{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,19]],"date-time":"2026-07-19T05:14:36Z","timestamp":1784438076434,"version":"3.55.0"},"reference-count":77,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2018,1,1]],"date-time":"2018-01-01T00:00:00Z","timestamp":1514764800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,26]],"date-time":"2020-08-26T00:00:00Z","timestamp":1598400000000},"content-version":"vor","delay-in-days":968,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000060","name":"HHS NIH National Institute of Allergy and Infectious Diseases (NIAID)","doi-asserted-by":"publisher","award":["R01-AI117235"],"award-info":[{"award-number":["R01-AI117235"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"HHS NIH National Institute of Allergy and Infectious Diseases (NIAID)","doi-asserted-by":"publisher","award":["1K22AI113078-01"],"award-info":[{"award-number":["1K22AI113078-01"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2018,1]]},"DOI":"10.1074\/jbc.ra117.000437","type":"journal-article","created":{"date-parts":[[2017,12,11]],"date-time":"2017-12-11T16:45:19Z","timestamp":1513010719000},"page":"1106-1119","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":43,"title":["Structural and functional insights into the role of BamD and BamE within the \u03b2-barrel assembly machinery in Neisseria gonorrhoeae"],"prefix":"10.1016","volume":"293","author":[{"given":"Aleksandra E.","family":"Sikora","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor H.","family":"Wierzbicki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryszard A.","family":"Zielke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rachael F.","family":"Ryner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Konstantin V.","family":"Korotkov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan K.","family":"Buchanan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas","family":"Noinaj","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA117.000437_bib1","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1038\/nature10823","article-title":"Structural basis for iron piracy by pathogenic Neisseria","volume":"483","author":"Noinaj","year":"2012","journal-title":"Nature"},{"key":"10.1074\/jbc.RA117.000437_bib2","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.sbi.2011.05.005","article-title":"The structural biology of \u03b2-barrel membrane proteins: a summary of recent reports","volume":"21","author":"Fairman","year":"2011","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib3","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nrmicro.2016.191","article-title":"The \u03b2-barrel assembly machinery in motion","volume":"15","author":"Noinaj","year":"2017","journal-title":"Nat. Rev. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib4","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1146\/annurev-biochem-061408-144611","article-title":"\u03b2-Barrel membrane protein assembly by the Bam complex","volume":"80","author":"Hagan","year":"2011","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.RA117.000437_bib5","doi-asserted-by":"crossref","first-page":"20150023","DOI":"10.1098\/rstb.2015.0023","article-title":"Outer membrane protein biogenesis in Gram-negative bacteria","volume":"370","author":"Rollauer","year":"2015","journal-title":"Philos. Trans. R Soc. Lond. B Biol. Sci"},{"key":"10.1074\/jbc.RA117.000437_bib6","doi-asserted-by":"crossref","first-page":"e0143304","DOI":"10.1371\/journal.pone.0143304","article-title":"Global estimates of the prevalence and incidence of four curable sexually transmitted infections in 2012 based on systematic review and global reporting","volume":"10","author":"Newman","year":"2015","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA117.000437_bib7","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1074\/mcp.M113.029538","article-title":"Quantitative proteomics of the Neisseria gonorrhoeae cell envelope and membrane vesicles for the discovery of potential therapeutic targets","volume":"13","author":"Zielke","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/jbc.RA117.000437_bib8","doi-asserted-by":"crossref","first-page":"2338","DOI":"10.1074\/mcp.M116.058800","article-title":"Proteomics-driven antigen discovery for development of vaccines against gonorrhea","volume":"15","author":"Zielke","year":"2016","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/jbc.RA117.000437_bib9","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/j.bbamem.2011.08.020","article-title":"The Bam machine: a molecular cooper","volume":"1818","author":"Ricci","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA117.000437_bib10","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1038\/nrmicro2069","article-title":"Membrane protein architects: the role of the BAM complex in outer membrane protein assembly","volume":"7","author":"Knowles","year":"2009","journal-title":"Nat. Rev. