{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T09:00:13Z","timestamp":1781168413959,"version":"3.54.1"},"reference-count":91,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T00:00:00Z","timestamp":1780272000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Mol. Biosci."],"abstract":"<jats:sec>\n                    <jats:title>Introduction<\/jats:title>\n                    <jats:p>\n                      Scorpion venom is a rich source of bioactive molecules with promising biomedical applications. Hyaluronidases are venom-associated enzymes that facilitate toxin diffusion by degrading extracellular matrix glycosaminoglycans, yet their structural diversity and substrate specificity in scorpion venoms remain insufficiently explored. This study aimed to identify and characterize a novel hyaluronidase from the venom gland of the Iranian endemic scorpion\n                      <jats:italic>Mesobuthus crucittii<\/jats:italic>\n                      and evaluate its biochemical and structural properties.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      Venom gland transcriptome profiling was performed. Hyaluronidase sequences were analyzed\n                      <jats:italic>in silico<\/jats:italic>\n                      via phylogenetic reconstruction, motif prediction, physicochemical property calculation, and structural modeling. Molecular docking was conducted to explore interactions with hyaluronic acid and chondroitin sulfate substrates. Enzymatic activity and thermal stability were experimentally evaluated using turbidimetric assays.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Transcriptomic analysis revealed a diverse toxin repertoire dominated by ion channel modulators and enzymatic components, including a novel precursor encoding a putative hyaluronidase exhibiting a unique cysteine framework with six disulfide bonds and three conserved diagnostic motifs (GDWW, FPDC, and GWGS). Structural modeling suggested catalytic and binding domains consistent with glycosyl hydrolase family 56 enzymes. Molecular docking supported preferential binding affinity toward hyaluronic acid tetrasaccharides rather than longer or highly sulfated glycosaminoglycans. Functional assays on crude venom confirmed strong hyaluronan degradation and slower chondroitin sulfate hydrolysis, indicating dual substrate activity.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion<\/jats:title>\n                    <jats:p>This study supports the existence of a structurally distinct scorpion venom hyaluronidase with putative bifunctional substrate activity. These findings expand current understanding of scorpion venom enzyme evolution and highlight the enzyme's translational potential.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fmolb.2026.1807239","type":"journal-article","created":{"date-parts":[[2026,6,8]],"date-time":"2026-06-08T07:58:27Z","timestamp":1780905507000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Venom gland transcriptomics and bioactivity profiling suggest bifunctional hyaluronidase activity in the venom of Mesobuthus crucittii (Scorpiones: Buthidae)"],"prefix":"10.3389","volume":"13","author":[{"given":"Masoumeh","family":"Baradaran","sequence":"first","affiliation":[{"name":"Toxicology Research Center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences","place":["Ahvaz, Iran"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fatemeh","family":"Salabi","sequence":"additional","affiliation":[{"name":"Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO)","place":["Ahvaz, Iran"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nasrin","family":"Payab","sequence":"additional","affiliation":[{"name":"Graduate of the Department of Biology, Faculty of Science, Shahrekord University","place":["Shahrekord, Iran"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seyed Mahdi","family":"Kazemi","sequence":"additional","affiliation":[{"name":"Zagros Herpetological Institute","place":["Qom, Iran"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos E.","family":"Santib\u00e1\u00f1ez-L\u00f3pez","sequence":"additional","affiliation":[{"name":"Department of Biology, Western Connecticut State University","place":["Danbury, CT, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tim","family":"L\u00fcddecke","sequence":"additional","affiliation":[{"name":"Fraunhofer