{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T04:39:14Z","timestamp":1790743154870,"version":"4.1.0"},"reference-count":64,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,3,1]],"date-time":"2021-03-01T00:00:00Z","timestamp":1614556800000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["303229\/2017-9"],"award-info":[{"award-number":["303229\/2017-9"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["303513\/2016-0"],"award-info":[{"award-number":["303513\/2016-0"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["304567\/2017-5"],"award-info":[{"award-number":["304567\/2017-5"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["P024092"],"award-info":[{"award-number":["P024092"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005639","name":"Universidade de S\u00e3o Paulo","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005639","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["150417\/2016-0"],"award-info":[{"award-number":["150417\/2016-0"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["2013\/207154"],"award-info":[{"award-number":["2013\/207154"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["2014\/00206-0"],"award-info":[{"award-number":["2014\/00206-0"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007605","name":"Aarhus Universitet","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007605","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"published-print":{"date-parts":[[2020,3]]},"DOI":"10.1016\/j.bbamem.2019.183173","type":"journal-article","created":{"date-parts":[[2019,12,26]],"date-time":"2019-12-26T02:20:53Z","timestamp":1577326853000},"page":"183173","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":14,"title":["Interactions of amphipathic \u03b1-helical MEG proteins from Schistosoma mansoni with membranes"],"prefix":"10.1016","volume":"1862","author":[{"given":"Ana P.","family":"Felizatti","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana E.","family":"Zeraik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis G.M.","family":"Basso","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia S.","family":"Kumagai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jose L.S.","family":"Lopes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B.A.","family":"Wallace","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana P.U.","family":"Araujo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ricardo","family":"DeMarco","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamem.2019.183173_bb0005","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1016\/S0140-6736(06)69440-3","article-title":"Human schistosomiasis","volume":"368","author":"Gryseels","year":"2006","journal-title":"Lancet"},{"key":"10.1016\/j.bbamem.2019.183173_bb0010","doi-asserted-by":"crossref","first-page":"1212","DOI":"10.1056\/NEJMra012396","article-title":"Schistosomiasis","volume":"346","author":"Ross","year":"2002","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bbamem.2019.183173_bb0015","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1038\/nature08160","article-title":"The genome of the blood fluke Schistosoma mansoni","volume":"460","author":"Berriman","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2019.183173_bb0020","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1101\/gr.100099.109","article-title":"Protein variation in blood-dwelling schistosome worms generated by differential splicing of micro-exon gene transcripts","volume":"20","author":"DeMarco","year":"2010","journal-title":"Genome Res."},{"key":"10.1016\/j.bbamem.2019.183173_bb0025","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1093\/gbe\/evu287","article-title":"Accelerated Evolution of schistosome Genes Coding for Proteins Located at the Host\u2013Parasite interface","volume":"7","author":"Philippsen","year":"2015","journal-title":"Genome Biol. Evol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0030","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0006235","article-title":"Microexon gene transcriptional profiles and evolution provide insights into blood processing by the Schistosoma japonicum esophagus","volume":"12","author":"Li","year":"2018","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.bbamem.2019.183173_bb0035","doi-asserted-by":"crossref","first-page":"2512","DOI":"10.1016\/j.bpj.2013.03.063","article-title":"Folding Factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14)","volume":"104","author":"Lopes","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2019.183173_bb0040","doi-asserted-by":"crossref","first-page":"3490","DOI":"10.1016\/j.bbagen.2016.09.015","article-title":"Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response","volume":"1861","author":"Orcia","year":"2017","journal-title":"Biochim. Biophys. Acta - Gen. Subj."},{"key":"10.1016\/j.bbamem.2019.183173_bb0045","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pntd.0004272","article-title":"The schistosome esophagus is a \u2018hotspot\u2019 for microexon and lysosomal hydrolase gene expression: implications for blood processing","volume":"9","author":"Wilson","year":"2015","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.bbamem.2019.183173_bb0050","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pntd.0002337","article-title":"The schistosome oesophageal gland: initiator of blood processing","volume":"7","author":"Li","year":"2013","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.bbamem.2019.183173_bb0055","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/nrd3591","article-title":"Designing antimicrobial peptides: form follows function","volume":"11","author":"Fjell","year":"2012","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bbamem.2019.183173_bb0060","doi-asserted-by":"crossref","first-page":"194","DOI":"10.3389\/fcimb.2016.00194","article-title":"Antimicrobial Peptides: an Emerging Category of Therapeutic Agents","volume":"6","author":"Mahlapuu","year":"2016","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0065","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1016\/j.bbamem.2006.02.021","article-title":"Peptide\u2013membrane interactions and mechanisms of membrane destruction by amphipathic \u03b1-helical antimicrobial peptides","volume":"1758","author":"Sato","year":"2006","journal-title":"Biochim. Biophys. Acta \u2010 Biomembr."