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib11","doi-asserted-by":"crossref","first-page":"7074","DOI":"10.1128\/JB.00737-09","article-title":"The \u03b2-barrel outer membrane protein assembly complex of Neisseria meningitidis","volume":"191","author":"Volokhina","year":"2009","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA117.000437_bib12","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1111\/j.1365-2958.2005.04906.x","article-title":"Molecular architecture and function of the Omp85 family of proteins","volume":"58","author":"Gentle","year":"2005","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib13","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.resmic.2003.11.007","article-title":"Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly","volume":"155","author":"Voulhoux","year":"2004","journal-title":"Res. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib14","doi-asserted-by":"crossref","first-page":"6400","DOI":"10.1073\/pnas.0701579104","article-title":"Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli","volume":"104","author":"Sklar","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000437_bib15","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/j.cell.2005.02.014","article-title":"Chemical conditionality: a genetic strategy to probe organelle assembly","volume":"121","author":"Ruiz","year":"2005","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000437_bib16","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1016\/S0959-440X(03)00099-X","article-title":"The versatile \u03b2-barrel membrane protein","volume":"13","author":"Wimley","year":"2003","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib17","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1126\/science.1188919","article-title":"Reconstitution of outer membrane protein assembly from purified components","volume":"328","author":"Hagan","year":"2010","journal-title":"Science"},{"key":"10.1074\/jbc.RA117.000437_bib18","doi-asserted-by":"crossref","first-page":"e04234","DOI":"10.7554\/eLife.04234","article-title":"Reconstitution of bacterial autotransporter assembly using purified components","volume":"3","author":"Roman-Hernandez","year":"2014","journal-title":"Elife"},{"key":"10.1074\/jbc.RA117.000437_bib19","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1126\/science.aad3460","article-title":"The structure of the \u03b2-barrel assembly machinery complex","volume":"351","author":"Bakelar","year":"2016","journal-title":"Science"},{"key":"10.1074\/jbc.RA117.000437_bib20","doi-asserted-by":"crossref","first-page":"12865","DOI":"10.1038\/ncomms12865","article-title":"Lateral opening in the intact \u03b2-barrel assembly machinery captured by cryo-EM","volume":"7","author":"Iadanza","year":"2016","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.RA117.000437_bib21","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1038\/nature17199","article-title":"Structural basis of outer membrane protein insertion by the BAM complex","volume":"531","author":"Gu","year":"2016","journal-title":"Nature"},{"key":"10.1074\/jbc.RA117.000437_bib22","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1038\/nsmb.3181","article-title":"Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins","volume":"23","author":"Han","year":"2016","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib23","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/j.jmb.2012.05.035","article-title":"Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC","volume":"422","author":"Webb","year":"2012","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib24","doi-asserted-by":"crossref","first-page":"1873","DOI":"10.1016\/j.str.2008.09.014","article-title":"Crystal structure of YaeT: conformational flexibility and substrate recognition","volume":"16","author":"Gatzeva-Topalova","year":"2008","journal-title":"Structure"},{"key":"10.1074\/jbc.RA117.000437_bib25","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1126\/science.1143993","article-title":"Structure and function of an essential component of the outer membrane protein assembly machine","volume":"317","author":"Kim","year":"2007","journal-title":"Science"},{"key":"10.1074\/jbc.RA117.000437_bib26","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/j.jmb.2010.12.020","article-title":"Crystal structure of Escherichia coli BamB, a lipoprotein component of the \u03b2-barrel assembly machinery complex","volume":"406","author":"Kim","year":"2011","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib27","doi-asserted-by":"crossref","first-page":"39116","DOI":"10.1074\/jbc.M111.298166","article-title":"Crystal structure of \u03b2-barrel assembly machinery BamCD protein complex","volume":"286","author":"Kim","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.000437_bib28","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1021\/bi101659u","article-title":"Structural characterization of Escherichia coli BamE, a lipoprotein component of the \u03b2-barrel assembly machinery