{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T10:20:34Z","timestamp":1792578034296,"version":"4.5.0"},"reference-count":133,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2019,6,19]],"date-time":"2019-06-19T00:00:00Z","timestamp":1560902400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["408633\/2018-2"],"award-info":[{"award-number":["408633\/2018-2"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004612","name":"Funda\u00e7\u00e3o Arauc\u00e1ria","doi-asserted-by":"publisher","award":["057\/2017"],"award-info":[{"award-number":["057\/2017"]}],"id":[{"id":"10.13039\/501100004612","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Brown spider envenomation results in dermonecrosis with gravitational spreading characterized by a marked inflammatory reaction and with lower prevalence of systemic manifestations such as renal failure and hematological disturbances. Several toxins make up the venom of these species, and they are mainly peptides and proteins ranging from 5\u201340 kDa. The venoms have three major families of toxins: phospholipases-D, astacin-like metalloproteases, and the inhibitor cystine knot (ICK) peptides. Serine proteases, serpins, hyaluronidases, venom allergens, and a translationally controlled tumor protein (TCTP) are also present. Toxins hold essential biological properties that enable interactions with a range of distinct molecular targets. Therefore, the application of toxins as research tools and clinical products motivates repurposing their uses of interest. This review aims to discuss possibilities for brown spider venom toxins as putative models for designing molecules likely for therapeutics based on the status quo of brown spider venoms. Herein, we explore new possibilities for the venom components in the context of their biochemical and biological features, likewise their cellular targets, three-dimensional structures, and mechanisms of action.<\/jats:p>","DOI":"10.3390\/toxins11060355","type":"journal-article","created":{"date-parts":[[2019,6,19]],"date-time":"2019-06-19T10:43:32Z","timestamp":1560941012000},"page":"355","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":31,"title":["Brown Spider (Loxosceles) Venom Toxins as Potential Biotools for the Development of Novel Therapeutics"],"prefix":"10.3390","volume":"11","author":[{"given":"Daniele","family":"Chaves-Moreira","sequence":"first","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fernando Hitomi","family":"Matsubara","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zelinda","family":"Schemczssen-Graeff","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elidiana","family":"De Bona","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vanessa Ribeiro","family":"Heidemann","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7698-3811","authenticated-orcid":false,"given":"Clara","family":"Guerra-Duarte","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica e Imunologia, Universidade Federal de Minas Gerais (UFMG), Belo Horizonte 31270-901, MG, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luiza Helena","family":"Gremski","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9390-7207","authenticated-orcid":false,"given":"Carlos","family":"Ch\u00e1vez-Ol\u00f3rtegui","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica e Imunologia, Universidade Federal de Minas Gerais (UFMG), Belo Horizonte 31270-901, MG, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Senff-Ribeiro","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga Meiri","family":"Chaim","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raghuvir Krishnaswamy","family":"Arni","sequence":"additional","affiliation":[{"name":"Centro Multiusu\u00e1rio de Inova\u00e7\u00e3o Biomolecular, Departamento de F\u00edsica, Universidade Estadual Paulista (UNESP), S\u00e3o Jos\u00e9 do Rio Preto 15054-000, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvio Sanches","family":"Veiga","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular, Universidade Federal do Paran\u00e1 (UFPR), Curitiba 81531-970, PR, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,6,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"7402","DOI":"10.1016\/S0021-9258(18)42531-8","article-title":"Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas","volume":"267","author":"Eng","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1096\/fj.03-0093life","article-title":"The discovery of captopril","volume":"17","author":"Smith","year":"2003","journal-title":"FASEB J."