{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T02:27:59Z","timestamp":1773282479410,"version":"3.50.1"},"reference-count":66,"publisher":"Elsevier BV","issue":"20","license":[{"start":{"date-parts":[[2016,5,1]],"date-time":"2016-05-01T00:00:00Z","timestamp":1462060800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,3]],"date-time":"2020-09-03T00:00:00Z","timestamp":1599091200000},"content-version":"vor","delay-in-days":1586,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01GM066861"],"award-info":[{"award-number":["R01GM066861"]}],"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":["R01GM061629"],"award-info":[{"award-number":["R01GM061629"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI097157, R01AI044239, R01AI090348, T32AI055397, F32AI115911, R21AI099539 & R37AI033493"],"award-info":[{"award-number":["R01AI097157, R01AI044239, R01AI090348, T32AI055397, F32AI115911, R21AI099539 & R37AI033493"]}],"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":[[2016,5]]},"DOI":"10.1074\/jbc.m116.715573","type":"journal-article","created":{"date-parts":[[2016,3,17]],"date-time":"2016-03-17T02:28:16Z","timestamp":1458181696000},"page":"10916-10933","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":31,"title":["Amidase Activity of AmiC Controls Cell Separation and Stem Peptide Release and Is Enhanced by NlpD in Neisseria gonorrhoeae"],"prefix":"10.1016","volume":"291","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2637-9720","authenticated-orcid":false,"given":"Jonathan D.","family":"Lenz","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elizabeth A.","family":"Stohl","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rosanna M.","family":"Robertson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kathleen T.","family":"Hackett","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kathryn","family":"Fisher","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kalia","family":"Xiong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mijoon","family":"Lee","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dusan","family":"Hesek","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shahriar","family":"Mobashery","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H. Steven","family":"Seifert","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher","family":"Davies","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joseph P.","family":"Dillard","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M116.715573_bib1","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1111\/j.1574-6976.2007.00088.x","article-title":"Structural variation in the glycan strands of bacterial peptidoglycan","volume":"32","author":"Vollmer","year":"2008","journal-title":"FEMS Microbiol. Rev"},{"key":"10.1074\/jbc.M116.715573_bib2","unstructured":"Centers for Disease Control and Prevention (2013) Antibiotic Resistance Threats in the United States, 2013, http:\/\/www.cdc.gov\/drugresistance\/threat-report-2013\/"},{"key":"10.1074\/jbc.M116.715573_bib3","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1093\/infdis\/143.3.432","article-title":"Toxic activity of purified lipopolysaccharide of Neisseria gonorrhoeae for human fallopian tube mucosa","volume":"143","author":"Gregg","year":"1981","journal-title":"J. Infect. Dis"},{"key":"10.1074\/jbc.M116.715573_bib4","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.4049\/jimmunol.168.4.1533","article-title":"Cutting edge: immune stimulation by neisserial porins is toll-like receptor 2 and MyD88 dependent","volume":"168","author":"Massari","year":"2002","journal-title":"J. Immunol"},{"key":"10.1074\/jbc.M116.715573_bib5","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1093\/infdis\/149.3.378","article-title":"Ability of monomeric peptidoglycan fragments from Neisseria gonorrhoeae to damage human fallopian tube mucosa","volume":"149","author":"Melly","year":"1984","journal-title":"J. Infect. Dis"},{"key":"10.1074\/jbc.M116.715573_bib6","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.mib.2004.12.008","article-title":"The role of peptidoglycan in pathogenesis","volume":"8","author":"Boneca","year":"2005","journal-title":"Curr. Opin. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib7","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.1128\/jb.126.3.1180-1185.1976","article-title":"Chemical composition and turnover of peptidoglycan in Neisseria gonorrhoeae","volume":"126","author":"Hebeler","year":"1976","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib8","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1128\/iai.24.3.869-878.1979","article-title":"Release of soluble peptidoglycan from growing gonococci: hexaminidase and amidase activities","volume":"24","author":"Rosenthal","year":"1979","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M116.715573_bib9","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1128\/iai.29.3.914-925.1980","article-title":"Release of soluble peptidoglycan from growing gonococci: demonstration of anhydro-muramyl-containing fragments","volume":"29","author":"Sinha","year":"1980","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M116.715573_bib10","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1128\/jb.162.1.391-397.1985","article-title":"Release of cell wall peptides into culture medium by exponentially growing Escherichia coli","volume":"162","author":"Goodell","year":"1985","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib11","doi-asserted-by":"crossref","first-page":"5634","DOI":"10.1128\/JB.00446-07","article-title":"An anhydro-N-acetylmuramyl-l-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coli","volume":"189","author":"Uehara","year":"2007","journal-title":"J. Bacteriol"},{"issue":"suppl.","key":"10.1074\/jbc.M116.715573_bib12","first-page":"187","article-title":"Structure and functions of the Bordetella tracheal cytotoxin","volume":"13","author":"Goldman","year":"1988","journal-title":"Tokai J. Exp. Clin. Med"},{"key":"10.1074\/jbc.M116.715573_bib13","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/j.mib.2013.09.005","article-title":"Peptidoglycan hydrolases, bacterial shape, and pathogenesis","volume":"16","author":"Frirdich","year":"2013","journal-title":"Curr. Opin. