{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T14:25:04Z","timestamp":1778941504846,"version":"3.51.4"},"reference-count":63,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2018,3,26]],"date-time":"2018-03-26T00:00:00Z","timestamp":1522022400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001411","name":"Indian Council of Medical Research","doi-asserted-by":"publisher","award":["59\/58\/2012\/online\/BMS\/TRM"],"award-info":[{"award-number":["59\/58\/2012\/online\/BMS\/TRM"]}],"id":[{"id":"10.13039\/501100001411","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0194498","type":"journal-article","created":{"date-parts":[[2018,3,26]],"date-time":"2018-03-26T17:32:46Z","timestamp":1522085566000},"page":"e0194498","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":16,"title":["Heterogeneity in glycan composition on the surface of HIV-1 envelope determines virus sensitivity to lectins"],"prefix":"10.1371","volume":"13","author":[{"given":"Muzafar","family":"Jan","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chitra","family":"Upadhyay","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9","family":"Alcami Pertejo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Catarina E.","family":"Hioe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8294-5360","authenticated-orcid":true,"given":"Sunil K.","family":"Arora","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2018,3,26]]},"reference":[{"issue":"6929","key":"ref1","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nature01470","article-title":"Antibody neutralization and escape by HIV-1","volume":"422","author":"X Wei","year":"2003","journal-title":"Nature"},{"issue":"6","key":"ref2","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/nm0698-679","article-title":"A role for carbohydrates in immune evasion in AIDS","volume":"4","author":"JN Reitter","year":"1998","journal-title":"Nat Med"},{"issue":"9","key":"ref3","doi-asserted-by":"crossref","first-page":"4199","DOI":"10.1128\/JVI.76.9.4199-4211.2002","article-title":"Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response","volume":"76","author":"MI Quinones-Kochs","year":"2002","journal-title":"J Virol"},{"issue":"2","key":"ref4","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.virol.2010.02.019","article-title":"Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function","volume":"401","author":"D Eggink","year":"2010","journal-title":"Virology"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/1742-4690-5-10","article-title":"The carbohydrate at asparagine 386 on HIV-1 gp120 is not essential for protein folding and function but is involved in immune evasion","volume":"5","author":"RW Sanders","year":"2008","journal-title":"Retrovirology"},{"issue":"11","key":"ref6","doi-asserted-by":"crossref","first-page":"5637","DOI":"10.1128\/JVI.00105-10","article-title":"Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization","volume":"84","author":"JM Binley","year":"2010","journal-title":"J Virol"},{"issue":"6277","key":"ref7","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1126\/science.aad2450","article-title":"Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer","volume":"351","author":"JH Lee","year":"2016","journal-title":"Science"},{"issue":"4","key":"ref8","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1016\/j.cell.2016.04.010","article-title":"Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G","volume":"165","author":"GB Stewart-Jones","year":"2016","journal-title":"Cell"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1146\/annurev-immunol-041015-055515","article-title":"Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design","volume":"34","author":"DR Burton","year":"2016","journal-title":"Annu Rev Immunol"},{"issue":"3","key":"ref10","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/j.immuni.2012.08.012","article-title":"Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies","volume":"37","author":"PD Kwong","year":"2012","journal-title":"Immunity"},{"issue":"7365","key":"ref11","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1038\/nature10373","article-title":"Broad neutralization coverage of HIV by multiple highly potent antibodies","volume":"477","author":"LM Walker","year":"2011","journal-title":"Nature"},{"issue":"6059","key":"ref12","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1126\/science.1213256","article-title":"A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield","volume":"334","author":"R Pejchal","year":"2011","journal-title":"Science"},{"issue":"4","key":"ref13","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/j.chom.2012.09.008","article-title":"A Blueprint for HIV Vaccine Discovery","volume":"12","author":"DR Burton","year":"2012","journal-title":"Cell Host Microbe"},{"issue":"6244","key":"ref14","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1126\/science.aac5894","article-title":"HIV-1 VACCINES. Priming a broadly neutralizing antibody response to HIV-1 using a germline-targeting immunogen","volume":"349","author":"JG