{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T01:07:12Z","timestamp":1791248832031,"version":"4.1.0"},"reference-count":54,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2010,7,1]],"date-time":"2010-07-01T00:00:00Z","timestamp":1277942400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2010,7,1]],"date-time":"2010-07-01T00:00:00Z","timestamp":1277942400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2010,7,1]],"date-time":"2010-07-01T00:00:00Z","timestamp":1277942400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2010,7,1]],"date-time":"2010-07-01T00:00:00Z","timestamp":1277942400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2010,7,1]],"date-time":"2010-07-01T00:00:00Z","timestamp":1277942400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2010,7,1]],"date-time":"2010-07-01T00:00:00Z","timestamp":1277942400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2010,7,1]],"date-time":"2010-07-01T00:00:00Z","timestamp":1277942400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE-AC02-05CH11231"],"award-info":[{"award-number":["DE-AC02-05CH11231"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006132","name":"Office of Science","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006132","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006151","name":"Basic Energy Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006151","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2010,7]]},"DOI":"10.1016\/j.jmb.2010.05.040","type":"journal-article","created":{"date-parts":[[2010,6,2]],"date-time":"2010-06-02T01:34:28Z","timestamp":1275442468000},"page":"998-1010","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":53,"title":["Crystal Structure of the AmpR Effector Binding Domain Provides Insight into the Molecular Regulation of Inducible AmpC \u03b2-Lactamase"],"prefix":"10.1016","volume":"400","author":[{"given":"Misty D.","family":"Balcewich","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas M.","family":"Reeve","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evan A.","family":"Orlikow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lynda J.","family":"Donald","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David J.","family":"Vocadlo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian L.","family":"Mark","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2010.05.040_bib1","first-page":"557","article-title":"Beta-lactamases in laboratory and clinical resistance","volume":"8","author":"Livermore","year":"1995","journal-title":"Am. Soc. Microbiol."},{"key":"10.1016\/j.jmb.2010.05.040_bib2","doi-asserted-by":"crossref","first-page":"6602","DOI":"10.1073\/pnas.85.18.6602","article-title":"A large family of bacterial activator proteins","volume":"85","author":"Henikoff","year":"1988","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.05.040_bib3","doi-asserted-by":"crossref","first-page":"3709","DOI":"10.1002\/j.1460-2075.1986.tb04704.x","article-title":"Inducible cephalosporinase production in clinical isolates of Enterobacter cloacae is controlled by a regulatory gene that has been deleted from Escherichia coli","volume":"5","author":"Honore","year":"1986","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2010.05.040_bib4","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/S0092-8674(00)81928-5","article-title":"Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in Gram-negative bacteria","volume":"88","author":"Jacobs","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2010.05.040_bib5","doi-asserted-by":"crossref","first-page":"3746","DOI":"10.1128\/jb.171.7.3746-3753.1989","article-title":"Binding of the Citrobacter freundii AmpR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC beta-lactamase gene","volume":"171","author":"Lindquist","year":"1989","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2010.05.040_bib6","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1111\/j.1365-2958.1991.tb01920.x","article-title":"Purification and mutant analysis of Citrobacter freundii AmpR, the regulator for chromosomal AmpC beta-lactamase","volume":"5","author":"Bartowsky","year":"1991","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2010.05.040_bib7","doi-asserted-by":"crossref","first-page":"2274","DOI":"10.1128\/AAC.01617-08","article-title":"Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal \u03b2-lactam resistance in Pseudomonas aeruginosa","volume":"53","author":"Asgarali","year":"2009","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.05.040_bib8","doi-asserted-by":"crossref","first-page":"6434","DOI":"10.1128\/JB.184.23.6434-6436.2002","article-title":"Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides","volume":"184","author":"Cheng","year":"2002","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2010.05.040_bib9","doi-asserted-by":"crossref","first-page":"2173","DOI":"10.1128\/AAC.40.9.2173","article-title":"Location of N-acetylmuramyl-l-alanyl-d-glutamylmesodiaminopimelic acid, presumed signal molecule for beta-lactamase induction, in the bacterial cell","volume":"40","author":"Dietz","year":"1996","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.05.040_bib10","doi-asserted-by":"crossref","first-page":"4836","DOI":"10.1128\/JB.182.17.4836-4840.2000","article-title":"Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling","volume":"182","author":"Cheng","year":"2000","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2010.05.040_bib11","doi-asserted-by":"crossref","first-page":"39032","DOI":"10.1074\/jbc.M004797200","article-title":"Characterization of a beta-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and beta-lactamase