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib14","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1046\/j.1365-2958.2001.02499.x","article-title":"Involvement of N-acetylmuramyl-l-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli","volume":"41","author":"Heidrich","year":"2001","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib15","doi-asserted-by":"crossref","first-page":"12604","DOI":"10.1021\/ja407445x","article-title":"Cell-wall remodeling by the zinc-protease AmpDh3 from Pseudomonas aeruginosa","volume":"135","author":"Lee","year":"2013","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.715573_bib16","doi-asserted-by":"crossref","first-page":"10318","DOI":"10.1021\/ja405464b","article-title":"Reaction products and the x-ray structure of AmpDh2, a virulence determinant of Pseudomonas aeruginosa","volume":"135","author":"Mart\u00ednez-Caballero","year":"2013","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.715573_bib17","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1111\/j.1574-6976.2007.00084.x","article-title":"Folds and activities of peptidoglycan amidases","volume":"31","author":"Firczuk","year":"2007","journal-title":"FEMS Microbiol. Rev"},{"key":"10.1074\/jbc.M116.715573_bib18","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1046\/j.1365-2958.2003.03511.x","article-title":"The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway","volume":"48","author":"Bernhardt","year":"2003","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib19","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1111\/mmi.12318","article-title":"Twin-arginine translocation system (TAT) mutants of Salmonella are attenuated due to envelope defects, not respiratory defects","volume":"89","author":"Craig","year":"2013","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib20","doi-asserted-by":"crossref","first-page":"4973","DOI":"10.1128\/JB.00316-11","article-title":"A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators","volume":"193","author":"Peters","year":"2011","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib21","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1111\/mmi.12361","article-title":"The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain","volume":"90","author":"Rocaboy","year":"2013","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib22","doi-asserted-by":"crossref","first-page":"5218","DOI":"10.1128\/JB.00912-12","article-title":"Cell wall amidase AmiC1 is required for cellular communication and heterocyst development in the cyanobacterium Anabaena PCC 7120 but not for filament integrity","volume":"194","author":"Berendt","year":"2012","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib23","doi-asserted-by":"crossref","DOI":"10.1111\/febs.13673","article-title":"Enabling cell-cell communication via nanopore formation: structure, function, and localization of the unique cell wall amidase, AmiC2 of Nostoc punctiforme","author":"B\u00fcttner","year":"2016","journal-title":"FEBS J"},{"key":"10.1074\/jbc.M116.715573_bib24","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1111\/j.1365-2958.2011.07554.x","article-title":"The morphogene AmiC2 is pivotal for multicellular development in the cyanobacterium Nostoc punctiforme","volume":"79","author":"Lehner","year":"2011","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib25","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1111\/mmi.12304","article-title":"Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site","volume":"89","author":"Peters","year":"2013","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib26","doi-asserted-by":"crossref","first-page":"1412","DOI":"10.1038\/emboj.2010.36","article-title":"Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis","volume":"29","author":"Uehara","year":"2010","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M116.715573_bib27","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1111\/j.1365-2958.2012.08138.x","article-title":"A conformational switch controls cell wall-remodelling enzymes required for bacterial cell division","volume":"85","author":"Yang","year":"2012","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib28","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1016\/j.jmb.2005.09.082","article-title":"Crystal structures of active LytM","volume":"354","author":"Firczuk","year":"2005","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M116.715573_bib29","doi-asserted-by":"crossref","first-page":"3937","DOI":"10.1128\/JB.02094-14","article-title":"Cell separation in Vibrio cholerae is mediated by a single amidase whose action is modulated by two nonredundant activators","volume":"196","author":"M\u00f6ll","year":"2014","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib30","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1128\/JB.00540-15","article-title":"The gonococcal NlpD protein facilitates cell separation by activating peptidoglycan cleavage by AmiC","volume":"198","author":"Stohl","year":"2015","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib31","doi-asserted-by":"crossref","first-page":"7211","DOI":"10.1128\/JB.00724-06","article-title":"AmiC