{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T22:16:47Z","timestamp":1792016207361,"version":"4.4.0"},"reference-count":146,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2019,6,25]],"date-time":"2019-06-25T00:00:00Z","timestamp":1561420800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Santander-UCM","award":["PR 75-18-21561"],"award-info":[{"award-number":["PR 75-18-21561"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Animal venoms are complex mixtures of highly specialized toxic molecules. Cnidarians and arachnids produce pore-forming proteins (PFPs) directed against the plasma membrane of their target cells. Among PFPs from cnidarians, actinoporins stand out for their small size and molecular simplicity. While native actinoporins require only sphingomyelin for membrane binding, engineered chimeras containing a recognition antibody-derived domain fused to an actinoporin isoform can nonetheless serve as highly specific immunotoxins. Examples of such constructs targeted against malignant cells have been already reported. However, PFPs from arachnid venoms are less well-studied from a structural and functional point of view. Spiders from the Latrodectus genus are professional insect hunters that, as part of their toxic arsenal, produce large PFPs known as latrotoxins. Interestingly, some latrotoxins have been identified as potent and highly-specific insecticides. Given the proteinaceous nature of these toxins, their promising future use as efficient bioinsecticides is discussed throughout this Perspective. Protein engineering and large-scale recombinant production are critical steps for the use of these PFPs as tools to control agriculturally important insect pests. In summary, both families of PFPs, from Cnidaria and Arachnida, appear to be molecules with promising biotechnological applications.<\/jats:p>","DOI":"10.3390\/toxins11060370","type":"journal-article","created":{"date-parts":[[2019,6,25]],"date-time":"2019-06-25T10:52:31Z","timestamp":1561459951000},"page":"370","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Pore-Forming Proteins from Cnidarians and Arachnids as Potential Biotechnological Tools"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0272-6150","authenticated-orcid":false,"given":"Esperanza","family":"Rivera-de-Torre","sequence":"first","affiliation":[{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de CC. Qu\u00edmicas, Universidad Complutense de Madrid, 28040 Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4629-0221","authenticated-orcid":false,"given":"Juan","family":"Palacios-Ortega","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de CC. Qu\u00edmicas, Universidad Complutense de Madrid, 28040 Madrid, Spain"},{"name":"Biochemistry, Faculty of Science and Engineering, \u00c5bo Akademi University, 20500 Turku, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9","family":"Gavilanes","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de CC. Qu\u00edmicas, Universidad Complutense de Madrid, 28040 Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0043-5939","authenticated-orcid":false,"given":"\u00c1lvaro","family":"Mart\u00ednez-del-Pozo","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica y Biolog\u00eda Molecular, Facultad de CC. Qu\u00edmicas, Universidad Complutense de Madrid, 28040 Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4983-5730","authenticated-orcid":false,"given":"Sara","family":"Garc\u00eda-Linares","sequence":"additional","affiliation":[{"name":"Cell Biology Department, Harvard Medical School, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,6,25]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.tree.2012.10.020","article-title":"Complex cocktails: The evolutionary novelty of venoms","volume":"28","author":"Casewell","year":"2013","journal-title":"Trends Ecol. Evol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1042\/BCJ20160577","article-title":"Venomics: Integrative venom proteomics and beyond","volume":"474","author":"Calvete","year":"2017","journal-title":"Biochem. J."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.toxicon.2017.10.026","article-title":"Coevolution takes the sting out of it: Evolutionary biology and mechanisms of toxin resistance in animals","volume":"140","author":"Arbuckle","year":"2017","journal-title":"Toxicon"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.1016\/j.toxicon.2008.03.005","article-title":"A multigene family of Heteractis magnificalysins (HMgs)","volume":"51","author":"Wang","year":"2008","journal-title":"Toxicon"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.toxicon.2015.06.028","article-title":"The multigene families of actinoporins (part I): Isoforms and genetic structure","volume":"103","author":"Valle","year":"2015","journal-title":"Toxicon"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.toxicon.2018.05.014","article-title":"Stichodactyla helianthus\u2019 de novo transcriptome assembly: Discovery of a new actinoporin isoform","volume":"150","author":"Garb","year":"2018","journal-title":"Toxicon"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1016\/j.bbamem.2014.01.006","article-title":"The basic structure and dynamics of cell membranes: An update of the Singer-Nicolson model","volume":"1838","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"6863","DOI":"10.1021\/acs.biochem.5b01112","article-title":"Bidirectional Transformation of a Metamorphic Protein between the Water-Soluble and Transmembrane Native States","volume":"54","author":"Tanaka","year":"2015","journal-title":"Biochemistry"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2971","DOI":"10.1021\/acs.biochem.7b00375","article-title":"Metamorphic Proteins: Emergence of Dual Protein Folds from One Primary Sequence","volume":"56","author":"Lella","year":"2017","journal-title":"Biochemistry"},{"key":"ref_10","unstructured":"Iglic, A., Garc\u00eda-S\u00e1ez, A., and Rappolt, M. (2017). The metamorphic transformation of a water-soluble monomeric protein into an oligomeric transmembrane pore. Advances in Biomembranes and Lipid Self-Assembly, Elsevier."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.pbiomolbio.2004.01.009","article-title":"Pore-forming protein toxins: From structure to function","volume":"88","author":"Parker","year":"2005","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2275","DOI":"10.1016\/j.bbamem.2011.05.012","article-title":"The behavior of sea anemone actinoporins at the water-membrane interface","volume":"1808","author":"Bruix","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/S0092-8674(00)80251-2","article-title":"Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form","volume":"89","author":"Rossjohn","year":"1997","journal-title":"Cell"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"6630","DOI":"10.1021\/acs.biochem.6b01007","article-title":"Differential Effect of Membrane Composition on the Pore-Forming Ability of Four Different Sea Anemone Actinoporins","volume":"55","author":"Morante","year":"2016","journal-title":"Biochemistry"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.tibs.2008.07.004","article-title":"Disparate proteins use similar architectures to damage membranes","volume":"33","author":"Anderluh","year":"2008","journal-title":"Trends Biochem. Sci."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"18665","DOI":"10.1074\/jbc.M708747200","article-title":"Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin","volume":"283","author":"Podlesek","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1529\/biophysj.108.129981","article-title":"Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence","volume":"95","author":"Malovrh","year":"2008","journal-title":"Biophys. J."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1040","DOI":"10.1016\/j.cell.2018.12.042","article-title":"Molecular Discrimination between Two Conformations of Sphingomyelin in Plasma Membranes","volume":"176","author":"Endapally","year":"2019","journal-title":"Cell"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1038\/71247","article-title":"Structure of alpha-latrotoxin oligomers reveals that divalent cation-dependent tetramers form membrane pores","volume":"7","author":"Orlova","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1038\/s41467-019-09681-1","article-title":"Molecular dissection of box jellyfish venom cytotoxicity highlights an effective venom antidote","volume":"10","author":"Lau","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_21","first-page":"105","article-title":"Rhabdomyolysis during envenomation by Physalia sp envenomation in New Caldonia","volume":"27","author":"Maldonado","year":"2017","journal-title":"Med. Sante Trop."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1111\/jtm.12223","article-title":"Severe Toxic Skin Reaction Caused by a Common Anemone and Identification of the Culprit Organism","volume":"22","author":"Tezcan","year":"2015","journal-title":"J. Travel Med."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1016\/j.bbamem.2015.09.007","article-title":"Pore formation by actinoporins, cytolysins from sea anemones","volume":"1858","author":"Rojko","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2358","DOI":"10.1093\/gbe\/evw155","article-title":"Tissue-Specific Venom Composition and Differential Gene Expression in Sea Anemones","volume":"8","author":"Macrander","year":"2016","journal-title":"Genome Biol. Evol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"558","DOI":"10.2174\/138920307783018686","article-title":"Sea anemone actinoporins: The transition from a folded soluble state to a functionally active membrane-bound oligomeric pore","volume":"8","author":"Gavilanes","year":"2007","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1073\/pnas.73.2.467","article-title":"Properties of a toxin from the sea anemone Stoichacis helianthus, including specific binding to sphingomyelin","volume":"73","author":"Bernheimer","year":"1976","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"3300","DOI":"10.1016\/j.bpj.2010.09.049","article-title":"Effect of sphingomyelin headgroup size on molecular properties and interactions with cholesterol","volume":"99","author":"Rog","year":"2010","journal-title":"Biophys. J."