Institute for Molecular Biology and Applied Ecology","place":["Gie\u00dfen, Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,6,1]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/j.toxicon.2008.12.007","article-title":"Intraspecific variation in the Egyptian scorpion Scorpio maurus palmatus venom collected from different biotopes","volume":"53","author":"Abdel-Rahman","year":"2009","journal-title":"Toxicon"},{"key":"B2","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1016\/j.toxicon.2013.08.064","article-title":"Venom proteomic and venomous glands transcriptomic analysis of the Egyptian scorpion Scorpio maurus palmatus (arachnida: scorpionidae)","volume":"74","author":"Abdel-Rahman","year":"2013","journal-title":"Toxicon"},{"key":"B3","doi-asserted-by":"publisher","first-page":"2011","DOI":"10.3389\/fimmu.2020.02011","article-title":"Pioneering study on rhopalurus crassicauda scorpion venom: isolation and characterization of the major toxin and hyaluronidase","volume":"11","author":"Abreu","year":"2020","journal-title":"Front. Immunol."},{"key":"B4","doi-asserted-by":"crossref","DOI":"10.1016\/0305-0491(72)90207-6","volume-title":"Hyaluronidase Activity of Extracts of Venom Sacs of a Number of Vespinae (Hymenoptera)","author":"Allalouf","year":"1972"},{"key":"B5","doi-asserted-by":"publisher","first-page":"210","DOI":"10.4236\/ojgen.2012.24027","article-title":"Transcriptome analysis of the Tityus serrulatus scorpion venom gland","volume":"2","author":"Alvarenga","year":"2012","journal-title":"Open J. Genet."},{"key":"B6","doi-asserted-by":"publisher","first-page":"3145","DOI":"10.1007\/s00253-018-8821-z","article-title":"Heterologous expression of rTsHyal-1: the first recombinant hyaluronidase of scorpion venom produced in Pichia pastoris system","volume":"102","author":"Amorim","year":"2018","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"B7","doi-asserted-by":"publisher","first-page":"730","DOI":"10.1186\/s12864-023-09851-y","article-title":"Genome-wide identification, structural homology analysis, and evolutionary diversification of the phospholipase D gene family in the venom gland of three scorpion species","volume":"24","author":"Baradaran","year":"2023","journal-title":"BMC Genomics"},{"key":"B8","first-page":"1488","article-title":"First transcriptome analysis of Iranian scorpion, Mesobuthus eupeus venom gland","volume":"17","author":"Baradaran","year":"2018","journal-title":"Iran J. Pharm. Res."},{"key":"B9","doi-asserted-by":"publisher","first-page":"497","DOI":"10.3390\/toxins16110497","article-title":"ScorpDb: a novel open-access database for integrative scorpion toxinology","volume":"16","author":"Baradaran","year":"2024","journal-title":"Toxins"},{"key":"B10","doi-asserted-by":"publisher","first-page":"2114","DOI":"10.1093\/bioinformatics\/btu170","article-title":"Trimmomatic: a flexible trimmer for illumina sequence data","volume":"30","author":"Bolger","year":"2014","journal-title":"Bioinformatics"},{"key":"B11","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1186\/s40409-015-0042-7","article-title":"Arthropod venom hyaluronidases: biochemical properties and potential applications in medicine and biotechnology","volume":"21","author":"Bordon","year":"2015","journal-title":"J. Venom. Animals Toxins Including Trop. Dis."},{"key":"B12","doi-asserted-by":"publisher","first-page":"1132","DOI":"10.3389\/fphar.2020.01132","article-title":"From animal poisons and venoms to medicines: achievements, challenges and perspectives in drug discovery","volume":"11","author":"Bordon","year":"2020","journal-title":"Front. Pharmacol."},{"key":"B13","doi-asserted-by":"publisher","first-page":"1193","DOI":"10.1007\/s00266-022-03207-9","article-title":"A scoping review of hyaluronidase use in managing the complications of aesthetic interventions","volume":"48","author":"Borzabadi-Farahani","year":"2024","journal-title":"Aesthetic Plast. Surg."