functions as an N-acetylmuramyl-l-alanine amidase necessary for cell separation and can promote autolysis in Neisseria gonorrhoeae","volume":"188","author":"Garcia","year":"2006","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib32","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1128\/jb.85.6.1274-1279.1963","article-title":"Neisseria gonorrhoeae. I. Virulence genetically linked to clonal variation","volume":"85","author":"Kellogg","year":"1963","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib33","doi-asserted-by":"crossref","first-page":"1418","DOI":"10.3181\/00379727-145-38025","article-title":"Factors affecting autolysis of Neisseria gonorrhoeae","volume":"145","author":"Morse","year":"1974","journal-title":"Proc. Soc. Exp. Biol. Med"},{"key":"10.1074\/jbc.M116.715573_bib34","doi-asserted-by":"crossref","DOI":"10.1002\/9780471729259.mc04a02s23","article-title":"Genetic manipulation of Neisseria gonorrhoeae","volume":"23","author":"Dillard","year":"2011","journal-title":"Curr. Protoc. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib35","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1038\/nprot.2015.053","article-title":"The Phyre2 web portal for protein modeling, prediction, and analysis","volume":"10","author":"Kelley","year":"2015","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.M116.715573_bib36","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.plasmid.2008.01.001","article-title":"Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli","volume":"59","author":"Rocco","year":"2008","journal-title":"Plasmid"},{"key":"10.1074\/jbc.M116.715573_bib37","doi-asserted-by":"crossref","first-page":"3068","DOI":"10.1128\/AEM.07871-11","article-title":"New complementation constructs for inducible and constitutive gene expression in Neisseria gonorrhoeae and Neisseria meningitidis","volume":"78","author":"Ramsey","year":"2012","journal-title":"Appl. Environ. Microbiol"},{"key":"10.1074\/jbc.M116.715573_bib38","doi-asserted-by":"crossref","first-page":"4718","DOI":"10.1128\/JB.183.16.4718-4726.2001","article-title":"Insertion-duplication mutagenesis of Neisseria: use in characterization of DNA transfer genes in the gonococcal genetic island","volume":"183","author":"Hamilton","year":"2001","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib39","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/0076-6879(94)35146-5","article-title":"Isolation of peptidoglycan and soluble peptidoglycan fragments","volume":"235","author":"Rosenthal","year":"1994","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.M116.715573_bib40","doi-asserted-by":"crossref","first-page":"2752","DOI":"10.1128\/IAI.70.6.2752-2757.2002","article-title":"A lytic transglycosylase of Neisseria gonorrhoeae is involved in peptidoglycan-derived cytotoxin production","volume":"70","author":"Cloud","year":"2002","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M116.715573_bib41","doi-asserted-by":"crossref","first-page":"5697","DOI":"10.1128\/IAI.73.9.5697-5705.2005","article-title":"Mutations affecting peptidoglycan acetylation in Neisseria gonorrhoeae and Neisseria meningitidis","volume":"73","author":"Dillard","year":"2005","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M116.715573_bib42","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.M116.715573_bib43","doi-asserted-by":"crossref","first-page":"11222","DOI":"10.1074\/jbc.M111.338830","article-title":"Neisseria gonorrhoeae virulence factor NG1686 is a bifunctional M23B family metallopeptidase that influences resistance to hydrogen peroxide and colony morphology","volume":"287","author":"Stohl","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715573_bib44","doi-asserted-by":"crossref","first-page":"2525","DOI":"10.1002\/cbic.201000626","article-title":"Synthetic peptidoglycan motifs for germination of bacterial spores","volume":"11","author":"Lee","year":"2010","journal-title":"Chembiochem"},{"key":"10.1074\/jbc.M116.715573_bib45","doi-asserted-by":"crossref","first-page":"3490","DOI":"10.1128\/IAI.00279-13","article-title":"Peptidoglycan fragment release from Neisseria meningitidis","volume":"81","author":"Woodhams","year":"2013","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M116.715573_bib46","doi-asserted-by":"crossref","first-page":"7811","DOI":"10.1128\/JB.186.22.7811-7814.2004","article-title":"Mutation of a single lytic transglycosylase causes aberrant septation and inhibits cell separation of Neisseria gonorrhoeae","volume":"186","author":"Cloud","year":"2004","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib47","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1128\/iai.28.3.867-875.1980","article-title":"Extent of peptide cross-linking in the peptidoglycan of Neisseria gonorrhoeae","volume":"28","author":"Rosenthal","year":"1980","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M116.715573_bib48","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1128\/jb.127.1.319-326.1976","article-title":"Amidase activity involved in peptidoglycan biosynthesis in membranes of Micrococcus luteus (sodonensis)","volume":"127","author":"Jensen","year":"1976","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib49","doi-asserted-by":"crossref","first-page":"28140","DOI":"10.1074\/jbc.M103903200","article-title":"Mutational analysis of catalytic sites of the cell wall lytic N-acetylmuramoyl-l-alanine amidases CwlC and CwlV","volume":"276","author":"Shida","year":"2001","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715573_bib50","doi-asserted-by":"crossref","first-page":"41702","DOI":"10.1074\/jbc.M307198200","article-title":"Peptidoglycan