{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,10]],"date-time":"2026-11-10T21:39:20Z","timestamp":1794346760355,"version":"4.9.0"},"reference-count":50,"publisher":"Springer Science and Business Media LLC","issue":"11","license":[{"start":{"date-parts":[[2019,7,15]],"date-time":"2019-07-15T00:00:00Z","timestamp":1563148800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2019,7,15]],"date-time":"2019-07-15T00:00:00Z","timestamp":1563148800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Microbiol"],"DOI":"10.1038\/s41564-019-0499-1","type":"journal-article","created":{"date-parts":[[2019,7,15]],"date-time":"2019-07-15T12:03:18Z","timestamp":1563192198000},"page":"1805-1814","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":64,"title":["Structure of S-layer protein Sap reveals a mechanism for therapeutic intervention in anthrax"],"prefix":"10.1038","volume":"4","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4065-0839","authenticated-orcid":false,"given":"Antonella","family":"Fioravanti","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Filip","family":"Van Hauwermeiren","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8783-1194","authenticated-orcid":false,"given":"Sander E.","family":"Van der Verren","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wim","family":"Jonckheere","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amanda","family":"Goncalves","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2466-0172","authenticated-orcid":false,"given":"Els","family":"Pardon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Steyaert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Henri","family":"De Greve","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4898-7663","authenticated-orcid":false,"given":"Mohamed","family":"Lamkanfi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9775-4102","authenticated-orcid":false,"given":"Han","family":"Remaut","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,7,15]]},"reference":[{"key":"499_CR1","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.3201\/eid0810.020353","volume":"8","author":"DB Jernigan","year":"2002","unstructured":"Jernigan, D. B. et al. Investigation of bioterrorism-related anthrax, United States, 2001: epidemiologic findings. Emerg. Infect. Dis. 8, 1019\u20131028 (2002).","journal-title":"Emerg. Infect. Dis."},{"key":"499_CR2","doi-asserted-by":"publisher","first-page":"1333","DOI":"10.1164\/rccm.201102-0209CI","volume":"184","author":"DA Sweeney","year":"2011","unstructured":"Sweeney, D. A., Hicks, C. W., Cui, X., Li, Y. & Eichacker, P. Q. Anthrax infection. Am. J. Respir. Crit. Care Med. 184, 1333\u20131341 (2011).","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"499_CR3","doi-asserted-by":"publisher","first-page":"6448","DOI":"10.1128\/JB.184.23.6448-6456.2002","volume":"184","author":"E Couture-Tosi","year":"2002","unstructured":"Couture-Tosi, E. et al. Structural analysis and evidence for dynamic emergence of Bacillus anthracis S-layer networks. J. Bacteriol. 184, 6448\u20136456 (2002).","journal-title":"J. Bacteriol."},{"key":"499_CR4","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1146\/annurev.cellbio.19.111301.140655","volume":"19","author":"RJ Collier","year":"2003","unstructured":"Collier, R. J. & Young, J. A. Anthrax toxin. Annu. Rev. Cell Dev. Biol. 19, 45\u201370 (2003).","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"499_CR5","doi-asserted-by":"publisher","first-page":"437","DOI":"10.1042\/bj0630437","volume":"63","author":"HT Zwartouw","year":"1956","unstructured":"Zwartouw, H. T. & Smith, H. Polyglutamic acid from Bacillus anthracis grown in vivo; structure and aggressin activity. Biochem. J. 63, 437\u2013442 (1956).","journal-title":"Biochem. J."},{"key":"499_CR6","doi-asserted-by":"publisher","first-page":"722","DOI":"10.1128\/jb.171.2.722-730.1989","volume":"171","author":"S Makino","year":"1989","unstructured":"Makino, S., Uchida, I., Terakado, N., Sasakawa, C. & Yoshikawa, M. Molecular characterization and protein analysis of the cap region, which is essential for encapsulation in Bacillus anthracis. J. Bacteriol. 