complex","volume":"50","author":"Kim","year":"2011","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA117.000437_bib29","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/j.jmb.2011.01.042","article-title":"The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex","volume":"407","author":"Noinaj","year":"2011","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib30","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/nature12521","article-title":"Structural insight into the biogenesis of \u03b2-barrel membrane proteins","volume":"501","author":"Noinaj","year":"2013","journal-title":"Nature"},{"key":"10.1074\/jbc.RA117.000437_bib31","doi-asserted-by":"crossref","first-page":"6303","DOI":"10.1021\/acs.biochem.5b00852","article-title":"Fitting the pieces of the \u03b2-barrel assembly machinery complex","volume":"54","author":"O'Neil","year":"2015","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA117.000437_bib32","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/j.jmb.2011.01.002","article-title":"Augmenting \u03b2-augmentation: structural basis of how BamB binds BamA and may support folding of outer membrane proteins","volume":"406","author":"Heuck","year":"2011","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib33","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1074\/jbc.M114.584524","article-title":"Crystal structure of BamB bound to a periplasmic domain fragment of BamA, the central component of the \u03b2-barrel assembly machine","volume":"290","author":"Jansen","year":"2015","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.000437_bib34","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.str.2015.10.030","article-title":"The structure of a BamA-BamD fusion illuminates the architecture of the \u03b2-barrel assembly machine core","volume":"24","author":"Bergal","year":"2016","journal-title":"Structure"},{"key":"10.1074\/jbc.RA117.000437_bib35","doi-asserted-by":"crossref","first-page":"27792","DOI":"10.1074\/jbc.M111.238931","article-title":"Structural basis of outer membrane protein biogenesis in bacteria","volume":"286","author":"Albrecht","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.000437_bib36","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.jmb.2011.03.035","article-title":"Crystal structure of BamD: an essential component of the \u03b2-barrel assembly machinery of Gram-negative bacteria","volume":"409","author":"Sandoval","year":"2011","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib37","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1038\/embor.2010.202","article-title":"Structure and function of BamE within the outer membrane and the \u03b2-barrel assembly machine","volume":"12","author":"Knowles","year":"2011","journal-title":"EMBO Rep"},{"key":"10.1074\/jbc.RA117.000437_bib38","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1107\/S1399004714007482","article-title":"Structure of BamA, an essential factor in outer membrane protein biogenesis","volume":"70","author":"Albrecht","year":"2014","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA117.000437_bib39","doi-asserted-by":"crossref","first-page":"2677","DOI":"10.1096\/fj.13-248450","article-title":"Structural and functional analysis of the \u03b2-barrel domain of BamA from Escherichia coli","volume":"28","author":"Ni","year":"2014","journal-title":"FASEB J"},{"key":"10.1074\/jbc.RA117.000437_bib40","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/j.str.2014.05.008","article-title":"Lateral opening and exit pore formation are required for BamA function","volume":"22","author":"Noinaj","year":"2014","journal-title":"Structure"},{"key":"10.1074\/jbc.RA117.000437_bib41","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1111\/j.1365-2958.2003.03903.x","article-title":"Structure of the OmpA-like domain of RmpM from Neisseria meningitidis","volume":"51","author":"Grizot","year":"2004","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib42","doi-asserted-by":"crossref","first-page":"e1003528","DOI":"10.1371\/journal.ppat.1003528","article-title":"Distinct binding and immunogenic properties of the gonococcal homologue of meningococcal factor h binding protein","volume":"9","author":"Jongerius","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.RA117.000437_bib43","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1046\/j.1365-2958.2002.03091.x","article-title":"Imp\/OstA is required for cell envelope biogenesis in Escherichia coli","volume":"45","author":"Braun","year":"2002","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib44","doi-asserted-by":"crossref","first-page":"9417","DOI":"10.1073\/pnas.0402340101","article-title":"Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface","volume":"101","author":"Bos","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000437_bib45","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1046\/j.1365-2958.1996.457984.x","article-title":"A novel peptidoglycan-linked lipoprotein (ComL) that functions in natural transformation competence of Neisseria