{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T17:20:09Z","timestamp":1787678409280,"version":"build-2784847793"},"reference-count":67,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100013908","name":"Universidad Andres Bello","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100013908","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100020884","name":"ANID","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100020884","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1016\/j.bioorg.2026.110138","type":"journal-article","created":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T16:30:03Z","timestamp":1781800203000},"page":"110138","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Targeting Bothrops asper venom enzymes: Steroidal derivatives as potential inhibitors of phospholipase A2 and serine proteinases"],"prefix":"10.1016","volume":"180","author":[{"given":"Mitchell","family":"Bacho","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yeray A.","family":"Rodr\u00edguez-N\u00fa\u00f1ez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cristi\u00e1n J.","family":"Guerra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Efra\u00edn","family":"Polo-Cuadrado","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge","family":"Soto-Delgado","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c1ngela Sofia Tejada","family":"Restrepo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juli\u00e1n Rodrigo M\u00e9ndez","family":"Anacona","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabel","family":"Henao-Casta\u00f1eda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lina Mar\u00eda Preciado","family":"Rojo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bioorg.2026.110138_bb0005","author":"World Health Organization"},{"key":"10.1016\/j.bioorg.2026.110138_bb0010","doi-asserted-by":"crossref","first-page":"17063","DOI":"10.1038\/nrdp.2017.63","article-title":"Snakebite envenoming","volume":"3","author":"Guti\u00e9rrez","year":"2017","journal-title":"Nat. Rev. Dis. Primers."},{"key":"10.1016\/j.bioorg.2026.110138_bb0015","author":"Instituto Nacional de Salud - Direcci\u00f3n de Vigilancia y An\u00e1lisis del Riesgo en Salud P\u00fablica"},{"key":"10.1016\/j.bioorg.2026.110138_bb0020","series-title":"Accidente Of\u00eddico","author":"Instituto Nacional de Salud","year":"2025"},{"key":"10.1016\/j.bioorg.2026.110138_bb0025","doi-asserted-by":"crossref","DOI":"10.1016\/j.toxicon.2022.106983","article-title":"Half a century of research on Bothrops asper venom variation: biological and biomedical implications","volume":"221","author":"Mora-Obando","year":"2023","journal-title":"Toxicon"},{"key":"10.1016\/j.bioorg.2026.110138_bb0030","series-title":"Snake Bites in Colombia","first-page":"3","author":"Otero-Pati\u00f1o","year":"2018"},{"key":"10.1016\/j.bioorg.2026.110138_bb0035","doi-asserted-by":"crossref","first-page":"290","DOI":"10.3390\/toxins9090290","article-title":"A review and database of Snake venom proteomes","volume":"9","author":"Tasoulis","year":"2017","journal-title":"Toxins (Basel)."},{"key":"10.1016\/j.bioorg.2026.110138_bb0040","doi-asserted-by":"crossref","first-page":"658","DOI":"10.3390\/toxins15110658","article-title":"Knowledge about Snake venoms and toxins from Colombia: A systematic review","volume":"15","author":"Perea\u00f1ez","year":"2023","journal-title":"Toxins (Basel)."},{"key":"10.1016\/j.bioorg.2026.110138_bb0045","author":"World Health Organization"},{"key":"10.1016\/j.bioorg.2026.110138_bb0050","doi-asserted-by":"crossref","first-page":"369","DOI":"10.2174\/187152811797200669","article-title":"Antivenoms for Snakebite Envenomings","volume":"10","author":"Maria Gutierrez","year":"2011","journal-title":"Inflamm. Allergy Drug Targets"},{"key":"10.1016\/j.bioorg.2026.110138_bb0055","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1002\/jms.1242","article-title":"Snake venomics. Strategy and applications","volume":"42","author":"Calvete","year":"2007","journal-title":"J. Mass Spectrom."