{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T19:44:45Z","timestamp":1792784685163,"version":"4.5.0"},"reference-count":52,"publisher":"American Chemical Society (ACS)","issue":"41","license":[{"start":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:00:00Z","timestamp":1791849600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:00:00Z","timestamp":1791849600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:00:00Z","timestamp":1791849600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100003453","name":"Natural Science Foundation of Guangdong Province","doi-asserted-by":"publisher","award":["2024A1515011506"],"award-info":[{"award-number":["2024A1515011506"]}],"id":[{"id":"10.13039\/501100003453","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003453","name":"Natural Science Foundation of Guangdong Province","doi-asserted-by":"publisher","award":["2025A1515012328"],"award-info":[{"award-number":["2025A1515012328"]}],"id":[{"id":"10.13039\/501100003453","id-type":"DOI","asserted-by":"publisher"}]},{"name":"National Natural Science Foundation of China (NSFC)","award":["32272606"],"award-info":[{"award-number":["32272606"]}],"id":[{"id":"https:\/\/ror.org\/01h0zpd94","id-type":"ROR","asserted-by":"crossref"}]},{"name":"National Natural Science Foundation of China (NSFC)","award":["32372616"],"award-info":[{"award-number":["32372616"]}],"id":[{"id":"https:\/\/ror.org\/01h0zpd94","id-type":"ROR","asserted-by":"crossref"}]},{"name":"National Natural Science Foundation of China (NSFC)","award":["U22A20488"],"award-info":[{"award-number":["U22A20488"]}],"id":[{"id":"https:\/\/ror.org\/01h0zpd94","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Membrane-bound alkaline phosphatases (mALPs) are established receptors for several Bacillus thuringiensis (Bt) Cry toxins, yet the role of soluble ALPs (sALPs) in the insecticidal mechanism remains unclear. Here, we characterized two midgut-abundant ALPs in Spodoptera litura, SlALP8 and SlALP5, whose expression was down-regulated upon the exposure to Cry1Ca. SlALP8 is a glycosylphosphatidylinositol (GPI)-anchored protein, whereas SlALP5 is secreted. Co-immunoprecipitation assays confirmed that both proteins bind directly to Cry1Ca. RNA interference-mediated knockdown of either SlALP8 or SlALP5 expression increased the larval tolerance to Cry1Ca. Conversely, dietary supplementation with recombinant SlALP8 or SlALP5 protein significantly potentiated the toxicity of Cry1Ca. We demonstrate that membrane-bound SlALP8 acts as a receptor for Cry1Ca and soluble SlALP5 interacts with the toxin to potentiate its toxicity. These findings unveil a coordinated role of mALP and sALP in the Cry toxin efficacy, providing new insight into the mode of action of Cry toxins.<\/jats:p>","DOI":"10.1021\/acs.jafc.6c06572","type":"journal-article","created":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T12:01:48Z","timestamp":1791892908000},"page":"32147-32157","source":"Crossref","is-referenced-by-count":0,"title":["Both Membrane-Bound\nand Soluble Alkaline Phosphatases\nBind Cry1Ca to Potentiate Its Toxicity in\n                    <i>Spodoptera litura<\/i>"],"prefix":"10.1021","volume":"74","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7200-5159","authenticated-orcid":true,"given":"Jin","family":"Li","sequence":"first","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wan-Ting","family":"Wei","sequence":"additional","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lijun","family":"Xiang","sequence":"additional","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinyue","family":"Deng","sequence":"additional","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mengge","family":"Li","sequence":"additional","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qilin","family":"Li","sequence":"additional","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ying","family":"Zheng","sequence":"additional","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1419-9009","authenticated-orcid":true,"given":"Xiao-Qiang","family":"Yu","sequence":"additional","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuzhen","family":"Lu","sequence":"additional","affiliation":[{"name":"South China Normal University , , ,","place":["Guangzhou, China, 510631"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,10,13]]},"reference":[{"issue":"12","key":"2026102109082915900_cit1","doi-asserted-by":"publisher","first-page":"3296","DOI":"10.3390\/toxins6123296","article-title":"Bacillus