{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,7]],"date-time":"2026-05-07T03:57:55Z","timestamp":1778126275764,"version":"3.51.4"},"reference-count":46,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2020,1,1]],"date-time":"2020-01-01T00:00:00Z","timestamp":1577836800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,1,1]],"date-time":"2020-01-01T00:00:00Z","timestamp":1577836800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2010\/09002-8"],"award-info":[{"award-number":["2010\/09002-8"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2008\/00108-8"],"award-info":[{"award-number":["2008\/00108-8"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2020,1]]},"DOI":"10.1016\/j.bbrc.2019.10.144","type":"journal-article","created":{"date-parts":[[2019,10,25]],"date-time":"2019-10-25T18:48:06Z","timestamp":1572029286000},"page":"402-407","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":12,"title":["Leukocyte recruitment induced by snake venom metalloproteinases: Role of the catalytic domain"],"prefix":"10.1016","volume":"521","author":[{"given":"Bianca Cestari","family":"Zychar","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patr\u00edcia Bianca","family":"Clissa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eneas","family":"Carvalho","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cristiani","family":"Baldo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8395-9150","authenticated-orcid":false,"given":"Luis Roberto C.","family":"Gon\u00e7alves","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2019.10.144_bib1","series-title":"Animais Pe\u00e7onhentos No Bras. Biol. Cl\u00ednica E Ter. Dos Acid.","first-page":"72","article-title":"Acidente botr\u00f3pico","author":"Fran\u00e7a","year":"2003"},{"key":"10.1016\/j.bbrc.2019.10.144_bib2","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. Prim."},{"key":"10.1016\/j.bbrc.2019.10.144_bib3","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1111\/j.2042-7158.1996.tb05887.x","article-title":"Pharmacological profile of rat pleurisy induced by Bothrops jararaca venom","volume":"48","author":"B\u00farigo","year":"1996","journal-title":"J.\u00a0Pharm. Pharmacol."},{"key":"10.1016\/j.bbrc.2019.10.144_bib4","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1080\/096293500411569","article-title":"Local haemorrhage induced by Bothrops jararaca venom: relationship to neurogenic inflammation","volume":"9","author":"Goncalves","year":"2000","journal-title":"Mediat. Inflamm."},{"key":"10.1016\/j.bbrc.2019.10.144_bib5","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1016\/S0041-0101(98)00145-7","article-title":"Neutralization of local tissue damage induced by Bothrops asper (terciopelo) snake venom","volume":"36","author":"Guti\u00e9rrez","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib6","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1007\/s00011-007-7054-x","article-title":"Effect of dexamethasone associated with serum therapy on treatment of Bothrops jararaca venom-induced paw edema in mice","volume":"56","author":"Ara\u00fajo","year":"2007","journal-title":"Inflamm. Res."},{"key":"10.1016\/j.bbrc.2019.10.144_bib7","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0005458","article-title":"Experimental Bothrops atrox envenomation: efficacy of antivenom therapy and the combination of Bothrops antivenom with dexamethasone","volume":"11","author":"Santos Barreto","year":"2017","journal-title":"PLoS Neglected Trop. Dis."},{"key":"10.1016\/j.bbrc.2019.10.144_bib8","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/j.toxicon.2006.07.008","article-title":"Bothrops jararaca venom gland transcriptome: analysis of the gene expression pattern","volume":"48","author":"Cidade","year":"2006","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib9","doi-asserted-by":"crossref","first-page":"4218","DOI":"10.1002\/pmic.201100287","article-title":"Bothrops jararaca venom proteome rearrangement upon neonate to adult transition","volume":"11","author":"Zelanis","year":"2011","journal-title":"Proteomics"},{"key":"10.1016\/j.bbrc.2019.10.144_bib10","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.jprot.2009.07.013","article-title":"Snake venomics and antivenomics of Bothrops atrox venoms from Colombia and the Amazon regions of Brazil, Per\u00fa and Ecuador suggest the occurrence of geographic variation of venom phenotype by a trend towards paedomorphism","volume":"73","author":"Nu\u00f1ez","year":"2009","journal-title":"J.\u00a0Proteomics."},{"key":"10.1016\/j.bbrc.2019.10.144_bib11","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.toxicon.2009.07.025","article-title":"Contribution of metalloproteases, serine proteases and phospholipases A2 to the inflammatory reaction induced by Bothrops jararaca crude venom in mice","volume":"55","author":"Zychar","year":"2010","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib12","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.bbrc.2019.10.144_bib13","doi-asserted-by":"crossref","DOI":"10.1016\/S0021-9258(18)50027-2","article-title":"Purification , cloning , and molecular characterization of a high molecular weight hemorrhagic metalloprotease , jararhagin , from Bothrops jararaca venom","volume":"267","author":"Paine","year":"1992","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bbrc.2019.10.144_bib14","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.toxicon.2012.03.026","article-title":"Jararhagin, a hemorrhagic snake venom metalloproteinase from Bothrops