{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T10:09:52Z","timestamp":1762250992686},"reference-count":78,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[1995,3,1]],"date-time":"1995-03-01T00:00:00Z","timestamp":794016000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":6713,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Current Biology"],"published-print":{"date-parts":[[1995,3]]},"DOI":"10.1016\/s0960-9822(95)00057-1","type":"journal-article","created":{"date-parts":[[2004,9,25]],"date-time":"2004-09-25T17:16:56Z","timestamp":1096132616000},"page":"265-274","source":"Crossref","is-referenced-by-count":97,"title":["Structural characterization of viral fusion proteins"],"prefix":"10.1016","volume":"5","author":[{"given":"Frederick M.","family":"Hughson","sequence":"first","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0960-9822(95)00057-1_BIB1","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1146\/annurev.bi.56.070187.002053","article-title":"The structure and function of the hemagglutinin membrane glycoprotein of influenza virus","volume":"56","author":"Wiley","year":"1987","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB2","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1146\/annurev.bb.18.060189.001155","article-title":"Protein-mediated membrane fusion","volume":"18","author":"Stegmann","year":"1989","journal-title":"Annu Rev Biophys Biophys Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB3","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1146\/annurev.ph.52.030190.003331","article-title":"Viral and cellular membrane fusion proteins","volume":"52","author":"White","year":"1990","journal-title":"Annu Rev Physiol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB4","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1126\/science.1439803","article-title":"Membrane fusion","volume":"258","author":"White","year":"1992","journal-title":"Science"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB5","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1038\/356248a0","article-title":"A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion","volume":"356","author":"Blobel","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB6","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/0968-0004(91)90138-L","article-title":"Intracellular membrane fusion","volume":"16","author":"Wilson","year":"1991","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB7","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/S0960-9822(00)00051-8","article-title":"Implications of the SNARE hypothesis for intracellular membrane topology and dynamics","volume":"4","author":"Rothman","year":"1994","journal-title":"Curr Biol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB8","series-title":"Viral Fusion Mechanisms","first-page":"475","article-title":"Modeling protein-induced fusion mechanisms: insights from the relative stability of lipidic structures","author":"Siegel","year":"1993"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB9","doi-asserted-by":"crossref","first-page":"1716","DOI":"10.1016\/S0021-9258(18)53911-9","article-title":"Influenza hemagglutinin-mediated membrane fusion does not involve inverted phase lipid intermediates","volume":"268","author":"Stegmann","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB10","doi-asserted-by":"crossref","first-page":"1977","DOI":"10.1021\/bi00174a002","article-title":"Fusion of influenza virus with sialic acid-bearing target membranes","volume":"33","author":"Alford","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB11","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1038\/342555a0","article-title":"Patch clamp studies of single cell-fusion events mediated by a viral fusion protein","volume":"342","author":"Spruce","year":"1989","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB12","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1146\/annurev.pc.44.100193.002101","article-title":"Hydration forces","volume":"44","author":"Leikin","year":"1993","journal-title":"Annu Rev Phys Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB13","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0014-5793(90)80492-2","article-title":"An architecture for the fusion site of influenza hemagglutinin","volume":"276","author":"Bentz","year":"1990","journal-title":"FEBS Lett"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB14","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1126\/science.2814514","article-title":"Molecular mechanisms and forces involved in the adhesion and fusion of amphiphilic bilayers","volume":"246","author":"Helm","year":"1989","journal-title":"Science"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB15","series-title":"Cellular Receptors for Animal Viruses","first-page":"281","article-title":"Fusion of influenza virus in endosomes: role of the hemagglutinin","author":"White","year":"1994"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB16","series-title":"Viral Fusion Mechanisms","first-page":"67","article-title":"Fusion-protein membrane interactions as studied by hydrophobic photolabeling","author":"Brunner","year":"1993"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB17","series-title":"Viral Fusion Mechanisms","first-page":"89","article-title":"Influenza virus fusion: from models toward a mechanism","author":"Stegmann","year":"1993"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB18","series-title":"Viral Fusion Mechanisms","first-page":"113","article-title":"Toward a dissection of the influenza hemagglutinin-mediated membrane fusion pathway","author":"Clague","year":"1993"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB19","series-title":"Viral Fusion Mechanisms","first-page":"133","article-title":"The influenza virus hemagglutinin: membrane fusion activity in intact virions and reconstituted virosomes","author":"Wilschut","year":"1993"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB20","series-title":"Viral