thuringiensis toxins: an overview of their biocidal activity","volume":"6","author":"Palma","year":"2014","journal-title":"Toxins"},{"issue":"4","key":"2026102109082915900_cit2","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1016\/j.toxicon.2006.11.022","article-title":"Mode of action of Bacillus thuringiensis Cry and Cyt toxins and their potential for\ninsect control","volume":"49","author":"Bravo","year":"2007","journal-title":"Toxicon"},{"issue":"4","key":"2026102109082915900_cit3","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1016\/S0168-9525(01)02237-5","article-title":"How Bacillus thuringiensis has evolved specific toxins to colonize\nthe insect world","volume":"17","author":"de Maagd","year":"2001","journal-title":"Trends Genet."},{"issue":"7","key":"2026102109082915900_cit4","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1016\/j.ibmb.2011.02.006","article-title":"Bacillus thuringiensis: A story of a successful bioinsecticide","volume":"41","author":"Bravo","year":"2011","journal-title":"Insect Biochem. Mol. Biol."},{"issue":"1","key":"2026102109082915900_cit5","doi-asserted-by":"publisher","DOI":"10.1128\/mmbr.00007-20","article-title":"Response Mechanisms of Invertebrates\nto Bacillus thuringiensis and Its Pesticidal Proteins","volume":"85","author":"Pinos","year":"2021","journal-title":"Microbiol. Mol. Biol. Rev."},{"issue":"47","key":"2026102109082915900_cit6","doi-asserted-by":"publisher","first-page":"32750","DOI":"10.1074\/jbc.M109.024968","article-title":"Domain II\nloop 3 of Bacillus thuringiensis Cry1Ab toxin is\ninvolved in a \u201cping pong\u201d binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors","volume":"284","author":"Pacheco","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2026102109082915900_cit7","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1146\/annurev-ento-052620-073348","article-title":"Mechanisms of Resistance to Insecticidal\nProteins from Bacillus thuringiensis","volume":"66","author":"Jurat-Fuentes","year":"2021","journal-title":"Annu. Rev. Entomol."},{"issue":"3","key":"2026102109082915900_cit8","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1007\/s12291-013-0408-y","article-title":"Alkaline phosphatase:\nan overview","volume":"29","author":"Sharma","year":"2014","journal-title":"Indian J. Clin. Biochem."},{"issue":"2","key":"2026102109082915900_cit9","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/S0965-1748(98)00115-5","article-title":"Cloning of soluble\nalkaline phosphatase cDNA and molecular basis of the polymorphic nature\nin alkaline phosphatase isozymes of Bombyx mori midgut","volume":"29","author":"Itoh","year":"1999","journal-title":"Insect Biochem. Mol. Biol."},{"issue":"3","key":"2026102109082915900_cit10","doi-asserted-by":"publisher","first-page":"294","DOI":"10.1002\/jez.1402580304","article-title":"Goblet cell\nalkaline phosphatase in silkworm midgut epithelium: Its entity and\nrole as an ATPase","volume":"258","author":"Azuma","year":"1991","journal-title":"J. Exp. Zool."},{"issue":"15","key":"2026102109082915900_cit11","doi-asserted-by":"publisher","first-page":"4543","DOI":"10.1128\/AEM.01062-13","article-title":"Differential\nrole of Manduca sexta aminopeptidase-N and alkaline\nphosphatase in the mode of action\nof Cry1Aa, Cry1Ab, and Cry1Ac toxins from Bacillus thuringiensis","volume":"79","author":"Flores-Escobar","year":"2013","journal-title":"Appl. Environ. Microbiol."},{"issue":"4","key":"2026102109082915900_cit12","doi-asserted-by":"publisher","first-page":"1023","DOI":"10.1128\/AEM.02871-15","article-title":"Field-Evolved\nMode 1 Resistance of the Fall Armyworm to Transgenic Cry1Fa-Expressing\nCorn Associated with Reduced Cry1Fa Toxin Binding and Midgut Alkaline\nPhosphatase Expression","volume":"82","author":"Jakka","year":"2016","journal-title":"Appl. Environ. Microbiol."},{"key":"2026102109082915900_cit13","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/j.peptides.2012.05.019","article-title":"A Tenebrio\nmolitor GPI-anchored alkaline phosphatase is involved in binding of Bacillus thuringiensis Cry3Aa to brush border membrane vesicles","volume":"41","author":"Zu\u0301n\u0303iga-Navarrete","year":"2013","journal-title":"Peptides"},{"issue":"3","key":"2026102109082915900_cit14","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1016\/j.ibmb.2010.11.006","article-title":"Functional\nexpression in insect cells of glycosylphosphatidylinositol-linked\nalkaline phosphatase from Aedes aegypti larval midgut:\na Bacillus thuringiensis Cry4Ba toxin receptor","volume":"41","author":"Dechklar","year":"2011","journal-title":"Insect Biochem. Mol. Biol."