171, 722\u2013730 (1989).","journal-title":"J. Bacteriol."},{"key":"499_CR7","doi-asserted-by":"publisher","first-page":"1626","DOI":"10.1128\/IAI.06061-11","volume":"80","author":"ZP Weiner","year":"2012","unstructured":"Weiner, Z. P. & Glomski, I. J. Updating perspectives on the initiation of Bacillus anthracis growth and dissemination through its host. Infect. Immun. 80, 1626\u20131633 (2012).","journal-title":"Infect. Immun."},{"key":"499_CR8","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1111\/j.1365-2958.2005.04718.x","volume":"57","author":"T Candela","year":"2005","unstructured":"Candela, T. & Fouet, A. Bacillus anthracis CapD, belonging to the gamma-glutamyltranspeptidase family, is required for the covalent anchoring of capsule to peptidoglycan. Mol. Microbiol. 57, 717\u2013726 (2005).","journal-title":"Mol. Microbiol."},{"key":"499_CR9","doi-asserted-by":"publisher","first-page":"859","DOI":"10.1128\/JB.182.4.859-868.2000","volume":"182","author":"M Sara","year":"2000","unstructured":"Sara, M. & Sleytr, U. B. S-layer proteins. J. Bacteriol. 182, 859\u2013868 (2000).","journal-title":"J. Bacteriol."},{"key":"499_CR10","doi-asserted-by":"publisher","first-page":"1877","DOI":"10.1007\/s11274-015-1952-9","volume":"31","author":"E Gerbino","year":"2015","unstructured":"Gerbino, E., Carasi, P., Mobili, P., Serradell, M. A. & Gomez-Zavaglia, A. Role of S-layer proteins in bacteria. World J. Microbiol. Biotechnol. 31, 1877\u20131887 (2015).","journal-title":"World J. Microbiol. Biotechnol."},{"key":"499_CR11","doi-asserted-by":"publisher","first-page":"1615","DOI":"10.1046\/j.1365-2958.2002.02852.x","volume":"43","author":"T Mignot","year":"2002","unstructured":"Mignot, T., Mesnage, S., Couture-Tosi, E., Mock, M. & Fouet, A. Developmental switch of S-layer protein synthesis in Bacillus anthracis. Mol. Microbiol. 43, 1615\u20131627 (2002).","journal-title":"Mol. Microbiol."},{"key":"499_CR12","doi-asserted-by":"publisher","first-page":"1147","DOI":"10.1046\/j.1365-2958.1997.2941659.x","volume":"23","author":"S Mesnage","year":"1997","unstructured":"Mesnage, S., Tosi-Couture, E., Mock, M., Gounon, P. & Fouet, A. Molecular characterization of the Bacillus anthracis main S-layer component: evidence that it is the major cell-associated antigen. Mol. Microbiol. 23, 1147\u20131155 (1997).","journal-title":"Mol. Microbiol."},{"key":"499_CR13","doi-asserted-by":"publisher","first-page":"3833","DOI":"10.1128\/JB.00402-12","volume":"194","author":"VJ Kern","year":"2012","unstructured":"Kern, V. J., Kern, J. W., Theriot, J. A., Schneewind, O. & Missiakas, D. Surface-layer (S-layer) proteins Sap and EA1 govern the binding of the S-layer-associated protein BslO at the cell septa of Bacillus anthracis. J. Bacteriol. 194, 3833\u20133840 (2012).","journal-title":"J. Bacteriol."},{"key":"499_CR14","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1038\/nature11155","volume":"487","author":"E Baranova","year":"2012","unstructured":"Baranova, E. et al. SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly. Nature 487, 119\u2013122 (2012).","journal-title":"Nature"},{"key":"499_CR15","doi-asserted-by":"publisher","first-page":"26042","DOI":"10.1074\/jbc.M111.248070","volume":"286","author":"J Kern","year":"2011","unstructured":"Kern, J. et al. Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein. J. Biol. Chem. 286, 26042\u201326049 (2011).","journal-title":"J. Biol. Chem."