induction","volume":"275","author":"Votsch","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.05.040_bib12","doi-asserted-by":"crossref","first-page":"2113","DOI":"10.1128\/AAC.41.10.2113","article-title":"The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide","volume":"41","author":"Dietz","year":"1997","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.05.040_bib13","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1111\/j.1574-6968.1994.tb07159.x","article-title":"The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-l-alanine amidase","volume":"122","author":"Holtje","year":"1994","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.jmb.2010.05.040_bib14","doi-asserted-by":"crossref","first-page":"4684","DOI":"10.1002\/j.1460-2075.1994.tb06792.x","article-title":"Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction","volume":"13","author":"Jacobs","year":"1994","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2010.05.040_bib15","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1016\/S1369-5274(01)00261-2","article-title":"Morphogenesis of Escherichia coli","volume":"4","author":"Vollmer","year":"2001","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.jmb.2010.05.040_bib16","doi-asserted-by":"crossref","first-page":"1780","DOI":"10.1128\/AAC.50.5.1780-1787.2006","article-title":"Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring high-level beta-lactam resistance involves three AmpD homologues","volume":"50","author":"Juan","year":"2006","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.05.040_bib17","doi-asserted-by":"crossref","first-page":"2955","DOI":"10.1128\/JCM.43.6.2955-2958.2005","article-title":"Gene mutations responsible for overexpression of AmpC beta-lactamase in some clinical isolates of Enterobacter cloacae","volume":"43","author":"Kaneko","year":"2005","journal-title":"J. Clin. Microbiol."},{"key":"10.1016\/j.jmb.2010.05.040_bib18","doi-asserted-by":"crossref","first-page":"4733","DOI":"10.1128\/AAC.49.11.4733-4738.2005","article-title":"Molecular mechanisms of \u03b2-lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains","volume":"49","author":"Juan","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.05.040_bib19","doi-asserted-by":"crossref","first-page":"1923","DOI":"10.1128\/jb.169.5.1923-1928.1987","article-title":"Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii beta-lactamase","volume":"169","author":"Lindberg","year":"1987","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2010.05.040_bib20","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.ppat.1000353","article-title":"\u03b2-Lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein","volume":"5","author":"Moya","year":"2009","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jmb.2010.05.040_bib21","doi-asserted-by":"crossref","first-page":"4620","DOI":"10.1073\/pnas.82.14.4620","article-title":"Regulatory components in Citrobacter freundii ampC beta-lactamase induction","volume":"82","author":"Lindberg","year":"1985","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.05.040_bib22","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1146\/annurev.mi.47.100193.003121","article-title":"Molecular biology of the LysR family of transcriptional regulators","volume":"47","author":"Schell","year":"1993","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.jmb.2010.05.040_bib23","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/S0022-2836(03)00312-7","article-title":"Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend","volume":"328","author":"Muraoka","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.05.040_bib24","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1007\/s00216-006-0505-3","article-title":"ClcR-based biosensing system in the detection of cis-dihydroxylated (chloro-) biphenyls","volume":"385","author":"Feliciano","year":"2006","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.jmb.2010.05.040_bib25","first-page":"2149","article-title":"Growth medium composition-determined regulatory mechanisms are superimposed on CatR-mediated transcription from the pheBA and catBCA promoters in Pseudomonas putida","volume":"147","author":"Tover","year":"2001","journal-title":"Soc. Gen. Microbiol."},{"key":"10.1016\/j.jmb.2010.05.040_bib26","doi-asserted-by":"crossref","first-page":"3609","DOI":"10.1099\/mic.0.2008\/022772-0","article-title":"Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins","volume":"154","author":"Maddocks","year":"2008","journal-title":"Microbiology"},{"key":"10.1016\/j.jmb.2010.05.040_bib27","series-title":"The PyMOL Molecular Graphics System","author":"DeLano","year":"2002"},{"key":"10.1016\/j.jmb.2010.05.040_bib28","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/S0969-2126(97)00254-2","article-title":"The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement","volume":"5","author":"Tyrrell","year":"1997","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2010.05.040_bib29","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1016\/j.jmb.2006.09.090","article-title":"Distinct effector-binding sites enable synergistic transcriptional activation by BenM, a LysR-type regulator","volume":"367","author":"Ezezika","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.05.040_bib30","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1016\/j.jmb.2007.06.076","article-title":"In vivo and in vitro investigation of transcriptional regulation by DntR","volume":"372","author":"L\u00f6nneborg","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.05.040_bib31","doi-asserted-by":"crossref","first-page":"4545","DOI":"10.1093\/nar\/gkp445","article-title":"The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators","volume":"37","author":"Sainsbury","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2010.05.040_bib32","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1016\/j.jmb.2009.12.033","article-title":"Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation","volume":"396","author":"Zhou","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.05.040_bib33","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1073\/pnas.181342398","article-title":"Electrostatics