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1358\/dot.2006.42.6.973534","article-title":"Ziconotide: A new option for refractory pain","volume":"42","author":"Prommer","year":"2006","journal-title":"Drugs Today"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.toxicon.2004.07.012","article-title":"Brown spiders and loxoscelism","volume":"44","author":"Appel","year":"2004","journal-title":"Toxicon"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.toxicon.2014.02.023","article-title":"Recent advances in the understanding of brown spider venoms: From the biology of spiders to the molecular mechanisms of toxins","volume":"83","author":"Gremski","year":"2014","journal-title":"Toxicon"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Ferrer, V.P., de Mari, T.L., Gremski, L.H., Trevisan-Silva, D., da Silveira, R.B., Gremski, W., Chaim, O.M., Senff-Ribeiro, A., Nader, H.B., and Veiga, S.S. (2013). A novel hyaluronidase from brown spider (Loxosceles intermedia) venom (Dietrich\u2019s Hyaluronidase): From cloning to functional characterization. PLoS Negl. Trop. Dis., 7.","DOI":"10.1371\/journal.pntd.0002206"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.toxicon.2004.05.028","article-title":"Identification and molecular cloning of insecticidal toxins from the venom of the brown spider Loxosceles intermedia","volume":"44","author":"Silvestre","year":"2004","journal-title":"Toxicon"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"170090","DOI":"10.1038\/sdata.2017.90","article-title":"A multi-protease, multi-dissociation, bottom-up-to-top-down proteomic view of the Loxosceles intermedia venom","volume":"4","author":"Bednaski","year":"2017","journal-title":"Sci. Data"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2403","DOI":"10.1039\/c004118a","article-title":"A novel expression profile of the Loxosceles intermedia spider venomous gland revealed by transcriptome analysis","volume":"19","author":"Gremski","year":"2010","journal-title":"Mol. Biosyst."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.biocel.2011.10.013","article-title":"Molecular cloning, heterologous expression and functional characterization of a novel translationally-controlled tumor protein (TCTP) family member from Loxosceles intermedia (brown spider) venom","volume":"44","author":"Sade","year":"2012","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1046\/j.1365-2613.2002.00241.x","article-title":"Histopathological findings in rabbits after experimental acute exposure to the Loxosceles intermedia (brown spider) venom","volume":"83","author":"Ospedal","year":"2002","journal-title":"Int. J. Exp. Pathol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1016\/j.toxicon.2010.06.022","article-title":"Inflammatory mediators generated at the site of inoculation of Loxosceles gaucho spider venom","volume":"56","author":"Barbaro","year":"2010","journal-title":"Toxicon"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1023\/A:1006995023982","article-title":"Loxosceles deserta spider venom induces the expression of vascular endothelial growth factor (VEGF) in keratinocytes","volume":"24","author":"Desai","year":"2000","journal-title":"Inflammation"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1590\/S0100-879X2001000700002","article-title":"Extracellular matrix molecules as targets for brown spider venom toxins","volume":"34","author":"Veiga","year":"2001","journal-title":"Braz. J. Med. Biol. Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1016\/j.toxicon.2006.02.006","article-title":"The effect of brown spider venom on endothelial cell morphology and adhesive structures","volume":"47","author":"Paludo","year":"2006","journal-title":"Toxicon"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0049-3848(01)00254-7","article-title":"In vivo and in vitro cytotoxicity of brown spider venom for blood vessel endothelial cells","volume":"102","author":"Veiga","year":"2001","journal-title":"Thromb. Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1264","DOI":"10.1038\/sj.jid.5700644","article-title":"Upregulation of IL-6, IL-8, CXCL1, and CXCL2 dominates gene expression in human fibroblast cells exposed to Loxosceles reclusa sphingomyelinase D: Insights into spider venom dermonecrosis","volume":"127","author":"Dragulev","year":"2007","journal-title":"J. Investig. Dermatol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.bbalip.2010.11.005","article-title":"Phospholipase-D activity and inflammatory response induced by brown spider dermonecrotic toxin: Endothelial cell membrane phospholipids as targets for toxicity","volume":"1811","author":"Chaim","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1002\/jcb.22148","article-title":"Identification of a direct hemolytic effect dependent on the catalytic activity induced by phospholipase-D (dermonecrotic toxin) from brown spider venom","volume":"107","author":"Chaim","year":"2009","journal-title":"J. Cell. Biochem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2529","DOI":"10.1002\/jcb.23177","article-title":"The relationship between calcium and the metabolism of plasma membrane phospholipids in hemolysis induced by brown spider venom phospholipase-D toxin","volume":"112","author":"Souza","year":"2011","journal-title":"J. Cell. Biochem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1046\/j.1365-2567.2002.01483.x","article-title":"Mechanism of induction of complement susceptibility of erythrocytes by spider and bacterial sphingomyelinases","volume":"107","author":"Tambourgi","year":"2002","journal-title":"Immunology"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.bbagen.2007.11.007","article-title":"Identification, cloning and functional characterization of a novel dermonecrotic toxin (phospholipase D) from brown