},{"key":"10.1016\/j.bbamem.2019.183173_bb0070","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1007\/s00018-011-0710-x","article-title":"Multifunctional cationic host defence peptides and their clinical applications","volume":"68","author":"Yeung","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbamem.2019.183173_bb0075","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.it.2008.12.003","article-title":"AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense","volume":"30","author":"Lai","year":"2009","journal-title":"Trends Immunol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0080","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1016\/j.jmb.2004.03.016","article-title":"A combined transmembrane topology and signal peptide prediction method","volume":"338","author":"K\u00e4ll","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0085","first-page":"175","article-title":"A hidden Markov model for predicting transmembrane helices in protein sequences","volume":"6","author":"Sonnhammer","year":"1998","journal-title":"Proceedings. Int. Conf. Intell. Syst. Mol. Biol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0090","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.molbiopara.2011.03.001","article-title":"Whole mount in situ hybridization methodology for Schistosoma mansoni","volume":"178","author":"Cogswell","year":"2011","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0095","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/0003-2697(71)90443-X","article-title":"An accurate and convenient organic phosphorus assay","volume":"39","author":"McClare","year":"1971","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamem.2019.183173_bb0100","doi-asserted-by":"crossref","first-page":"1284","DOI":"10.1182\/blood-2006-07-036954","article-title":"Tropomyosin modulates erythrocyte membrane stability","volume":"109","author":"An","year":"2006","journal-title":"Blood"},{"key":"10.1016\/j.bbamem.2019.183173_bb0105","doi-asserted-by":"crossref","first-page":"37131","DOI":"10.1038\/srep37131","article-title":"SARS-CoV fusion peptides induce membrane surface ordering and curvature","volume":"6","author":"Basso","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamem.2019.183173_bb0110","doi-asserted-by":"crossref","first-page":"1717","DOI":"10.1002\/pro.3474","article-title":"CDtoolX, a downloadable software package for processing and analyses of circular dichroism spectroscopic data","volume":"27","author":"Miles","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbamem.2019.183173_bb0115","doi-asserted-by":"crossref","first-page":"W668","DOI":"10.1093\/nar\/gkh371","article-title":"DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data","volume":"32","author":"Whitmore","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.bbamem.2019.183173_bb0120","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.1093\/bioinformatics\/btl327","article-title":"Structural bioinformatics A reference database for circular dichroism spectroscopy covering fold and secondary structure space","volume":"22","author":"Lees","year":"2006","journal-title":"Bioinformatics"},{"key":"10.1016\/j.bbamem.2019.183173_bb0125","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.bbamem.2019.183173_bb0130","doi-asserted-by":"crossref","first-page":"3004","DOI":"10.1128\/AAC.06262-11","article-title":"Effects of dimerization on the structure and biological activity of antimicrobial peptide Ctx-Ha","volume":"56","author":"Lorenz\u00f3n","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbamem.2019.183173_bb0135","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/biom8030077","article-title":"Membrane active peptides and their biophysical characterization","volume":"8","author":"Avci","year":"2018","journal-title":"Biomolecules"},{"key":"10.1016\/j.bbamem.2019.183173_bb0140","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.chemphyslip.2014.12.003","article-title":"Interactions of the antimalarial amodiaquine with lipid model membranes","volume":"186","author":"Barroso","year":"2015","journal-title":"Chem. Phys. Lipids."},{"key":"10.1016\/j.bbamem.2019.183173_bb0145","doi-asserted-by":"crossref","first-page":"2155","DOI":"10.1016\/j.bbamem.2018.08.012","article-title":"Biophysical characterization and antitumor activity of synthetic Pantinin peptides from scorpion\u2019s venom","volume":"1860","author":"Crusca","year":"2018","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.bbamem.2019.183173_bb0150","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/nrmicro1098","article-title":"Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?","volume":"3","author":"Brogden","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0155","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1007\/s12551-016-0199-5","article-title":"The two sides of a lipid-protein story","volume":"8","author":"Basso","year":"2016","journal-title":"Biophys. Rev."