{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T16:43:11Z","timestamp":1786984991791,"version":"build-2736575974"},"reference-count":58,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2016,8,1]],"date-time":"2016-08-01T00:00:00Z","timestamp":1470009600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,8,1]],"date-time":"2017-08-01T00:00:00Z","timestamp":1501545600000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Basic Research Program of China (973 program)","doi-asserted-by":"crossref","award":["2013CB910700"],"award-info":[{"award-number":["2013CB910700"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["21372026"],"award-info":[{"award-number":["21372026"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["21402006"],"award-info":[{"award-number":["21402006"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005090","name":"Beijing NOVA Program","doi-asserted-by":"publisher","award":["Z131102000413010"],"award-info":[{"award-number":["Z131102000413010"]}],"id":[{"id":"10.13039\/501100005090","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"crossref","award":["2050205"],"award-info":[{"award-number":["2050205"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"crossref","award":["20130801"],"award-info":[{"award-number":["20130801"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"crossref","award":["YS1407"],"award-info":[{"award-number":["YS1407"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"published-print":{"date-parts":[[2016,8]]},"DOI":"10.1016\/j.bbamem.2016.05.012","type":"journal-article","created":{"date-parts":[[2016,5,17]],"date-time":"2016-05-17T12:21:09Z","timestamp":1463487669000},"page":"1914-1925","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":33,"title":["From a pro-apoptotic peptide to a lytic peptide: One single residue mutation"],"prefix":"10.1016","volume":"1858","author":[{"given":"Xi-Rui","family":"Zhou","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qiang","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xi-Bo","family":"Tian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yi-Meng","family":"Cao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhu-Qing","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruru","family":"Fan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiu-Fang","family":"Ding","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhentai","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Long","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shi-Zhong","family":"Luo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamem.2016.05.012_bb0005","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.bbamem.2007.11.008","article-title":"Studies on anticancer activities of antimicrobial peptides","volume":"1778","author":"Hoskin","year":"2008","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0010","doi-asserted-by":"crossref","first-page":"3012","DOI":"10.1021\/cr900019j","article-title":"Impact of natural products on developing new anticancer agents","volume":"109","author":"Cragg","year":"2009","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0015","doi-asserted-by":"crossref","first-page":"294","DOI":"10.3389\/fmicb.2013.00294","article-title":"From antimicrobial to anticancer peptides. A review","volume":"4","author":"Gaspar","year":"2013","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0020","doi-asserted-by":"crossref","first-page":"8027","DOI":"10.3390\/ijms12118027","article-title":"Oncolytic activities of host defense peptides","volume":"12","author":"Al-Benna","year":"2011","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0025","doi-asserted-by":"crossref","first-page":"2731","DOI":"10.1016\/j.biomaterials.2012.12.039","article-title":"Dual modes of antitumor action of an amphiphilic peptide A9K","volume":"34","author":"Xu","year":"2013","journal-title":"Biomaterials"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0030","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1007\/s12272-013-0112-8","article-title":"Design of potent, non-toxic anticancer peptides based on the structure of the antimicrobial peptide, temporin-1CEa","volume":"36","author":"Yang","year":"2013","journal-title":"Arch. Pharm. Res."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0035","doi-asserted-by":"crossref","first-page":"12732","DOI":"10.1021\/ja3042004","article-title":"Gain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening","volume":"134","author":"Krauson","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0040","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1139\/o98-026","article-title":"Structure-function relationship of antimicrobial peptides","volume":"76","author":"Hwang","year":"1998","journal-title":"Biochem. Cell Biol."