Fusion Mechanisms","first-page":"163","article-title":"Architecture of the influenza hemagglutinin fusion site","author":"Bentz","year":"1993"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB21","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1038\/newbio238145a0","article-title":"Crystalline antigen from the influenza virus envelope","volume":"238","author":"Brand","year":"1972","journal-title":"Nature New Biol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB22","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1038\/289366a0","article-title":"Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 \u00e5 resolution","volume":"289","author":"Wilson","year":"1981","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB23","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1038\/333426a0","article-title":"Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid","volume":"333","author":"Weis","year":"1988","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB24","doi-asserted-by":"crossref","first-page":"8388","DOI":"10.1021\/bi00447a018","article-title":"Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study","volume":"28","author":"Sauter","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB25","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/S0042-6822(83)80015-4","article-title":"Changes in the antigenicity of the hemagglutinin molecule of H3 influenza virus at acidic pH","volume":"126","author":"Webster","year":"1983","journal-title":"Virology"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB26","series-title":"The Origin of Pandemic Influenza Viruses","first-page":"8","article-title":"Antigenic structure of influenza virus haemagglutinin","author":"Daniels","year":"1985"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB27","doi-asserted-by":"crossref","first-page":"1459","DOI":"10.1002\/j.1460-2075.1987.tb02387.x","article-title":"The receptor-binding and membrane-fusion properties of influenza virus variants selected using anti-haemagglutinin monoclonal antibodies","volume":"6","author":"Daniels","year":"1987","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB28","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/371037a0","article-title":"Structure of influenza haemagglutinin at the pH of membrane fusion","volume":"371","author":"Bullough","year":"1994","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB29","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/0092-8674(85)90157-6","article-title":"Fusion mutants of the influenza virus hemagglutinin glycoprotein","volume":"40","author":"Daniels","year":"1985","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB30","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1128\/JVI.57.2.603-613.1986","article-title":"Variant influenza virus hemagglutinin that induces fusion at elevated pH","volume":"57","author":"Doms","year":"1986","journal-title":"J Virol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB31","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1128\/JVI.48.1.239-248.1983","article-title":"Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A\/PR\/8\/34-mediated hemolysis","volume":"48","author":"Yewdell","year":"1983","journal-title":"J Virol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB32","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1099\/0022-1317-64-8-1657","article-title":"Analyses of the antigenicity of influenza haemagglutinin at the pH optimum for virus- mediated membrane fusion","volume":"64","author":"Daniels","year":"1983","journal-title":"J Gen Virol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB33","doi-asserted-by":"crossref","first-page":"2887","DOI":"10.1083\/jcb.105.6.2887","article-title":"Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin","volume":"105","author":"White","year":"1987","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB34","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1002\/j.1460-2075.1986.tb04175.x","article-title":"Electron microscopy of the low pH structure of influenza virus haemagglutinin","volume":"5","author":"Ruigrok","year":"1986","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB35","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1099\/0022-1317-69-11-2785","article-title":"Studies on the structure of the influenza virus haemagglutinin at the pH of membrane fusion","volume":"69","author":"Ruigrok","year":"1988","journal-title":"J Gen Virol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB36","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/0092-8674(93)90260-W","article-title":"A spring-loaded mechanism for the conformational change of influenza hemagglutinin","volume":"73","author":"Carr","year":"1993","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB37","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1071\/BI9800441","article-title":"Influenza virus haemagglutinin. Structural predictions suggest that the fibrillar appearance is due to the presence of a coiled-coil","volume":"33","author":"Ward","year":"1980","journal-title":"Aust J Biol Sci"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB38","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1002\/j.1460-2075.1990.tb08075.x","article-title":"The structure of a membrane fusion mutant of the influenza virus haemagglutinin","volume":"9","author":"Weis","year":"1990","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB39","doi-asserted-by":"crossref","first-page":"4093","DOI":"10.1021\/bi00517a023","article-title":"Use of resonance energy transfer to monitor membrane fusion","volume":"20","author":"Struck","year":"1981","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB40","doi-asserted-by":"crossref","first-page":"5675","DOI":"10.1021\/bi00319a002","article-title":"Fluorescence method for measuring the kinetics of fusion between biological