spider (Loxosceles intermedia) venom","volume":"1780","author":"Appel","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1016\/j.biochi.2006.02.008","article-title":"Molecular cloning and functional characterization of two isoforms of dermonecrotic toxin from Loxosceles intermedia (brown spider) venom gland","volume":"88","author":"Pigozzo","year":"2006","journal-title":"Biochimie"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.biochi.2006.12.002","article-title":"Two novel dermonecrotic toxins LiRecDT4 and LiRecDT5 from brown spider (Loxosceles intermedia) venom: From cloning to functional characterization","volume":"89","author":"Pigozzo","year":"2007","journal-title":"Biochimie"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1177\/0960327110393761","article-title":"Loxosceles gaucho spider venom and its sphingomyelinase fraction trigger the main functions of human and rabbit platelets","volume":"30","author":"Tavares","year":"2011","journal-title":"Hum. Exp. Toxicol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0041-0101(03)00127-2","article-title":"Hematological cell findings in bone marrow and peripheral blood of rabbits after experimental acute exposure to Loxosceles intermedia (brown spider) venom","volume":"42","author":"Hashimoto","year":"2003","journal-title":"Toxicon"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.taap.2005.05.015","article-title":"Brown spider dermonecrotic toxin directly induces nephrotoxicity","volume":"211","author":"Chaim","year":"2006","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1016\/j.biochi.2008.07.011","article-title":"Nephrotoxicity caused by brown spider venom phospholipase-D (dermonecrotic toxin) depends on catalytic activity","volume":"90","author":"Kusma","year":"2008","journal-title":"Biochimie"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1016\/S0041-0101(97)00083-4","article-title":"Detection and characterization of metalloproteinases with gelatinolytic, fibronectinolytic and fibrinogenolytic activities in brown spider (Loxosceles intermedia) venom","volume":"36","author":"Feitosa","year":"1998","journal-title":"Toxicon"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/S0041-0101(02)00078-8","article-title":"Identification of proteases in the extract of venom glands from brown spider","volume":"40","author":"Filho","year":"2002","journal-title":"Toxicon"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.biotechadv.2007.12.003","article-title":"Biotechnological applications of brown spider (Loxosceles genus) venom toxins","volume":"26","author":"Chaim","year":"2008","journal-title":"Biotechnol. Adv."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1016\/S0006-291X(02)02521-4","article-title":"Molecular cloning and expression of a functional dermonecrotic and haemolytic factor from Loxosceles laeta venom","volume":"298","author":"Ramos","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2479","DOI":"10.1002\/jcb.24594","article-title":"Brown spider phospholipase-D containing a conservative mutation (D233E) in the catalytic site: Identification and functional characterization","volume":"114","author":"Vuitika","year":"2013","journal-title":"J. Cell. Biochem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1042\/BJ20050043","article-title":"Brown recluse spider (Loxosceles reclusa) venom phospholipase D (PLD) generates lysophosphatidic acid (LPA)","volume":"391","author":"Lee","year":"2005","journal-title":"Biochem. J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/j.toxicon.2005.09.002","article-title":"Characterization of the venom from the Brazilian Brown Spider Loxosceles similis Moenkhaus, 1898 (Araneae, Sicariidae)","volume":"46","author":"Silvestre","year":"2005","journal-title":"Toxicon"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.toxicon.2004.06.013","article-title":"Genetic and enzymatic characterization of sphingomyelinase D isoforms from the North American fiddleback spiders Loxosceles boneti and Loxosceles reclusa","volume":"44","author":"Olvera","year":"2004","journal-title":"Toxicon"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"768","DOI":"10.2174\/1389203716666150505231625","article-title":"Structural Insights into Substrate Binding of Brown Spider Venom Class II Phospholipases D","volume":"16","author":"Coronado","year":"2015","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1016\/j.bbrc.2011.05.053","article-title":"Structure of a novel class II phospholipase D: Catalytic cleft is modified by a disulphide bridge","volume":"409","author":"Ullah","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/j.bbrc.2006.01.123","article-title":"Structural insights into the catalytic mechanism of sphingomyelinases D and evolutionary relationship to glycerophosphodiester phosphodiesterases","volume":"342","author":"Murakami","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"13658","DOI":"10.1074\/jbc.M412437200","article-title":"Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D","volume":"280","author":"Murakami","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.toxicon.2013.08.065","article-title":"Differential metalloprotease content and activity of three Loxosceles spider venoms revealed using two-dimensional electrophoresis approaches","volume":"76","author":"Bednaski","year":"2013","journal-title":"Toxicon"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1042\/BJ20070363","article-title":"Identification, cloning, expression and functional characterization of an astacin-like metalloprotease toxin from Loxosceles intermedia (brown spider) venom","volume":"406","author":"Wille","year":"2007","journal-title":"Biochem. J."