{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T21:14:57Z","timestamp":1778793297032,"version":"3.51.4"},"reference-count":72,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T00:00:00Z","timestamp":1793923200000},"content-version":"am","delay-in-days":370,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T00:00:00Z","timestamp":1761955200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R24 GM154192"],"award-info":[{"award-number":["R24 GM154192"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01GM123169"],"award-info":[{"award-number":["R01GM123169"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000968","name":"American Heart Association Inc","doi-asserted-by":"publisher","award":["909066"],"award-info":[{"award-number":["909066"]}],"id":[{"id":"10.13039\/100000968","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006377","name":"Purdue University","doi-asserted-by":"publisher","award":["GM132024"],"award-info":[{"award-number":["GM132024"]}],"id":[{"id":"10.13039\/100006377","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000893","name":"Simons Foundation","doi-asserted-by":"publisher","award":["SF349247"],"award-info":[{"award-number":["SF349247"]}],"id":[{"id":"10.13039\/100000893","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000893","name":"Simons Foundation","doi-asserted-by":"publisher","award":["1R01GM127896"],"award-info":[{"award-number":["1R01GM127896"]}],"id":[{"id":"10.13039\/100000893","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000893","name":"Simons Foundation","doi-asserted-by":"publisher","award":["R01GM148586"],"award-info":[{"award-number":["R01GM148586"]}],"id":[{"id":"10.13039\/100000893","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000893","name":"Simons Foundation","doi-asserted-by":"publisher","award":["1R01GM127884"],"award-info":[{"award-number":["1R01GM127884"]}],"id":[{"id":"10.13039\/100000893","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000893","name":"Simons Foundation","doi-asserted-by":"publisher","award":["R01GM123169"],"award-info":[{"award-number":["R01GM123169"]}],"id":[{"id":"10.13039\/100000893","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["ACI-1548562"],"award-info":[{"award-number":["ACI-1548562"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["1828187"],"award-info":[{"award-number":["1828187"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100015326","name":"National Institutes of Health Common Fund","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100015326","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006975","name":"Indiana Clinical and Translational Sciences Institute","doi-asserted-by":"publisher","award":["UL1TR002529"],"award-info":[{"award-number":["UL1TR002529"]}],"id":[{"id":"10.13039\/100006975","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Structure"],"published-print":{"date-parts":[[2025,11]]},"DOI":"10.1016\/j.str.2025.08.009","type":"journal-article","created":{"date-parts":[[2025,9,2]],"date-time":"2025-09-02T14:41:30Z","timestamp":1756824090000},"page":"1893-1903.e3","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Structural insights into outer membrane protein biogenesis in pathogenic Neisseria"],"prefix":"10.1016","volume":"33","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8555-8008","authenticated-orcid":false,"given":"Evan","family":"Billings","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zixing","family":"Fan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Moloud Aflaki","family":"Sooreshjani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"James C.","family":"Gumbart","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6361-2336","authenticated-orcid":false,"given":"Nicholas","family":"Noinaj","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.str.2025.08.009_bib1","series-title":"Antibiotic Resistance Threats in the United States","year":"2019"},{"key":"10.1016\/j.str.2025.08.009_bib2","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.annemergmed.2012.10.014","article-title":"Update on Emerging Infections: news from the Centers for Disease Control and Prevention. Update to the CDC's Sexually Transmitted Diseases Treatment Guidelines, 2010: Oral cephalosporins no longer a recommended treatment for gonococcal infections","volume":"61","author":"Maldonado","year":"2013","journal-title":"Ann. Emerg. Med."},{"key":"10.1016\/j.str.2025.08.009_bib3","series-title":"Sexually Transmitted Disease Surveillance 2015","year":"2016"},{"key":"10.1016\/j.str.2025.08.009_bib4","doi-asserted-by":"crossref","first-page":"830","DOI":"10.3201\/eid2305.170088","article-title":"Azithromycin Resistance and Decreased Ceftriaxone Susceptibility in Neisseria gonorrhoeae, Hawaii, USA","volume":"23","author":"Papp","year":"2017","journal-title":"Emerg. Infect. Dis."},{"key":"10.1016\/j.str.2025.08.009_bib5","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1080\/22221751.2019.1681242","article-title":"Identification of multidrug-resistant Neisseria gonorrhoeae isolates with combined resistance to both ceftriaxone and azithromycin, China, 2017-2018","volume":"8","author":"Yuan","year":"2019","journal-title":"Emerg. Microbes Infect."},{"key":"10.1016\/j.str.2025.08.009_bib6","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1093\/cid\/cix485","article-title":"Cluster of Neisseria gonorrhoeae Isolates With High-level Azithromycin Resistance and Decreased Ceftriaxone Susceptibility, Hawaii, 2016","volume":"65","author":"Katz","year":"2017","journal-title":"Clin. Infect. Dis."