membranes","volume":"23","author":"Hoekstra","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB41","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1038\/300658a0","article-title":"Haemagglutinin of influenza virus expressed from a cloned gene promotes membrane fusion","volume":"300","author":"White","year":"1982","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB42","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1083\/jcb.101.1.19","article-title":"An efficient method for introducing macromolecules into living cells","volume":"101","author":"Doxsey","year":"1985","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB43","doi-asserted-by":"crossref","first-page":"3972","DOI":"10.1016\/S0021-9258(19)84948-7","article-title":"Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells","volume":"264","author":"Morris","year":"1989","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB44","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1083\/jcb.109.1.113","article-title":"Initial stages of influenza hemagglutinin-induced cell fusion monitored simultaneously by two fluorescent events: cytoplasmic continuity and lipid mixing","volume":"109","author":"Sarkar","year":"1989","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB45","doi-asserted-by":"crossref","first-page":"3824","DOI":"10.1128\/JVI.64.8.3824-3832.1990","article-title":"Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatment","volume":"64","author":"Puri","year":"1990","journal-title":"J Virol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB46","doi-asserted-by":"crossref","first-page":"4231","DOI":"10.1002\/j.1460-2075.1990.tb07871.x","article-title":"Intermediates in influenza induced membrane fusion","volume":"9","author":"Stegmann","year":"1990","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB47","doi-asserted-by":"crossref","first-page":"3153","DOI":"10.1073\/pnas.80.11.3153","article-title":"Hemolytic activity of influenza virus hemagglutinin glycoproteins activated in mildly acidic environments","volume":"80","author":"Sato","year":"1983","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB48","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/0005-2736(86)90111-2","article-title":"Temperature and pH dependence of the haemolytic activity of influenza virus and of the rotational mobility of the spike glycoproteins","volume":"854","author":"Junankar","year":"1986","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB49","doi-asserted-by":"crossref","first-page":"17744","DOI":"10.1016\/S0021-9258(18)45442-7","article-title":"Effects of low pH on influenza virus: activation and inactivation of the membrane fusion capacity of the hemagglutinin","volume":"262","author":"Stegmann","year":"1987","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB50","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1021\/bi00052a014","article-title":"Effects of exposure to low pH on the lateral mobility of influenza hemagglutinin expresses at the cell surface: correlation between mobility inhibition and inactivation","volume":"32","author":"Gutman","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB51","doi-asserted-by":"crossref","first-page":"2771","DOI":"10.1021\/bi00062a006","article-title":"A common mechanism for influenza virus fusion activity and inactivation","volume":"32","author":"Ramalho-Santos","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB52","series-title":"Viral Fusion Mechanisms","first-page":"437","article-title":"Kinetics and extent of virus-cell aggregation and fusion","author":"Nir","year":"1993"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB53","doi-asserted-by":"crossref","first-page":"3623","DOI":"10.1073\/pnas.88.9.3623","article-title":"The first milliseconds of the pore formed by a fusogenic viral envelope protein during membrane fusion","volume":"88","author":"Spruce","year":"1991","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB54","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/0092-8674(92)90140-8","article-title":"Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity","volume":"68","author":"Godley","year":"1992","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB55","doi-asserted-by":"crossref","first-page":"4940","DOI":"10.1128\/JVI.66.8.4940-4950.1992","article-title":"Intermonomer disulphide bonds impair the fusion activity of influenza virus hemagglutinin","volume":"66","author":"Kemble","year":"1992","journal-title":"J Virol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB56","doi-asserted-by":"crossref","first-page":"2973","DOI":"10.1016\/S0021-9258(18)89461-3","article-title":"Membrane fusion activity of the influenza virus hemagglutinin","volume":"260","author":"Doms","year":"1985","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB57","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1099\/0022-1317-73-4-995","article-title":"Low pH deforms the influenza virus envelope","volume":"73","author":"Ruigrok","year":"1992","journal-title":"J Gen Virol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB58","doi-asserted-by":"crossref","first-page":"18353","DOI":"10.1016\/S0021-9258(17)32314-1","article-title":"Evidence for H+-induced insertion of the influenza hemagglutinin HA2 N-terminal segment Into the viral membrane","volume":"269","author":"Weber","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB59","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/0042-6822(77)90380-4","article-title":"Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses","volume":"80","author":"Scheid","year":"1977","journal-title":"Virology"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB60","doi-asserted-by":"crossref","first-page":"2737","DOI":"10.1073\/pnas.75.6.2737","article-title":"Purification of the fusion protein of Sendai virus: analysis of the NH2-terminal sequence generated during precursor activation","volume":"75","author":"Gething","year":"1978","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB61","doi-asserted-by":"crossref","first-page":"3557","DOI":"10.1016\/S0021-9258(19)69645-6","article-title":"Activation