{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T03:48:01Z","timestamp":1790826481312,"version":"4.1.0"},"reference-count":37,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,7,1]],"date-time":"2019-07-01T00:00:00Z","timestamp":1561939200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,7,1]],"date-time":"2019-07-01T00:00:00Z","timestamp":1561939200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,4,27]],"date-time":"2020-04-27T00:00:00Z","timestamp":1587945600000},"content-version":"am","delay-in-days":301,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R15HL137134-01"],"award-info":[{"award-number":["R15HL137134-01"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P40OD010960-14"],"award-info":[{"award-number":["P40OD010960-14"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010859","name":"Texas A&M University\u2019s Presidential Undergraduate Research Program (TAMUK)","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010859","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000928","name":"Robert A. Welch Foundation Department","doi-asserted-by":"publisher","award":["AC-0006"],"award-info":[{"award-number":["AC-0006"]}],"id":[{"id":"10.13039\/100000928","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2019,7]]},"DOI":"10.1016\/j.toxicon.2019.04.006","type":"journal-article","created":{"date-parts":[[2019,4,20]],"date-time":"2019-04-20T10:28:36Z","timestamp":1555756116000},"page":"22-30","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":25,"special_numbering":"C","title":["The isolation and characterization of a new snake venom cysteine-rich secretory protein (svCRiSP) from the venom of the Southern Pacific rattlesnake and its effect on vascular permeability"],"prefix":"10.1016","volume":"165","author":[{"given":"Montamas","family":"Suntravat","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Walter E.","family":"Cromer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jessenia","family":"Marquez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacob A.","family":"Galan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David C.","family":"Zawieja","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"Davies","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emelyn","family":"Salazar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elda E.","family":"S\u00e1nchez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2019.04.006_bib1","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0099-2399(06)81589-X","article-title":"Morphological cell changes due to chemical toxicity of a dental material: an electron microscopic study on human periodontal ligament fibroblasts and L929 cells","volume":"16","author":"Al-Nazhan","year":"1990","journal-title":"J. Endod."},{"key":"10.1016\/j.toxicon.2019.04.006_bib2","doi-asserted-by":"crossref","first-page":"G1234","DOI":"10.1152\/ajpgi.2001.280.6.G1234","article-title":"iNOS upregulation mediates oxidant-induced disruption of F-actin and barrier of intestinal monolayers","volume":"280","author":"Banan","year":"2001","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib3","doi-asserted-by":"crossref","DOI":"10.1155\/2016\/1574971","article-title":"Bothrops jararaca and Bothrops erythromelas snake venoms promote cell cycle arrest and induce apoptosis via the mitochondrial depolarization of cervical cancer cells","author":"Bernardes-Oliveira","year":"2016","journal-title":"Evid. Based. Complement. Alternat. Med."},{"key":"10.1016\/j.toxicon.2019.04.006_bib4","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.mvr.2008.06.003","article-title":"The role of cytoskeleton in the regulation of vascular endothelial barrier function","volume":"76","author":"Bogatcheva","year":"2008","journal-title":"Microvasc. Res."},{"key":"10.1016\/j.toxicon.2019.04.006_bib5","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1007\/s10616-014-9820-2","article-title":"Evaluation of cytotoxic activities of snake venoms toward breast (MCF-7) and skin cancer (A-375) cell lines","volume":"68","author":"Bradshaw","year":"2016","journal-title":"Cytotechnology"},{"key":"10.1016\/j.toxicon.2019.04.006_bib6","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1073\/pnas.96.2.754","article-title":"Pseudechetoxin: a peptide blocker of cyclic nucleotide-gated ion channels","volume":"96","author":"Brown","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.toxicon.2019.04.006_bib7","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1007\/s10456-013-9393-2","article-title":"The effects of inflammatory cytokines on lymphatic endothelial barrier function","volume":"17","author":"Cromer","year":"2014","journal-title":"Angiogenesis"},{"key":"10.1016\/j.toxicon.2019.04.006_bib8","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3891\/acta.chem.scand.04-0283","article-title":"Method for determination of the amino acid sequence in peptides","volume":"4","author":"Edman","year":"1950","journal-title":"Acta Chem. Scand."