},{"issue":"9","key":"2026102109082915900_cit15","doi-asserted-by":"publisher","first-page":"683","DOI":"10.1016\/j.ibmb.2012.06.001","article-title":"Aedes aegypti alkaline phosphatase ALP1 is a functional receptor\nof Bacillus thuringiensis Cry4Ba and Cry11Aa toxins","volume":"42","author":"Jime\u0301nez","year":"2012","journal-title":"Insect Biochem. Mol. Biol."},{"issue":"6","key":"2026102109082915900_cit16","first-page":"774","article-title":"Insecticidal Activity of Four Different Bt Toxins against Six Important\nLepidopteran Pests","volume":"33","author":"Liu","year":"2017","journal-title":"Chin. J. Biol. Control"},{"key":"2026102109082915900_cit17","first-page":"39","article-title":"Diversity of Bacillus thuringiensis Crystal Toxins and Mechanism of Action","volume-title":"Advances in Insect Physiology","author":"Adang","year":"2014"},{"issue":"6","key":"2026102109082915900_cit18","doi-asserted-by":"publisher","first-page":"460","DOI":"10.1111\/j.1472-765X.2005.01712.x","article-title":"The synergistic\nactivity between Cry1Aa and Cry1c from Bacillus thuringiensis against Spodoptera exigua and Helicoverpa armigera","volume":"40","author":"Xue","year":"2005","journal-title":"Lett. Appl. Microbiol."},{"issue":"1","key":"2026102109082915900_cit19","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1127\/entomologia\/2020\/0995","article-title":"Insecticidal activity of Bacillus thuringiensis Cry1, Cry2 and Vip3 toxin combinations\nin Spodoptera exigua control: highlights on synergism\nand data scoring","volume":"41","author":"Baranek","year":"2021","journal-title":"Entomol. 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Pathol."},{"issue":"49","key":"2026102109082915900_cit22","doi-asserted-by":"publisher","first-page":"46849","DOI":"10.1074\/jbc.C200523200","article-title":"Silencing\nof midgut aminopeptidase N of Spodoptera litura by\ndouble-stranded RNA establishes its role as Bacillus thuringiensis toxin receptor","volume":"277","author":"Rajagopal","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2026102109082915900_cit23","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/j.ijbiomac.2021.11.174","article-title":"ABCC2 is a\nfunctional receptor of Bacillus thuringiensis Cry1Ca\nin Spodoptera litura","volume":"194","author":"Yao","year":"2022","journal-title":"Int.\nJ. Biol. Macromol."},{"issue":"18","key":"2026102109082915900_cit24","doi-asserted-by":"publisher","first-page":"5576","DOI":"10.1128\/AEM.01519-13","article-title":"A Spodoptera exigua Cadherin Serves as a Putative Receptor for Bacillus thuringiensis Cry1Ca Toxin and Shows Differential\nEnhancement of Cry1Ca and Cry1Ac Toxicity","volume":"79","author":"Ren","year":"2013","journal-title":"Appl.\nEnviron. Microbiol."},{"issue":"3","key":"2026102109082915900_cit25","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1016\/j.jip.2013.09.006","article-title":"RNA interference of cadherin gene expression in Spodoptera exigua reveals its significance as a specific Bt target","volume":"114","author":"Park","year":"2013","journal-title":"J. Invertebr. Pathol."},{"issue":"4","key":"2026102109082915900_cit26","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1093\/molbev\/mst010","article-title":"MAFFT multiple sequence alignment\nsoftware version\n7: improvements in performance and usability","volume":"30","author":"Katoh","year":"2013","journal-title":"Mol. Biol. Evol."},{"issue":"15","key":"2026102109082915900_cit27","doi-asserted-by":"publisher","first-page":"1972","DOI":"10.1093\/bioinformatics\/btp348","article-title":"trimAl: a\ntool for automated alignment trimming in large-scale phylogenetic\nanalyses","volume":"25","author":"Capella-Gutie\u0301rrez","year":"2009","journal-title":"Bioinformatics"},{"issue":"5","key":"2026102109082915900_cit28","doi-asserted-by":"publisher","first-page":"1530","DOI":"10.1093\/molbev\/msaa015","article-title":"IQ-TREE 2: New Models and Efficient\nMethods for Phylogenetic Inference in the Genomic Era","volume":"37","author":"Minh","year":"2020","journal-title":"Mol. Biol. Evol."