Jardine","year":"2015","journal-title":"Science"},{"issue":"10","key":"ref15","doi-asserted-by":"crossref","first-page":"2061","DOI":"10.1084\/jem.20132494","article-title":"Passive transfer of modest titers of potent and broadly neutralizing anti-HIV monoclonal antibodies block SHIV infection in macaques","volume":"211","author":"M Shingai","year":"2014","journal-title":"J Exp Med"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"14954","DOI":"10.1038\/ncomms14954","article-title":"Global site-specific N-glycosylation analysis of HIV envelope glycoprotein","volume":"8","author":"L Cao","year":"2017","journal-title":"Nat Commun"},{"issue":"11","key":"ref17","doi-asserted-by":"crossref","first-page":"2695","DOI":"10.1016\/j.celrep.2016.02.058","article-title":"Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein","volume":"14","author":"AJ Behrens","year":"2016","journal-title":"Cell Rep"},{"issue":"2","key":"ref18","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1021\/acschembio.6b00854","article-title":"Global N-Glycan Site Occupancy of HIV-1 gp120 by Metabolic Engineering and High-Resolution Intact Mass Spectrometry","volume":"12","author":"WB Struwe","year":"2017","journal-title":"ACS Chem Biol"},{"issue":"6","key":"ref19","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1007\/s13361-014-0859-2","article-title":"Absolute quantitation of glycosylation site occupancy using isotopically labeled standards and LC-MS","volume":"25","author":"Z Zhu","year":"2014","journal-title":"J Am Soc Mass Spectrom"},{"issue":"3","key":"ref20","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1038\/nprot.2007.73","article-title":"Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry","volume":"2","author":"H Hernandez","year":"2007","journal-title":"Nat Protoc"},{"issue":"3","key":"ref21","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1021\/pr300870t","article-title":"Characterization of host-cell line specific glycosylation profiles of early transmitted\/founder HIV-1 gp120 envelope proteins","volume":"12","author":"EP Go","year":"2013","journal-title":"J Proteome Res"},{"issue":"1","key":"ref22","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/10409239709085144","article-title":"Glycosylation: heterogeneity and the 3D structure of proteins","volume":"32","author":"PM Rudd","year":"1997","journal-title":"Crit Rev Biochem Mol Biol"},{"issue":"27","key":"ref23","doi-asserted-by":"crossref","first-page":"20860","DOI":"10.1074\/jbc.M109.085472","article-title":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition","volume":"285","author":"M Raska","year":"2010","journal-title":"J Biol Chem"},{"issue":"1","key":"ref24","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.jmb.2010.08.033","article-title":"Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity","volume":"403","author":"L Kong","year":"2010","journal-title":"J Mol Biol"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"7479","DOI":"10.1038\/ncomms8479","article-title":"Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies","volume":"6","author":"LK Pritchard","year":"2015","journal-title":"Nat Commun"},{"issue":"8","key":"ref26","doi-asserted-by":"crossref","first-page":"e23521","DOI":"10.1371\/journal.pone.0023521","article-title":"The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade","volume":"6","author":"C Bonomelli","year":"2011","journal-title":"PLoS One"},{"issue":"19","key":"ref27","doi-asserted-by":"crossref","first-page":"8644","DOI":"10.1128\/JVI.00853-16","article-title":"Induction of Heterologous Tier 2 HIV-1-Neutralizing and Cross-Reactive V1\/V2-Specific Antibodies in Rabbits by Prime-Boost Immunization","volume":"90","author":"S Townsley","year":"2016","journal-title":"J Virol"},{"issue":"5","key":"ref28","doi-asserted-by":"crossref","first-page":"e1004932","DOI":"10.1371\/journal.ppat.1004932","article-title":"Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site","volume":"11","author":"ET Crooks","year":"2015","journal-title":"PLoS Pathog"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1111\/j.1749-6632.1993.tb26256.x","article-title":"Reservoirs of HIV infection or carriage: monocytic, dendritic, follicular dendritic, and B cells","volume":"693","author":"J Laurence","year":"1993","journal-title":"Ann N Y Acad Sci"},{"issue":"9","key":"ref30","doi-asserted-by":"crossref","first-page":"4676","DOI":"10.4049\/jimmunol.1101876","article-title":"HIV-1 N-glycan composition governs a balance between dendritic cell-mediated viral transmission and antigen presentation","volume":"187","author":"T van Montfort","year":"2011","journal-title":"Journal of immunology"},{"issue":"8","key":"ref31","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1089\/aid.2016.0290","article-title":"Innate Sensing of HIV-1 by Dendritic Cell-Specific ICAM-3 Grabbing Nonintegrin on Dendritic Cells: Degradation and Presentation Versus Transmission of Virus to T Cells Is Determined by Glycan Composition of Viral Envelope","volume":"33","author":"M Jan","year":"2017","journal-title":"AIDS Res Hum Retroviruses"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.antiviral.2017.03.007","article-title":"Antiviral