{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T02:06:08Z","timestamp":1793066768406,"version":"4.5.0"},"reference-count":77,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,5,1]],"date-time":"2023-05-01T00:00:00Z","timestamp":1682899200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2023,5]]},"DOI":"10.1016\/j.ijbiomac.2023.124357","type":"journal-article","created":{"date-parts":[[2023,4,5]],"date-time":"2023-04-05T13:27:18Z","timestamp":1680701238000},"page":"124357","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":25,"special_numbering":"C","title":["Therapeutic applications of snake venoms: An invaluable potential of new drug candidates"],"prefix":"10.1016","volume":"238","author":[{"given":"Rafaela","family":"Diniz-Sousa","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cle\u00f3patra A. da S.","family":"Caldeira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Soraya S.","family":"Pereira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saulo L.","family":"Da Silva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pedro A.","family":"Fernandes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lu\u00eds M.C.","family":"Teixeira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juliana P.","family":"Zuliani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreimar M.","family":"Soares","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2023.124357_bb0005","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.jprot.2009.01.018","article-title":"Venomics: digging into the evolution of venomous systems and learning to twist nature to fight pathology","volume":"72","author":"Calvete","year":"2009","journal-title":"J. Proteome"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0010","first-page":"149","article-title":"Isolation and molecular characterization of microorganisms producing novel antibiotics from soil sample","volume":"4","author":"Abbas","year":"2014","journal-title":"Eur. J. Exp. Biol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0015","article-title":"Anticancer and antitumor potential of fucoidan and fucoxanthin, two main metabolites isolated from brown algae","volume":"2014","author":"Moghadamtousi","year":"2014","journal-title":"Sci. World J."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0020","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/s12906-016-1007-2","article-title":"In vitro antibacterial activity of selected medicinal plants traditionally used in Vietnam against human pathogenic bacteria","volume":"16","author":"Vu","year":"2016","journal-title":"BMC Complement. Altern. Med."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0025","first-page":"118","article-title":"Identification of compounds from white frog (Anura: Hylidae) cutaneous secretions with potential to be used in biotechnological processes","volume":"2","author":"Lamadrid-Feris","year":"2015","journal-title":"Pharmacologyonline."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0030","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.toxicon.2015.05.006","article-title":"Synthesis, antimicrobial activity and toxicity of analogs of the scorpion venom BmKn peptides","volume":"101","author":"Bea","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0035","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1590\/S1678-91992008000400007","article-title":"Antibacterial activity of venom from funnel web spider Agelena labyrinthica (Araneae: Agelenidae)","volume":"14","author":"Benli","year":"2008","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0040","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/1678-9199-20-22","article-title":"In vitro antibacterial effect of wasp (Vespa orientalis) venom","volume":"20","author":"Jalaei","year":"2014","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0045","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1590\/0001-3765201520130511","article-title":"Antimicrobial activity of apitoxin, melittin and phospholipase A2 of honey bee (Apis mellifera) venom against oral pathogens","volume":"87","author":"Leandro","year":"2015","journal-title":"An. Acad. Bras. Cienc."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0050","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0003252","article-title":"Crovirin, a Snake venom cysteine-rich secretory protein (CRISP) with promising activity against trypanosomes and leishmania","volume":"8","author":"Adade","year":"2014","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0055","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.toxicon.2014.12.009","article-title":"Effects of vipoxin and its components on HepG2 cells","volume":"94","author":"Doumanov","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0060","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.toxicon.2011.01.006","article-title":"Haemostatically active proteins in snake venoms","volume":"57","author":"Sajevic","year":"2011","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0065","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1590\/1678-9199-jvatitd-14-63-18","article-title":"Spider venom peptides as potential drug candidates due to their anticancer and antinociceptive activities","volume":"25","author":"Wu","year":"2019","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0070","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":"De Castro","year":"2004","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0075","doi-asserted-by":"crossref","first-page":"1518","DOI":"10.1016\/j.peptides.2011.05.015","article-title":"Virucidal activity of a scorpion venom peptide variant mucroporin-M1 against measles, SARS-CoV and influenza H5N1 viruses","volume":"32","author":"Li","year":"2011","journal-title":"Peptides"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0080","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1074\/jbc.RA118.005015","article-title":"A scorpion venom peptide Ev37 restricts viral late entry by alkalizing acidic organelles","volume":"294","author":"Li","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0085","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40409-016-0089-0","article-title":"Antiviral activity of animal venom peptides and related compounds","volume":"23","author":"da Mata","year":"2017","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0090","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1517\/17425247.4.2.175","article-title":"Targeted delivery of antitumoral therapy to glioma and other malignancies with synthetic chlorotoxin (TM-601)","volume":"4","author":"Mamelak","year":"2007","journal-title":"Expert Opin. Drug Deliv."