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.biochi.2009.10.003","article-title":"Astacin-like metalloproteases are a gene family of toxins present in the venom of different species of the brown spider (genus Loxosceles)","volume":"92","author":"Gremski","year":"2010","journal-title":"Biochimie"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/j.toxicon.2013.05.014","article-title":"A novel ICK peptide from the Loxosceles intermedia (brown spider) venom gland: Cloning, heterologous expression and immunological crossreactivity approaches","volume":"71","author":"Matsubara","year":"2013","journal-title":"Toxicon"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Lajoie, D.M., Zobel-Thropp, P.A., Kumirov, V.K., Bandarian, V., Binford, G.J., and Cordes, M.H. (2013). Phospholipase D toxins of brown spider venom convert lysophosphatidylcholine and sphingomyelin to cyclic phosphates. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0072372"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1773","DOI":"10.1016\/j.biochi.2013.06.002","article-title":"Cloning, expression and characterization of a phospholipase D from Loxosceles gaucho venom gland","volume":"95","author":"Caporrino","year":"2013","journal-title":"Biochimie"},{"key":"ref_47","unstructured":"De Bona, E. Personal communication."},{"key":"ref_48","unstructured":"Da Justa, H.C. Personal communication."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1573","DOI":"10.1016\/S0041-0101(98)00149-4","article-title":"The cystine knot structure of ion channel toxins and related polypeptides","volume":"36","author":"Norton","year":"1998","journal-title":"Toxicon"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2851","DOI":"10.3390\/toxins2122851","article-title":"Spider-venom peptides as therapeutics","volume":"2","author":"Saez","year":"2010","journal-title":"Toxins"},{"key":"ref_51","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 \u03c9-Hexatoxin-Hv1a","volume":"7","author":"Herzig","year":"2015","journal-title":"Toxins"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1124\/mol.115.098178","article-title":"Identification and Characterization of ProTx-III [mu-TRTX-Tp1a], a New Voltage-Gated Sodium Channel Inhibitor from Venom of the Tarantula Thrixopelma pruriens","volume":"88","author":"Cardoso","year":"2015","journal-title":"Mol. Pharmacol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2784","DOI":"10.1523\/JNEUROSCI.4116-12.2013","article-title":"Axons giving rise to the palisade endings of feline extraocular muscles display motor features","volume":"33","author":"Zimmermann","year":"2013","journal-title":"J. Neurosci."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2445","DOI":"10.1111\/bph.13081","article-title":"Seven novel modulators of the analgesic target NaV 1.7 uncovered using a high-throughput venom-based discovery approach","volume":"172","author":"Klint","year":"2015","journal-title":"Br. J. Pharmacol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.cbpa.2017.03.004","article-title":"Progress and challenges in the optimization of toxin peptides for development as pain therapeutics","volume":"38","author":"Netirojjanakul","year":"2017","journal-title":"Curr. Opin. Chem. Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.toxicon.2013.04.008","article-title":"Venom toxins in the exploration of molecular, physiological and pathophysiological functions of acid-sensing ion channels","volume":"75","author":"Baron","year":"2013","journal-title":"Toxicon"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1038\/nn1940","article-title":"A tarantula peptide against pain via ASIC1a channels and opioid mechanisms","volume":"10","author":"Mazzuca","year":"2007","journal-title":"Nat. Neurosci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1093\/brain\/awl325","article-title":"Prolonged activation of ASIC1a and the time window for neuroprotection in cerebral ischaemia","volume":"130","author":"Pignataro","year":"2007","journal-title":"Brain"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2037","DOI":"10.1016\/j.peptides.2011.08.026","article-title":"Evaluating antioxidative activities of amino acid substitutions on mastoparan-B","volume":"32","author":"Yang","year":"2011","journal-title":"Peptides"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.toxicon.2013.03.017","article-title":"New insights on arthropod toxins that potentiate erectile function","volume":"69","author":"Nunes","year":"2013","journal-title":"Toxicon"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.toxicon.2017.02.026","article-title":"Phoneutria nigriventer spider toxin Tx2-6 induces