","journal-title":"Chim. Int. J. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"10414","DOI":"10.1021\/bi049323o","article-title":"Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases","volume":"43","author":"Yang","year":"2004","journal-title":"Biochemistry"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1104\/pp.103.034082","article-title":"The crystal structures of zea mays and arabidopsis 4-hydroxyphenylpyruvate dioxygenase","volume":"134","author":"Fritze","year":"2004","journal-title":"Plant Physiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1016\/S0969-2126(99)80124-5","article-title":"Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: An enzyme involved in the tyrosine degradation pathway","volume":"7","author":"Serre","year":"1999","journal-title":"Structure"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1021\/bi049317s","article-title":"Structure of the ferrous form of (4-Hydroxyphenyl) pyruvate Dioxygenase from Streptomyces avermitilisin complex with the therapeutic herbicide, NTBC","volume":"43","author":"Brownlee","year":"2004","journal-title":"Biochemistry"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2602414","DOI":"10.34133\/2019\/2602414","article-title":"Crystal structure of 4-hydroxyphenylpyruvate dioxygenase in complex with substrate reveals a new starting point for herbicide discovery","volume":"2019","author":"Lin","year":"2019","journal-title":"Research"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"5587","DOI":"10.1021\/acs.jafc.5b01530","article-title":"Synthesis and herbicidal activity of triketone\u2013quinoline hybrids as novel 4-hydroxyphenylpyruvate dioxygenase inhibitors","volume":"63","author":"Wang","year":"2015","journal-title":"J. Agric. Food Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1002\/ps.3894","article-title":"Design, synthesis and herbicidal activity of novel quinazoline-2,4-diones as 4-hydroxyphenylpyruvate dioxygenase inhibitors","volume":"71","author":"Wang","year":"2014","journal-title":"Pest Manag. Sci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1111\/febs.14747","article-title":"Molecular insights into the mechanism of 4-hydroxyphenylpyruvate dioxygenase inhibition: Enzyme kinetics, X-ray crystallography and computational simulations","volume":"286","author":"Lin","year":"2019","journal-title":"FEBS J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"8523","DOI":"10.1021\/acs.jafc.7b03851","article-title":"4-Hydroxyphenylpyruvate dioxygenase inhibitors: From chemical biology to agrochemicals ferdinand ndikuryayo","volume":"65","author":"Moosavi","year":"2017","journal-title":"J. Agri. Food Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"22072","DOI":"10.1073\/pnas.1012039107","article-title":"Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden","volume":"107","author":"Yu","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/s41586-018-0319-4","article-title":"Resistance-gene-directed discovery of a natural-product herbicide with a new mode of action","volume":"559","author":"Yan","year":"2018","journal-title":"Nature"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1016\/j.molcel.2011.05.011","article-title":"The molecular basis of ABA-independent inhibition of PP2Cs by a subclass of PYL proteins","volume":"42","author":"Hao","year":"2011","journal-title":"Mol. Cell"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1230","DOI":"10.1038\/nsmb.1730","article-title":"Structural insights into the mechanism of abscisic acid signaling by PYL proteins","volume":"16","author":"Yin","year":"2009","journal-title":"Nat. Struct. Mol. Boil."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"12132","DOI":"10.1073\/pnas.1305919110","article-title":"Activation of dimeric ABA receptors elicits guard cell closure, ABA-regulated gene expression, and drought tolerance","volume":"110","author":"Okamoto","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1038\/nature09430","article-title":"Jasmonate perception by inositol-phosphate-potentiated COI1\u2013JAZ co-receptor","volume":"468","author":"Sheard","year":"2010","journal-title":"Nature"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1038\/nature07546","article-title":"Structural basis for gibberellin recognition by its receptor GID1","volume":"456","author":"Shimada","year":"2008","journal-title":"Nature"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1038\/nature19073","article-title":"DWARF14 is a non-canonical hormone receptor for strigolactone","volume":"536","author":"Yao","year":"2016","journal-title":"Nature"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1038\/s41467-018-08124-7","article-title":"Strigolactone perception and deactivation by a hydrolase receptor DWARF14","volume":"10","author":"Seto","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1843","DOI":"10.1042\/BCJ20190288","article-title":"Chemical synthesis and characterization of a new quinazolinedione competitive antagonist for strigolactone receptors with an unexpected binding mode","volume":"476","author":"Hamiaux","year":"2019","journal-title":"Biochem. J."