{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T21:17:36Z","timestamp":1788297456142,"version":"build-2803163510"},"reference-count":44,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100013306","name":"National Institute of Science Education and Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100013306","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001502","name":"Department of Atomic Energy, Government of India","doi-asserted-by":"publisher","award":["RIN4002"],"award-info":[{"award-number":["RIN4002"]}],"id":[{"id":"10.13039\/501100001502","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2026,3]]},"DOI":"10.1016\/j.bpj.2026.01.045","type":"journal-article","created":{"date-parts":[[2026,1,29]],"date-time":"2026-01-29T17:46:50Z","timestamp":1769708810000},"page":"1366-1383","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Chikungunya virus E1 fusion loop-membrane interaction: Conserved residues and shallow insertion"],"prefix":"10.1016","volume":"125","author":[{"given":"Naresh Kumar","family":"Gudigamolla","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Birupaksha","family":"Das","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Preeti Pragya","family":"Panda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geetanjali","family":"Meher","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Saleem","family":"Mohammed","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tirumala Kumar","family":"Chowdary","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpj.2026.01.045_bib1","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1038\/nsmb.1455","article-title":"Mechanics of membrane fusion","volume":"15","author":"Chernomordik","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpj.2026.01.045_bib2","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1038\/nsmb.1456","article-title":"Viral membrane fusion","volume":"15","author":"Harrison","year":"2008","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bpj.2026.01.045_bib3","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1080\/10409230802058320","article-title":"Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme","volume":"43","author":"White","year":"2008","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.bpj.2026.01.045_bib4","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1038\/nrmicro1326","article-title":"Virus membrane-fusion proteins: more than one way to make a hairpin","volume":"4","author":"Kielian","year":"2006","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.bpj.2026.01.045_bib5","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1002\/cbic.200700386","article-title":"Fusion Peptides and Transmembrane Domains of Fusion Proteins are Characterized by Different but Specific Structural Properties","volume":"9","author":"Weise","year":"2008","journal-title":"Chembiochem"},{"key":"10.1016\/j.bpj.2026.01.045_bib6","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1023\/A:1010406920417","article-title":"Viral Fusion Peptides: A Tool Set to Disrupt and Connect Biological Membranes","volume":"20","author":"Tamm","year":"2000","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.bpj.2026.01.045_bib7","doi-asserted-by":"crossref","first-page":"12065","DOI":"10.1128\/JVI.79.18.12065-12076.2005","article-title":"Membrane Structures of the Hemifusion-Inducing Fusion Peptide Mutant G1S and the Fusion-Blocking Mutant G1V of Influenza Virus Hemagglutinin Suggest a Mechanism for Pore Opening in Membrane Fusion","volume":"79","author":"Li","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.bpj.2026.01.045_bib8","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1038\/289366a0","article-title":"Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 \u00c5 resolution","volume":"289","author":"Wilson","year":"1981","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2026.01.045_bib9","doi-asserted-by":"crossref","first-page":"13417","DOI":"10.1074\/jbc.271.23.13417","article-title":"H+-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region","volume":"271","author":"Durrer","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpj.2026.01.045_bib10","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 HA-2","volume":"262","author":"Lear","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpj.2026.01.045_bib11","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1006\/jmbi.1997.0931","article-title":"The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR","volume":"267","author":"Macosko","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpj.2026.01.045_bib12","doi-asserted-by":"crossref","first-page":"37467","DOI":"10.1074\/jbc.M110.153700","article-title":"Shallow boomerang-shaped influenza hemagglutinin G13A mutant structure promotes leaky membrane fusion","volume":"285","author":"Lai","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpj.2026.01.045_bib13","doi-asserted-by":"crossref","first-page":"3253","DOI":"10.1002\/2211-5463.13323","article-title":"Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies","volume":"11","author":"Lousa","year":"2021","journal-title":"FEBS