},{"key":"B14","doi-asserted-by":"publisher","first-page":"247","DOI":"10.3390\/toxins11050247","article-title":"Dissecting toxicity: the venom gland transcriptome and the venom proteome of the highly venomous scorpion Centruroides limpidus (karsch, 1879)","volume":"11","author":"Cid-Uribe","year":"2019","journal-title":"Toxins"},{"key":"B15","doi-asserted-by":"publisher","first-page":"1223","DOI":"10.1016\/j.toxicon.2012.08.018","article-title":"Identification, cDNA cloning and heterologous expression of a hyaluronidase from the tarantula Brachypelma vagans venom","volume":"60","author":"Clement","year":"2012","journal-title":"Toxicon"},{"key":"B16","doi-asserted-by":"publisher","first-page":"1511","DOI":"10.1002\/pro.5560020916","article-title":"Verification of protein structures: patterns of nonbonded atomic interactions","volume":"2","author":"Colovos","year":"1993","journal-title":"Protein Sci."},{"key":"B17","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/1471-2105-14-346","article-title":"Disulfide by design 2.0: a web-based tool for disulfide engineering in proteins","volume":"14","author":"Craig","year":"2013","journal-title":"BMC Bioinforma."},{"key":"B18","doi-asserted-by":"publisher","first-page":"248","DOI":"10.3390\/toxins14040248","article-title":"The enzymatic core of scorpion venoms","volume":"14","author":"Delgado-Prudencio","year":"2022","journal-title":"Toxins"},{"key":"B19","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1038\/s44386-026-00041-w","article-title":"Vector venom: venomics of Aedes albopictus reveals a large enzyme repertoire and novel cecropins with activity against E. coli","volume":"3","author":"Dersch","year":"2026","journal-title":"Npj Drug Discovery"},{"key":"B20","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/1471-2164-15-295","article-title":"The mediterranean scorpion Mesobuthus gibbosus (scorpiones, buthidae): transcriptome analysis and organization of the genome encoding chlorotoxin-like peptides","volume":"15","author":"Diego-Garc\u00eda","year":"2014","journal-title":"BMC Genomics"},{"key":"B21","doi-asserted-by":"publisher","first-page":"172","DOI":"10.1016\/j.toxicon.2018.04.029","article-title":"Diversity of peptidic and proteinaceous toxins from social Hymenoptera venoms","volume":"148","author":"dos Santos-Pinto","year":"2018","journal-title":"Toxicon"},{"key":"B22","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1038\/s44185-024-00058-2","article-title":"Enlightening the toxinological dark matter of spider venom enzymes","volume":"3","author":"Dresler","year":"","journal-title":"Npj Biodivers."},{"key":"B23","doi-asserted-by":"publisher","first-page":"1445500","DOI":"10.3389\/frchs.2024.1445500","article-title":"A roadmap to the enzymes from spider venom: biochemical ecology, molecular diversity, and value for the bioeconomy","volume":"3","author":"Dresler","year":"","journal-title":"Front. Arachnid Sci."},{"key":"B24","doi-asserted-by":"publisher","first-page":"108667","DOI":"10.1016\/j.toxicon.2025.108667","article-title":"Bioactivity profiling of spider venoms reveals predominant hyaluronidase activities","volume":"269","author":"Dresler","year":"2025","journal-title":"Toxicon"},{"key":"B25","doi-asserted-by":"publisher","first-page":"818","DOI":"10.3390\/toxins14120818","article-title":"The pharmacological potential of novel melittin variants from the honeybee and solitary bees against inflammation and cancer","volume":"14","author":"Erkoc","year":"2022","journal-title":"Toxins"},{"key":"B26","doi-asserted-by":"publisher","first-page":"250","DOI":"10.1016\/j.cbpc.2008.06.003","article-title":"Isolation and characterization of a hyaluronidase from the venom of Chinese red scorpion Buthus martensi","volume":"148","author":"Feng","year":"2008","journal-title":"Comp. Biochem. Physiology Part C Toxicol. and Pharmacol."},{"key":"B27","doi-asserted-by":"publisher","first-page":"e20200110","DOI":"10.1590\/1678-9199-JVATITD-2020-0110","article-title":"Effects of climate variables on the incidence of scorpion stings in Iran for five years","volume":"27","author":"Ghorbani","year":"2021","journal-title":"J. Venom. Animals Toxins Including Trop. Dis."},{"key":"B28","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1016\/j.toxicon.2019.06.019","article-title":"Determination of hyaluronidase activity in tityus spp. scorpion venoms and its inhibition by Brazilian antivenoms","volume":"167","author":"Guerra-Duarte","year":"2019","journal-title":"Toxicon"},{"key":"B29","doi-asserted-by":"publisher","first-page":"1494","DOI":"10.1038\/nprot.2013.084","article-title":"De novo transcript sequence reconstruction from RNA-seq using the Trinity platform for reference generation and analysis","volume":"8","author":"Haas","year":"2013","journal-title":"Nat. Protoc."