},{"key":"10.1016\/j.toxicon.2019.04.006_bib9","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1007\/s00204-010-0597-6","article-title":"Characterization of toxins from the broad-banded water snake Helicops angulatus (Linnaeus, 1758): isolation of a cysteine-rich secretory protein, Helicopsin","volume":"85","author":"Estrella","year":"2011","journal-title":"Arch. Toxicol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib10","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1128\/MCB.25.1.136-146.2005","article-title":"Cyclic AMP potentiates vascular endothelial cadherin-mediated cell-cell contact to enhance endothelial barrier function through an Epac-Rap1 signaling pathway","volume":"25","author":"Fukuhara","year":"2005","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib11","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1210\/er.2008-0032","article-title":"The CAP superfamily: cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins-roles in reproduction, cancer, and immune defense","volume":"29","author":"Gibbs","year":"2008","journal-title":"Endocr. Rev."},{"key":"10.1016\/j.toxicon.2019.04.006_bib12","article-title":"Cytotoxic and morphological effects of microcystin-LR, cylindrospermopsin, and their combinations on the human hepatic cell line HepG2","volume":"20","author":"Guti\u00e9rrez-Praena","year":"2018","journal-title":"Environ Toxicol. Nov"},{"key":"10.1016\/j.toxicon.2019.04.006_bib13","series-title":"Handbook of Venoms and Toxins of Reptiles","first-page":"325","article-title":"Cysteine-rich secretory proteins in reptile venoms","author":"Heyborne","year":"2010"},{"key":"10.1016\/j.toxicon.2019.04.006_bib14","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1023\/A:1020295718728","article-title":"Different reactions of aortic and venular endothelial cell monolayers to histamine on macromolecular permeability: role of cAMP, cytosolic Ca2+ and F-actin","volume":"23","author":"Ikeda","year":"1999","journal-title":"Inflammation"},{"key":"10.1016\/j.toxicon.2019.04.006_bib15","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1016\/j.bbagen.2015.02.002","article-title":"Anti-angiogenic activities of snake venom CRISP isolated from Echis carinatus sochureki","volume":"1850","author":"Lecht","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2019.04.006_bib16","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.toxicon.2013.11.005","article-title":"Anti-angiogenic activities of two recombinant disintegrins derived from the Mohave and Prairie rattlesnakes","volume":"78","author":"Lucena","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2019.04.006_bib17","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1002\/jcp.1041640311","article-title":"Cytoskeletal regulation of Caco-2 intestinal monolayer paracellular permeability","volume":"164","author":"Ma","year":"1995","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib18","article-title":"High-content, high-throughput screening for the identification of cytotoxic compounds based on cell morphology and cell proliferation markers","volume":"9","author":"Martin","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.toxicon.2019.04.006_bib19","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1093\/jb\/mvn174","article-title":"Structural divergence of cysteine-rich secretory proteins in snake venoms","volume":"145","author":"Matsunaga","year":"2009","journal-title":"J. Biochem."},{"key":"10.1016\/j.toxicon.2019.04.006_bib20","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1016\/S0076-6879(73)27039-8","article-title":"Automated Edman degradation: the protein sequenator","volume":"27","author":"Niall","year":"1973","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib21","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1152\/jappl.1988.64.3.1196","article-title":"Hyperoxia causes increased albumin permeability of cultured endothelial monolayers","volume":"64","author":"Phillips","year":"1985","journal-title":"J. Appl. Physiol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib22","first-page":"185","article-title":"Bacterial toxins modifying the actin cytoskeleton","volume":"2","author":"Richard","year":"1999","journal-title":"Int. Microbiol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib23","doi-asserted-by":"crossref","first-page":"2379","DOI":"10.1083\/jcb.103.6.2379","article-title":"Histamine type I receptor occupancy increases endothelial cytosolic calcium, reduces F-actin, and promotes albumin diffusion across cultured endothelial monolayers","volume":"103","author":"Rotrosen","year":"1986","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib24","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1161\/01.RES.51.5.657","article-title":"Role of endothelial cell cytoskeleton in control of endothelial permeability","volume":"51","author":"Shasby","year":"1982","journal-title":"Circ. Res."