Open Bio"},{"key":"10.1016\/j.bpj.2026.01.045_bib14","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1002\/2211-5463.13908","article-title":"Viral entry mechanisms: the role of molecular simulation in unlocking a key step in viral infections","volume":"15","author":"Val\u00e9rio","year":"2025","journal-title":"FEBS Open Bio"},{"key":"10.1016\/j.bpj.2026.01.045_bib15","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1093\/oxfordjournals.jbchem.a122137","article-title":"pH-Dependent Membrane Fusion Activity of a Synthetic Twenty Amino Acid Peptide with the Same Sequence as That of the Hydrophobic Segment of Influenza Virus Hemagglutinin 1","volume":"102","author":"Murata","year":"1987","journal-title":"J. Biochem."},{"key":"10.1016\/j.bpj.2026.01.045_bib16","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/0014-5793(89)81574-1","article-title":"Testing topological models for the membrane penetration of the fusion peptide of influenza virus hemagglutinin","volume":"257","author":"Brunner","year":"1989","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bpj.2026.01.045_bib17","doi-asserted-by":"crossref","first-page":"6103","DOI":"10.1021\/acs.langmuir.4c05071","article-title":"gp41 Fusion Peptide Alters the Properties of Lipid Monolayer at the Air\u2013Water Interface in a Cholesterol-Dependent Fashion: Implications in Membrane Fusion","volume":"41","author":"Panda","year":"2025","journal-title":"Langmuir"},{"key":"10.1016\/j.bpj.2026.01.045_bib18","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1529\/biophysj.107.109181","article-title":"HIV-1 Fusion Peptide Decreases Bending Energy and Promotes Curved Fusion Intermediates","volume":"93","author":"Tristram-Nagle","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2026.01.045_bib19","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1038\/nature09555","article-title":"Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography","volume":"468","author":"Voss","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2026.01.045_bib20","doi-asserted-by":"crossref","first-page":"4772","DOI":"10.1038\/s41467-022-32431-9","article-title":"Visualization of conformational changes and membrane remodeling leading to genome delivery by viral class-II fusion machinery","volume":"13","author":"Mangala Prasad","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpj.2026.01.045_bib21","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1083\/jcb.200507075","article-title":"Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion","volume":"171","author":"Liao","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bpj.2026.01.045_bib22","doi-asserted-by":"crossref","first-page":"4858","DOI":"10.1128\/JVI.02755-06","article-title":"Mutational Evidence of Internal Fusion Loops in Herpes Simplex Virus Glycoprotein B","volume":"81","author":"Hannah","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.bpj.2026.01.045_bib23","doi-asserted-by":"crossref","first-page":"3811","DOI":"10.1016\/j.bpj.2022.09.011","article-title":"The interaction of viral fusion peptides with lipid membranes","volume":"121","author":"Surmeier","year":"2022","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2026.01.045_bib24","doi-asserted-by":"crossref","first-page":"13362","DOI":"10.1073\/pnas.1301911110","article-title":"Characterization of an early-stage fusion intermediate of Sindbis virus using cryoelectron microscopy","volume":"110","author":"Cao","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2026.01.045_bib25","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4582","article-title":"Using evolutionary data to make sense of macromolecules with a \u201cface-lifted\u201d ConSurf","volume":"32","author":"Yariv","year":"2023","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpj.2026.01.045_bib26","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1002\/pro.256","article-title":"MPEx: A tool for exploring membrane proteins","volume":"18","author":"Snider","year":"2009","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpj.2026.01.045_bib27","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01561-20","article-title":"Acidic pH-induced conformational changes in chikungunya virus fusion protein, E1 - a spring-twisted region in the domain I-III linker acts as a hinge point for swivelling motion of domains","volume":"94","author":"Sahoo","year":"2020","journal-title":"J. Virol."},{"key":"10.1016\/j.bpj.2026.01.045_bib28","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1021\/bi00375a006","article-title":"Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids","volume":"26","author":"Chattopadhyay","year":"1987","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2026.01.045_bib29","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1007\/s00232-022-00224-2","article-title":"Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins","volume":"255","author":"Brahma","year":"2022","journal-title":"J. Membr. Biol."