},{"key":"B30","doi-asserted-by":"publisher","first-page":"1","DOI":"10.21769\/bioprotoc.45","article-title":"Bradford protein assay","volume":"6","author":"He","year":"2011","journal-title":"Bio-protocol, e45"},{"key":"B31","doi-asserted-by":"publisher","first-page":"518","DOI":"10.1093\/molbev\/msx281","article-title":"UFBoot2: improving the ultrafast bootstrap approximation","volume":"35","author":"Hoang","year":"2018","journal-title":"Mol. Biol. Evol."},{"key":"B32","doi-asserted-by":"publisher","first-page":"549","DOI":"10.3390\/biom2040549","article-title":"Hyaluronidases have strong hydrolytic activity toward chondroitin 4-sulfate comparable to that for hyaluronan","volume":"2","author":"Honda","year":"2012","journal-title":"Biomolecules"},{"key":"B33","doi-asserted-by":"publisher","first-page":"e2693","DOI":"10.1371\/journal.pntd.0002693","article-title":"Molecular, immunological, and biological characterization of Tityus serrulatus venom hyaluronidase: new insights into its role in envenomation","volume":"8","author":"Horta","year":"2014","journal-title":"PLoS Neglected Trop. Dis."},{"key":"B34","doi-asserted-by":"publisher","first-page":"25","DOI":"10.3390\/molecules22010025","article-title":"Impact of bee venom enzymes on diseases and immune responses","volume":"22","author":"Hossen","year":"2016","journal-title":"Molecules"},{"key":"B35","doi-asserted-by":"publisher","first-page":"358","DOI":"10.3390\/toxins14050358","article-title":"Venomics of the Central European myrmicine ants Myrmica rubra and Myrmica ruginodis","volume":"14","author":"Hurka","year":"2022","journal-title":"Toxins"},{"key":"B36","doi-asserted-by":"publisher","first-page":"28287","DOI":"10.1074\/jbc.M112009200","article-title":"Mechanism of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase: structures of complexes with the substrate","volume":"277","author":"Jedrzejas","year":"2002","journal-title":"J. Biol. Chem."},{"key":"B37","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1152\/physrev.00052.2009","article-title":"Hyaluronan as an immune regulator in human diseases","volume":"91","author":"Jiang","year":"2011","journal-title":"Physiol. Rev."},{"key":"B38","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"B39","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1038\/nmeth.4285","article-title":"ModelFinder: fast model selection for accurate phylogenetic estimates","volume":"14","author":"Kalyaanamoorthy","year":"2017","journal-title":"Nat. Methods"},{"key":"B40","doi-asserted-by":"publisher","first-page":"772","DOI":"10.1093\/molbev\/mst010","article-title":"MAFFT multiple sequence alignment software version 7: improvements in performance and usability","volume":"30","author":"Katoh","year":"2013","journal-title":"Mol. Biol. Evol."},{"key":"B41","doi-asserted-by":"publisher","first-page":"2670","DOI":"10.3390\/molecules24142670","article-title":"Venoms of Iranian scorpions (arachnida, Scorpiones) and their potential for drug discovery","volume":"24","author":"Kazemi","year":"2019","journal-title":"Molecules"},{"key":"B42","doi-asserted-by":"publisher","first-page":"108033","DOI":"10.1016\/j.toxicon.2024.108033","article-title":"The need for a refined scorpion antivenom for Iran","volume":"248","author":"Kazemi","year":"2024","journal-title":"Toxicon"},{"key":"B43","doi-asserted-by":"publisher","first-page":"1","DOI":"10.18590\/euscorpius.2019.vol2019.iss288.1","article-title":"Taxonomic reassessment of the genera lychas, mesobuthus, and olivierus, with descriptions of four new genera","volume":"288","author":"Kova\u0159\u00edk","year":"2019","journal-title":"Euscorpius"},{"key":"B44","doi-asserted-by":"publisher","first-page":"154","DOI":"10.1006\/abbi.2000.2204","article-title":"Characterization of hyaluronidase isolated from Agkistrodon contortrix contortrix (southern copperhead) venom","volume":"386","author":"Kudo","year":"2001","journal-title":"Archives Biochem. Biophysics"},{"key":"B45","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1107\/s0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"Appl. Crystallogr."