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0045","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.bpj.2012.06.004","article-title":"Membrane-active peptides and the clustering of anionic lipids","volume":"103","author":"Wadhwani","year":"2012","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0050","doi-asserted-by":"crossref","first-page":"7738","DOI":"10.1074\/jbc.M111.303602","article-title":"Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions","volume":"287","author":"Yin","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2016.05.012_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":"2011","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0060","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/s10989-012-9295-y","article-title":"Anticancer activity of proapoptotic peptides is highly improved by thermal targeting using elastin-like polypeptides","volume":"18","author":"Moktan","year":"2012","journal-title":"Int. J. Pept. Res. Ther."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0065","first-page":"1","article-title":"Antibacterial action of a bee venom fraction (melittin) against a penicillin-resistant Staphylococcus and other microorganisms. USNRDL-TR-67-101","volume":"5","author":"Fennell","year":"1967","journal-title":"Res. Dev. Tech. Rep."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0070","doi-asserted-by":"crossref","first-page":"2561","DOI":"10.1007\/s00726-014-1801-4","article-title":"Vipericidins: a novel family of cathelicidin-related peptides from the venom gland of South American pit vipers","volume":"46","author":"Falcao","year":"2014","journal-title":"Amino Acids"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0075","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1007\/s10989-013-9350-3","article-title":"Mauriporin, a novel cationic \u03b1-helical peptide with selective cytotoxic activity against prostate cancer cell lines from the venom of the scorpion Androctonus mauritanicus","volume":"19","author":"Almaaytah","year":"2013","journal-title":"Int. J. Pept. Res. Ther."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0080","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1007\/s10989-014-9405-0","article-title":"Antimicrobial and antibiofilm activity of mauriporin, a multifunctional scorpion venom peptide","volume":"20","author":"Almaaytah","year":"2014","journal-title":"Int. J. Pept. Res. Ther."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0085","doi-asserted-by":"crossref","first-page":"1508","DOI":"10.1002\/jps.23043","article-title":"Lytic peptides with improved stability and selectivity designed for cancer treatment","volume":"101","author":"Chen","year":"2012","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0090","doi-asserted-by":"crossref","first-page":"3804","DOI":"10.1074\/jbc.M807191200","article-title":"Melittin, a major component of bee venom, sensitizes human hepatocellular carcinoma cells to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis by activating CaMKII-TAK1-JNK\/p38 and inhibiting IkappaBalpha kinase-NFkappaB","volume":"284","author":"Wang","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0095","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1517\/13543784.15.8.933","article-title":"Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment","volume":"15","author":"Mader","year":"2006","journal-title":"Expert Opin. Investig. Drugs."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0100","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1023\/B:AGEN.0000037335.17717.bf","article-title":"Inhibition of agiogenesis by Abeta peptides","volume":"7","author":"Paris","year":"2004","journal-title":"Angiogenesis"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0105","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1158\/1535-7163.MCT-10-0811","article-title":"Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework","volume":"10","author":"Huang","year":"2011","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0110","first-page":"3062","article-title":"Elevated expression of phosphatidylserine in the outer leaflet of human tumor cells and recognition by activated human blood monocytes","volume":"51","author":"Utsugit","year":"1991","journal-title":"Cancer Res."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0115","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1016\/j.chemphyslip.2011.09.004","article-title":"Membrane-active host defense peptides-challenges and perspectives for the development of novel anticancer drugs","volume":"164","author":"Riedl","year":"2011","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0120","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/s11010-005-3557-3","article-title":"Changes in electric charge and phospholipids composition in human colorectal cancer cells","volume":"276","author":"Dobrzynska","year":"2005","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0125","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1006\/bbrc.1996.0806","article-title":"Effect of O-glycosylated mucin on invasion and metastasis of HM7 human colon cancer cells","volume":"222","author":"Yoon","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0135","doi-asserted-by":"crossref","first-page":"3839","DOI":"10.1021\/bm201098j","article-title":"Designed antimicrobial and antitumor peptides with high selectivity","volume":"12","author":"Hu","year":"2011","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0140","doi-asserted-by":"crossref","first-page":"2174","DOI":"10.3748\/wjg.14.2174","article-title":"Detection of apoptosis induced by new type gosling viral enteritis virus in vitro through fluorescein annexin V-FITC\/PI double labeling","volume":"14","author":"Chen","year":"2008","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0145","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1084\/jem.182.5.1545","article-title":"Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl","volume":"182","author":"Martin","year":"1995","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0150","doi-asserted-by":"crossref","first-page":"417","DOI":"10.3109\/02841869309093620","article-title":"Quantification of apoptosis and necrosis by flow cytometry","volume":"32","author":"Ormerod","year":"1993","journal-title":"Acta Oncol."