},{"key":"10.1016\/j.bpj.2026.01.045_bib31","series-title":"Measurement Techniques and Practices of Colloid and Interface Phenomena","first-page":"29","article-title":"Surface Pressure","author":"Imura","year":"2019"},{"key":"10.1016\/j.bpj.2026.01.045_bib30","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1002\/bip.10261","article-title":"Structure and function of membrane fusion peptides","volume":"66","author":"Tamm","year":"2002","journal-title":"Biopolymers"},{"key":"10.1016\/j.bpj.2026.01.045_bib32","series-title":"Membrane Protein \u2013 Lipid Interactions: Physics and Chemistry in the Bilayer","author":"Borrell","year":"2016"},{"key":"10.1016\/j.bpj.2026.01.045_bib33","doi-asserted-by":"crossref","first-page":"13226","DOI":"10.1074\/jbc.M110.181297","article-title":"The Final Conformation of the Complete Ectodomain of the HA2 Subunit of Influenza Hemagglutinin Can by Itself Drive Low pH-dependent Fusion","volume":"286","author":"Kim","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpj.2026.01.045_bib34","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/s42003-025-08040-9","article-title":"Viral fusion proteins of classes II and III recognize and reorganize complex biological membranes","volume":"8","author":"Poojari","year":"2025","journal-title":"Commun. Biol."},{"key":"10.1016\/j.bpj.2026.01.045_bib35","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/nature02165","article-title":"Structure of the dengue virus envelope protein after membrane fusion","volume":"427","author":"Modis","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.bpj.2026.01.045_bib36","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.chemphyslip.2014.03.003","article-title":"The three lives of viral fusion peptides","volume":"181","author":"Apell\u00e1niz","year":"2014","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.bpj.2026.01.045_bib37","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.virol.2005.09.036","article-title":"Class II virus membrane fusion proteins","volume":"344","author":"Kielian","year":"2006","journal-title":"Virology"},{"key":"10.1016\/j.bpj.2026.01.045_bib38","doi-asserted-by":"crossref","first-page":"14713","DOI":"10.1021\/bi980809c","article-title":"The preference of tryptophan for membrane interfaces","volume":"37","author":"Yau","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2026.01.045_bib39","first-page":"1457","article-title":"High-Resolution Conformation of Gramicidin A in a Lipid Bilayer by Solid-State NMR","volume":"261","author":"Ketchem","year":"1993","journal-title":"Science (1979)"},{"key":"10.1016\/j.bpj.2026.01.045_bib40","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1529\/biophysj.107.124206","article-title":"Role of Tryptophan Residues in Gramicidin Channel Organization and Function","volume":"95","author":"Chattopadhyay","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2026.01.045_bib41","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1529\/biophysj.104.043596","article-title":"Interaction of Melittin with Membrane Cholesterol: A Fluorescence Approach","volume":"87","author":"Raghuraman","year":"2004","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2026.01.045_bib42","doi-asserted-by":"crossref","first-page":"35a","DOI":"10.1016\/j.bpj.2016.11.221","article-title":"Study of Insertion of Dengue E into Lipid Bilayers by Neutron Reflectivity and Molecular Dynamics Simulations","volume":"112","author":"Vanegas","year":"2017","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2026.01.045_bib43","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01203-17","article-title":"Structure-Function Dissection of Pseudorabies Virus Glycoprotein B Fusion Loops","volume":"92","author":"Vallbracht","year":"2018","journal-title":"J. Virol."},{"key":"10.1016\/j.bpj.2026.01.045_bib44","doi-asserted-by":"crossref","first-page":"38141","DOI":"10.1074\/jbc.M206998200","article-title":"Sphingolipid and Cholesterol Dependence of Alphavirus Membrane Fusion","volume":"277","author":"Waarts","year":"2002","journal-title":"J. Biol. Chem."}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349526000615?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349526000615?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T20:43:31Z","timestamp":1788295411000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349526000615"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3]]},"references-count":44,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2026,3]]}},"alternative-id":["S0006349526000615"],"URL":"https:\/\/doi.org\/10.1016\/j.bpj.2026.01.045","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2026,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Chikungunya virus E1 fusion loop-membrane interaction: Conserved residues and shallow insertion","name":"articletitle","label":"Article Title"},{"value":"Biophysical Journal","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpj.2026.01.045","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Biophysical Society. Published by Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}