},{"issue":"11","key":"2026102109082915900_cit29","doi-asserted-by":"publisher","first-page":"1733","DOI":"10.1016\/j.molp.2023.09.010","article-title":"TBtools-II:\nA \u201cone for all, all for one\u201d bioinformatics platform\nfor biological big-data mining","volume":"16","author":"Chen","year":"2023","journal-title":"Mol. Plant"},{"issue":"8016","key":"2026102109082915900_cit30","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure\nprediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"issue":"W1","key":"2026102109082915900_cit31","doi-asserted-by":"publisher","first-page":"W365","DOI":"10.1093\/nar\/gkx407","article-title":"HDOCK:\na web server for protein-protein and protein-DNA\/RNA docking based\non a hybrid strategy","volume":"45","author":"Yan","year":"2017","journal-title":"Nucleic Acids Res."},{"issue":"7","key":"2026102109082915900_cit32","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkr1293","article-title":"MCScanX: a toolkit for detection\nand evolutionary analysis of gene synteny and collinearity","volume":"40","author":"Wang","year":"2012","journal-title":"Nucleic Acids Res."},{"issue":"5","key":"2026102109082915900_cit33","doi-asserted-by":"publisher","first-page":"1039","DOI":"10.1007\/s10343-024-01026-3","article-title":"Genome-wide Analysis\nof Developmental Stage-specific Transcriptome in Spodoptera litura for the Identification of Effective Control Method","volume":"76","author":"Wang","year":"2024","journal-title":"J. Crop Health"},{"issue":"6","key":"2026102109082915900_cit34","doi-asserted-by":"publisher","first-page":"5680","DOI":"10.1002\/ps.70671","article-title":"A Toll7\u20131-Spa\u0308tzle7\u20131\npathway in Spodoptera litura against Bacillus thuringiensis","volume":"82","author":"Li","year":"2026","journal-title":"Pest Manage. Sci."},{"issue":"8","key":"2026102109082915900_cit35","doi-asserted-by":"publisher","first-page":"907","DOI":"10.1038\/s41587-019-0201-4","article-title":"Graph-based\ngenome alignment and genotyping with HISAT2 and HISAT-genotype","volume":"37","author":"Kim","year":"2019","journal-title":"Nat. Biotechnol."},{"issue":"16","key":"2026102109082915900_cit36","doi-asserted-by":"publisher","first-page":"2078","DOI":"10.1093\/bioinformatics\/btp352","article-title":"The Sequence\nAlignment\/Map format and SAMtools","volume":"25","author":"Li","year":"2009","journal-title":"Bioinformatics"},{"issue":"7","key":"2026102109082915900_cit37","doi-asserted-by":"publisher","first-page":"923","DOI":"10.1093\/bioinformatics\/btt656","article-title":"featureCounts:\nan efficient general\npurpose program for assigning sequence reads to genomic features","volume":"30","author":"Liao","year":"2014","journal-title":"Bioinformatics"},{"issue":"4","key":"2026102109082915900_cit38","doi-asserted-by":"publisher","first-page":"2379","DOI":"10.1002\/ps.8635","article-title":"The effect of population\ndensity\non the phenotype, metabolic and immunological adaptations in the cuticle\nof Spodoptera litura larvae","volume":"81","author":"Wen","year":"2025","journal-title":"Pest Manage. Sci."},{"key":"2026102109082915900_cit39","doi-asserted-by":"publisher","first-page":"103451","DOI":"10.1016\/j.ibmb.2020.103451","article-title":"Comparative genomic\nanalysis of C-type lectin-domain genes in seven holometabolous insect\nspecies","volume":"126","author":"Lu","year":"2020","journal-title":"Insect Biochem. Mol. Biol."},{"issue":"4","key":"2026102109082915900_cit40","doi-asserted-by":"publisher","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression\ndata using real-time\nquantitative PCR and the 2(-Delta Delta C(T)) Method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"issue":"6","key":"2026102109082915900_cit41","doi-asserted-by":"publisher","first-page":"3148","DOI":"10.1002\/ps.8685","article-title":"Characterization\nand functional analysis of Spodoptera litura galectins","volume":"81","author":"Zhong","year":"2025","journal-title":"Pest Manage. Sci."},{"issue":"44","key":"2026102109082915900_cit42","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2415398121","article-title":"A myeloid differentiation-like protein\nin partnership with Toll5 from the pest insect Spodoptera litura senses baculovirus infection","volume":"121","author":"Zhang","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"3","key":"2026102109082915900_cit43","doi-asserted-by":"publisher","first-page":"783","DOI":"10.1111\/1744-7917.12961","article-title":"Genome-wide\nidentification and comparative analysis of Cry toxin receptor families\nin 7 insect species with a focus on Spodoptera litura","volume":"29","author":"Li","year":"2022","journal-title":"Insect Sci."