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0155","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1111\/j.1582-4934.2002.tb00313.x","article-title":"Kinetics of apoptotic markers in exogenously induced apoptosis of EL4 cells","volume":"6","author":"Jessel","year":"2002","journal-title":"J. Cell. Mol. Med."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0160","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0092-8674(00)81334-3","article-title":"Human ICE\/CED-3 protease nomenclature","volume":"87","author":"Alnemri","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0165","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1038\/12469","article-title":"Anti-cancer activity of targeted pro-apoptotic peptides","volume":"5","author":"Ellerby","year":"1999","journal-title":"Nat. Med."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0170","doi-asserted-by":"crossref","first-page":"3468","DOI":"10.1038\/srep03468","article-title":"Dual-targeting pro-apoptotic peptide for programmed cancer cell death via specific mitochondria damage","volume":"3","author":"Chen","year":"2013","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0175","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1126\/science.281.5381.1309","article-title":"Mitochondria and apoptosis","volume":"281","author":"Green","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0180","doi-asserted-by":"crossref","first-page":"3671","DOI":"10.1073\/pnas.88.9.3671","article-title":"Intracellular heterogeneity in mitochondrial membrane potentials revealed by a J-aggregate-forming lipophilic cation JC-1","volume":"88","author":"Smiley","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0185","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S1357-2725(99)00088-6","article-title":"Role of reactive oxygen species in apoptosis: implications for cancer therapy","volume":"32","author":"Mat\u00e9s","year":"2000","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0190","doi-asserted-by":"crossref","first-page":"3327","DOI":"10.1021\/bm301106p","article-title":"Peptide self-assembly on cell membranes to induce cell lysis","volume":"13","author":"Chen","year":"2012","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0195","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1002\/psc.678","article-title":"Investigation of penetratin peptides. Part 2. In vitro uptake of penetratin and two of its derivatives","volume":"11","author":"Letoha","year":"2005","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0200","article-title":"A novel cell penetrating peptide derived from human eosinophil cationic protein","volume":"8","author":"Fang","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0205","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1111\/j.1432-1033.1997.0240a.x","article-title":"The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rathepatocytes","volume":"243","author":"Blommaart","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0210","doi-asserted-by":"crossref","first-page":"10207","DOI":"10.1073\/pnas.92.22.10207","article-title":"Evidence for phosphatidylinositol 3-kinase as a regulator of endocytosis via activation of Rab5","volume":"92","author":"Li","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0215","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.jconrel.2009.01.018","article-title":"Cellular uptake mechanism and intracellular fate of hydrophobically modified glycol chitosan nanoparticles","volume":"135","author":"Nam","year":"2009","journal-title":"J. Control. Release"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0220","doi-asserted-by":"crossref","first-page":"3371","DOI":"10.1074\/jbc.M111240200","article-title":"Caveolin-1 is a negative regulator of caveolae-mediated endocytosis to the endoplasmic reticulum","volume":"277","author":"Le","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0225","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1042\/bj20031253","article-title":"Size-dependent internalization of particles via the pathways of clathrin- and caveolae-mediated endocytosis","volume":"377","author":"Rejman","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0230","doi-asserted-by":"crossref","first-page":"14845","DOI":"10.1021\/bi971843e","article-title":"Interaction of Alzheimer beta-amyloid peptide (1\u201340) with lipid membranes","volume":"36","author":"Terzi","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0235","doi-asserted-by":"crossref","first-page":"2326","DOI":"10.1021\/bm400618m","article-title":"Peptide