},{"key":"10.1016\/j.bbamem.2019.183173_bb0160","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1126\/science.291.5502.266","article-title":"Electron spin resonance in studies of membranes and proteins","volume":"291","author":"Borbat","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.bbamem.2019.183173_bb0165","doi-asserted-by":"crossref","first-page":"1789","DOI":"10.1016\/j.bpj.2016.02.038","article-title":"Selective membrane disruption mechanism of an antibacterial \u03b3-AApeptide defined by EPR spectroscopy","volume":"110","author":"Kaur","year":"2016","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2019.183173_bb0170","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/S0006-3495(97)78711-3","article-title":"Interaction of bee venom melittin with zwitterionic and negatively charged phospholipid bilayers: a spin-label electron spin resonance study","volume":"72","author":"Kleinschmidt","year":"1997","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2019.183173_bb0175","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1002\/psc.1062","article-title":"Cholesterol prevents interaction of the cell-penetrating peptide transportan with model lipid membranes","volume":"14","author":"Arsov","year":"2008","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.bbamem.2019.183173_bb0180","doi-asserted-by":"crossref","first-page":"4925","DOI":"10.1016\/j.bpj.2009.04.015","article-title":"Fusion Peptide from Influenza hemagglutinin Increases Membrane Surface Order: an electron-Spin Resonance Study","volume":"96","author":"Ge","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2019.183173_bb0185","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1002\/pro.2274","article-title":"A common landscape for membrane- active peptides","volume":"22","author":"Last","year":"2013","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbamem.2019.183173_bb0190","doi-asserted-by":"crossref","first-page":"1130","DOI":"10.1021\/acs.accounts.6b00074","article-title":"How Membrane-Active Peptides Get into Lipid Membranes","volume":"49","author":"Sani","year":"2016","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.bbamem.2019.183173_bb0195","doi-asserted-by":"crossref","first-page":"12844","DOI":"10.1021\/bi800860k","article-title":"Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA","volume":"47","author":"Sanchez","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2019.183173_bb0200","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1016\/S0006-3495(01)76183-8","article-title":"Mechanisms of Tryptophan Fluorescence Shifts in Proteins","volume":"80","author":"Vivian","year":"2001","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2019.183173_bb0205","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/S0304-4157(96)00009-3","article-title":"Lateral pressure in membranes","volume":"1286","author":"Marsh","year":"1996","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2019.183173_bb0210","doi-asserted-by":"crossref","first-page":"5478","DOI":"10.1128\/IAI.00614-08","article-title":"Evidence for pore formation in host cell membranes by ESX-1-secreted ESAT-6 and its role in Mycobacterium marinum escape from the vacuole","volume":"76","author":"Smith","year":"2008","journal-title":"Infect. Immun."},{"key":"10.1016\/j.bbamem.2019.183173_bb0215","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1021\/acs.accounts.5b00346","article-title":"Oriented Circular dichroism: A method to Characterize Membrane-Active Peptides in Oriented Lipid Bilayers","volume":"49","author":"B\u00fcrck","year":"2016","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.bbamem.2019.183173_bb0220","doi-asserted-by":"crossref","first-page":"4859","DOI":"10.1039\/C5CS00084J","article-title":"Circular dichroism spectroscopy of membrane proteins","volume":"45","author":"Miles","year":"2016","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.bbamem.2019.183173_bb0225","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/j.bcmd.2006.02.002","article-title":"Alterations in erythrocyte membrane protein composition in advanced non-small cell lung cancer","volume":"36","author":"Hern\u00e1ndez-Hern\u00e1ndez","year":"2006","journal-title":"Blood Cells, Mol. Dis."},{"key":"10.1016\/j.bbamem.2019.183173_bb0230","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.rvsc.2018.05.001","article-title":"Identification of erythrocyte membrane proteins interacting with Mycoplasma suis GAPDH and OSGEP","volume":"119","author":"Song","year":"2018","journal-title":"Res. Vet. Sci."},{"key":"10.1016\/j.bbamem.2019.183173_bb0235","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/j.jprot.2015.06.014","article-title":"Hemoglobin interacting proteins and implications of spectrin hemoglobin interaction","volume":"128","author":"Basu","year":"2015","journal-title":"J. Proteomics"},{"key":"10.1016\/j.bbamem.2019.183173_bb0240","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0177543","article-title":"Involvement of Band3 in the efflux of sphingosine 1-phosphate from erythrocytes","volume":"12","author":"Kurano","year":"2017","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamem.2019.183173_bb0245","first-page":"1025","article-title":"Band 3 protein: physiology, function and structure","volume":"42","author":"Hamasaki","year":"1996","journal-title":"Cell. Mol. Biol. (Noisy-Le-Grand)."