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Immunofocusing of the antibody response to mimic natural host\u2013receptor interactions reveals a key point of vulnerability on the JUNV surface.<\/jats:p>","DOI":"10.1073\/pnas.1702127114","type":"journal-article","created":{"date-parts":[[2017,7,3]],"date-time":"2017-07-03T16:10:43Z","timestamp":1499098243000},"page":"7031-7036","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":42,"title":["Convergent immunological solutions to Argentine hemorrhagic fever virus neutralization"],"prefix":"10.1073","volume":"114","author":[{"given":"Antra","family":"Zeltina","sequence":"first","affiliation":[{"name":"Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefanie A.","family":"Krumm","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, Guy\u2019s Hospital, King\u2019s College London, London SE1 9RT, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mehmet","family":"Sahin","sequence":"additional","affiliation":[{"name":"Division of Experimental Virology, Department of Biomedicine, University of Basel, Basel CH-4051, Switzerland;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weston B.","family":"Struwe","sequence":"additional","affiliation":[{"name":"Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl","family":"Harlos","sequence":"additional","affiliation":[{"name":"Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jack H.","family":"Nunberg","sequence":"additional","affiliation":[{"name":"Montana Biotechnology Center, University of Montana, Missoula, MT 59812;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Max","family":"Crispin","sequence":"additional","affiliation":[{"name":"Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;"},{"name":"Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel D.","family":"Pinschewer","sequence":"additional","affiliation":[{"name":"Division of Experimental Virology, Department of Biomedicine, University of Basel, Basel CH-4051, Switzerland;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katie J.","family":"Doores","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, Guy\u2019s Hospital, King\u2019s College London, London SE1 9RT, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas A.","family":"Bowden","sequence":"additional","affiliation":[{"name":"Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2017,6,19]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3390\/pathogens4020283","article-title":"Human hemorrhagic fever causing arenaviruses: Molecular mechanisms contributing to virus virulence and disease pathogenesis","volume":"4","author":"Shao J","year":"2015","unstructured":"J Shao, Y Liang, H Ly, Human hemorrhagic fever causing arenaviruses: Molecular mechanisms contributing to virus virulence and disease pathogenesis. 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Science 336, 1030\u20131033 (2012).","journal-title":"Science"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy AJ","year":"2007","unstructured":"AJ McCoy, , Phaser crystallographic software. J Appl Crystallogr 40, 658\u2013674 (2007).","journal-title":"J Appl Crystallogr"},{"key":"e_1_3_4_46_2","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1002\/pro.2619","article-title":"Structural features of interfacial tyrosine residue in ROBO1 fibronectin domain-antibody complex: Crystallographic, thermodynamic, and molecular dynamic analyses","volume":"24","author":"Nakayama T","year":"2015","unstructured":"T Nakayama, , Structural features of interfacial tyrosine residue in ROBO1 fibronectin domain-antibody complex: Crystallographic, thermodynamic, and molecular dynamic analyses. Protein Sci 24, 328\u2013340 (2015).","journal-title":"Protein Sci"},{"key":"e_1_3_4_47_2","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: Model-building tools for molecular graphics","volume":"60","author":"Emsley P","year":"2004","unstructured":"P Emsley, K Cowtan, Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126\u20132132 (2004).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_48_2","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov GN","year":"2011","unstructured":"GN Murshudov, , REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67, 355\u2013367 (2011).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_49_2","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/S0076-6879(03)74014-2","article-title":"Macromolecular TLS refinement in REFMAC at moderate resolutions","volume":"374","author":"Winn MD","year":"2003","unstructured":"MD Winn, GN Murshudov, MZ Papiz, Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol 374, 300\u2013321 (2003).","journal-title":"Methods Enzymol"},{"key":"e_1_3_4_50_2","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1107\/S0907444906005270","article-title":"Optimal description of a protein structure in terms of multiple groups undergoing TLS motion","volume":"62","author":"Painter J","year":"2006","unstructured":"J Painter, EA Merritt, Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 62, 439\u2013450 (2006).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_51_2","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: All-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen VB","year":"2010","unstructured":"VB Chen, , MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_52_2","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1038\/nsmb.3115","article-title":"Privateer: Software for the conformational validation of carbohydrate structures","volume":"22","author":"Agirre J","year":"2015","unstructured":"J Agirre, , Privateer: Software for the conformational validation of carbohydrate structures. Nat Struct Mol Biol 22, 833\u2013834 (2015).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_53_2","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1038\/cr.2009.6","article-title":"DOG 1.0: Illustrator of protein domain structures","volume":"19","author":"Ren J","year":"2009","unstructured":"J Ren, , DOG 1.0: Illustrator of protein domain structures. Cell Res 19, 271\u2013273 (2009).","journal-title":"Cell Res"},{"key":"e_1_3_4_54_2","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel E","year":"2007","unstructured":"E Krissinel, K Henrick, Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774\u2013797 (2007).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_55_2","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","volume":"7","author":"Sievers F","year":"2011","unstructured":"F Sievers, , Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 7, 539 (2011).","journal-title":"Mol Syst Biol"},{"key":"e_1_3_4_56_2","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert X","year":"2014","unstructured":"X Robert, P Gouet, Deciphering key features in protein structures with the new ENDscript server. 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