fibrils with altered stability, activity, and cell selectivity","volume":"14","author":"Chen","year":"2013","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0240","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1016\/j.bbamem.2009.08.021","article-title":"Structure-function study of cathelicidin-derived bovine antimicrobial peptide BMAP-28: design of its cell-selective analogs by amino acid substitutions in the heptad repeat sequences","volume":"1788","author":"Ahmad","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0245","doi-asserted-by":"crossref","first-page":"2531","DOI":"10.1007\/s00726-014-1802-3","article-title":"Design and characterization of short antimicrobial peptides using leucine zipper templates with selectivity towards microorganisms","volume":"46","author":"Ahmad","year":"2014","journal-title":"Amino Acids"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0250","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1007\/s00726-010-0744-7","article-title":"Studies on the assembly of a leucine zipper antibacterial peptides and its analogs on to mammalian cells and bacteria","volume":"40","author":"Ahmad","year":"2011","journal-title":"Amino Acids"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0255","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1042\/BJ20110056","article-title":"Inducing toxicity by introducing a leucine-zipper-like motif in from antimicrobial peptide, magainin 2","volume":"436","author":"Pandey","year":"2011","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0260","doi-asserted-by":"crossref","first-page":"7920","DOI":"10.1021\/bi100729m","article-title":"Cell-selective lysis by novel analogues of melittin against human red blood cells and Escherichia coli","volume":"49","author":"Pandey","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0265","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1021\/jm301407k","article-title":"Characterization of antimicrobial, cytotoxic, and antiendotoxin properties of short peptides with different hydrophobic amino acids at \u201ca\u201d and \u201cd\u201d positions of a heptad repeat sequence","volume":"56","author":"Azmi","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0270","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1016\/j.peptides.2011.03.024","article-title":"Cell selectivity, mechanism of action and LPS-neutralizing activity of bovine myeloid antimicrobial peptide-18 (BMAP-18) and its analogs","volume":"32","author":"Lee","year":"2011","journal-title":"Peptides"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0275","doi-asserted-by":"crossref","first-page":"22029","DOI":"10.1074\/jbc.M602378200","article-title":"Utilization of an amphipathic leucine zipper sequence to design antibacterial peptides with simultaneous modulation of toxic activity against human red blood cells","volume":"281","author":"Ahmad","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0280","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1021\/cb500759p","article-title":"Computational design and experimental characterization of peptides intended for pH-dependent membrane insertion and pore formation","volume":"10","author":"Zhang","year":"2015","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0285","doi-asserted-by":"crossref","first-page":"2549","DOI":"10.1016\/j.bbamem.2007.06.012","article-title":"Membrane interactions of the hydrophobic segment of diacylglycerol kinase epsilon","volume":"1768","author":"Glukhov","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2016.05.012_bb0290","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1515\/BC.2004.035","article-title":"Degradation, receptor binding, insulin secreting and antihyperglycaemic actions of palmitate-derivatised native and Ala8-substituted GLP-1 analogues","volume":"385","author":"Green","year":"2004","journal-title":"Biol. Chem."},{"key":"10.1016\/j.bbamem.2016.05.012_bb0295","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1002\/cbdv.200690136","article-title":"Enzymatic degradation of beta- and mixed alpha, beta-oligopeptides","volume":"3","author":"Heck","year":"2006","journal-title":"Chem. Biodivers."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273616301869?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273616301869?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,5,16]],"date-time":"2020-05-16T17:17:33Z","timestamp":1589649453000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0005273616301869"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,8]]},"references-count":58,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2016,8]]}},"alternative-id":["S0005273616301869"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamem.2016.05.012","relation":{},"ISSN":["0005-2736"],"issn-type":[{"value":"0005-2736","type":"print"}],"subject":[],"published":{"date-parts":[[2016,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"From a pro-apoptotic peptide to a lytic peptide: One single residue mutation","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.2016.05.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}