},{"key":"10.1016\/j.str.2025.08.009_bib7","unstructured":"(2021). Enhanced Gonococcal Antimicrobial Surveillance Programme (EGASP). https:\/\/www.who.int\/publications\/i\/item\/9789240021341."},{"key":"10.1016\/j.str.2025.08.009_bib8","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1146\/annurev-micro-090816-093754","article-title":"Outer Membrane Biogenesis","volume":"71","author":"Konovalova","year":"2017","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.str.2025.08.009_bib9","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1042\/BJ20121025","article-title":"Structure and function of the PorB porin from disseminating Neisseria gonorrhoeae","volume":"449","author":"Zeth","year":"2013","journal-title":"Biochem. J."},{"key":"10.1016\/j.str.2025.08.009_bib10","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1000629","article-title":"Bacterial porin disrupts mitochondrial membrane potential and sensitizes host cells to apoptosis","volume":"5","author":"Kozjak-Pavlovic","year":"2009","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.str.2025.08.009_bib11","doi-asserted-by":"crossref","first-page":"4383","DOI":"10.1128\/IAI.00367-13","article-title":"Structure-function studies of the Neisseria gonorrhoeae major outer membrane porin","volume":"81","author":"Chen","year":"2013","journal-title":"Infect. Immun."},{"key":"10.1016\/j.str.2025.08.009_bib12","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/s42003-022-03039-y","article-title":"TdfH selectively binds metal-loaded tetrameric calprotectin for zinc import","volume":"5","author":"Bera","year":"2022","journal-title":"Commun. Biol."},{"key":"10.1016\/j.str.2025.08.009_bib13","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":"10.1016\/j.str.2025.08.009_bib14","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1111\/mmi.14666","article-title":"The assembly of beta-barrel membrane proteins by BAM and SAM","volume":"115","author":"Lundquist","year":"2021","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.str.2025.08.009_bib15","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nrmicro.2016.191","article-title":"The beta-barrel assembly machinery in motion","volume":"15","author":"Noinaj","year":"2017","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.str.2025.08.009_bib16","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.3389\/fmicb.2020.01252","article-title":"Identification of a Compound That Inhibits the Growth of Gram-Negative Bacteria by Blocking BamA-BamD Interaction","volume":"11","author":"Li","year":"2020","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.str.2025.08.009_bib17","doi-asserted-by":"crossref","first-page":"2011","DOI":"10.1073\/pnas.1415955112","article-title":"Inhibition of the beta-barrel assembly machine by a peptide that binds BamD","volume":"112","author":"Hagan","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.str.2025.08.009_bib18","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1007\/s10858-019-00250-8","article-title":"Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach","volume":"73","author":"Kaur","year":"2019","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.str.2025.08.009_bib19","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/s41586-019-1791-1","article-title":"A new antibiotic selectively kills Gram-negative pathogens","volume":"576","author":"Imai","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.str.2025.08.009_bib20","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/s41586-019-1665-6","article-title":"Chimeric peptidomimetic antibiotics against Gram-negative bacteria","volume":"576","author":"Luther","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.str.2025.08.009_bib21","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/s41586-021-03455-w","article-title":"The antibiotic darobactin mimics a beta-strand to inhibit outer membrane insertase","volume":"593","author":"Kaur","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.str.2025.08.009_bib22","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":"10.1016\/j.str.2025.08.009_bib23","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":"10.1016\/j.str.2025.08.009_bib24","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1016\/j.tim.2012.08.006","article-title":"Evolution of the beta-barrel assembly machinery","volume":"20","author":"Webb","year":"2012","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.str.2025.08.009_bib25","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1126\/science.aad3460","article-title":"The structure of the beta-barrel assembly machinery complex","volume":"351","author":"Bakelar","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.str.2025.08.009_bib26","doi-asserted-by":"crossref","first-page":"1778","DOI":"10.1111\/febs.13960","article-title":"Structural snapshots of the beta-barrel assembly machinery","volume":"284","author":"Bakelar","year":"2017","journal-title":"FEBS J."