gonorrhoeae","volume":"19","author":"Fussenegger","year":"1996","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib46","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.cell.2005.02.015","article-title":"Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli","volume":"121","author":"Wu","year":"2005","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000437_bib47","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1111\/j.1365-2958.2006.05211.x","article-title":"YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli","volume":"61","author":"Malinverni","year":"2006","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib48","doi-asserted-by":"crossref","first-page":"4552","DOI":"10.1128\/JB.187.13.4552-4561.2005","article-title":"Characterization of six lipoproteins in the \u03c3E regulon","volume":"187","author":"Onufryk","year":"2005","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA117.000437_bib49","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1186\/s12866-015-0453-1","article-title":"The Neisseria gonorrhoeae Obg protein is an essential ribosome-associated GTPase and a potential drug target","volume":"15","author":"Zielke","year":"2015","journal-title":"BMC Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib50","doi-asserted-by":"crossref","first-page":"e00432","DOI":"10.1002\/mbo3.432","article-title":"Functional and structural studies on the Neisseria gonorrhoeae GmhA, the first enzyme in the glycero-manno-heptose biosynthesis pathways, demonstrate a critical role in lipooligosaccharide synthesis and gonococcal viability","volume":"6","author":"Wierzbicki","year":"2017","journal-title":"Microbiologyopen"},{"key":"10.1074\/jbc.RA117.000437_bib51","doi-asserted-by":"crossref","first-page":"e00037","DOI":"10.1128\/JB.00037-17","article-title":"Deciphering function of new gonococcal vaccine antigens using phenotypic microarrays","volume":"199","author":"Baarda","year":"2017","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA117.000437_bib52","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1099\/mic.0.035055-0","article-title":"The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane \u03b2-barrel proteins in Caulobacter crescentus","volume":"156","author":"Ryan","year":"2010","journal-title":"Microbiology"},{"key":"10.1074\/jbc.RA117.000437_bib53","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1099\/mic.0.2007\/011999-0","article-title":"Small outer-membrane lipoprotein, SmpA, is regulated by \u03c3E and has a role in cell envelope integrity and virulence of Salmonella enterica serovar Typhimurium","volume":"154","author":"Lewis","year":"2008","journal-title":"Microbiology"},{"key":"10.1074\/jbc.RA117.000437_bib54","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1128\/JB.181.4.1099-1109.1999","article-title":"Pseudomonas aeruginosa fur overlaps with a gene encoding a novel outer membrane lipoprotein, OmlA","volume":"181","author":"Ochsner","year":"1999","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA117.000437_bib55","doi-asserted-by":"crossref","first-page":"4A.3.1","DOI":"10.1002\/9780471729259.mc04a03s34","article-title":"Isolation of cell envelopes and naturally released membrane vesicles of Neisseria gonorrhoeae","volume":"34","author":"Zielke","year":"2014","journal-title":"Curr. Protoc. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib56","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1128\/JB.06426-11","article-title":"BamE modulates the Escherichia coli \u03b2-barrel assembly machine component BamA","volume":"194","author":"Rigel","year":"2012","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA117.000437_bib57","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1146\/annurev.micro.091208.073413","article-title":"Biological functions and biogenesis of secreted bacterial outer membrane vesicles","volume":"64","author":"Kulp","year":"2010","journal-title":"Annu. Rev. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib58","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1107\/S0907444911051031","article-title":"Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly","volume":"68","author":"Dong","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA117.000437_bib59","doi-asserted-by":"crossref","first-page":"3487","DOI":"10.1073\/pnas.1201362109","article-title":"Activation of the Escherichia coli \u03b2-barrel assembly machine (Bam) is required for essential components to interact properly with substrate","volume":"109","author":"Ricci","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000437_bib60","doi-asserted-by":"crossref","first-page":"e8619","DOI":"10.1371\/journal.pone.0008619","article-title":"A modular BAM complex in the outer membrane of the \u03b1-proteobacterium Caulobacter crescentus","volume":"5","author":"Anwari","year":"2010","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA117.000437_bib61","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1111\/j.1365-2958.1988.tb00024.x","article-title":"Recombination among protein II genes of Neisseria gonorrhoeae generates new coding sequences and increases structural variability in the protein II family","volume":"2","author":"Connell","year":"1988","journal-title":"Mol. Microbiol"},{"issue":"Suppl. 