priapism in mice even after cavernosal denervation","volume":"130","author":"Ravelli","year":"2017","journal-title":"Toxicon"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1016\/j.juro.2015.06.081","article-title":"PnPP-19, a Synthetic and Nontoxic Peptide Designed from a Phoneutria nigriventer Toxin, Potentiates Erectile Function via NO\/cGMP","volume":"194","author":"Nunes","year":"2015","journal-title":"J. Urol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"191","DOI":"10.3390\/toxins4030191","article-title":"Spider-venom peptides as bioinsecticides","volume":"4","author":"Windley","year":"2012","journal-title":"Toxins"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1111\/imb.12268","article-title":"Insecticidal activity of a recombinant knottin peptide from Loxosceles intermedia venom and recognition of these peptides as conserved family in the genus","volume":"26","author":"Matsubara","year":"2017","journal-title":"Insect Mol. Biol."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Stock, R.P., Brewer, J., Wagner, K., Ramos-Cerrillo, B., Duelund, L., Jernshoj, K.D., Olsen, L.F., and Bagatolli, L.A. (2012). Sphingomyelinase D activity in model membranes: Structural effects of in situ generation of ceramide-1-phosphate. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0036003"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"10833","DOI":"10.1074\/jbc.C300563200","article-title":"Spider and bacterial sphingomyelinases D target cellular lysophosphatidic acid receptors by hydrolyzing lysophosphatidylcholine","volume":"279","author":"Frederiks","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1016\/j.toxicon.2007.07.001","article-title":"The Loxtox protein family in Loxosceles intermedia (Mello-Leitao) venom","volume":"50","author":"Kalapothakis","year":"2007","journal-title":"Toxicon"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.toxicon.2013.01.027","article-title":"Modulation of membrane phospholipids, the cytosolic calcium influx and cell proliferation following treatment of B16-F10 cells with recombinant phospholipase-D from Loxosceles intermedia (brown spider) venom","volume":"67","author":"Wille","year":"2013","journal-title":"Toxicon"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1002\/pmic.200401096","article-title":"Proteome analysis of brown spider venom: Identification of loxnecrogin isoforms in Loxosceles gaucho venom","volume":"5","author":"Machado","year":"2005","journal-title":"Proteomics"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"970","DOI":"10.1016\/j.bbalip.2016.05.009","article-title":"Active site mapping of Loxosceles phospholipases D: Biochemical and biological features","volume":"1861","author":"Vuitika","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1002\/jcb.25678","article-title":"Potential implications for drug design against phospholipase-D from Brown spider venom","volume":"118","author":"Moraes","year":"2017","journal-title":"J. Cell. Biochem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"6064","DOI":"10.1021\/cr200296t","article-title":"Phospholipase D: Enzymology, functionality, and chemical modulation","volume":"111","author":"Selvy","year":"2011","journal-title":"Chem. Rev."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"2412","DOI":"10.1096\/fj.09-130542","article-title":"Resveratrol attenuates C5ainduced inflammatory responses in vitro and in vivo by inhibiting phospholipase D and sphingosine kinase activities","volume":"23","author":"Issuree","year":"2009","journal-title":"FASEB J."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1632","DOI":"10.1016\/j.drudis.2014.06.007","article-title":"Harnessing the anti-inflammatory potential of palmitoylethanolamide","volume":"19","author":"Alhouayek","year":"2014","journal-title":"Drug Discov. Today"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/S0041-0101(99)00197-X","article-title":"Identification of high molecular weight serine-proteases in Loxosceles intermedia (brown spider) venom","volume":"38","author":"Veiga","year":"2000","journal-title":"Toxicon"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1023\/A:1004031019827","article-title":"Effect of brown spider venom on basement membrane structures","volume":"32","author":"Veiga","year":"2000","journal-title":"Histochem. J."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0041-0101(00)00145-8","article-title":"Comparison of enzymatic activity from three species of necrotising arachnids in Australia: Loxosceles rufescens, Badumna insignis and Lampona cylindrata","volume":"39","author":"Young","year":"2001","journal-title":"Toxicon"},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Fernandes-Pedrosa, F., Junqueira-de-Azevedo, L., Goncalves-de-Andrade, R.M., Kobashi, L.S., Almeida, D.D., Ho, P.L., and ambourgi, D.V. (2008). Transcriptome analysis of Loxosceles laeta (Araneae, Sicariidae) spider venomous gland using expressed sequence tags. BMC Genom., 9.","DOI":"10.1186\/1471-2164-9-279"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"309","DOI":"10.3390\/toxins3030309","article-title":"Brown spider (Loxosceles genus) venom toxins: Tools for biological purposes","volume":"3","author":"Chaim","year":"2011","journal-title":"Toxins"},{"key":"ref_80","first-page":"568","article-title":"Protease: An enzyme with multiple industrial applications","volume":"3","author":"Sawant","year":"2014","journal-title":"J. Pharm. Pharm. Sci."