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.toxicon.2006.09.019","article-title":"Effect of sphingomyelin and cholesterol on the interaction of St II with lipidic interfaces","volume":"49","author":"Otero","year":"2007","journal-title":"Toxicon"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1016\/j.bbamem.2014.12.017","article-title":"Cholesterol stimulates and ceramide inhibits Sticholysin II-induced pore formation in complex bilayer membranes","volume":"1848","author":"Alm","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.3390\/md13041647","article-title":"The effect of cholesterol on the long-range network of interactions established among sea anemone Sticholysin II residues at the water-membrane interface","volume":"13","author":"Alm","year":"2015","journal-title":"Mar. Drugs"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"3476","DOI":"10.1021\/acs.langmuir.6b00082","article-title":"Regulation of Sticholysin II-Induced Pore Formation by Lipid Bilayer Composition, Phase State, and Interfacial Properties","volume":"32","author":"Astrand","year":"2016","journal-title":"Langmuir"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1016\/j.bbamem.2015.12.019","article-title":"Neutron reflection study of the interaction of the eukaryotic pore-forming actinoporin equinatoxin II with lipid membranes reveals intermediate states in pore formation","volume":"1858","author":"Wacklin","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"11018","DOI":"10.1021\/acs.langmuir.7b01765","article-title":"Differential Effect of Bilayer Thickness on Sticholysin Activity","volume":"33","author":"Gavilanes","year":"2017","journal-title":"Langmuir"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1016\/j.bpj.2019.05.010","article-title":"Sticholysin, Sphingomyelin, and Cholesterol: A Closer Look at a Tripartite Interaction","volume":"116","author":"Gavilanes","year":"2019","journal-title":"Biophys. J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"3186","DOI":"10.1016\/S0006-3495(00)76855-X","article-title":"Two-dimensional crystallization on lipid monolayers and three-dimensional structure of sticholysin II, a cytolysin from the sea anemone Stichodactyla helianthus","volume":"78","author":"Gavilanes","year":"2000","journal-title":"Biophys. J."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1016\/j.str.2003.09.019","article-title":"Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation","volume":"11","author":"Gavilanes","year":"2003","journal-title":"Structure"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.str.2010.11.013","article-title":"Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins","volume":"19","author":"Mechaly","year":"2011","journal-title":"Structure"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"23704","DOI":"10.1074\/jbc.M113.481572","article-title":"Membrane damage by an alpha-helical pore-forming protein, Equinatoxin II, proceeds through a succession of ordered steps","volume":"288","author":"Rojko","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Antonini, V., P\u00e9rez-Barzaga, V., Bampi, S., Penton, D., Mart\u00ednez, D., Dalla-Serra, M., and Tejuca, M. (2014). Functional characterization of sticholysin I and W111C mutant reveals the sequence of the actinoporin\u2019s pore assembly. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0110824"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2139","DOI":"10.1002\/cbic.201300799","article-title":"Photobleaching reveals heterogeneous stoichiometry for equinatoxin II oligomers","volume":"15","author":"Baker","year":"2014","journal-title":"Chembiochem"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"4856","DOI":"10.1074\/jbc.M114.600676","article-title":"Toxicity of an alpha-pore-forming toxin depends on the assembly mechanism on the target membrane as revealed by single molecule imaging","volume":"290","author":"Subburaj","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"6337","DOI":"10.1038\/ncomms7337","article-title":"Structural basis for self-assembly of a cytolytic pore lined by protein and lipid","volume":"6","author":"Tanaka","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1391","DOI":"10.1016\/S0041-0101(99)00082-3","article-title":"Equinatoxins, pore-forming proteins from the sea anemone Actinia equina, belong to a multigene family","volume":"37","author":"Anderluh","year":"1999","journal-title":"Toxicon"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1470","DOI":"10.1016\/j.toxicon.2010.09.002","article-title":"Molecular characterization on the genome structure of hemolysin toxin isoforms isolated from sea anemone Actineria villosa and Phyllodiscus semoni","volume":"56","author":"Uechi","year":"2010","journal-title":"Toxicon"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1006\/prep.1999.1174","article-title":"Overproduction in Escherichia coli and purification of the hemolytic protein sticholysin II from the sea anemone Stichodactyla helianthus","volume":"18","author":"Lacadena","year":"2000","journal-title":"Protein Expr. Purif."