2","key":"10.1074\/jbc.RA117.000437_bib62","first-page":"A111","article-title":"Phenotypic, genetic and genomic characterisation of the WHO Neisseria gonorrhoeae reference strains for quality assurance of laboratory investigations globally","volume":"91","author":"Unemo","year":"2015","journal-title":"Sex. Transm. Infect"},{"key":"10.1074\/jbc.RA117.000437_bib63","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/0022-2836(80)90283-1","article-title":"Analysis of gene control signals by DNA fusion and cloning in Escherichia coli","volume":"138","author":"Casadaban","year":"1980","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib64","doi-asserted-by":"crossref","DOI":"10.1002\/9780471729259.mc04a01s8","article-title":"Laboratory maintenance of Neisseria gonorrhoeae","author":"Spence","year":"2008","journal-title":"Curr. Protoc. Microbiol"},{"key":"10.1074\/jbc.RA117.000437_bib65","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1093\/genetics\/154.2.523","article-title":"A homologue of the recombination-dependent growth gene, rdgC, is involved in gonococcal pilin antigenic variation","volume":"154","author":"Mehr","year":"2000","journal-title":"Genetics"},{"key":"10.1074\/jbc.RA117.000437_bib66","doi-asserted-by":"crossref","first-page":"5899","DOI":"10.1128\/jb.175.18.5899-5906.1993","article-title":"Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells","volume":"175","author":"M\u00e9nard","year":"1993","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA117.000437_bib67","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1093\/ajcp\/45.4_ts.493","article-title":"Antibiotic susceptibility testing by a standardized single disk method","volume":"45","author":"Bauer","year":"1966","journal-title":"Am. J. Clin. Pathol"},{"key":"10.1074\/jbc.RA117.000437_bib68","doi-asserted-by":"crossref","first-page":"257","DOI":"10.15698\/mic2016.06.508","article-title":"Bacterial outer membrane vesicle biogenesis: a new mechanism and its implications","volume":"3","author":"Roier","year":"2016","journal-title":"Microb. Cell"},{"key":"10.1074\/jbc.RA117.000437_bib69","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.RA117.000437_bib70","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1107\/S0021889809045701","article-title":"xia2: an expert system for macromolecular crystallography data reduction","volume":"43","author":"Winter","year":"2010","journal-title":"J. Appl. Crystallogr"},{"key":"10.1074\/jbc.RA117.000437_bib71","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA117.000437_bib72","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA117.000437_bib73","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","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA117.000437_bib74","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1002\/prot.22879","article-title":"Automated minimization of steric clashes in protein structures","volume":"79","author":"Ramachandran","year":"2011","journal-title":"Proteins"},{"key":"10.1074\/jbc.RA117.000437_bib75","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1128\/JB.02329-14","article-title":"A metalloprotease secreted by the type II secretion system links Vibrio cholerae with collagen","volume":"197","author":"Park","year":"2015","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA117.000437_bib76","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","year":"2011","journal-title":"Mol. Syst. Biol"},{"key":"10.1074\/jbc.RA117.000437_bib77","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1186\/1471-2105-11-595","article-title":"BIGSdb: scalable analysis of bacterial genome variation at the population level","volume":"11","author":"Jolley","year":"2010","journal-title":"BMC Bioinformatics"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582039116X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582039116X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA117.000437","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T09:46:44Z","timestamp":1641289604000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002192582039116X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,1]]},"references-count":77,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2018,1]]}},"alternative-id":["S002192582039116X"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra117.000437","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2018,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural and functional insights into the role of BamD and BamE within the \u03b2-barrel assembly machinery in Neisseria gonorrhoeae","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA117.000437","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"name":"copyright","label":"Copyright"}]}}