},{"key":"499_CR16","doi-asserted-by":"publisher","first-page":"1949","DOI":"10.1021\/acs.biochem.8b00060","volume":"57","author":"D Sychantha","year":"2018","unstructured":"Sychantha, D. et al. Molecular basis for the attachment of S-layer proteins to the cell wall of Bacillus anthracis. Biochemistry 57, 1949\u20131953 (2018).","journal-title":"Biochemistry"},{"key":"499_CR17","doi-asserted-by":"publisher","first-page":"1485","DOI":"10.1099\/mic.0.27832-0","volume":"151","author":"T Candela","year":"2005","unstructured":"Candela, T., Mignot, T., Hagnerelle, X., Haustant, M. & Fouet, A. Genetic analysis of Bacillus anthracis Sap S-layer protein crystallization domain. Microbiology 151, 1485\u20131490 (2005).","journal-title":"Microbiology"},{"key":"499_CR18","doi-asserted-by":"publisher","first-page":"1226","DOI":"10.1016\/j.str.2008.05.012","volume":"16","author":"T Pavkov","year":"2008","unstructured":"Pavkov, T. et al. The structure and binding behavior of the bacterial cell surface layer protein SbsC. Structure 16, 1226\u20131237 (2008).","journal-title":"Structure"},{"key":"499_CR19","doi-asserted-by":"publisher","first-page":"147","DOI":"10.1002\/mabi.200900175","volume":"10","author":"LM Teixeira","year":"2010","unstructured":"Teixeira, L. M. et al. Entropically driven self-assembly of Lysinibacillus sphaericus S-layer proteins analyzed under various environmental conditions. Macromol. Biosci. 10, 147\u2013155 (2010).","journal-title":"Macromol. Biosci."},{"key":"499_CR20","doi-asserted-by":"publisher","first-page":"180","DOI":"10.1021\/nn502992x","volume":"9","author":"B Rad","year":"2015","unstructured":"Rad, B. et al. Ion-specific control of the self-assembly dynamics of a nanostructured protein lattice. ACS Nano 9, 180\u2013190 (2015).","journal-title":"ACS Nano"},{"key":"499_CR21","doi-asserted-by":"publisher","first-page":"eaah6813","DOI":"10.1126\/scitranslmed.aah6813","volume":"9","author":"JA Kirk","year":"2017","unstructured":"Kirk, J. A. et al. New class of precision antimicrobials redefines role of Clostridium difficile S-layer in virulence and viability. Sci. Transl. Med. 9, eaah6813 (2017).","journal-title":"Sci. Transl. Med."},{"key":"499_CR22","doi-asserted-by":"publisher","first-page":"5826","DOI":"10.1002\/smll.201501413","volume":"11","author":"XY Wang","year":"2015","unstructured":"Wang, X. Y. et al. A S-layer protein of Bacillus anthracis as a building block for functional protein arrays by in vitro self-assembly. Small 11, 5826\u20135832 (2015).","journal-title":"Small"},{"key":"499_CR23","doi-asserted-by":"publisher","first-page":"1314","DOI":"10.1073\/pnas.1008560108","volume":"108","author":"K Domanska","year":"2011","unstructured":"Domanska, K. et al. Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic \u03b22-microglobulin variant. Proc. Natl Acad. Sci. USA 108, 1314\u20131319 (2011).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"499_CR24","doi-asserted-by":"publisher","first-page":"2807","DOI":"10.1128\/AAC.45.10.2807-2812.2001","volume":"45","author":"KE Conrath","year":"2001","unstructured":"Conrath, K. E. et al. \u03b2-lactamase inhibitors derived from single-domain antibody fragments elicited in the Camelidae. Antimicrob. Agents Chemother. 45, 2807\u20132812 (2001).","journal-title":"Antimicrob. Agents Chemother."},{"key":"499_CR25","doi-asserted-by":"publisher","first-page":"674","DOI":"10.1038\/nprot.2014.039","volume":"9","author":"E Pardon","year":"2014","unstructured":"Pardon, E. et al. A general protocol for the generation of nanobodies for structural biology. Nat. Protoc. 9, 674\u2013693 (2014).","journal-title":"Nat. Protoc."},{"key":"499_CR26","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1107\/S0907444909047337","volume":"66","author":"W Kabsch","year":"2010","unstructured":"Kabsch, W. Xds. Acta Crystallogr. D 66, 125\u2013132 (2010).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR27","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1107\/S0907444911007773","volume":"67","author":"C Vonrhein","year":"2011","unstructured":"Vonrhein, C. et al. Data processing and analysis with the autoPROC toolbox. Acta Crystallogr. D 67, 293\u2013302 (2011).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR28","doi-asserted-by":"publisher","first-page":"479","DOI":"10.1107\/S0907444909038360","volume":"66","author":"GM Sheldrick","year":"2010","unstructured":"Sheldrick, G. M. Experimental phasing with SHELXC\/D\/E: combining chain tracing with density modification. Acta Crystallogr. D 66, 479\u2013485 (2010).