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0095","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/molecules24162997","article-title":"Bee venom: overview of main compounds and bioactivities for therapeutic interests","volume":"24","author":"Wehbe","year":"2019","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0100","doi-asserted-by":"crossref","DOI":"10.3390\/molecules26082223","article-title":"Snake venom components: tools and cures to target cardiovascular diseases","volume":"26","author":"Frangieh","year":"2021","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0105","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.toxicon.2010.07.010","article-title":"Structure, function and evolution of three-finger toxins: mini proteins with multiple targets","volume":"56","author":"Kini","year":"2010","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0110","doi-asserted-by":"crossref","first-page":"2402","DOI":"10.3390\/molecules25102402","article-title":"Antimicrobials from venomous animals: an overview","volume":"25","author":"Yacoub","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0115","doi-asserted-by":"crossref","DOI":"10.3390\/toxins10110474","article-title":"Snake venom peptides: tools of biodiscovery","volume":"10","author":"Munawar","year":"2018","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0120","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.toxicon.2018.08.009","article-title":"Detection and identification of antibacterial proteins in snake venoms using at-line nanofractionation coupled to LC-MS","volume":"155","author":"Mladic","year":"2018","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0125","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0226807","article-title":"Predicting antibacterial activity from snake venom proteomes","volume":"15","author":"Rheubert","year":"2020","journal-title":"PLoS One."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0130","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1042\/BST20200110","article-title":"Cytotoxicity of snake venom enzymatic toxins: phospholipase A2 and L-amino acid oxidase","volume":"48","author":"Hiu","year":"2020","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0135","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0080199","article-title":"Wound healing activity and mechanisms of action of an antibacterial protein from the venom of the eastern diamondback rattlesnake (Crotalus adamanteus)","volume":"9","author":"Samy","year":"2014","journal-title":"PLoS One."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0140","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/j.ejmech.2018.02.055","article-title":"A novel synthetic peptide inspired on Lys49 phospholipase A2 from Crotalus oreganus abyssus snake venom active against multidrug-resistant clinical isolates","volume":"149","author":"Almeida","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0145","doi-asserted-by":"crossref","first-page":"1536","DOI":"10.1074\/jbc.RA117.000125","article-title":"Mechanisms of bacterial membrane permeabilization by crotalicidin (Ctn) and its fragment Ctn(15\u201334), antimicrobial peptides from rattlesnake venom","volume":"293","author":"P\u00e9rez-Peinado","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0150","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/S0076-6879(84)05005-9","article-title":"Biochemistry of oxygen radical species","volume":"105","author":"Brunori","year":"1984","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0155","doi-asserted-by":"crossref","first-page":"1220","DOI":"10.1126\/science.1355616","article-title":"Protein oxidation and aging","volume":"257","author":"Stadtman","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0160","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/j.ijbiomac.2015.07.004","article-title":"Evaluating the microbicidal, antiparasitic and antitumor effects of CR-LAAO from Calloselasma rhodostoma venom","volume":"80","author":"Costa","year":"2015","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0165","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.toxicon.2012.05.001","article-title":"Past decade study of snake venom l-amino acid oxidase","volume":"60","author":"Guo","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0170","doi-asserted-by":"crossref","first-page":"215","DOI":"10.2174\/1871520621666210608095512","article-title":"Reactive oxygen species (ROS): key components in cancer therapies","volume":"22","author":"Sahoo","year":"2022","journal-title":"Anti Cancer Agents Med. Chem."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0175","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.3390\/molecules23061388","article-title":"Cytotoxic, anti-proliferative and apoptosis activity of L-amino acid oxidase from Malaysian cryptelytrops purpureomaculatus (CP-LAAO) venom on human colon cancer cells","volume":"23","author":"Abidin","year":"2018","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0180","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.toxicon.2018.06.064","article-title":"L-amino acid oxidase from Cerastes vipera snake venom: isolation, characterization and biological effects on bacteria and tumor cell lines","volume":"150","author":"Salama","year":"2018","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0185","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.ijbiomac.2016.01.069","article-title":"CR-LAAO antileukemic effect against Bcr-Abl+ cells is mediated by apoptosis and hydrogen peroxide","volume":"86","author":"Burin","year":"2016","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0190","doi-asserted-by":"crossref","DOI":"10.1038\/srep18215","article-title":"Akbu-LAAO exhibits potent anti-tumor activity to HepG2 cells partially through produced H2O2 via TGF-\u03b2 signal pathway","volume":"5","author":"Guo","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0195","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.toxicon.2019.06.220","article-title":"Cytotoxicity of Nubein6.8 peptide isolated from the snake venom of Naja nubiae on melanoma and ovarian carcinoma cell lines","volume":"168","author":"Abdel-Ghani","year":"2019","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0200","doi-asserted-by":"crossref","first-page":"258","DOI":"10.3390\/biom12020258","article-title":"A new approach to inhibiting triple-negative breast cancer: in vitro, ex vivo and in vivo antiangiogenic effect of BthTX-II, a PLA2-Asp-49 from Bothrops jararacussu venom","volume":"12","author":"de Vasconcelos Azevedo","year":"2022","journal-title":"Biomolecules"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0205","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/203639","article-title":"Antitumoral activity of snake venom proteins: new trends in cancer therapy","volume":"2014","author":"Calderon","year":"2014","journal-title":"Biomed. Res. Int."