lectins: Selective inhibitors of viral entry","volume":"142","author":"CA Mitchell","year":"2017","journal-title":"Antiviral Res"},{"issue":"4927","key":"ref33","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1126\/science.2552581","article-title":"Lectins as cell recognition molecules","volume":"246","author":"N Sharon","year":"1989","journal-title":"Science"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.coviro.2014.05.006","article-title":"Antiviral lectins as potential HIV microbicides","volume":"7","author":"LM Koharudin","year":"2014","journal-title":"Curr Opin Virol"},{"issue":"9","key":"ref35","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1089\/aid.2016.0262","article-title":"Short Communication: Manalpha1-2Man-Binding Anti-HIV Lectins Enhance the Exposure of V2i and V3 Crown Neutralization Epitopes on the V1\/V2 and V3 Hypervariable Loops of HIV-1 Envelope","volume":"33","author":"M Jan","year":"2017","journal-title":"AIDS Res Hum Retroviruses"},{"issue":"2\u20133","key":"ref36","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.antiviral.2006.02.004","article-title":"Inhibition of HIV entry by carbohydrate-binding proteins","volume":"71","author":"J Balzarini","year":"2006","journal-title":"Antiviral Res"},{"issue":"2","key":"ref37","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.pbiomolbio.2004.05.001","article-title":"Proteins that bind high-mannose sugars of the HIV envelope","volume":"88","author":"I Botos","year":"2005","journal-title":"Prog Biophys Mol Biol"},{"issue":"1","key":"ref38","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1124\/mol.106.030155","article-title":"Carbohydrate-binding agents efficiently prevent dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN)-directed HIV-1 transmission to T lymphocytes","volume":"71","author":"J Balzarini","year":"2007","journal-title":"Mol Pharmacol"},{"issue":"17","key":"ref39","doi-asserted-by":"crossref","first-page":"9039","DOI":"10.1128\/JVI.02675-10","article-title":"Binding of the mannose-specific lectin, griffithsin, to HIV-1 gp120 exposes the CD4-binding site","volume":"85","author":"KB Alexandre","year":"2011","journal-title":"J Virol"},{"issue":"50","key":"ref40","doi-asserted-by":"crossref","first-page":"42900","DOI":"10.1074\/jbc.M111.274456","article-title":"The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entry","volume":"286","author":"KO Francois","year":"2011","journal-title":"J Biol Chem"},{"issue":"17","key":"ref41","doi-asserted-by":"crossref","first-page":"8411","DOI":"10.1128\/JVI.00369-06","article-title":"Mutational pathways, resistance profile, and side effects of cyanovirin relative to human immunodeficiency virus type 1 strains with N-glycan deletions in their gp120 envelopes","volume":"80","author":"J Balzarini","year":"2006","journal-title":"J Virol"},{"issue":"1","key":"ref42","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.virol.2007.06.029","article-title":"High-mannose-specific deglycosylation of HIV-1 gp120 induced by resistance to cyanovirin-N and the impact on antibody neutralization","volume":"368","author":"Q Hu","year":"2007","journal-title":"Virology"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"2367","DOI":"10.1099\/vir.0.033092-0","article-title":"Removal of two high-mannose N-linked glycans on gp120 renders human immunodeficiency virus 1 largely resistant to the carbohydrate-binding agent griffithsin","volume":"92","author":"X Huang","year":"2011","journal-title":"J Gen Virol"},{"issue":"7","key":"ref44","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1128\/AAC.41.7.1521","article-title":"Discovery of cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development","volume":"41","author":"MR Boyd","year":"1997","journal-title":"Antimicrob Agents Chemother"},{"issue":"10","key":"ref45","doi-asserted-by":"crossref","first-page":"9345","DOI":"10.1074\/jbc.M411122200","article-title":"Isolation and characterization of griffithsin, a novel HIV-inactivating protein, from the red alga Griffithsia sp","volume":"280","author":"T Mori","year":"2005","journal-title":"J Biol Chem"},{"issue":"9","key":"ref46","doi-asserted-by":"crossref","first-page":"2578","DOI":"10.1021\/bi0205698","article-title":"A potent novel anti-HIV protein from the cultured cyanobacterium Scytonema varium","volume":"42","author":"HR Bokesch","year":"2003","journal-title":"Biochemistry"},{"issue":"5","key":"ref47","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1016\/j.str.2017.03.015","article-title":"The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans","volume":"25","author":"JTS Hopper","year":"2017","journal-title":"Structure"},{"issue":"11","key":"ref48","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1021\/acsinfecdis.6b00139","article-title":"Binding Site Geometry and Subdomain Valency Control Effects of Neutralizing Lectins on HIV-1 Viral Particles","volume":"2","author":"S Lusvarghi","year":"2016","journal-title":"ACS Infect Dis"},{"issue":"5","key":"ref49","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.1042\/BST20130154","article-title":"The