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"531","DOI":"10.18388\/abp.1999_4128","article-title":"Protein inhibitors of serine proteinases","volume":"46","author":"Otlewski","year":"1999","journal-title":"Acta Biochim. Pol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"2427","DOI":"10.1007\/s00018-003-3120-x","article-title":"Canonical protein inhibitors of serine proteases","volume":"60","author":"Krowarsch","year":"2003","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1111\/j.1538-7836.2011.04360.x","article-title":"Serpin structure, function and dysfunction","volume":"9","author":"Huntington","year":"2011","journal-title":"J Thromb. Haemost."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1007\/s12016-013-8353-3","article-title":"Serpins, immunity and autoimmunity: Old molecules, new functions","volume":"45","author":"Gatto","year":"2013","journal-title":"Clin. Rev. Allergy Immunol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"25","DOI":"10.3389\/fmed.2019.00025","article-title":"SERPINs-From Trap to Treatment","volume":"6","author":"Sanrattana","year":"2019","journal-title":"Front. Med."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1038\/nm0696-632","article-title":"Serine protease inhibitors (SERPINS): Where mechanism meets medicine","volume":"2","author":"Rubin","year":"1996","journal-title":"Nat. Med."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1016\/j.biocel.2007.12.017","article-title":"The molecular aetiology of the serpinopathies","volume":"40","author":"Davies","year":"2008","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_88","first-page":"132","article-title":"Psoriasis pathogenesis\u2013Pso p27 constitutes a compact structure forming large aggregates","volume":"2","author":"Lysvand","year":"2015","journal-title":"Biochem. Biophys. Rep."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1007\/978-1-4939-8645-3_17","article-title":"Serpins: Development for Therapeutic Applications","volume":"Volume 1826","author":"Lucas","year":"2018","journal-title":"Serpins Methods in Molecular Biology"},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Yuan, C.H., He, Q.Y., Peng, K., Diao, J.B., Jiang, L.P., Tang, X., and Liang, S.P. (2008). Discovery of a distinct superfamily of Kunitz-type toxin (KTT) from tarantulas. PLoS ONE, 3.","DOI":"10.1371\/annotation\/a7561dde-3b04-4fd9-9267-463b23cc7dd0"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.jprot.2016.01.013","article-title":"Venomous extract protein profile of Brazilian tarantula Grammostola iheringi: Searching for potential biotechnological applications","volume":"136","author":"Borges","year":"2016","journal-title":"J. Proteom."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/S0014-5793(03)00693-8","article-title":"Adaptive evolution in the snake venom Kunitz\/BPTI protein family","volume":"547","author":"Zupunski","year":"2003","journal-title":"FEBS Lett."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Mulenga, A., Khumthong, R., and Chalaire, K.C. (2009). Ixodes scapularis tick serine proteinase inhibitor (serpin) gene family; annotation and transcriptional analysis. BMC Genom., 10.","DOI":"10.1186\/1471-2164-10-217"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.semcdb.2016.09.001","article-title":"Serpins in arthropod biology","volume":"62","author":"Meekins","year":"2017","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1111\/imb.12024","article-title":"Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross-class inhibitor of serine proteases and papain-like cysteine proteases that delays plasma clotting and inhibits platelet aggregation","volume":"22","author":"Mulenga","year":"2013","journal-title":"Insect Mol. Biol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/j.ijpara.2015.03.009","article-title":"Conserved Amblyomma americanum tick Serpin19, an inhibitor of blood clotting factors Xa and XIa, trypsin and plasmin, has anti-haemostatic functions","volume":"45","author":"Kim","year":"2015","journal-title":"Int. J. Parasitol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1182\/blood-2010-06-293241","article-title":"A tick salivary protein targets cathepsin G and chymase and inhibits host inflammation and platelet aggregation","volume":"117","author":"Chmelar","year":"2011","journal-title":"Blood"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1097\/SHK.0b013e31825a3522","article-title":"Effects of C1 Inhibitor on Tissue Damage in a Porcine Model of Controlled Hemorrhage","volume":"38","author":"Li","year":"2012","journal-title":"Shock"},{"key":"ref_99","first-page":"418","article-title":"Recombinant alpha 1-antitrypsin Pittsburgh attenuates experimental gram-negative septicemia","volume":"130","author":"Colman","year":"1988","journal-title":"Am. J. Pathol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.4161\/cbt.4.9.2057","article-title":"Hypoxia effects: Implications for maspin regulation of the uPA\/uPAR complex","volume":"4","author":"Schaefer","year":"2005","journal-title":"Cancer Biol. Ther."