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0210","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2023.123367","article-title":"Snake venom, a potential treatment for melanoma. A systematic review","volume":"231","author":"Bialves","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0215","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1007\/s00436-002-0626-3","article-title":"Ultrastructural alterations and growth inhibition of trypanosoma cruzi and leishmania major induced by Bothrops jararaca venom","volume":"88","author":"Gon\u00e7alves","year":"2002","journal-title":"Parasitol. Res."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0220","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.toxicon.2015.09.005","article-title":"BbMP-1, a new metalloproteinase isolated from Bothrops brazili snake venom with in vitro antiplasmodial properties","volume":"106","author":"Kayano","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0225","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1016\/j.toxicon.2012.08.008","article-title":"Isolation and biochemical, functional and structural characterization of a novel l-amino acid oxidase from Lachesis muta snake venom","volume":"60","author":"Bregge-Silva","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0230","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/jbt.22018","article-title":"Isolation and characterization of an anti-leishmanial disintegrin from Cerastes cerastes venom","volume":"32","author":"Allane","year":"2018","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0235","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/j.ijbiomac.2018.08.064","article-title":"In vitro effect of Bothrops leucurus lectin (BLL) against leishmania amazonensis and leishmania braziliensis infection","volume":"120","author":"Aranda-Souza","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0240","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbpc.2019.108612","article-title":"Potential use of 13-mer peptides based on phospholipase and oligoarginine as leishmanicidal agents","volume":"226","author":"Mendes","year":"2019","journal-title":"Comp. Biochem. Physiol. Part - C Toxicol. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0245","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/195356","article-title":"Purification and biochemical characterization of three myotoxins from Bothrops mattogrossensis Snake venom with toxicity against leishmania and tumor cells","volume":"2014","author":"de Moura","year":"2014","journal-title":"Biomed. Res. Int."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0250","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/j.ijbiomac.2017.04.013","article-title":"BmajPLA 2 -II, a basic Lys49-phospholipase A2 homologue from Bothrops marajoensis snake venom with parasiticidal potential","volume":"102","author":"Grabner","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0255","doi-asserted-by":"crossref","DOI":"10.3390\/toxins11070379","article-title":"In vitro and in vivo antimalarial activity of LZ1, a peptide derived from snake cathelicidin","volume":"11","author":"Fang","year":"2019","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0260","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.biochi.2019.04.009","article-title":"Identification of a peptide derived from a Bothrops moojeni metalloprotease with in vitro inhibitory action on the Plasmodium falciparum purine nucleoside phosphorylase enzyme (PfPNP)","volume":"162","author":"Martins","year":"2019","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0265","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.peptides.2016.01.013","article-title":"Inhibition of malaria parasite plasmodium falciparum development by crotamine, a cell penetrating peptide from the snake venom","volume":"78","author":"El Chamy Maluf","year":"2016","journal-title":"Peptides"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0270","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":"10.1016\/j.ijbiomac.2023.124357_bb0275","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1016\/j.toxicon.2005.02.016","article-title":"Practical applications of snake venom toxins in haemostasis","volume":"45","author":"Marsh","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0280","doi-asserted-by":"crossref","first-page":"332","DOI":"10.3390\/toxins10080332","article-title":"Purification and characterization of a novel antiplatelet peptide from Deinagkistrodon acutus venom","volume":"10","author":"Kong","year":"2018","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0285","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.biochi.2014.07.006","article-title":"A new peptide (Ruviprase) purified from the venom of Daboia russelii russelii shows potent anticoagulant activity via non-enzymatic inhibition of thrombin and factor xa","volume":"105","author":"Thakur","year":"2014","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0290","doi-asserted-by":"crossref","DOI":"10.3390\/molecules24193489","article-title":"Atroxlysin-III, a metalloproteinase from the venom of the peruvian pit viper Snake Bothrops atrox (Jerg\u00f3n) induces glycoprotein VI shedding and impairs platelet function","volume":"24","author":"Oliveira","year":"2019","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0295","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.ijbiomac.2016.11.063","article-title":"Antithrombotic activity of batroxase, a metalloprotease from Bothrops atrox venom, in a model of venous thrombosis","volume":"95","author":"Jacob-Ferreira","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0300","doi-asserted-by":"crossref","first-page":"1132","DOI":"10.3389\/fphar.2020.01132","article-title":"From animal poisons and venoms to medicines: achievements, challenges and perspectives in drug discovery","volume":"11","author":"Bordon","year":"2020","journal-title":"Front. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0305","article-title":"\u00dcber die phosphomonoesterase und die phosphodiesterase","volume":"19\u201328","author":"Uzawa","year":"1932","journal-title":"J. Biochem."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0310","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1590\/0001-3765201920190105","article-title":"The role of natural products in modern drug discovery","volume":"91","author":"Calixto","year":"2019","journal-title":"An. Acad. Bras. Cienc."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0315","first-page":"554","article-title":"Using bradykinin-potentiating peptide structures to develop new antihypertensive drugs","author":"Fernandez","year":"2004","journal-title":"Genet. Mol. Res."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0320","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1152\/ajplegacy.1949.156.2.261","article-title":"Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin","volume":"156","author":"Rocha e Silva","year":"1949","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0325","doi-asserted-by":"crossref","first-page":"28","DOI":"10.4331\/wjbc.v6.i2.28","article-title":"Animal venom studies: current benefits and future developments","volume":"6","author":"Utkin","year":"2015","journal-title":"WorldJ. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0330","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.jmgm.2018.06.004","article-title":"L-captopril and its derivatives as potential inhibitors of microbial enzyme DapE: a combined approach of drug repurposing and similarity screening","volume":"84","author":"Dutta","year":"2018","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0335","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fevo.2019.00218","article-title":"Multifunctional toxins in snake venoms and therapeutic implications: from pain to hemorrhage and necrosis","volume":"7","author":"Ferraz","year":"2019","journal-title":"Front. Ecol. Evol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0340","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1016\/j.neuron.2020.03.012","article-title":"Structure of the native muscle-type nicotinic receptor and inhibition by snake venom toxins","volume":"106","author":"Rahman","year":"2020","journal-title":"Neuron"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0345","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-020-60768-y","article-title":"Complex approach for analysis of snake venom \u03b1-neurotoxins binding to HAP, the high-affinity peptide","volume":"10","author":"Kudryavtsev","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0350","doi-asserted-by":"crossref","first-page":"4495","DOI":"10.1039\/C6AN00327C","article-title":"A single-label fluorescent derivatization method for quantitative determination of neurotoxin: in vivo by capillary electrophoresis coupled with laser-induced fluorescence detection","volume":"141","author":"Chen","year":"2016","journal-title":"Analyst"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0355","first-page":"192","article-title":"Chemical structures and mode of action of intravenous glycoprotein IIb\/IIIa receptor blockers: a review","volume":"13","author":"Hashemzadeh","year":"2008","journal-title":"Exp. Clin. Cardiol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0360","doi-asserted-by":"crossref","DOI":"10.1088\/1748-6041\/9\/2\/025002","article-title":"The effective control of a bleeding injury using a medical adhesive containing batroxobin","volume":"9","author":"You","year":"2014","journal-title":"Biomed. Mater."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0365","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1159\/000092430","article-title":"The use of Snake venom-derived compounds for new functional diagnostic test kits in the field of haemostasis","volume":"34","author":"Sch\u00f6ni","year":"2005","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0370","series-title":"Venom Genomics and Proteomics","first-page":"393","article-title":"Applications of snake toxins in biomedicine","author":"Markland","year":"2016"},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0375","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fphar.2018.00145","article-title":"Animal toxins as therapeutic tools to treat neurodegenerative diseases","volume":"9","author":"de Souza","year":"2018","journal-title":"Front. Pharmacol."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0380","doi-asserted-by":"crossref","first-page":"30559","DOI":"10.1074\/jbc.M113.511410","article-title":"Factor v activator from Daboia russelli russelli venom destabilizes \u03b2\u03b2-amyloid aggregate, the hallmark of alzheimer disease","volume":"288","author":"Bhattacharjee","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2023.124357_bb0385","series-title":"Chapter in Handbook of Venoms and Toxins of Reptiles","article-title":"Toxins to drugs \u2013 biochemistry and pharmacology","author":"Takacs","year":"2021"}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813023012515?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813023012515?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T10:14:46Z","timestamp":1758881686000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813023012515"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,5]]},"references-count":77,"alternative-id":["S0141813023012515"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2023.124357","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2023,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Therapeutic applications of snake venoms: An invaluable potential of new drug candidates","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2023.124357","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"124357"}}