molecular requirements allowing detection by Nod1 and Nod2","volume":"278","author":"Girardin","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715573_bib51","doi-asserted-by":"crossref","first-page":"23818","DOI":"10.1074\/jbc.M109.033670","article-title":"pH-dependent internalization of muramyl peptides from early endosomes enables Nod1 and Nod2 signaling","volume":"284","author":"Lee","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715573_bib52","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.1038\/sj.embor.7400552","article-title":"Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin","volume":"6","author":"Magalhaes","year":"2005","journal-title":"EMBO Rep"},{"key":"10.1074\/jbc.M116.715573_bib53","doi-asserted-by":"crossref","first-page":"5989","DOI":"10.1128\/JB.00506-08","article-title":"Neisseria gonorrhoeae uses two lytic transglycosylases to produce cytotoxic peptidoglycan monomers","volume":"190","author":"Cloud-Hansen","year":"2008","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib54","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1177\/1753425913493453","article-title":"Activation of NOD receptors by Neisseria gonorrhoeae modulates the innate immune response","volume":"20","author":"Mavrogiorgos","year":"2014","journal-title":"Innate Immun"},{"key":"10.1074\/jbc.M116.715573_bib55","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1128\/AAC.19.2.316","article-title":"Properties of penicillin-binding proteins in Neisseria gonorrhoeae","volume":"19","author":"Barbour","year":"1981","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.M116.715573_bib56","doi-asserted-by":"crossref","first-page":"14614","DOI":"10.1021\/bi0350607","article-title":"Neisseria gonorrhoeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and \u03b2-lactam binding activities","volume":"42","author":"Stefanova","year":"2003","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.715573_bib57","doi-asserted-by":"crossref","first-page":"5345","DOI":"10.1128\/JB.00476-06","article-title":"Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli","volume":"188","author":"Priyadarshini","year":"2006","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib58","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1111\/j.1574-6976.2008.00105.x","article-title":"The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis","volume":"32","author":"Sauvage","year":"2008","journal-title":"FEMS Microbiol. Rev"},{"key":"10.1074\/jbc.M116.715573_bib59","doi-asserted-by":"crossref","first-page":"e1005338","DOI":"10.1371\/journal.pgen.1005338","article-title":"Common cell shape evolution of two nasopharyngeal pathogens","volume":"11","author":"Veyrier","year":"2015","journal-title":"PLoS Genet"},{"key":"10.1074\/jbc.M116.715573_bib60","unstructured":"Garcia, D. L., (2007) Liberation of Pro-inflammatory Peptidoglycan Fragments from the Gonococcal Cell. Ph.D. thesis, University of Wisconsin, Madison"},{"key":"10.1074\/jbc.M116.715573_bib61","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1128\/jb.126.3.1186-1193.1976","article-title":"Mechanism of autolysis of Neisseria gonorrhoeae","volume":"126","author":"Hebeler","year":"1976","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.715573_bib62","doi-asserted-by":"crossref","first-page":"2543","DOI":"10.1107\/S0907444913026371","article-title":"The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis","volume":"69","author":"Kumar","year":"2013","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.M116.715573_bib63","doi-asserted-by":"crossref","first-page":"31549","DOI":"10.1074\/jbc.M113.510792","article-title":"Structural and biochemical analyses of Mycobacterium tuberculosis N-acetylmuramyl-l-alanine amidase Rv3717 point to a role in peptidoglycan fragment recycling","volume":"288","author":"Prigozhin","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715573_bib64","doi-asserted-by":"crossref","first-page":"31714","DOI":"10.1074\/jbc.M111.264366","article-title":"Crystal structures of bacterial peptidoglycan amidase AmpD and an unprecedented activation mechanism","volume":"286","author":"Carrasco-L\u00f3pez","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715573_bib65","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1097\/QCO.0000000000000058","article-title":"Preparing for an era of untreatable gonorrhea","volume":"27","author":"Barbee","year":"2014","journal-title":"Curr. Opin. Infect. Dis"},{"key":"10.1074\/jbc.M116.715573_bib66","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.bioorg.2014.03.007","article-title":"Bacterial cell division proteins as antibiotic targets","volume":"55","author":"den Blaauwen","year":"2014","journal-title":"Bioorg. Chem"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820401218?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820401218?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M116.715573","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,6,15]],"date-time":"2024-06-15T01:58:45Z","timestamp":1718416725000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820401218"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,5]]},"references-count":66,"journal-issue":{"issue":"20","published-print":{"date-parts":[[2016,5]]}},"alternative-id":["S0021925820401218"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m116.715573","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2016,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Amidase Activity of AmiC Controls Cell Separation and Stem Peptide Release and Is Enhanced by NlpD 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.M116.715573","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}