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1002\/jcb.25969","article-title":"The Opportunity of Precision Medicine for Breast Cancer with Context-Sensitive Tumor Suppressor Maspin","volume":"118","author":"Bernardo","year":"2017","journal-title":"J. Cell. Biochem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1016\/j.cub.2018.04.022","article-title":"Serpin Facilitates Tumor-Suppressive Cell Competition by Blocking Toll-Mediated Yki Activation in Drosophila","volume":"28","author":"Katsukawa","year":"2018","journal-title":"Curr. Biol."},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Mika, A., Reynolds, S.L., Mohlin, F.C., Willis, C., Swe, P.M., Pickering, D.A., Halilovic, V., Wijeyewickrema, L.C., Pike, R.N., and Blom, A.M. (2012). Novel scabies mite serpins inhibit the three pathways of the human complement system. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0040489"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"439","DOI":"10.2174\/0929866054395329","article-title":"Plant serine proteinase inhibitors","volume":"12","author":"Christeller","year":"2005","journal-title":"Prot. Pept. Lett."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1016\/j.toxicon.2007.08.001","article-title":"Biological and structural comparison of recombinant phospholipase D toxins from Loxosceles intermedia (brown spider) venom","volume":"50","author":"Ribeiro","year":"2007","journal-title":"Toxicon"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"2261","DOI":"10.2174\/092986709788453078","article-title":"Hyaluronidase inhibitors: A biological and therapeutic perspective","volume":"16","author":"Girish","year":"2009","journal-title":"Curr. Med. Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.toxicon.2012.09.009","article-title":"A brief review of the scientific history of several lesser-known snake venom proteins: L-amino acid oxidases, hyaluronidases and phosphodiesterases","volume":"62","author":"Fox","year":"2013","journal-title":"Toxicon"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1016\/j.lfs.2007.02.037","article-title":"The magic glue hyaluronan and its eraser hyaluronidase: A biological overview","volume":"80","author":"Girish","year":"2007","journal-title":"Life Sci"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"51","DOI":"10.2147\/JAA.S28868","article-title":"Potential role of histamine releasing factor (HRF) as a therapeutic target for treating asthma and allergy","volume":"5","author":"Macdonald","year":"2012","journal-title":"J. Asthma Allergy"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1007\/s10493-005-3261-8","article-title":"The molecular and biological analysis of ixodid ticks histamine release factors","volume":"37","author":"Mulenga","year":"2005","journal-title":"Exp. Appl. Acarol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.toxicon.2015.09.041","article-title":"Brown spider (Loxosceles genus) venom toxins: Evaluation of biological conservation by immune cross-reactivity","volume":"108","author":"Buch","year":"2015","journal-title":"Toxicon"},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Kimura, T., Ono, S., and Kubo, T. (2012). Molecular Cloning and Sequence Analysis of the cDNAs Encoding Toxin-Like Peptides from the Venom Glands of Tarantula Grammostola rosea. Int. J. Pept., 731293.","DOI":"10.1155\/2012\/731293"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1021\/pr400875s","article-title":"Spit and venom from scytodes spiders: A diverse and distinct cocktail","volume":"13","author":"Correa","year":"2014","journal-title":"J. Proteome Res."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.msec.2015.04.036","article-title":"Translationally controlled tumor protein supplemented chitosan modified glass ionomer cement promotes osteoblast proliferation and function","volume":"54","author":"Sangsuwan","year":"2015","journal-title":"Mater. Sci. Eng. C Mater. Biol. Appl."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1111\/pim.12158","article-title":"Immunization of mice with Plasmodium TCTP delays establishment of Plasmodium infection","volume":"37","author":"Taylor","year":"2015","journal-title":"Parasite Immunol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"21","DOI":"10.3347\/kjp.2014.52.1.21","article-title":"Expression of translationally controlled tumor protein (TCTP) gene of Dirofilaria immitis guided by transcriptomic screening","volume":"52","author":"Fu","year":"2014","journal-title":"Korean J. Parasitol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"19","DOI":"10.2174\/1874838401205010019","article-title":"Cellular Function and Regulation of the Translationally Controlled Tumour Protein TCTP","volume":"5","author":"Bommer","year":"2012","journal-title":"Open Allergy J."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1172\/JCI59072","article-title":"Histamine-releasing factor has a proinflammatory role in mouse models of asthma and allergy","volume":"122","author":"Kashiwakura","year":"2011","journal-title":"J. Clin. Investig."