},{"key":"B46","doi-asserted-by":"publisher","first-page":"1658","DOI":"10.1093\/bioinformatics\/btl158","article-title":"Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences","volume":"22","author":"Li","year":"2006","journal-title":"Bioinformatics"},{"key":"B47","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-94-007-6404-0_15","article-title":"Scorpion diversity and distribution; past and present patterns","volume-title":"Scorpion Venoms, Toxinology","author":"Louren\u00e7o","year":"2015"},{"key":"B48","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1111\/brv.12793","article-title":"The biology and evolution of spider venoms","volume":"97","author":"L\u00fcddecke","year":"2022","journal-title":"Biol. Rev."},{"key":"B49","doi-asserted-by":"publisher","first-page":"1496","DOI":"10.1038\/s42003-025-09015-6","article-title":"Comparative venomics suggests an evolutionary adaption of spider venom from predation to defense","volume":"8","author":"L\u00fcddecke","year":"2025","journal-title":"Commun. Biol."},{"key":"B50","doi-asserted-by":"publisher","first-page":"e0127883","DOI":"10.1371\/journal.pone.0127883","article-title":"Whole transcriptome of the venom gland from Urodacus yaschenkoi scorpion","volume":"10","author":"Luna-Ram\u00edrez","year":"2015","journal-title":"PLoS One"},{"key":"B51","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1038\/356083a0","article-title":"Assessment of protein models with three-dimensional profiles","volume":"356","author":"L\u00fcthy","year":"1992","journal-title":"Nature"},{"key":"B52","doi-asserted-by":"publisher","first-page":"4647","DOI":"10.1093\/molbev\/msab199","article-title":"BUSCO update: Novel and streamlined workflows along with broader and deeper phylogenetic coverage for scoring of eukaryotic, prokaryotic, and viral genomes","volume":"38","author":"Manni","year":"2021","journal-title":"Mol. Biol. Evol."},{"key":"B53","doi-asserted-by":"publisher","first-page":"1025","DOI":"10.1016\/s0969-2126(00)00511-6","article-title":"Crystal structure of hyaluronidase, a major allergen of bee venom","volume":"8","author":"Markovi\u0107-Housley","year":"2000","journal-title":"Structure"},{"key":"B54","doi-asserted-by":"publisher","first-page":"1530","DOI":"10.1093\/molbev\/msaa015","article-title":"IQ-TREE 2: new models and efficient methods for phylogenetic inference in the genomic era","volume":"37","author":"Minh","year":"2020","journal-title":"Mol. Biol. Evol."},{"key":"B55","doi-asserted-by":"publisher","first-page":"1126","DOI":"10.3390\/toxins7041126","article-title":"Three valuable peptides from bee and wasp venoms for therapeutic and biotechnological use: melittin, apamin and mastoparan","volume":"7","author":"Moreno","year":"2015","journal-title":"Toxins"},{"key":"B56","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1016\/j.toxicon.2005.10.014","article-title":"Purification and properties of hyaluronidase from palamneus gravimanus (Indian black scorpion) venom","volume":"47","author":"Morey","year":"2006","journal-title":"Toxicon"},{"key":"B57","doi-asserted-by":"publisher","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"B58","first-page":"95","article-title":"Production of the first effective immune equine serum antivenom against iranian honey bees (Apis mellifera meda)","volume":"15","author":"Nazari","year":"2024","journal-title":"Res. Animal Prod."},{"key":"B59","volume-title":"Isolation, Characterization, and Biological Activity of Phospholipase A2 (PLA2) and Hyaluronidase from Iranian Honey Bee Venom (","author":"Nazari","year":"2023"},{"key":"B60","doi-asserted-by":"publisher","first-page":"e0007048","DOI":"10.1371\/journal.pntd.0007048","article-title":"Inhibition of Tityus serrulatus venom hyaluronidase affects venom biodistribution","volume":"13","author":"Oliveira-Mendes","year":"2019","journal-title":"PLoS Neglected Trop. Dis."},{"key":"B61","doi-asserted-by":"publisher","first-page":"1495","DOI":"10.1016\/s0041-0101(01)00122-2","article-title":"A hyaluronidase from Tityus serrulatus scorpion venom: isolation, characterization and inhibition by flavonoids","volume":"39","author":"Pessini","year":"2001","journal-title":"Toxicon"},{"key":"B62","first-page":"329","article-title":"Species diversity of androctonus crassicauda and hemiscorpius lepturus using different metabolic genes expressed in RNA-seq data","volume":"15","author":"Pondehnezhadan","year":"2023","journal-title":"Animal Environ. J."