},{"key":"10.1016\/j.bioorg.2026.110138_bb0060","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.aay8314","article-title":"Preclinical validation of a repurposed metal chelator as an early-intervention therapeutic for hemotoxic snakebite","volume":"12","author":"Albulescu","year":"2020","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.bioorg.2026.110138_bb0065","doi-asserted-by":"crossref","first-page":"391","DOI":"10.3390\/toxins14060391","article-title":"Early light chains removal and albumin levels with a double filter-based extracorporeal treatment for acute myeloma kidney","volume":"14","author":"Donati","year":"2022","journal-title":"Toxins (Basel)."},{"key":"10.1016\/j.bioorg.2026.110138_bb0070","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1016\/j.toxicon.2009.03.015","article-title":"Neutralization of Bothrops asper venom by antibodies, natural products and synthetic drugs: contributions to understanding snakebite envenomings and their treatment","volume":"54","author":"Lomonte","year":"2009","journal-title":"Toxicon"},{"key":"10.1016\/j.bioorg.2026.110138_bb0075","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1038\/s41570-022-00393-7","article-title":"The chemistry of snake venom and its medicinal potential","volume":"6","author":"Oliveira","year":"2022","journal-title":"Nat. Rev. Chem."},{"key":"10.1016\/j.bioorg.2026.110138_bb0080","doi-asserted-by":"crossref","first-page":"5364","DOI":"10.1021\/acs.jmedchem.3c00097","article-title":"Catalytically active Snake venom PLA 2 enzymes: an overview of its elusive mechanisms of reaction","volume":"66","author":"Castro-Amorim","year":"2023","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2026.110138_bb0085","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1016\/j.phymed.2006.12.006","article-title":"Ergosterol peroxides as phospholipase A2 inhibitors from the fungus Lactarius hatsudake","volume":"14","author":"Gao","year":"2007","journal-title":"Phytomedicine"},{"key":"10.1016\/j.bioorg.2026.110138_bb0090","doi-asserted-by":"crossref","first-page":"3867","DOI":"10.1021\/bi982693q","article-title":"Evidence for a regulatory role of cholesterol Superlattices in the hydrolytic activity of secretory phospholipase A2 in lipid membranes","volume":"38","author":"Liu","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bioorg.2026.110138_bb0095","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1016\/S0022-2275(20)32002-2","article-title":"Sphingolipids and cholesterol modulate membrane susceptibility to cytosolic phospholipase A2","volume":"41","author":"Klapisz","year":"2000","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bioorg.2026.110138_bb0100","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1111\/jth.12252","article-title":"Thrombin inhibition by the serpins","volume":"11","author":"Huntington","year":"2013","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.bioorg.2026.110138_bb0105","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.toxicon.2017.04.001","article-title":"Peptidomimetic hydroxamate metalloproteinase inhibitors abrogate local and systemic toxicity induced by Echis ocellatus (saw-scaled) snake venom","volume":"132","author":"Arias","year":"2017","journal-title":"Toxicon"},{"key":"10.1016\/j.bioorg.2026.110138_bb0110","first-page":"18","article-title":"Beyond traditional antivenoms: exploring human proteins and plant-based ligands for viper venom neutralisation through molecular interaction studies","volume":"38","author":"Hussain","year":"2026","journal-title":"Toxicol. Anal. Clin."},{"key":"10.1016\/j.bioorg.2026.110138_bb0115","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.959688","article-title":"Every gene everywhere all at once: high-precision measurement of 3D chromosome architecture with single-cell hi-C","volume":"9","author":"Chi","year":"2022","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.bioorg.2026.110138_bb0120","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1007\/BF03246076","article-title":"Metal-free catalytic oxidation of urazoles under mild and heterogeneous conditions via combination of ammonium nitrate and catalytic amounts of silica sulfuric acid","volume":"7","author":"Ghorbani-Choghamarani","year":"2010","journal-title":"J. Iran. Chem. Soc."