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR29","doi-asserted-by":"publisher","first-page":"2023","DOI":"10.1107\/S0907444903017694","volume":"59","author":"G Bricogne","year":"2003","unstructured":"Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M. & Paciorek, W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D 59, 2023\u20132030 (2003).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR30","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1107\/S0907444995008754","volume":"52","author":"JP Abrahams","year":"1996","unstructured":"Abrahams, J. P. & Leslie, A. G. W. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D 52, 30\u201342 (1996).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR31","doi-asserted-by":"publisher","first-page":"760","DOI":"10.1107\/S0907444994003112","volume":"50","author":"Collaborative Computational Project, Number 4.","year":"1994","unstructured":"Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760\u2013763 (1994).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR32","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1107\/S090744499500761X","volume":"52","author":"KD Cowtan","year":"1996","unstructured":"Cowtan, K. D. & Main, P. Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr. D 52, 43\u201348 (1996).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR33","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR34","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1107\/S0907444996012255","volume":"53","author":"GN Murshudov","year":"1997","unstructured":"Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240\u2013255 (1997).","journal-title":"Acta Crystallogr. D"},{"key":"499_CR35","doi-asserted-by":"crossref","unstructured":"BUSTER v.2.10.3 (Global Phasing Ltd, 2017).","DOI":"10.1016\/S1365-6937(17)30049-7"},{"key":"499_CR36","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1107\/S0021889807021206","volume":"40","author":"AJ McCoy","year":"2007","unstructured":"McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658\u2013674 (2007).","journal-title":"J. Appl. Cryst."},{"key":"499_CR37","doi-asserted-by":"publisher","first-page":"478","DOI":"10.1016\/S0968-0004(00)89105-7","volume":"20","author":"L Holm","year":"1995","unstructured":"Holm, L. & Sander, C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20, 478\u2013480 (1995).","journal-title":"Trends Biochem. Sci."},{"key":"499_CR38","first-page":"275","volume":"8","author":"DT Jones","year":"1992","unstructured":"Jones, D. T., Taylor, W. R. & Thornton, J. M. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8, 275\u2013282 (1992).","journal-title":"Comput. Appl. Biosci."},{"key":"499_CR39","doi-asserted-by":"publisher","first-page":"1792","DOI":"10.1093\/nar\/gkh340","volume":"32","author":"RC Edgar","year":"2004","unstructured":"Edgar, R. C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792\u20131797 (2004).","journal-title":"Nucleic Acids Res."},{"key":"499_CR40","doi-asserted-by":"publisher","first-page":"1870","DOI":"10.1093\/molbev\/msw054","volume":"33","author":"S Kumar","year":"2016","unstructured":"Kumar, S., Stecher, G. & Tamura, K. MEGA7: Molecular Evolutionary Genetics Analysis version 7.0 for bigger datasets. Mol. Biol. Evol. 33, 1870\u20131874 (2016).","journal-title":"Mol. Biol. Evol."},{"key":"499_CR41","doi-asserted-by":"publisher","first-page":"342","DOI":"10.1107\/S0021889812007662","volume":"45","author":"MV Petoukhov","year":"2012","unstructured":"Petoukhov, M. V. et al. New developments in the ATSAS program package for small-angle scattering data analysis. J. Appl. Cryst. 45, 342\u2013350 (2012).","journal-title":"J. Appl. Cryst."},{"key":"499_CR42","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1107\/S0021889892001663","volume":"25","author":"D Svergun","year":"1992","unstructured":"Svergun, D. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 25, 495\u2013503 (1992).","journal-title":"J. Appl. Cryst."},{"key":"499_CR43","doi-asserted-by":"publisher","first-page":"768","DOI":"10.1107\/S0021889895007047","volume":"28","author":"D Svergun","year":"1995","unstructured":"Svergun, D., Barberato, C. & Koch, M. H. J. CRYSOL\u2014a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Cryst. 28, 768\u2013773 (1995).","journal-title":"J. Appl. Cryst."},{"key":"499_CR44","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1107\/S0021889800014126","volume":"34","author":"MB Kozin","year":"2001","unstructured":"Kozin, M. B. & Svergun, D. I. Automated matching of high- and low-resolution structural models. J. Appl. Cryst. 34, 33\u201341 (2001).","journal-title":"J. Appl. Cryst."},{"key":"499_CR45","doi-asserted-by":"publisher","first-page":"331","DOI":"10.1038\/nmeth.4193","volume":"14","author":"SQ Zheng","year":"2017","unstructured":"Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331\u2013332 (2017).","journal-title":"Nat. Methods"},{"key":"499_CR46","doi-asserted-by":"publisher","first-page":"216","DOI":"10.1016\/j.jsb.2015.08.008","volume":"192","author":"A Rohou","year":"2015","unstructured":"Rohou, A. & Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216\u2013221 (2015).","journal-title":"J. Struct. Biol."},{"key":"499_CR47","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","volume":"180","author":"SH Scheres","year":"2012","unstructured":"Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519\u2013530 (2012).","journal-title":"J. Struct. Biol."},{"key":"499_CR48","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1016\/j.jsb.2006.07.020","volume":"157","author":"B Gipson","year":"2007","unstructured":"Gipson, B., Zeng, X., Zhang, Z. Y. & Stahlberg, H. 2dx\u2014user-friendly image processing for 2D crystals. J. Struct. Biol. 157, 64\u201372 (2007).","journal-title":"J. Struct. Biol."},{"key":"499_CR49","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1016\/S0076-6879(88)65019-1","volume":"165","author":"SH Leppla","year":"1988","unstructured":"Leppla, S. H. Production and purification of anthrax toxin. Methods Enzymol. 165, 103\u2013116 (1988).","journal-title":"Methods Enzymol."},{"key":"499_CR50","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1128\/aem.57.4.1094-1101.1991","volume":"57","author":"MH Zwietering","year":"1991","unstructured":"Zwietering, M. H., de Koos, J. T., Hasenack, B. E., de Witt, J. C. & van\u2019t Riet, K. Modeling of bacterial growth as a function of temperature. Appl. Environ. Microbiol. 57, 1094\u20131101 (1991).","journal-title":"Appl. Environ. Microbiol."}],"container-title":["Nature Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41564-019-0499-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41564-019-0499-1","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41564-019-0499-1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,7,20]],"date-time":"2024-07-20T19:50:54Z","timestamp":1721505054000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41564-019-0499-1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,7,15]]},"references-count":50,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2019,11]]}},"alternative-id":["499"],"URL":"https:\/\/doi.org\/10.1038\/s41564-019-0499-1","relation":{},"ISSN":["2058-5276"],"issn-type":[{"value":"2058-5276","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,7,15]]},"assertion":[{"value":"21 August 2018","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 May 2019","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"15 July 2019","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"A priority application on compounds used to inhibit bacterial S-layer protein assembly has been filed by VIB and Vrije Universiteit Brussel at the European Patent Office listing A.F. and H.R. as inventors. The other authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}