},{"key":"B63","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1046\/j.1432-1327.1999.00625.x","article-title":"Scorpion toxins specific for Na+ channels","volume":"264","author":"Possani","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"B64","doi-asserted-by":"publisher","first-page":"437","DOI":"10.3390\/toxins16100437","article-title":"Optimizing scorpion toxin processing through artificial intelligence","volume":"16","author":"Psenicnik","year":"2024","journal-title":"Toxins"},{"key":"B65","doi-asserted-by":"publisher","first-page":"629","DOI":"10.1016\/0041-0101(88)90245-0","article-title":"The hyaluronidase activities of some Southeast Asian snake venoms","volume":"26","author":"Pukrittayakamee","year":"1988","journal-title":"Toxicon"},{"key":"B66","first-page":"301","article-title":"Isolation and characterization of hyaluronidase from scorpion (Heterometrus fulvipes) venom","volume":"20","author":"Ramanaiah","year":"1990","journal-title":"Biochem. Int."},{"key":"B67","volume-title":"The Scorpion Files","author":"Rein","year":"2023"},{"key":"B68","doi-asserted-by":"publisher","first-page":"1222","DOI":"10.17179\/excli2022-5078","article-title":"Intraspecific differences in androctunus crassicauda venom and envenomation symptoms","volume":"21","author":"Safdarian","year":"2022","journal-title":"EXCLI J."},{"key":"B69","doi-asserted-by":"publisher","first-page":"8","DOI":"10.61186\/jams.26.3.8","article-title":"Production of monovalent antivenom effective against Androctonus crassicauda scorpion venom","volume":"26","author":"Salabi","year":"","journal-title":"J. Arak. Uni. Med. Sci."},{"key":"B70","doi-asserted-by":"publisher","first-page":"111247","DOI":"10.1016\/j.compbiomed.2025.111247","article-title":"A computational study of venom as drug library: discovery of multifunctional astacin-like metalloproteases from Androctonus zagrosensis venom gland transcriptome","volume":"198","author":"Salabi","year":"","journal-title":"Comput. Biol. Med."},{"key":"B71","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1080\/15569543.2021.2018613","article-title":"New insights about scorpion venom hyaluronidase; isoforms, expression and phylogeny","volume":"42","author":"Salabi","year":"2023","journal-title":"Toxin Rev."},{"key":"B72","doi-asserted-by":"publisher","first-page":"e23658","DOI":"10.1096\/fj.202400178RR","article-title":"Whole transcriptome sequencing reveals the activity of the PLA2 family members in androctonus crassicauda (scorpionida: Buthidae) venom gland","volume":"38","author":"Salabi","year":"","journal-title":"FASEB J."},{"key":"B73","doi-asserted-by":"publisher","first-page":"110629","DOI":"10.1016\/j.dib.2024.110629","article-title":"Dataset of PLA2 family identified from transcriptomic high-throughput sequencing of androctonus crassicauda (scorpionida: Buthidae) venom gland","volume":"55","author":"Salabi","year":"","journal-title":"Data Brief"},{"key":"B74","doi-asserted-by":"publisher","first-page":"1567","DOI":"10.32598\/ARI.80.6.3928","article-title":"Androctonus nazarii, a new species of scorpions from Khuzestan Province, Iran (Scorpiones: Buthidae)","volume":"80","author":"Salabi","year":"","journal-title":"Archives of Razi Institute"},{"key":"B75","doi-asserted-by":"publisher","first-page":"4720","DOI":"10.1038\/s41598-021-83815-8","article-title":"Systematic and computational identification of androctonus crassicauda long non-coding RNAs","volume":"11","author":"Salabi","year":"2021","journal-title":"Sci. Rep."},{"key":"B76","doi-asserted-by":"publisher","first-page":"22277","DOI":"10.1038\/s41598-023-49556-6","article-title":"Identification, classification, and characterization of alpha and beta subunits of LVP1 protein from the venom gland of four Iranian scorpion species","volume":"13","author":"Salabi","year":"","journal-title":"Sci. Rep."},{"key":"B77","first-page":"109","article-title":"Fractionation and enzymes activity measurement of the scorpion androctonus crassicauda (scorpionida: Buthidae) venom","volume":"20","author":"Salabi","year":"2024","journal-title":"Iran. Veterinary J."