},{"key":"10.1016\/j.bioorg.2026.110138_bb0125","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1039\/J39670001905","article-title":"Diels\u2013Alder reactions of 4-phenyl-1,2,4-triazoline-3,5-dione","volume":"0","author":"Cookson","year":"1967","journal-title":"J. Chem. Soc. C"},{"key":"10.1016\/j.bioorg.2026.110138_bb0130","doi-asserted-by":"crossref","first-page":"1627","DOI":"10.1016\/S0040-4020(00)01150-9","article-title":"An efficient method for the oxidation of urazoles with [NO+\u00b7crown\u00b7H(NO3)2\u2212]","volume":"57","author":"Zolfigol","year":"2001","journal-title":"Tetrahedron"},{"key":"10.1016\/j.bioorg.2026.110138_bb0135","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1002\/jlcr.4067","article-title":"Synthesis of trifold-labeled versatile reagent [3,5\u201313 C 2,4\u201315 N]4-phenyl-1,2,4-triazoline-3,5-dione","volume":"66","author":"Bourgeois","year":"2023","journal-title":"J. Labelled Comp. Radiopharm."},{"key":"10.1016\/j.bioorg.2026.110138_bb0140","doi-asserted-by":"crossref","first-page":"4879","DOI":"10.1039\/D2AY01705A","article-title":"Simultaneous determination of deuterium-labeled ergosterol and brassicasterol in stroke-prone spontaneously hypertensive rats by ultra-high performance liquid chromatography-electrospray ionization-tandem mass spectrometry","volume":"14","author":"Machida","year":"2022","journal-title":"Anal. Methods"},{"key":"10.1016\/j.bioorg.2026.110138_bb0145","doi-asserted-by":"crossref","first-page":"11855","DOI":"10.1021\/ja9033473","article-title":"Direct interaction between amphotericin B and ergosterol in lipid bilayers as revealed by 2H NMR spectroscopy","volume":"131","author":"Matsumori","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bioorg.2026.110138_bb0150","series-title":"SYNTHESIS AND BIOLOGICAL ACTIVITY OF 3\/l-FLUOROVITAMIN D,: COMPARISON OF THE BIOLOGICAL ACTIVITY OF 3\/3-FLUOROVITAMIN D, AND 3-DEOXYVITAMIN D","author":"Revelle","year":"1985"},{"key":"10.1016\/j.bioorg.2026.110138_bb0155","doi-asserted-by":"crossref","DOI":"10.1016\/j.jprot.2020.103945","article-title":"Venom variation in Bothrops asper lineages from North-Western South America","volume":"229","author":"Mora-Obando","year":"2020","journal-title":"J. Proteomics"},{"key":"10.1016\/j.bioorg.2026.110138_bb0160","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1186\/s40409-017-0117-8","article-title":"Strategies in \u2018snake venomics\u2019 aiming at an integrative view of compositional, functional, and immunological characteristics of venoms","volume":"23","author":"Lomonte","year":"2017","journal-title":"J. Venomous Animals Toxins Including Tropical Dis."},{"key":"10.1016\/j.bioorg.2026.110138_bb0165","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.toxicon.2012.09.003","article-title":"The long road of research on snake venom serine proteinases","volume":"62","author":"Serrano","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.bioorg.2026.110138_bb0170","doi-asserted-by":"crossref","DOI":"10.3390\/toxins17120583","article-title":"Snake venom PLA2 as anticoagulant agents: role of crotoxin, from Crotalus durissus rattlesnake, in hemostasis","volume":"17","author":"Brasileiro-Martins","year":"2025","journal-title":"Toxins (Basel)."},{"key":"10.1016\/j.bioorg.2026.110138_bb0175","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1038\/ja.2012.42","article-title":"Inhibition of human neutrophil elastase by ergosterol derivatives from the mycelium of Phellinus linteus","volume":"65","author":"Lee","year":"2012","journal-title":"J. Antibiot. (Tokyo)"},{"key":"10.1016\/j.bioorg.2026.110138_bb0180","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1042\/BJ20060302","article-title":"Anticoagulant proteins from snake venoms: structure, function and mechanism","volume":"397","author":"Kini","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.bioorg.2026.110138_bb0185","series-title":"Snake Venoms","first-page":"49","article-title":"Cellular Mechanisms of Action of Snake Phospholipase A2 Toxins","author":"Tonello","year":"2017"},{"key":"10.1016\/j.bioorg.2026.110138_bb0190","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/j.phytochem.2005.03.026","article-title":"Inhibitory effects of Piper umbellatum and Piper peltatum extracts towards myotoxic phospholipases A2 from Bothrops snake venoms: isolation of 4-nerolidylcatechol as active