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Chen, Z., Zeng, M., Song, B., Hou, C., Hu, D., Li, X., Wang, Z., Fan, H., Bi, L., and Liu, J. (2012). Dufulin activates HrBP1 to produce antiviral responses in tobacco. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0037944"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1094\/MPMI-02-13-0037-R","article-title":"Effects of the Crinivirus coat protein\u2013interacting plant protein SAHH on post-transcriptional RNA silencing and its suppression","volume":"26","author":"Canto","year":"2013","journal-title":"Mol. Plant-Microbe Interact."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.virol.2008.06.020","article-title":"Multiple suppressors of RNA silencing encoded by both genomic RNAs of the crinivirus, Tomato chlorosis virus","volume":"379","author":"Moriones","year":"2008","journal-title":"Virology"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"7243","DOI":"10.1021\/acs.jafc.9b01265","article-title":"First anti-ToCV activity evaluation of glucopyranoside derivatives containing a dithioacetal moiety through a novel ToCVCP-oriented screening method","volume":"67","author":"Xie","year":"2019","journal-title":"J. Agric. Food Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"6280","DOI":"10.1021\/acs.jafc.0c00987","article-title":"Design, synthesis, and anti-ToCV activity of novel pyrimidine derivatives bearing a dithioacetal moiety that targets ToCV coat protein","volume":"68","author":"Zan","year":"2020","journal-title":"J. Agric. Food Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"5539","DOI":"10.1021\/acs.jafc.0c00086","article-title":"Design, synthesis, and anti-ToCV activity of novel 4(3H)-quinazolinone derivatives bearing dithioacetal moiety","volume":"68","author":"Zu","year":"2020","journal-title":"J. Agric. Food Chem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"5302","DOI":"10.1021\/acs.jafc.0c00686","article-title":"Discovery of potent and novel quinazolinone sulfide inhibitors with Anti-ToCV activity","volume":"68","author":"Ran","year":"2020","journal-title":"J. Agric. Food Chem."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"3425","DOI":"10.1021\/acs.jafc.9b08215","article-title":"Tomato chlorosis virus minor coat protein as a novel target to screen antiviral drugs","volume":"68","author":"Yang","year":"2020","journal-title":"J. Agric. Food Chem."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"35834","DOI":"10.1074\/jbc.M111.262303","article-title":"Structures of phytophthora RXLR effector proteins","volume":"286","author":"Boutemy","year":"2011","journal-title":"J. Boil. Chem."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"20270","DOI":"10.1074\/jbc.M116.744995","article-title":"Structural basis of host autophagy-related Protein 8 (ATG8) binding by the Irish potato famine pathogen effector protein PexRD54","volume":"291","author":"Maqbool","year":"2016","journal-title":"J. Boil. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1016\/j.molp.2019.01.017","article-title":"Phytophthora sojae effector PsAvh240 inhibits host aspartic protease secretion to promote infection","volume":"12","author":"Guo","year":"2019","journal-title":"Mol. Plant"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"11637","DOI":"10.1073\/pnas.1810705115","article-title":"Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces","volume":"115","author":"Guo","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1107\/S2053230X18003618","article-title":"Crystallization of the rice immune receptor RGA5A_S with the rice blast fungus effector AVR1-CO39 prepared via mixture and tandem strategies","volume":"74","author":"Guo","year":"2018","journal-title":"Acta Crystallogr. Sect. F."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1356","DOI":"10.1021\/ci500159q","article-title":"Key amino acid associated with acephate detoxification bycydia pomonellacarboxylesterase based on molecular dynamics with alanine scanning and site-directed mutagenesis","volume":"54","author":"Yang","year":"2014","journal-title":"J. Chem. Inf. Model."},{"key":"ref_95","first-page":"1","article-title":"Structural basis for diamide modulation of ryanodine receptor","volume":"10","author":"Ma","year":"2020","journal-title":"Nat. Methods"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.cell.2020.01.021","article-title":"A deep learning approach to antibiotic discovery","volume":"180","author":"Stokes","year":"2020","journal-title":"Cell"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/19\/7144\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T10:14:20Z","timestamp":1760177660000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/19\/7144"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,9,28]]},"references-count":96,"journal-issue":{"issue":"19","published-online":{"date-parts":[[2020,10]]}},"alternative-id":["ijms21197144"],"URL":"https:\/\/doi.org\/10.3390\/ijms21197144","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,9,28]]}}}