jararaca","volume":"60","author":"Moura-da-Silva","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib15","doi-asserted-by":"crossref","first-page":"2000","DOI":"10.1002\/eji.1830260905","article-title":"Processing of pro-tumor necrosis factor-a by venom metalloproteinases: a hypothesis explaining local tissue damage following snake bite","volume":"26","author":"Moura-da-Silva","year":"1996","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.bbrc.2019.10.144_bib16","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1016\/S0041-0101(01)00131-3","article-title":"The effect of jararhagin, a metalloproteinase from Bothrops jararaca venom, on pro-inflammatory cytokines released by murine peritoneal adherent cells","volume":"39","author":"Clissa","year":"2001","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib17","doi-asserted-by":"crossref","first-page":"3458","DOI":"10.1002\/eji.200324475","article-title":"Inflammatory pathogenesis of snake venom metalloproteinase-induced skin necrosis","volume":"33","author":"Laing","year":"2003","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.bbrc.2019.10.144_bib18","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.peptides.2003.12.008","article-title":"The C-terminus of murine S100A9 inhibits hyperalgesia and edema induced by jararhagin","volume":"25","author":"Dale","year":"2004","journal-title":"Peptides"},{"key":"10.1016\/j.bbrc.2019.10.144_bib19","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/j.toxicon.2006.02.001","article-title":"Importance of jararhagin disintegrin-like and cysteine-rich domains in the early events of local inflammatory response","volume":"47","author":"Clissa","year":"2006","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib20","doi-asserted-by":"crossref","first-page":"e727","DOI":"10.1371\/journal.pntd.0000727","article-title":"Mechanisms of vascular damage by hemorrhagic snake venom metalloproteinases: tissue distribution and in situ hydrolysis","volume":"4","author":"Baldo","year":"2010","journal-title":"PLoS Neglected Trop. Dis."},{"key":"10.1016\/j.bbrc.2019.10.144_bib21","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1016\/j.ijbiomac.2018.08.051","article-title":"Inflammation, angiogenesis and fibrogenesis are differentially modulated by distinct domains of the snake venometalloproteinase jararhagin","volume":"119","author":"Ferreira","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbrc.2019.10.144_bib22","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1016\/j.bbrc.2019.03.152","article-title":"Site mutation of residues in a loop surrounding the active site of a P-1 snake venom metalloproteinase abrogates its hemorrhagic activity","volume":"512","author":"Camacho","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2019.10.144_bib23","doi-asserted-by":"crossref","first-page":"121","DOI":"10.3109\/15569548809059729","article-title":"Hemorrhagic toxins from snake venoms","volume":"7","author":"Bjarnason","year":"1988","journal-title":"J.\u00a0Toxicol. - Toxin Rev."},{"key":"10.1016\/j.bbrc.2019.10.144_bib24","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0003731","article-title":"Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage","volume":"9","author":"Herrera","year":"2015","journal-title":"PLoS Neglected Trop. Dis."},{"key":"10.1016\/j.bbrc.2019.10.144_bib25","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/S0003-9861(02)00598-2","article-title":"Evidence for heterogeneous forms of the snake venom metalloproteinase jararhagin: a factor contributing to snake venom variability","volume":"409","author":"Moura-Da-Silva","year":"2003","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbrc.2019.10.144_bib26","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.toxicon.2007.08.005","article-title":"BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: biological effects benchmarking relatively to jararhagin, a P-III SVMP","volume":"51","author":"Baldo","year":"2008","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib27","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during assembly of head of bacteriophage-T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2019.10.144_bib28","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/S0041-0101(96)00193-6","article-title":"Inhibition of the hemorrhagic activity of Bothrops asper venom by a novel neutralizing mixture","volume":"35","author":"Borkow","year":"1997","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib29","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1016\/j.toxicon.2010.07.001","article-title":"Preclinical assessment of the neutralizing capacity of antivenoms produced in six Latin American countries against medically-relevant Bothrops snake venoms","volume":"56","author":"Segura","year":"2010","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib30","first-page":"301","article-title":"A\u00a0study of the fibrin plate assay of fibrinolytic agents. Optimal conditions, reproducibility and precision","volume":"13","author":"Jespersen","year":"1983","journal-title":"Haemostasis"},{"key":"10.1016\/j.bbrc.2019.10.144_bib31","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/0026-2862(73)90054-X","article-title":"Open cremaster muscle preparation for study of blood-vessels by in-vivo microscopy","volume":"5","author":"Baez","year":"1973","journal-title":"Microvasc. Res."