},{"key":"10.1016\/j.bbamem.2019.183173_bb0250","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.jcis.2018.10.103","article-title":"Membrane targeting cationic antimicrobial peptides","volume":"537","author":"Ciumac","year":"2019","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.bbamem.2019.183173_bb0255","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1016\/j.bpj.2011.02.018","article-title":"Transmembrane pores formed by human antimicrobial peptide LL-37","volume":"100","author":"Lee","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2019.183173_bb0260","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1016\/S0006-3495(97)78115-3","article-title":"Pore formation and translocation of melittin","volume":"73","author":"Matsuzaki","year":"1997","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2019.183173_bb0265","doi-asserted-by":"crossref","first-page":"1362","DOI":"10.1002\/pro.5560030902","article-title":"Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores","volume":"3","author":"Wimley","year":"1994","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbamem.2019.183173_bb0270","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.bbamem.2003.08.010","article-title":"The hemolytic activity of six arachnid cationic peptides is affected by the phosphatidylcholine-to-sphingomyelin ratio in lipid bilayers","volume":"1617","author":"Belokoneva","year":"2003","journal-title":"Biochim. Biophys. Acta \u2010 Biomembr."},{"key":"10.1016\/j.bbamem.2019.183173_bb0275","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1007\/s00253-011-3675-7","article-title":"A hemolytic peptide from the mycophilic fungus Sepedonium chrysospermum (Bull) Fr","volume":"94","author":"Sanguineti","year":"2012","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0280","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fimmu.2012.00195","article-title":"Does cholesterol play a role in the bacterial selectivity of antimicrobial peptides?","volume":"3","author":"Brender","year":"2012","journal-title":"Front. Immunol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0285","doi-asserted-by":"crossref","unstructured":"X.H. Li, Y.X. Xu, G. Vance, Y. Wang, L.B. Lv, G.J. Van Dam, J.P. Cao, R.A. Wilson, Evidence that rhesus macaques self-cure from a Schistosoma japonicum infection by disrupting worm esophageal function: a new route to an effective vaccine?, PLoS Negl. Trop. Dis., 9 (2015) e0003925.","DOI":"10.1371\/journal.pntd.0003925"},{"key":"10.1016\/j.bbamem.2019.183173_bb0290","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1017\/S0031182000045765","article-title":"The tegument of Schistosoma mansoni: observations on the formation, structure and composition of cytoplasmic inclusions in relation to tegument function","volume":"68","author":"Wilson","year":"1974","journal-title":"Parasitology"},{"key":"10.1016\/j.bbamem.2019.183173_bb0295","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/S0966-842X(00)01823-0","article-title":"The role of cationic antimicrobial peptides in innate host defences","volume":"8","author":"Hancock","year":"2000","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0300","doi-asserted-by":"crossref","first-page":"7684","DOI":"10.4049\/jimmunol.179.11.7684","article-title":"Host defense peptide LL-37, in synergy with inflammatory mediator IL-1beta, augments immune responses by multiple pathways","volume":"179","author":"Yu","year":"2007","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamem.2019.183173_bb0305","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002042","article-title":"A family of helminth molecules that modulate innate cell responses via molecular mimicry of host antimicrobial peptides","volume":"7","author":"Robinson","year":"2011","journal-title":"Plos Pathog."},{"key":"10.1016\/j.bbamem.2019.183173_bb0310","doi-asserted-by":"crossref","first-page":"4614","DOI":"10.1096\/fj.12-213876","article-title":"A helminth cathelicidin-like protein suppresses antigen processing and presentation in macrophages via inhibition of lysosomal vATPase","volume":"26","author":"Robinson","year":"2012","journal-title":"FASEB J."},{"key":"10.1016\/j.bbamem.2019.183173_bb0315","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1074\/jbc.M113.499517","article-title":"The MF6p\/FhHDM-1 major antigen secreted by the trematode parasite fasciola hepatica is a heme-binding protein","volume":"289","author":"Mart\u00ednez-Sern\u00e1ndez","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2019.183173_bb0320","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.molbiopara.2007.11.005","article-title":"Haemozoin formation","volume":"157","author":"Egan","year":"2008","journal-title":"Mol. Biochem. Parasitol."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273619303219?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273619303219?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T13:50:43Z","timestamp":1762091443000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0005273619303219"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3]]},"references-count":64,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2020,3]]}},"alternative-id":["S0005273619303219"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamem.2019.183173","relation":{},"ISSN":["0005-2736"],"issn-type":[{"value":"0005-2736","type":"print"}],"subject":[],"published":{"date-parts":[[2020,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Interactions of amphipathic \u03b1-helical MEG proteins from Schistosoma mansoni with membranes","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Biomembranes","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamem.2019.183173","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"183173"}}