principle","volume":"66","author":"N\u00fa\u00f1ez","year":"2005","journal-title":"Phytochemistry"},{"key":"10.1016\/j.bioorg.2026.110138_bb0195","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/S0014-5793(02)03408-7","article-title":"Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery","volume":"531","author":"J\u00f8rgensen","year":"2002","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bioorg.2026.110138_bb0200","doi-asserted-by":"crossref","first-page":"1999","DOI":"10.1021\/acs.jmedchem.8b01568","article-title":"Substrate-specific inhibition constants for phospholipase A 2 acting on unique phospholipid substrates in mixed micelles and membranes using Lipidomics","volume":"62","author":"Mouchlis","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2026.110138_bb0205","doi-asserted-by":"crossref","first-page":"S237","DOI":"10.1194\/jlr.R800033-JLR200","article-title":"Phospholipase A2 structure\/function, mechanism, and signaling","volume":"50","author":"Burke","year":"2009","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bioorg.2026.110138_bb0210","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.toxicon.2005.02.012","article-title":"Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases","volume":"45","author":"Fox","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.bioorg.2026.110138_bb0215","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/j.toxicon.2005.02.029","article-title":"Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage","volume":"45","author":"Guti\u00e9rrez","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.bioorg.2026.110138_bb0220","doi-asserted-by":"crossref","first-page":"2662","DOI":"10.3390\/molecules23102662","article-title":"Inhibition of a Snake venom metalloproteinase by the flavonoid Myricetin","volume":"23","author":"Preciado","year":"2018","journal-title":"Molecules"},{"key":"10.1016\/j.bioorg.2026.110138_bb0225","first-page":"v","article-title":"Matrix metalloproteinase inhibitors: specificity of binding and structure-activity relationships","volume":"103","author":"Gupta","year":"2012","journal-title":"Experientia Suppl."},{"key":"10.1016\/j.bioorg.2026.110138_bb0230","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.biochi.2016.12.015","article-title":"Crystal structure of a phospholipase A2 from Bothrops asper venom: insights into a new putative \u201cmyotoxic cluster,\u201d","volume":"133","author":"Salvador","year":"2017","journal-title":"Biochimie"},{"key":"10.1016\/j.bioorg.2026.110138_bb0235","doi-asserted-by":"crossref","DOI":"10.1111\/cbdd.14466","article-title":"Interactions of small molecule inhibitors with secreted phospholipase <scp> A 2 <\/scp>\u00a0: A review of the structural data","volume":"103","author":"Crous","year":"2024","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.bioorg.2026.110138_bb0240","doi-asserted-by":"crossref","first-page":"2178","DOI":"10.1021\/acs.jcim.8b00512","article-title":"TTClust: A versatile molecular simulation trajectory clustering program with graphical summaries","volume":"58","author":"Tubiana","year":"2018","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.bioorg.2026.110138_bb0245","doi-asserted-by":"crossref","first-page":"4264","DOI":"10.1080\/00397910902898619","article-title":"Supported nitric acid on silica gel and polyvinyl pyrrolidone (PVP) as an efficient oxidizing agent for the oxidation of urazoles and bis-urazoles","volume":"39","author":"Ghorbani-Choghamarani","year":"2009","journal-title":"Synth. Commun."},{"key":"10.1016\/j.bioorg.2026.110138_bb0250","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.biochi.2009.12.006","article-title":"Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: biochemical and toxicological characterization\u2606","volume":"92","author":"Fern\u00e1ndez","year":"2010","journal-title":"Biochimie"},{"key":"10.1016\/j.bioorg.2026.110138_bb0255","first-page":"949","article-title":"Development of simple standard assay procedures for the characterization of snake venom","volume":"61","author":"Theakston","year":"1983","journal-title":"Bull. World Health Organ."