},{"key":"10.1016\/j.str.2025.08.009_bib27","doi-asserted-by":"crossref","first-page":"7131","DOI":"10.1038\/s41467-021-27449-4","article-title":"Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM","volume":"12","author":"Wu","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.str.2025.08.009_bib28","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":"10.1016\/j.str.2025.08.009_bib29","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":"10.1016\/j.str.2025.08.009_bib30","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1111\/mmi.15127","article-title":"BamE directly interacts with BamA and BamD coordinating their functions","volume":"120","author":"Kumar","year":"2023","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.str.2025.08.009_bib31","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1128\/JB.06192-11","article-title":"Substitutions in the BamA beta-barrel domain overcome the conditional lethal phenotype of a DeltabamB DeltabamE strain of Escherichia coli","volume":"194","author":"Tellez","year":"2012","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.str.2025.08.009_bib32","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1128\/JB.06426-11","article-title":"BamE modulates the Escherichia coli beta-barrel assembly machine component BamA","volume":"194","author":"Rigel","year":"2012","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.str.2025.08.009_bib33","doi-asserted-by":"crossref","DOI":"10.1128\/JB.00401-20","article-title":"Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA","volume":"202","author":"Hart","year":"2020","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.str.2025.08.009_bib34","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbamem.2019.183062","article-title":"The big BAM theory: An open and closed case?","volume":"1862","author":"Wu","year":"2020","journal-title":"Biochim. Biophys. Acta. Biomembr."},{"key":"10.1016\/j.str.2025.08.009_bib35","doi-asserted-by":"crossref","first-page":"6009","DOI":"10.1021\/acs.biochem.5b00950","article-title":"BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism","volume":"54","author":"Plummer","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2025.08.009_bib36","doi-asserted-by":"crossref","first-page":"3358","DOI":"10.1038\/s41467-019-11230-9","article-title":"Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA beta-barrel","volume":"10","author":"Doyle","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.str.2025.08.009_bib37","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1016\/j.cell.2022.02.016","article-title":"Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding","volume":"185","author":"Doyle","year":"2022","journal-title":"Cell"},{"key":"10.1016\/j.str.2025.08.009_bib38","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1038\/s41586-020-2370-1","article-title":"Structure of a nascent membrane protein as it folds on the BAM complex","volume":"583","author":"Tomasek","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.str.2025.08.009_bib39","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1111\/j.1365-2958.2012.08059.x","article-title":"The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex","volume":"84","author":"Anwari","year":"2012","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.str.2025.08.009_bib40","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1111\/mmi.13492","article-title":"The TamB ortholog of Borrelia burgdorferi interacts with the beta-barrel assembly machine (BAM) complex protein BamA","volume":"102","author":"Iqbal","year":"2016","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.str.2025.08.009_bib41","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1126\/science.1078973","article-title":"Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly","volume":"299","author":"Voulhoux","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.str.2025.08.009_bib42","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1074\/jbc.RA117.000437","article-title":"Structural and functional insights into the role of BamD and BamE within the beta-barrel assembly machinery in Neisseria gonorrhoeae","volume":"293","author":"Sikora","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2025.08.009_bib43","doi-asserted-by":"crossref","first-page":"7074","DOI":"10.1128\/JB.00737-09","article-title":"The beta-barrel outer membrane protein assembly complex of Neisseria meningitidis","volume":"191","author":"Volokhina","year":"2009","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.str.2025.08.009_bib44","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":"10.1016\/j.str.2025.08.009_bib45","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/nature12521","article-title":"Structural insight into the biogenesis of beta-barrel membrane proteins","volume":"501","author":"Noinaj","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.str.2025.08.009_bib46","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 beta-Barrel Assembly Machine Core","volume":"24","author":"Bergal","year":"2016","journal-title":"Structure"},{"key":"10.1016\/j.str.2025.08.009_bib47","doi-asserted-by":"crossref","first-page":"3487","DOI":"10.1073\/pnas.1201362109","article-title":"Activation of the Escherichia coli beta-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. USA"},{"key":"10.1016\/j.str.2025.08.009_bib48","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":"10.1016\/j.str.2025.08.009_bib49","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms12865","article-title":"Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM","volume":"7","author":"Iadanza","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.str.2025.08.009_bib50","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.49787","article-title":"Formation of a beta-barrel membrane protein is catalyzed by the interior surface of the assembly machine protein BamA","volume":"8","author":"Lee","year":"2019","journal-title":"eLife"},{"key":"10.1016\/j.str.2025.08.009_bib51","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/s41586-023-05988-8","article-title":"Structural basis of BAM-mediated outer membrane beta-barrel protein