},{"issue":"17","key":"2026102109082915900_cit44","doi-asserted-by":"publisher","first-page":"12497","DOI":"10.1074\/jbc.M109.085266","article-title":"Role of alkaline\nphosphatase from Manduca sexta in the mechanism of\naction of Bacillus thuringiensis Cry1Ab toxin","volume":"285","author":"Arenas","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"41","key":"2026102109082915900_cit45","doi-asserted-by":"publisher","first-page":"9785","DOI":"10.1021\/bi9014538","article-title":"Anopheles gambiae alkaline phosphatase is a functional receptor of Bacillus thuringiensis jegathesan Cry11Ba toxin","volume":"48","author":"Hua","year":"2009","journal-title":"Biochemistry"},{"issue":"16","key":"2026102109082915900_cit46","doi-asserted-by":"publisher","first-page":"5690","DOI":"10.1128\/AEM.00523-12","article-title":"Association of Cry1Ac toxin resistance\nin Helicoverpa zea (Boddie) with increased alkaline\nphosphatase levels in the midgut lumen","volume":"78","author":"Caccia","year":"2012","journal-title":"Appl.\nEnviron. Microbiol."},{"issue":"4","key":"2026102109082915900_cit47","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pgen.1005124","article-title":"MAPK signaling pathway alters expression of midgut ALP and ABCC genes\nand causes resistance to Bacillus thuringiensis Cry1Ac\ntoxin in diamondback moth","volume":"11","author":"Guo","year":"2015","journal-title":"PLoS Genet."},{"issue":"1","key":"2026102109082915900_cit48","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1002\/arch.20437","article-title":"Characterization of soluble and membrane-bound\nalkaline phosphatase in Nilaparvata lugens and their\npotential relation to development and insecticide resistance","volume":"78","author":"Wang","year":"2011","journal-title":"Arch. Insect Biochem. Physiol."},{"issue":"3","key":"2026102109082915900_cit49","doi-asserted-by":"publisher","first-page":"3_041-3_048","DOI":"10.11416\/jibs.90.3_041","article-title":"Co-localization of two alkaline phosphatases at the brush border\nof the columnar cells in the larval midgut of the silkworm, Bombyx mori","volume":"90","author":"Hashimoto","year":"2021","journal-title":"J. Insect Biotechnol.\nSericol."},{"issue":"10","key":"2026102109082915900_cit50","doi-asserted-by":"publisher","first-page":"999","DOI":"10.1016\/S0965-1748(03)00114-0","article-title":"Identification of\nnovel Bacillus thuringiensis Cry1Ac binding proteins\nin Manduca sexta midgut\nthrough proteomic analysis","volume":"33","author":"McNall","year":"2003","journal-title":"Insect Biochem.\nMol. Biol."},{"issue":"4","key":"2026102109082915900_cit51","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0126288","article-title":"A toxin-binding alkaline phosphatase\nfragment synergizes Bt toxin Cry1Ac against susceptible and resistant Helicoverpa armigera","volume":"10","author":"Chen","year":"2015","journal-title":"PLoS One"},{"issue":"12","key":"2026102109082915900_cit52","doi-asserted-by":"publisher","first-page":"2575","DOI":"10.3390\/ijms18122575","article-title":"Identification and\nCharacterization\nof Hyphantria cunea Aminopeptidase N as a Binding\nProtein of Bacillus thuringiensis Cry1Ab35 Toxin","volume":"18","author":"Zhang","year":"2017","journal-title":"Int. J. Mol. Sci."}],"container-title":["Journal of Agricultural\nand Food Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.jafc.6c06572","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jafcau\/article-pdf\/74\/41\/32147\/68832139\/acs.jafc.6c06572.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jafcau\/article-pdf\/74\/41\/32147\/68832139\/acs.jafc.6c06572.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T13:30:25Z","timestamp":1792589425000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jafcau\/article\/74\/41\/32147\/5449636\/Both-Membrane-Bound-and-Soluble-Alkaline"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,13]]},"references-count":52,"journal-issue":{"issue":"41","published-online":{"date-parts":[[2026,10,13]]},"published-print":{"date-parts":[[2026,10,21]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.jafc.6c06572","relation":{},"ISSN":["0021-8561","1520-5118"],"issn-type":[{"value":"0021-8561","type":"print"},{"value":"1520-5118","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,10,13]]}}}