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"14109","DOI":"10.1074\/jbc.M115.710491","article-title":"Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores","volume":"291","author":"Lacadena","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/S0969-2126(01)00592-5","article-title":"Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina","volume":"9","author":"Athanasiadis","year":"2001","journal-title":"Structure"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1006\/jmbi.2001.5321","article-title":"Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: Implications for pore formation","volume":"315","author":"Hinds","year":"2002","journal-title":"J. Mol. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.abb.2013.01.005","article-title":"Three-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function","volume":"532","author":"Castrillo","year":"2013","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"22678","DOI":"10.1074\/jbc.M300622200","article-title":"A novel mechanism of pore formation: Membrane penetration by the N-terminal amphipathic region of equinatoxin","volume":"278","author":"Malovrh","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.bbamem.2015.09.013","article-title":"Assembling the puzzle: Oligomerization of alpha-pore forming proteins in membranes","volume":"1858","author":"Cosentino","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1007\/s00232-015-9820-y","article-title":"More Than a Pore: The Interplay of Pore-Forming Proteins and Lipid Membranes","volume":"248","author":"Ros","year":"2015","journal-title":"J. Membr. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"46509","DOI":"10.1074\/jbc.M406193200","article-title":"Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich","volume":"279","author":"Kristan","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1111\/j.1742-4658.2006.05608.x","article-title":"The equinatoxin N-terminus is transferred across planar lipid membranes and helps to stabilize the transmembrane pore","volume":"274","author":"Kristan","year":"2007","journal-title":"FEBS J."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"3191","DOI":"10.1529\/biophysj.106.102566","article-title":"Infrared spectroscopy study on the conformational changes leading to pore formation of the toxin sticholysin II","volume":"93","author":"Gavilanes","year":"2007","journal-title":"Biophys. J."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"45216","DOI":"10.1074\/jbc.M305916200","article-title":"Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures","volume":"278","author":"Anderluh","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"3073","DOI":"10.1021\/acs.accounts.5b00403","article-title":"How Lipid Membranes Affect Pore Forming Toxin Activity","volume":"48","author":"Rojko","year":"2015","journal-title":"Acc. Chem. Res."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"19210","DOI":"10.1074\/jbc.M116.734053","article-title":"Identification of a Membrane-Bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins","volume":"291","author":"Morante","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1630","DOI":"10.1016\/j.bpj.2013.11.4507","article-title":"Imaging the lipid-phase-dependent pore formation of equinatoxin II in droplet interface bilayers","volume":"106","author":"Rojko","year":"2014","journal-title":"Biophys. J."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.jen.2014.01.004","article-title":"Black widow spider envenomation","volume":"40","author":"Camp","year":"2014","journal-title":"J. Emerg. Nurs."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Prentis, P.J., Pavasovic, A., and Norton, R.S. (2018). Sea Anemones: Quiet Achievers in the Field of Peptide Toxins. Toxins, 10.","DOI":"10.3390\/toxins10010036"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"11519","DOI":"10.1038\/s41598-018-29826-4","article-title":"Gomesin inhibits melanoma growth by manipulating key signaling cascades that control cell death and proliferation","volume":"8","author":"Ikonomopoulou","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/j.toxicon.2004.02.008","article-title":"The multiple actions of black widow spider toxins and their selective use in neurosecretion studies","volume":"43","author":"Ushkaryov","year":"2004","journal-title":"Toxicon"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/978-3-540-74805-2_7","article-title":"alpha-Latrotoxin and its receptors","volume":"184","author":"Ushkaryov","year":"2008","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"5055","DOI":"10.3390\/toxins7124862","article-title":"Recent Advances in Research on Widow Spider Venoms and Toxins","volume":"7","author":"Yan","year":"2015","journal-title":"Toxins"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1002\/ps.5206","article-title":"Molecular basis and mechanism underlying the insecticidal activity of venoms and toxins from Latrodectus spiders","volume":"75","author":"Wang","year":"2019","journal-title":"Pest Manag. Sci."