},{"key":"B78","doi-asserted-by":"publisher","first-page":"105415","DOI":"10.1016\/j.jprot.2025.105415","article-title":"Revisiting toxins with transcriptomics-informed proteomics of venom glands and crude venom from Centruroides bicolor from Panama","volume":"316","author":"Samudio","year":"2025","journal-title":"J. Proteomics"},{"key":"B79","doi-asserted-by":"publisher","first-page":"e5902","DOI":"10.7717\/peerj.5902","article-title":"Integration of phylogenomics and molecular modeling reveals lineage-specific diversification of toxins in scorpions","volume":"6","author":"Santib\u00e1\u00f1ez-L\u00f3pez","year":"2018","journal-title":"PeerJ"},{"key":"B80","doi-asserted-by":"publisher","first-page":"1281","DOI":"10.1093\/sysbio\/syac021","article-title":"Phylogenomics of scorpions reveal contemporaneous diversification of scorpion mammalian predators and mammal-active sodium channel toxins","volume":"71","author":"Santib\u00e1\u00f1ez-L\u00f3pez","year":"2022","journal-title":"Syst. Biol."},{"key":"B81","doi-asserted-by":"publisher","first-page":"533","DOI":"10.1111\/cla.12551","article-title":"Congruence between ultraconserved element-based matrices and phylotranscriptomic datasets in the scorpion tree of life","volume":"39","author":"Santib\u00e1\u00f1ez-L\u00f3pez","year":"2023","journal-title":"Cladistics"},{"key":"B82","doi-asserted-by":"publisher","first-page":"6699","DOI":"10.1038\/s41467-024-51071-9","article-title":"Post-translational modification prediction via prompt-based fine-tuning of a GPT-2 model","volume":"15","author":"Shrestha","year":"2024","journal-title":"Nat. Commun."},{"key":"B83","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1186\/s12915-018-0486-7","article-title":"A software tool \u2018CroCo\u2019 detects pervasive cross-species contamination in next generation sequencing data","volume":"16","author":"Simion","year":"2018","journal-title":"BMC Biol."},{"key":"B84","doi-asserted-by":"publisher","first-page":"96","DOI":"10.3390\/toxins10030096","article-title":"True lies: using proteomics to assess the accuracy of transcriptome-based venomics in centipedes uncovers false positives and reveals startling variation in Scolopendra subspinipes","volume":"10","author":"Smith","year":"2018","journal-title":"Toxins"},{"key":"B85","doi-asserted-by":"publisher","first-page":"818","DOI":"10.1021\/cr050247k","article-title":"Hyaluronidases: their genomics, structures, and mechanisms of action","volume":"106","author":"Stern","year":"2006","journal-title":"Chem. Rev."},{"key":"B86","doi-asserted-by":"publisher","first-page":"e0258712","DOI":"10.1371\/journal.pone.0258712","article-title":"A non-lethal method for studying scorpion venom gland transcriptomes, with a review of potentially suitable taxa to which it can be applied","volume":"16","author":"Vonk","year":"2021","journal-title":"PLoS One"},{"key":"B87","doi-asserted-by":"publisher","first-page":"354","DOI":"10.1007\/s10600-023-03992-y","article-title":"Simplified two-step purification of hyaluronidase from Buthus martensii Manchurian scorpion venom","volume":"59","author":"Wali","year":"2023","journal-title":"Chem. Nat. Compd."},{"key":"B88","doi-asserted-by":"publisher","first-page":"e1900324","DOI":"10.1002\/pmic.201900324","article-title":"Deadly proteomes: a practical guide to proteotranscriptomics of animal venoms","author":"Walker","year":"2020","journal-title":"Proteomics"},{"key":"B89","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1016\/j.toxicon.2018.07.007","article-title":"A global accounting of medically significant scorpions: epidemiology, major toxins, and comparative resources in harmless counterparts","volume":"151","author":"Ward","year":"2018","journal-title":"Toxicon"},{"key":"B90","doi-asserted-by":"publisher","first-page":"1338","DOI":"10.12688\/f1000research.15931.2","article-title":"FastQ screen: a tool for multi-genome mapping and quality control","volume":"7","author":"Wingett","year":"2018","journal-title":"F1000Research"},{"key":"B91","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/j.jprot.2015.07.030","article-title":"Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis","volume":"128","author":"Zhang","year":"2015","journal-title":"J. Proteomics"}],"container-title":["Frontiers in Molecular Biosciences"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmolb.2026.1807239\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T08:36:27Z","timestamp":1781166987000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmolb.2026.1807239\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,1]]},"references-count":91,"alternative-id":["10.3389\/fmolb.2026.1807239"],"URL":"https:\/\/doi.org\/10.3389\/fmolb.2026.1807239","relation":{},"ISSN":["2296-889X"],"issn-type":[{"value":"2296-889X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,1]]},"article-number":"1807239"}}