},{"key":"10.1016\/j.bbrc.2019.10.144_bib32","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1002\/bip.20853","article-title":"Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases","volume":"89","author":"Whitmore","year":"2008","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbrc.2019.10.144_bib33","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1006\/abio.1993.1079","article-title":"A\u00a0self-consistent method for the analysis of protein secondary structure from circular dichroism","volume":"299","author":"Sreerama","year":"1993","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbrc.2019.10.144_bib34","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.biochi.2007.11.009","article-title":"Collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases","volume":"90","author":"Moura-da-Silva","year":"2008","journal-title":"Biochimie"},{"key":"10.1016\/j.bbrc.2019.10.144_bib35","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0168643","article-title":"Effects of PI and PIII snake venom haemorrhagic metalloproteinases on the microvasculature: a confocal microscopy study on the mouse cremaster muscle","volume":"11","author":"Herrera","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.bbrc.2019.10.144_bib36","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.abb.2005.06.007","article-title":"Role of the snake venom toxin jararhagin in proinflammatory pathogenesis: In\u00a0vitro and in\u00a0vivo gene expression analysis of the effects of the toxin","volume":"441","author":"Gallagher","year":"2005","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbrc.2019.10.144_bib37","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1080\/09629350020025728","article-title":"Bothrops asper snake venom and its metalloproteinase BaP-1 activate the complement system: role in leucocyte recruitment","volume":"9","author":"Farsky","year":"2000","journal-title":"Mediat. Inflamm."},{"key":"10.1016\/j.bbrc.2019.10.144_bib38","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1006\/bbrc.1994.1706","article-title":"A\u00a028 kDa-protein with disintegrine-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen and ADP-induced platelet aggregation","volume":"201","author":"Usami","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2019.10.144_bib39","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1016\/j.toxicon.2009.02.019","article-title":"Simplified procedures for the isolation of HF3, bothropasin, disintegrin-like\/cysteine-rich protein and a novel P-I metalloproteinase from Bothrops jararaca venom","volume":"53","author":"Oliveira","year":"2009","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib40","doi-asserted-by":"crossref","first-page":"3915","DOI":"10.1016\/j.febslet.2008.10.034","article-title":"Activation of leukocyte rolling by the cysteine-rich domain and the hyper-variable region of HF3, a snake venom hemorrhagic metalloproteinase","volume":"582","author":"Menezes","year":"2008","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbrc.2019.10.144_bib41","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.biochi.2010.10.007","article-title":"Disintegrin-like\/cysteine-rich domains of the reprolysin HF3: site-directed mutagenesis reveals essential role of specific residues","volume":"93","author":"Menezes","year":"2011","journal-title":"Biochimie"},{"key":"10.1016\/j.bbrc.2019.10.144_bib42","doi-asserted-by":"crossref","first-page":"70566","DOI":"10.1039\/C5RA14693C","article-title":"Zn2+ ion of the snake venom metalloproteinase (SVMP) plays a critical role in ligand binding\u202f: a molecular dynamics simulation study","volume":"5","author":"Chinnasamy","year":"2015","journal-title":"RSC Adv."},{"key":"10.1016\/j.bbrc.2019.10.144_bib43","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0014-5793(03)00799-3","article-title":"Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function","volume":"549","author":"Kamiguti","year":"2003","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbrc.2019.10.144_bib44","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1016\/j.toxicon.2003.10.010","article-title":"Snake venom metalloproteinases: structure\/function relationships studies using monoclonal antibodies","volume":"42","author":"Tanjoni","year":"2003","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib45","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1016\/j.toxicon.2009.12.010","article-title":"Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to apha2 beta1 integrin and collagen","volume":"55","author":"Tanjoni","year":"2010","journal-title":"Toxicon"},{"key":"10.1016\/j.bbrc.2019.10.144_bib46","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1042\/BJ20050483","article-title":"Function of the cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A: targeting adhesion proteins collagen I and von Willebrand factor","volume":"391","author":"Serrano","year":"2005","journal-title":"Biochem. J."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X19320522?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X19320522?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T15:34:34Z","timestamp":1777390474000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X19320522"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,1]]},"references-count":46,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2020,1]]}},"alternative-id":["S0006291X19320522"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2019.10.144","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2020,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Leukocyte recruitment induced by snake venom metalloproteinases: Role of the catalytic domain","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2019.10.144","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}