assembly","volume":"617","author":"Shen","year":"2023","journal-title":"Nature"},{"key":"10.1016\/j.str.2025.08.009_bib52","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.jsb.2005.03.010","article-title":"Automated molecular microscopy: the new Leginon system","volume":"151","author":"Suloway","year":"2005","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.str.2025.08.009_bib53","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nmeth.4193","article-title":"MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy","volume":"14","author":"Zheng","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.str.2025.08.009_bib54","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/nmeth.4169","article-title":"cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination","volume":"14","author":"Punjani","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.str.2025.08.009_bib55","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1038\/s41592-020-00990-8","article-title":"Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction","volume":"17","author":"Punjani","year":"2020","journal-title":"Nat. Methods"},{"key":"10.1016\/j.str.2025.08.009_bib56","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":"10.1016\/j.str.2025.08.009_bib57","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":"10.1016\/j.str.2025.08.009_bib58","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1002\/pro.3943","article-title":"UCSF ChimeraX: Structure visualization for researchers, educators, and developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.str.2025.08.009_bib59","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.str.2025.08.009_bib60","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1002\/jcc.23702","article-title":"CHARMM-GUI Membrane Builder toward realistic biological membrane simulations","volume":"35","author":"Wu","year":"2014","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.str.2025.08.009_bib61","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips","year":"2005","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.str.2025.08.009_bib62","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1073\/pnas.1914677117","article-title":"Improved protein structure prediction using predicted interresidue orientations","volume":"117","author":"Yang","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.str.2025.08.009_bib63","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1002\/jcc.20945","article-title":"CHARMM-GUI: a web-based graphical user interface for CHARMM","volume":"29","author":"Jo","year":"2008","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.str.2025.08.009_bib64","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1008355","article-title":"Membrane thinning and lateral gating are consistent features of BamA across multiple species","volume":"16","author":"Liu","year":"2020","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.str.2025.08.009_bib72","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.str.2025.08.009_bib66","doi-asserted-by":"crossref","DOI":"10.1063\/5.0014475","article-title":"Scalable molecular dynamics on CPU and GPU architectures with NAMD","volume":"153","author":"Phillips","year":"2020","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.str.2025.08.009_bib67","doi-asserted-by":"crossref","first-page":"3257","DOI":"10.1021\/ct300400x","article-title":"Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone phi, psi and side-chain chi(1) and chi(2) dihedral angles","volume":"8","author":"Best","year":"2012","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.str.2025.08.009_bib68","doi-asserted-by":"crossref","first-page":"7830","DOI":"10.1021\/jp101759q","article-title":"Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types","volume":"114","author":"Klauda","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.str.2025.08.009_bib65","doi-asserted-by":"crossref","first-page":"4177","DOI":"10.1063\/1.467468","article-title":"Constant-Pressure Molecular-Dynamics Algorithms","volume":"101","author":"Martyna","year":"1994","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.str.2025.08.009_bib69","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1021\/acs.jctc.9b00160","article-title":"Accelerating Membrane Simulations with Hydrogen Mass Repartitioning","volume":"15","author":"Balusek","year":"2019","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.str.2025.08.009_bib70","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle Mesh Ewald - an N.Log(N) Method for Ewald Sums in Large Systems","volume":"98","author":"Darden","year":"1993","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.str.2025.08.009_bib71","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212625003132?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212625003132?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T20:54:40Z","timestamp":1778792080000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212625003132"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11]]},"references-count":72,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2025,11]]}},"alternative-id":["S0969212625003132"],"URL":"https:\/\/doi.org\/10.1016\/j.str.2025.08.009","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[2025,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural insights into outer membrane protein biogenesis in pathogenic Neisseria","name":"articletitle","label":"Article Title"},{"value":"Structure","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.str.2025.08.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}