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/j.toxicon.2006.11.021","article-title":"Insecticidal toxins from black widow spider venom","volume":"49","author":"Rohou","year":"2007","journal-title":"Toxicon"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1002\/jbt.20244","article-title":"Proteomic Analysis of Latrodectus tredecimguttatus Venom for Uncovering Potential Latrodectism-Related Proteins","volume":"22","author":"Duan","year":"2008","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"7535","DOI":"10.1074\/jbc.271.13.7535","article-title":"Cloning and structure of delta-latroinsectotoxin, a novel insect-specific member of the latrotoxin family: Functional expression requires C-terminal truncation","volume":"271","author":"Dulubova","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/j.gene.2013.11.054","article-title":"Recruitment and diversification of an ecdysozoan family of neuropeptide hormones for black widow spider venom expression","volume":"536","author":"McCowan","year":"2014","journal-title":"Gene"},{"key":"ref_71","first-page":"1138","article-title":"Isolation and properties of insect-specific neurotoxins from venoms of the spider Lactodectus mactans tredecimguttatus","volume":"16","author":"Krasnoperov","year":"1990","journal-title":"Bioorg. Khim."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1693","DOI":"10.1016\/S0041-0101(98)00162-7","article-title":"Black widow spider toxins: The present and the future","volume":"36","author":"Grishin","year":"1998","journal-title":"Toxicon"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/0014-5793(90)81250-R","article-title":"Cloning and structure of cDNA encoding alpha-latrotoxin from black widow spider venom","volume":"270","author":"Kiyatkin","year":"1990","journal-title":"FEBS Lett."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/0041-0101(92)90012-T","article-title":"Structure of the low molecular weight protein copurified with alpha-latrotoxin","volume":"30","author":"Kiyatkin","year":"1992","journal-title":"Toxicon"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/0041-0101(94)00166-6","article-title":"Low molecular weight components from black widow spider venom","volume":"33","author":"Volkova","year":"1995","journal-title":"Toxicon"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/0014-5793(93)80803-3","article-title":"Modulation of functional activities of the neurotoxin from black widow spider venom","volume":"336","author":"Grishin","year":"1993","journal-title":"FEBS Lett."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1111\/j.1432-1033.1995.0854g.x","article-title":"Functional characterization of black widow spider neurotoxins synthesised in insect cells","volume":"230","author":"Kiyatkin","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"ref_78","first-page":"322","article-title":"The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the alpha-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae)","volume":"230","author":"Pescatori","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"19803","DOI":"10.1016\/S0021-9258(17)32091-4","article-title":"The low molecular weight protein which co-purifies with alpha-latrotoxin is structurally related to crustacean hyperglycemic hormones","volume":"269","author":"Gasparini","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1590\/S1678-91992012000400002","article-title":"African Society of Toxinology: A new opportunity for integrating the control of envenomations in Africa","volume":"18","author":"Chippaux","year":"2012","journal-title":"J. Venom. Anim. Toxins Trop. Dis."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Olombrada, M., L\u00e1zaro-Gorines, R., L\u00f3pez-Rodriguez, J.C., Mart\u00ednez-del-Pozo, \u00c1., O\u00f1aderra, M., Maestro-L\u00f3pez, M., Lacadena, J., Gavilanes, J.G., and Garc\u00eda-Ortega, L. (2017). Fungal Ribotoxins: A Review of Potential Biotechnological Applications. Toxins, 9.","DOI":"10.3390\/toxins9020071"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.toxicon.2017.11.006","article-title":"Immune drug discovery from venoms","volume":"141","author":"Ikonomopoulou","year":"2018","journal-title":"Toxicon"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"22186","DOI":"10.1074\/jbc.M110.105122","article-title":"A toxin-based probe reveals cytoplasmic exposure of Golgi sphingomyelin","volume":"285","author":"Kladnik","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Sko\u010daj, M., Resnik, N., Grundner, M., Ota, K., Rojko, N., Hodnik, V., Anderluh, G., Sobota, A., Macek, P., and Veranic, P. (2014). Tracking cholesterol\/sphingomyelin-rich membrane domains with the ostreolysin A-mCherry protein. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0092783"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"E532","DOI":"10.1208\/aapsj080363","article-title":"Immunotoxins for targeted cancer therapy","volume":"8","author":"Kreitman","year":"2006","journal-title":"AAPS J."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1016\/j.hoc.2006.06.009","article-title":"Immunotoxins in the treatment of refractory hairy cell leukemia","volume":"20","author":"Kreitman","year":"2006","journal-title":"Hematol. Oncol. Clin. N. Am."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1093\/protein\/gzs032","article-title":"Production and characterization of a colon cancer-specific immunotoxin based on the fungal ribotoxin alpha-sarcin","volume":"25","author":"Batt","year":"2012","journal-title":"Protein Eng. Des. Sel."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"3022","DOI":"10.1111\/j.1742-4658.2012.08683.x","article-title":"Production and characterization of scFvA33T1, an immunoRNase targeting colon cancer cells","volume":"279","author":"Batt","year":"2012","journal-title":"FEBS J."