of the Sendai virus fusion protein (F) involves a conformational change with exposure of a new hydrophobic region","volume":"256","author":"Hsu","year":"1981","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB62","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1083\/jcb.102.1.11","article-title":"Studies on the mechanism of membrane fusion: site specific mutagenesis of the hemagglutinin of influenza virus","volume":"102","author":"Gething","year":"1986","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB63","doi-asserted-by":"crossref","first-page":"1856","DOI":"10.1021\/bi00406a010","article-title":"Hydrophobic photolabeling identifies BHA2 as the subunit mediating the interaction of bromelain-solubilized influenza virus hemagglutinin with liposomes at low pH","volume":"27","author":"Harter","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB64","doi-asserted-by":"crossref","first-page":"6459","DOI":"10.1016\/S0021-9258(18)83370-1","article-title":"Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the \u2018fusion peptide\u2019","volume":"264","author":"Harter","year":"1989","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB65","doi-asserted-by":"crossref","first-page":"18404","DOI":"10.1016\/S0021-9258(18)55284-4","article-title":"The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion","volume":"266","author":"Stegmann","year":"1991","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB66","doi-asserted-by":"crossref","first-page":"20225","DOI":"10.1016\/S0021-9258(19)88690-8","article-title":"Lipid interactions of the hemagglutinin HA2 NH2-terminal segment during influenza virus-induced membrane fusion","volume":"267","author":"Tsurudome","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB67","doi-asserted-by":"crossref","first-page":"10211","DOI":"10.1021\/bi00106a020","article-title":"Membrane fusion activity of the influenza virus hemagglutinin: interaction of HA2 N-terminal peptides with phospholipid vesicles","volume":"30","author":"Rafalski","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB68","doi-asserted-by":"crossref","first-page":"6500","DOI":"10.1016\/S0021-9258(18)48270-1","article-title":"Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA2","volume":"262","author":"Lear","year":"1987","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB69","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.1099\/0022-1317-69-8-1847","article-title":"Membrane fusion by peptide analogues of influenza virus haemagglutinin","volume":"69","author":"Wharton","year":"1988","journal-title":"J Gen Virol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB70","doi-asserted-by":"crossref","first-page":"6257","DOI":"10.1021\/bi00478a021","article-title":"Conformation of membrane fusion-active 20-residue peptides with or without lipid bilayers. Implication of alpha-helix formation for membrane fusion","volume":"29","author":"Takahashi","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB71","doi-asserted-by":"crossref","first-page":"9792","DOI":"10.1021\/bi00088a034","article-title":"Orientation of fusion-active synthetic peptides in phospholipid bilayers: determination by Fourier transform infrared spectroscopy","volume":"32","author":"Ishiguro","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB72","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0005-2736(90)90163-I","article-title":"Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins","volume":"1029","author":"Brasseur","year":"1990","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB73","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1126\/science.7939662","article-title":"Insertion of a coiled-coil peptide from influenza hemagglutinin into membranes","volume":"266","author":"Yu","year":"1994","journal-title":"Science"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB74","series-title":"The Origin of Pandemic Influenza Viruses","first-page":"1","article-title":"Studies of the influenza virus haemagglutinin in the pH5 conformation","author":"Daniels","year":"1985"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB75","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/0092-8674(94)90344-1","article-title":"Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion","volume":"76","author":"Kemble","year":"1994","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB76","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1083\/jcb.122.6.1253","article-title":"GPI-\u00a0 and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity","volume":"122","author":"Kemble","year":"1993","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB77","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1107\/S0021889891004399","article-title":"MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures","volume":"24","author":"Kraulis","year":"1991","journal-title":"J Appl Cryst"},{"key":"10.1016\/S0960-9822(95)00057-1_BIB78","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/0022-2836(90)90234-D","article-title":"Refinement of the influenza virus hemagglutinin by simulated annealing","volume":"212","author":"Weis","year":"1990","journal-title":"J Molec Biol"}],"container-title":["Current Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0960982295000571?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0960982295000571?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,25]],"date-time":"2021-06-25T23:11:26Z","timestamp":1624662686000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0960982295000571"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,3]]},"references-count":78,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1995,3]]}},"alternative-id":["S0960982295000571"],"URL":"https:\/\/doi.org\/10.1016\/s0960-9822(95)00057-1","relation":{},"ISSN":["0960-9822"],"issn-type":[{"value":"0960-9822","type":"print"}],"subject":[],"published":{"date-parts":[[1995,3]]}}}