antiviral lectin cyanovirin-N: probing multivalency and glycan recognition through experimental and computational approaches","volume":"41","author":"BW Woodrum","year":"2013","journal-title":"Biochem Soc Trans"},{"issue":"4","key":"ref50","doi-asserted-by":"crossref","first-page":"2855","DOI":"10.1128\/JVI.72.4.2855-2864.1998","article-title":"Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1","volume":"72","author":"EJ Platt","year":"1998","journal-title":"J Virol"},{"issue":"3","key":"ref51","doi-asserted-by":"crossref","first-page":"1414","DOI":"10.1128\/JVI.80.3.1414-1426.2006","article-title":"Characterization of antibody responses elicited by human immunodeficiency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants","volume":"80","author":"Y Li","year":"2006","journal-title":"J Virol"},{"issue":"16","key":"ref52","doi-asserted-by":"crossref","first-page":"10108","DOI":"10.1128\/JVI.79.16.10108-10125.2005","article-title":"Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies","volume":"79","author":"M Li","year":"2005","journal-title":"Journal of virology"},{"issue":"13","key":"ref53","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1089\/aid.1998.14.1129","article-title":"Effect of major deletions in the V1 and V2 loops of a macrophage-tropic HIV type 1 isolate on viral envelope structure, cell entry, and replication","volume":"14","author":"L Stamatatos","year":"1998","journal-title":"AIDS Res Hum Retroviruses"},{"key":"ref54","first-page":"Unit 12.1","article-title":"Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays","volume":"Chapter 12","author":"DC Montefiori","year":"2005","journal-title":"Curr Protoc Immunol"},{"issue":"17","key":"ref55","doi-asserted-by":"crossref","first-page":"9002","DOI":"10.1128\/JVI.00423-09","article-title":"The infectious molecular clone and pseudotyped virus models of human immunodeficiency virus type 1 exhibit significant differences in virion composition with only moderate differences in infectivity and inhibition sensitivity","volume":"83","author":"NM Provine","year":"2009","journal-title":"J Virol"},{"issue":"31","key":"ref56","doi-asserted-by":"crossref","first-page":"13800","DOI":"10.1073\/pnas.1006498107","article-title":"Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens","volume":"107","author":"KJ Doores","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/1479-5876-5-28","article-title":"Differential in vitro inhibitory activity against HIV-1 of alpha-(1\u20133)- and alpha-(1\u20136)-D-mannose specific plant lectins: implication for microbicide development","volume":"5","author":"H Saidi","year":"2007","journal-title":"J Transl Med"},{"issue":"3","key":"ref58","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1128\/AAC.35.3.410","article-title":"Alpha-(1\u20133)- and alpha-(1\u20136)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro","volume":"35","author":"J Balzarini","year":"1991","journal-title":"Antimicrob Agents Chemother"},{"issue":"1","key":"ref59","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.virol.2010.03.021","article-title":"Mannose-rich glycosylation patterns on HIV-1 subtype C gp120 and sensitivity to the lectins, Griffithsin, Cyanovirin-N and Scytovirin","volume":"402","author":"KB Alexandre","year":"2010","journal-title":"Virology"},{"issue":"21","key":"ref60","doi-asserted-by":"crossref","first-page":"13419","DOI":"10.1073\/pnas.212519299","article-title":"Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line","volume":"99","author":"PJ Reeves","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"23","key":"ref61","doi-asserted-by":"crossref","first-page":"9248","DOI":"10.1073\/pnas.85.23.9248","article-title":"Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1","volume":"85","author":"DC Montefiori","year":"1988","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"issue":"3","key":"ref62","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.str.2007.01.011","article-title":"Glycoprotein structural genomics: solving the glycosylation problem","volume":"15","author":"VT Chang","year":"2007","journal-title":"Structure"},{"issue":"9","key":"ref63","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1016\/j.str.2010.05.016","article-title":"Monomerization of viral entry inhibitor griffithsin elucidates the relationship between multivalent binding to carbohydrates and anti-HIV activity","volume":"18","author":"T Moulaei","year":"2010","journal-title":"Structure"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0194498","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,10,30]],"date-time":"2020-10-30T05:55:25Z","timestamp":1604037325000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0194498"}},"subtitle":[],"editor":[{"given":"Stefan","family":"P\u00f6hlmann","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2018,3,26]]},"references-count":63,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2018,3,26]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0194498","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,3,26]]}}}