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.jconrel.2013.06.010","article-title":"On employing a translationally controlled tumor protein-derived protein transduction domain analog for transmucosal delivery of drugs","volume":"170","author":"Bae","year":"2013","journal-title":"J. Control. Release"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.ab.2012.11.029","article-title":"Transduction of translationally controlled tumor protein employing TCTP-derived protein transduction domain","volume":"435","author":"Maeng","year":"2012","journal-title":"Anal. Biochem."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1479","DOI":"10.1007\/s10856-011-4328-1","article-title":"Translationally controlled tumor protein against apoptosis from 2-hydroxy-ethyl methacrylate in human dental pulp cells","volume":"22","author":"Wanachottrakul","year":"2011","journal-title":"J. Mater. Sci. Mater. Med."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.tcb.2012.10.002","article-title":"TPT1\/TCTP-regulated pathways in phenotypic reprogramming","volume":"23","author":"Amson","year":"2012","journal-title":"Trends Cell Biol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1016\/j.toxicon.2009.01.033","article-title":"Analysis of therapeutic benefits of antivenin at different time intervals after experimental envenomation in rabbits by venom of the brown spider (Loxosceles intermedia)","volume":"53","author":"Pauli","year":"2009","journal-title":"Toxicon"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/j.toxicon.2006.06.019","article-title":"Functional characterization and epitope analysis of a recombinant dermonecrotic protein from Loxosceles intermedia spider","volume":"48","author":"Felicori","year":"2006","journal-title":"Toxicon"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.toxicon.2014.10.023","article-title":"Anti-loxoscelic horse serum produced against a recombinant dermonecrotic protein of Brazilian Loxosceles intermedia spider neutralize lethal effects of Loxosceles laeta venom from Peru","volume":"93","author":"Duarte","year":"2014","journal-title":"Toxicon"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"463","DOI":"10.4269\/ajtmh.2008.79.463","article-title":"A new anti-loxoscelic serum produced against recombinant sphingomyelinase D: Results of preclinical trials","volume":"79","author":"Marcelino","year":"2008","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.toxicon.2006.04.010","article-title":"North and South American Loxosceles spiders: Development of a polyvalent antivenom with recombinant sphingomyelinases D as antigens","volume":"48","author":"Olvera","year":"2006","journal-title":"Toxicon"},{"key":"ref_128","first-page":"481","article-title":"A protective immune response against lethal, dermonecrotic and hemorrhagic effects of Loxosceles intermedia venom elicited by a 27-residue peptide","volume":"55","author":"Felicori","year":"2009","journal-title":"Toxicon"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1016\/j.toxicon.2003.09.006","article-title":"Production of monoclonal antibodies capable of neutralizing dermonecrotic activity of Loxosceles intermedia spider venom and their use in a specific immunometric assay","volume":"42","author":"Alvarenga","year":"2003","journal-title":"Toxicon"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"7992","DOI":"10.1016\/j.vaccine.2011.08.065","article-title":"Protection against the toxic effects of Loxosceles intermedia spider venom elicited by mimotope peptides","volume":"29","author":"Felicori","year":"2011","journal-title":"Vaccine"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"2749","DOI":"10.1016\/j.vaccine.2013.03.048","article-title":"Generation and characterization of a recombinant chimeric protein (rCpLi) consisting of B-cell epitopes of a dermonecrotic protein from Loxosceles intermedia spider venom","volume":"31","author":"Mendes","year":"2013","journal-title":"Vaccine"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.toxicon.2014.05.007","article-title":"Innovative immunization protocols using chimeric recombinant protein for the production of polyspecific loxoscelic antivenom in horses","volume":"86","author":"Figueiredo","year":"2014","journal-title":"Toxicon"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"653","DOI":"10.3389\/fimmu.2018.00653","article-title":"Recombinant protein containing B-cell epitopes of different Loxosceles spider toxins generates neutralizing antibodies in immunized rabbits","volume":"9","author":"Mendes","year":"2018","journal-title":"Front. Immunol."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/11\/6\/355\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T12:59:33Z","timestamp":1760187573000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/11\/6\/355"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,6,19]]},"references-count":133,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2019,6]]}},"alternative-id":["toxins11060355"],"URL":"https:\/\/doi.org\/10.3390\/toxins11060355","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,6,19]]}}}