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2131","DOI":"10.1111\/febs.13262","article-title":"Preparation of an engineered safer immunotoxin against colon carcinoma based on the ribotoxin hirsutellin A","volume":"282","author":"Gavilanes","year":"2015","journal-title":"FEBS J."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1186\/s40064-015-0943-5","article-title":"Efficient in vivo antitumor effect of an immunotoxin based on ribotoxin alpha-sarcin in nude mice bearing human colorectal cancer xenografts","volume":"4","author":"Olombrada","year":"2015","journal-title":"Springerplus"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1111\/febs.13169","article-title":"alpha-sarcin and RNase T1 based immunoconjugates: The role of intracellular trafficking in cytotoxic efficiency","volume":"282","author":"Gavilanes","year":"2015","journal-title":"FEBS J."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1080\/14712598.2019.1614558","article-title":"Moxetumomab pasudotox for the treatment of hairy cell leukemia","volume":"19","author":"Janus","year":"2019","journal-title":"Expert Opin. Biol. Ther."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1007\/s00280-016-3160-1","article-title":"Application of bee venom and its main constituent melittin for cancer treatment","volume":"78","author":"Liu","year":"2016","journal-title":"Cancer Chemother. Pharmacol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"2151","DOI":"10.1016\/j.transproceed.2006.06.045","article-title":"Selective depletion of activated T cells by recombinant immunotoxin containing anti-CTLA-4 single-chain fragment of variable antibody and N-terminal fragment of perforin","volume":"38","author":"Zeng","year":"2006","journal-title":"Transplant. Proc."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1016\/j.toxicon.2009.02.025","article-title":"Sea anemone cytolysins as toxic components of immunotoxins","volume":"54","author":"Tejuca","year":"2009","journal-title":"Toxicon"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1002\/ijc.2910420417","article-title":"A new immunotoxin built by linking a hemolytic toxin to a monoclonal antibody specific for immature T lymphocytes","volume":"42","author":"Lage","year":"1988","journal-title":"Int. J. Cancer"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1002\/ijc.2910430533","article-title":"A carcinoembryonic antigen-directed immunotoxin built by linking a monoclonal antibody to a hemolytic toxin","volume":"43","author":"Lage","year":"1989","journal-title":"Int. J. Cancer"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/j.intimp.2004.02.010","article-title":"Construction of an immunotoxin with the pore forming protein StI and ior C5, a monoclonal antibody against a colon cancer cell line","volume":"4","author":"Tejuca","year":"2004","journal-title":"Int. Immunopharmacol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1390","DOI":"10.1016\/j.bbamem.2013.01.018","article-title":"2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes","volume":"1828","author":"Maula","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1465","DOI":"10.1111\/febs.12717","article-title":"The sea anemone actinoporin (Arg-Gly-Asp) conserved motif is involved in maintaining the competent oligomerization state of these pore-forming toxins","volume":"281","author":"Richmond","year":"2014","journal-title":"FEBS J."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1016\/j.bbamem.2016.03.013","article-title":"Toxin-induced pore formation is hindered by intermolecular hydrogen bonding in sphingomyelin bilayers","volume":"1858","author":"Yasuda","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"6406","DOI":"10.1021\/acs.biochem.6b00935","article-title":"Role of the Tryptophan Residues in the Specific Interaction of the Sea Anemone Stichodactyla helianthus\u2019s Actinoporin Sticholysin II with Biological Membranes","volume":"55","author":"Maula","year":"2016","journal-title":"Biochemistry"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1007\/978-1-4419-6327-7_9","article-title":"Molecular mechanism of sphingomyelin-specific membrane binding and pore formation by actinoporins","volume":"677","author":"Anderluh","year":"2010","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1002\/path.5225","article-title":"Recent advances in understanding the roles of matrix metalloproteinases in tumour invasion and metastasis","volume":"247","author":"Conlon","year":"2019","journal-title":"J. Pathol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.4155\/fmc.14.73","article-title":"The current stage of cathepsin B inhibitors as potential anticancer agents","volume":"6","author":"Kos","year":"2014","journal-title":"Future Med. Chem."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1002\/ijc.30714","article-title":"The proprotein convertase furin in tumour progression","volume":"141","author":"Jaaks","year":"2017","journal-title":"Int. J. Cancer"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1021\/bc049873z","article-title":"Cytotoxic activity of a tumor protease-activated pore-forming toxin","volume":"16","author":"Potrich","year":"2005","journal-title":"Bioconjug. Chem."