},{"key":"10.1016\/j.bioorg.2026.110138_bb0260","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0003-9861(61)90145-X","article-title":"The preparation and properties of two new chromogenic substrates of trypsin","volume":"95","author":"Erlanger","year":"1961","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bioorg.2026.110138_bb0265","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.bbrc.2004.09.031","article-title":"A novel P-I class metalloproteinase with broad substrate-cleaving activity, agkislysin, from Agkistrodon acutus venom","volume":"324","author":"Wang","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bioorg.2026.110138_bb0270","article-title":"Inhibici\u00f3n de las actividades proteol\u00edtica, coagulante y hemol\u00edtica indirecta inducidas por el veneno de Bothrops asper por extractos etan\u00f3licos de tres especies de heliconias","volume":"15","author":"J.A., J.S.L., Q.J.C., N.V., F.M., & R.Y.J. Perea\u00f1ez","year":"2009","journal-title":"Vitae"},{"key":"10.1016\/j.bioorg.2026.110138_bb0275","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1016\/0041-0101(96)00057-8","article-title":"An aqueous endpoint assay of snake venom phospholipase A2","volume":"34","author":"Holzer","year":"1996","journal-title":"Toxicon"},{"key":"10.1016\/j.bioorg.2026.110138_bb0280","doi-asserted-by":"crossref","first-page":"D609","DOI":"10.1093\/nar\/gkae1010","article-title":"UniProt: the universal protein knowledgebase in 2025","volume":"53","author":"Bateman","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bioorg.2026.110138_bb0285","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Cryst."},{"key":"10.1016\/j.bioorg.2026.110138_bb0290","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bioorg.2026.110138_bb0295","series-title":"The PyMOL molecular graphics system, Version 2.5","author":"Schr\u00f6dinger LLC","year":"2024"},{"key":"10.1016\/j.bioorg.2026.110138_bb0300","first-page":"455","article-title":"AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","author":"Trott","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bioorg.2026.110138_bb0305","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1016\/0040-4020(80)80168-2","article-title":"Iterative partial equalization of orbital electronegativity\u2014a rapid access to atomic charges","volume":"36","author":"Gasteiger","year":"1980","journal-title":"Tetrahedron"},{"key":"10.1016\/j.bioorg.2026.110138_bb0310","doi-asserted-by":"crossref","first-page":"W463","DOI":"10.1093\/nar\/gkaf361","article-title":"PLIP 2025: introducing protein\u2013protein interactions to the protein\u2013ligand interaction profiler","volume":"53","author":"Schake","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bioorg.2026.110138_bb0315","unstructured":"D.A., Case, H.M., Aktulga, K., Belfon, I.Y., Ben-Shalom, J.T., Berryman, S.R., Brozell, Amber 2023, University of California, San Francisco, 2023."},{"key":"10.1016\/j.bioorg.2026.110138_bb0320","doi-asserted-by":"crossref","DOI":"10.1093\/bioinformatics\/btad350","article-title":"The ACPYPE web server for small-molecule MD topology generation","volume":"39","author":"Kagami","year":"2023","journal-title":"Bioinformatics"},{"key":"10.1016\/j.bioorg.2026.110138_bb0325","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1186\/1756-0500-5-367","article-title":"ACPYPE - AnteChamber PYthon parser interfacE","volume":"5","author":"Sousa da Silva","year":"2012","journal-title":"BMC. Res. Notes"},{"key":"10.1016\/j.bioorg.2026.110138_bb0330","doi-asserted-by":"crossref","first-page":"3314","DOI":"10.1021\/ct300418h","article-title":"MMPBSA.Py\u00a0: an efficient program for end-state free energy calculations","volume":"8","author":"Miller","year":"2012","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.bioorg.2026.110138_bb0335","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206826006747?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206826006747?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T16:40:40Z","timestamp":1787676040000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206826006747"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":67,"alternative-id":["S0045206826006747"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2026.110138","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Targeting Bothrops asper venom enzymes: Steroidal derivatives as potential inhibitors of phospholipase A2 and serine proteinases","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2026.110138","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"110138"}}