},{"key":"10.1016\/j.toxicon.2019.04.006_bib25","series-title":"Venomous Reptiles and Their Toxins","first-page":"241","article-title":"Cysteine-rich secretory proteins","author":"Sunagar","year":"2015"},{"key":"10.1016\/j.toxicon.2019.04.006_bib26","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.jprot.2014.01.013","article-title":"Intraspecific venom variation in the medically significant Southern Pacific Rattlesnake (Crotalus oreganus helleri): biodiscovery, clinical and evolutionary implications","volume":"99","author":"Sunagar","year":"2014","journal-title":"J. Proteomics"},{"key":"10.1016\/j.toxicon.2019.04.006_bib27","doi-asserted-by":"crossref","first-page":"E290","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.toxicon.2019.04.006_bib28","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1189\/jlb.72.3.462","article-title":"Identification of human cysteine-rich secretory protein 3 (CRISP-3) as a matrix protein in a subset of peroxidase-negative granules of neutrophils and in the granules of eosinophils","volume":"72","author":"Udby","year":"2002","journal-title":"J. Leukoc. Biol."},{"key":"10.1016\/j.toxicon.2019.04.006_bib29","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/S0022-1759(02)00033-9","article-title":"An ELISA for SGP28\/CRISP-3, a cysteine-rich secretory protein in human neutrophils, plasma, and exocrine secretions","volume":"263","author":"Udby","year":"2002","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.toxicon.2019.04.006_bib30","doi-asserted-by":"crossref","first-page":"12877","DOI":"10.1021\/bi048823e","article-title":"Cysteine-rich secretory protein 3 is a ligand of alpha1B-glycoprotein in human plasma","volume":"43","author":"Udby","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2019.04.006_bib31","doi-asserted-by":"crossref","first-page":"37872","DOI":"10.1074\/jbc.M110.146290","article-title":"Cobra CRISP functions as an inflammatory modulator via a novel Zn2+- and heparan sulfate-dependent transcriptional regulation of endothelial cell adhesion molecules","volume":"285","author":"Wang","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2019.04.006_bib32","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.bbrc.2006.10.067","article-title":"Structural and functional analysis of natrin, a venom protein that targets various ion channels","volume":"351","author":"Wang","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2019.04.006_bib33","doi-asserted-by":"crossref","first-page":"10145","DOI":"10.1021\/bi050614m","article-title":"Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel","volume":"44","author":"Wang","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2019.04.006_bib34","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0014-4827(03)00183-6","article-title":"Activation of MMP-2, cleavage of matrix proteins, and adherens junctions during a snake venom metalloproteinase-induced endothelial cell apoptosis","volume":"288","author":"Wu","year":"2003","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.toxicon.2019.04.006_bib35","doi-asserted-by":"crossref","first-page":"11331","DOI":"10.1021\/bi026132h","article-title":"Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels","volume":"41","author":"Yamazaki","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2019.04.006_bib36","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0003-9861(03)00028-6","article-title":"Wide distribution of cysteine-rich secretory proteins in snake venoms: isolation and cloning of novel snake venom cysteine-rich secretory proteins","volume":"412","author":"Yamazaki","year":"2003","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.toxicon.2019.04.006_bib37","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.toxicon.2004.05.023","article-title":"Structure and function of snake venom cysteine-rich secretory proteins","volume":"44","author":"Yamazaki","year":"2004","journal-title":"Toxicon"}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010119301187?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010119301187?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T21:11:33Z","timestamp":1758575493000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010119301187"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,7]]},"references-count":37,"alternative-id":["S0041010119301187"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2019.04.006","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2019,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The isolation and characterization of a new snake venom cysteine-rich secretory protein (svCRiSP) from the venom of the Southern Pacific rattlesnake and its effect on vascular permeability","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2019.04.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}