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.abb.2017.11.005","article-title":"One single salt bridge explains the different cytolytic activities shown by actinoporins sticholysin I and II from the venom of Stichodactyla helianthus","volume":"636","author":"Gavilanes","year":"2017","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1126\/science.aat3466","article-title":"Increase in crop losses to insect pests in a warming climate","volume":"361","author":"Deutsch","year":"2018","journal-title":"Science"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1186\/s40409-015-0019-6","article-title":"The unfulfilled promises of scorpion insectotoxins","volume":"21","author":"Ortiz","year":"2015","journal-title":"J. Venom Anim. Toxins Trop. Dis."},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"King, G.F. (2019). Tying pest insects in knots: The deployment of spider-venom-derived knottins as bioinsecticides. Pest Manag. Sci., 2019.","DOI":"10.1002\/ps.5452"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1093\/toxsci\/kfx249","article-title":"Food and Feed Safety of Genetically Engineered Food Crops","volume":"162","author":"Delaney","year":"2018","journal-title":"Toxicol. Sci."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1002\/jsfa.9227","article-title":"Legislation governing genetically modified and genome-edited crops in Europe: The need for change","volume":"99","author":"Halford","year":"2019","journal-title":"J. Sci. Food Agric."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1574-6976.2012.00341.x","article-title":"Bacillus thuringiensis insecticidal three-domain Cry toxins: Mode of action, insect resistance and consequences for crop protection","volume":"37","author":"Bravo","year":"2013","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Wei, J., Zhang, Y., and An, S. (2019). The progress in insect cross-resistance among Bacillus thuringiensis toxins. Arch. Insect. Biochem. Physiol., 2019.","DOI":"10.1002\/arch.21547"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1007\/978-1-4419-6327-7_11","article-title":"Pore Formation by Cry Toxins","volume":"677","author":"Pardo","year":"2010","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"4366","DOI":"10.3390\/toxins7104366","article-title":"The Cystine Knot Is Responsible for the Exceptional Stability of the Insecticidal Spider Toxin omega-Hexatoxin-Hv1a","volume":"7","author":"Herzig","year":"2015","journal-title":"Toxins"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"537508","DOI":"10.1155\/2015\/537508","article-title":"High Proteolytic Resistance of Spider-Derived Inhibitor Cystine Knots","volume":"2015","author":"Kikuchi","year":"2015","journal-title":"Int. J. Pept."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Hardy, M.C., Daly, N.L., Mobli, M., Morales, R.A.V., and Keng, G.F. (2013). Isolation of an Orally Active Insecticidal Toxin from the Venom of an Australian Tarantula. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0073136"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3389\/fpls.2015.00283","article-title":"The food and environmental safety of Bt crops","volume":"6","author":"Koch","year":"2015","journal-title":"Front. Plant Sci."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1146\/annurev-ento-120811-153650","article-title":"Spider-venom peptides: Structure, pharmacology, and potential for control of insect pests","volume":"58","author":"King","year":"2013","journal-title":"Annu. Rev. Entomol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.tibtech.2013.08.001","article-title":"Delivery of intrahemocoelic peptides for insect pest management","volume":"32","author":"Bonning","year":"2014","journal-title":"Trends Biotechnol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1038\/370138a0","article-title":"Field Trial of a Genetically Improved Baculovirus Insecticide","volume":"370","author":"Cory","year":"1994","journal-title":"Nature"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1002\/ps.393","article-title":"Recombinant baculoviruses for insect control","volume":"57","author":"Inceoglu","year":"2001","journal-title":"Pest Manag. Sci."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.3389\/fmicb.2017.01337","article-title":"Covert Infection of Insects by Baculoviruses","volume":"8","author":"Williams","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.biotechadv.2005.09.001","article-title":"Baculoviruses\u2014re-emerging biopesticides","volume":"24","author":"Szewczyk","year":"2006","journal-title":"Biotechnol. Adv."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1126\/science.aaw8737","article-title":"Transgenic Metarhizium rapidly kills mosquitoes in a malaria-endemic region of Burkina Faso","volume":"364","author":"Lovett","year":"2019","journal-title":"Science"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1161\/01.HYP.17.4.589","article-title":"History of the design of captopril and related inhibitors of angiotensin converting enzyme","volume":"17","author":"Cushman","year":"1991","journal-title":"Hypertension"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.tibs.2018.12.004","article-title":"Friends or Foes? Emerging Impacts of Biological Toxins","volume":"44","author":"Clark","year":"2019","journal-title":"Trends Biochem. Sci."