of nanosystems: application to microtubules and the ribosome","volume":"98","author":"Baker","year":"2001","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.05.040_bib34","series-title":"APBS Plugin for PyMOL","author":"Lerner","year":"2006"},{"key":"10.1016\/j.jmb.2010.05.040_bib35","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1128\/MMBR.00027-07","article-title":"How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)","volume":"72","author":"Park","year":"2008","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.jmb.2010.05.040_bib36","doi-asserted-by":"crossref","first-page":"21382","DOI":"10.1074\/jbc.M700084200","article-title":"Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance","volume":"282","author":"Stubbs","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.05.040_bib37","doi-asserted-by":"crossref","first-page":"4567","DOI":"10.1128\/AAC.49.11.4567-4575.2005","article-title":"Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB \u03b2-lactamases, proteases, quorum sensing, and other virulence factors","volume":"49","author":"Kong","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.05.040_bib38","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1006\/jmbi.1993.1012","article-title":"Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin","volume":"229","author":"Van Duyne","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.05.040_bib39","first-page":"204","article-title":"Waterbug dialysis","volume":"19","author":"Orr","year":"1995","journal-title":"Biotechniques"},{"key":"10.1016\/j.jmb.2010.05.040_bib40","series-title":"Cell Biology: A Laboratory Handbook","first-page":"457","article-title":"Mass spectrometry in noncovalent protein interactions and protein assemblies","author":"Donald","year":"2006"},{"key":"10.1016\/j.jmb.2010.05.040_bib41","author":"Kozlovski","year":"2005"},{"key":"10.1016\/j.jmb.2010.05.040_bib42","article-title":"Mosflm","volume":"26","author":"Leslie","year":"1992","journal-title":"Jt. CCP4 ESF-EACBM Newsl."},{"key":"10.1016\/j.jmb.2010.05.040_bib43","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jmb.2010.05.040_bib44","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1107\/S090744499900935X","article-title":"The finer things in X-ray diffraction data collection","volume":"55","author":"Pflugrath","year":"1999","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jmb.2010.05.040_bib45","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1107\/S0907444902016657","article-title":"PHENIX: building new software for automated crystallographic structure determination","volume":"58","author":"Adams","year":"2002","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jmb.2010.05.040_bib46","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1038\/355472a0","article-title":"Free R-value\u2014a novel statistical quantity for assessing the accuracy of crystal-structures","volume":"355","author":"Brunger","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2010.05.040_bib47","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jmb.2010.05.040_bib48","doi-asserted-by":"crossref","first-page":"W375","DOI":"10.1093\/nar\/gkm216","article-title":"MolProbity: all-atom contacts and structure validation for proteins and nucleic acids","volume":"35","author":"Davis","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2010.05.040_bib49","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jmb.2010.05.040_bib50","doi-asserted-by":"crossref","DOI":"10.1002\/jcc.20634","article-title":"A semiempirical free energy force field with charge-based desolvation","volume":"28","author":"Huey","year":"2007","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmb.2010.05.040_bib51","first-page":"370","article-title":"Estimation of the number of [agr]-helical and [bgr]-strand segments in proteins using circular dichroism spectroscopy","volume":"8","author":"Sreerama","year":"1999","journal-title":"PRS"},{"key":"10.1016\/j.jmb.2010.05.040_bib52","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1006\/abio.1993.1079","article-title":"A self-consistent method for the analysis of protein secondary structure from circular dichroism","volume":"209","author":"Sreerama","year":"1993","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jmb.2010.05.040_bib53","doi-asserted-by":"crossref","first-page":"W668","DOI":"10.1093\/nar\/gkh371","article-title":"DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data","volume":"32","author":"Whitmore","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2010.05.040_bib54","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1093\/bioinformatics\/18.1.211","article-title":"DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra","volume":"18","author":"Lobley","year":"2002","journal-title":"Bioinformatics"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283610005322?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283610005322?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T06:11:17Z","timestamp":1762668677000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283610005322"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,7]]},"references-count":54,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2010,7]]}},"alternative-id":["S0022283610005322"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2010.05.040","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2010,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Crystal Structure of the AmpR Effector Binding Domain Provides Insight into the Molecular Regulation of Inducible AmpC \u03b2-Lactamase","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2010.05.040","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2010 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}