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Schwager, E.E., Sharma, P.P., Clarke, T., Leite, D.J., Wierschin, T., Pechmann, M., Akiyama-Oda, Y., Esposito, L., Bechsgaard, J., and Bilde, T. (2017). The house spider genome reveals an ancient whole-genome duplication during arachnid evolution. BMC Biol., 15.","DOI":"10.1186\/s12915-017-0399-x"},{"key":"ref_131","first-page":"e51618","article-title":"Extraction of venom and venom gland microdissections from spiders for proteomic and transcriptomic analyses","volume":"93","author":"Garb","year":"2014","journal-title":"J. Vis. Exp."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Von Reumont, B.M. (2018). Studying Smaller and Neglected Organisms in Modern Evolutionary Venomics Implementing RNASeq (Transcriptomics)-A Critical Guide. Toxins, 10.","DOI":"10.3390\/toxins10070292"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1016\/j.ympev.2003.10.012","article-title":"The black widow spider genus Latrodectus (Araneae: Theridiidae): Phylogeny, biogeography, and invasion history","volume":"31","author":"Garb","year":"2004","journal-title":"Mol. Phylogenet. Evol."},{"key":"ref_134","doi-asserted-by":"crossref","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":"ref_135","doi-asserted-by":"crossref","unstructured":"Clarke, T.H., Garb, J.E., Hayashi, C.Y., Haney, R.A., Lancaster, A.K., Corbett, S., and Ayoub, N.A. (2014). Multi-tissue transcriptomics of the black widow spider reveals expansions, co-options, and functional processes of the silk gland gene toolkit. BMC Genom., 15.","DOI":"10.1186\/1471-2164-15-365"},{"key":"ref_136","doi-asserted-by":"crossref","unstructured":"Wilson, D., and Daly, N.L. (2018). Venomics: A Mini-Review. High Throughput, 7.","DOI":"10.3390\/ht7030019"},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Haney, R.A., Ayoub, N.A., Clarke, T.H., Hayashi, C.Y., and Garb, J.E. (2014). Dramatic expansion of the black widow toxin arsenal uncovered by multi-tissue transcriptomics and venom proteomics. BMC Genom., 15.","DOI":"10.1186\/1471-2164-15-366"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Macrander, J., Brugler, M.R., and Daly, M. (2015). A RNA-seq approach to identify putative toxins from acrorhagi in aggressive and non-aggressive Anthopleura elegantissima polyps. BMC Genom., 16.","DOI":"10.1186\/s12864-015-1417-4"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Xie, B., Huang, Y., Baumann, K., Fry, B.G., and Shi, Q. (2017). From Marine Venoms to Drugs: Efficiently Supported by a Combination of Transcriptomics and Proteomics. Mar. Drugs, 15.","DOI":"10.3390\/md15040103"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.jprot.2017.07.007","article-title":"Revisiting venom of the sea anemone Stichodactyla haddoni: Omics techniques reveal the complete toxin arsenal of a well-studied sea anemone genus","volume":"166","author":"Madio","year":"2017","journal-title":"J. Proteom."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Zancolli, G., Sanz, L., Calvete, J.J., and Wuster, W. (2017). Venom On-a-Chip: A Fast and Efficient Method for Comparative Venomics. Toxins, 9.","DOI":"10.3390\/toxins9060179"},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Brinkman, D.L., Jia, X., Potriquet, J., Kumar, D., Dash, D., Kvaskoff, D., and Mulvenna, J. (2015). Transcriptome and venom proteome of the box jellyfish Chironex fleckeri. BMC Genom., 16.","DOI":"10.1186\/s12864-015-1568-3"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.toxicon.2015.09.038","article-title":"Multi-copy venom genes hidden in de novo transcriptome assemblies, a cautionary tale with the snakelocks sea anemone Anemonia sulcata (Pennant, 1977)","volume":"108","author":"Macrander","year":"2015","journal-title":"Toxicon"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1186\/2041-9139-4-16","article-title":"A quantitative reference transcriptome for Nematostella vectensis early embryonic development: A pipeline for de novo assembly in emerging model systems","volume":"4","author":"Tulin","year":"2013","journal-title":"Evodevo"},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Gao, B., Peng, C., Yang, J., Yi, Y., Zhang, J., and Shi, Q. (2017). Cone Snails: A Big Store of Conotoxins for Novel Drug Discovery. Toxins, 9.","DOI":"10.3390\/toxins9120397"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"e5361","DOI":"10.7717\/peerj.5361","article-title":"Venomix: A simple bioinformatic pipeline for identifying and characterizing toxin gene candidates from transcriptomic data","volume":"6","author":"Macrander","year":"2018","journal-title":"PeerJ"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/11\/6\/370\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T13:00:58Z","timestamp":1760187658000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/11\/6\/370"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,6,25]]},"references-count":146,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2019,6]]}},"alternative-id":["toxins11060370"],"URL":"https:\/\/doi.org\/10.3390\/toxins11060370","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,6,25]]}}}