{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,8]],"date-time":"2026-06-08T10:10:51Z","timestamp":1780913451185,"version":"3.54.1"},"reference-count":64,"publisher":"Elsevier BV","issue":"49","license":[{"start":{"date-parts":[[2012,11,1]],"date-time":"2012-11-01T00:00:00Z","timestamp":1351728000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,6]],"date-time":"2020-09-06T00:00:00Z","timestamp":1599350400000},"content-version":"vor","delay-in-days":2866,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2012,11]]},"DOI":"10.1074\/jbc.m112.412809","type":"journal-article","created":{"date-parts":[[2012,9,20]],"date-time":"2012-09-20T00:13:02Z","timestamp":1348099982000},"page":"41089-41102","source":"Crossref","is-referenced-by-count":33,"title":["Certhrax Toxin, an Anthrax-related ADP-ribosyltransferase from Bacillus cereus"],"prefix":"10.1016","volume":"287","author":[{"given":"Danielle","family":"Visschedyk","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amanda","family":"Rochon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfram","family":"Tempel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Svetoslav","family":"Dimov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hee-Won","family":"Park","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.Rod","family":"Merrill","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M112.412809_bib1","series-title":"Bacterial Protein Toxins","author":"Burns","year":"2003"},{"key":"10.1074\/jbc.M112.412809_bib2","doi-asserted-by":"crossref","first-page":"933","DOI":"10.3201\/eid0706.010604","article-title":"Bioterrorism-related inhalational anthrax. The first 10 cases reported in the United States","volume":"7","author":"Jernigan","year":"2001","journal-title":"Emerg. Infect. Dis."},{"key":"10.1074\/jbc.M112.412809_bib3","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1126\/science.280.5364.734","article-title":"Proteolytic inactivation of MAP kinase kinase by anthrax lethal factor","volume":"280","author":"Duesbery","year":"1998","journal-title":"Science"},{"key":"10.1074\/jbc.M112.412809_bib4","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/j.mam.2009.07.006","article-title":"The anthrax lethal factor and its MAPK kinase-specific metalloprotease activity","volume":"30","author":"Tonello","year":"2009","journal-title":"Mol. Aspects Med."},{"key":"10.1074\/jbc.M112.412809_bib5","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1006\/bbrc.1998.9040","article-title":"Anthrax lethal factor cleaves the N terminus of MAPKKs and induces tyrosine\/threonine phosphorylation of MAPKs in cultured macrophages","volume":"248","author":"Vitale","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1074\/jbc.M112.412809_bib6","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1038\/415396a","article-title":"Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin","volume":"415","author":"Drum","year":"2002","journal-title":"Nature"},{"key":"10.1074\/jbc.M112.412809_bib7","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1038\/sj.emboj.7600574","article-title":"Calcium-independent calmodulin binding and two-metal ion catalytic mechanism of anthrax edema factor","volume":"24","author":"Shen","year":"2005","journal-title":"EMBO J."},{"key":"10.1074\/jbc.M112.412809_bib8","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1111\/j.1365-2958.2006.05179.x","article-title":"Poly-\u03b3-glutamate in bacteria","volume":"60","author":"Candela","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1074\/jbc.M112.412809_bib9","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1128\/CMR.00073-09","article-title":"Bacillus cereus, a volatile human pathogen","volume":"23","author":"Bottone","year":"2010","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1074\/jbc.M112.412809_bib10","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1086\/510429","article-title":"Fatal pneumonia among metalworkers due to inhalation exposure to Bacillus cereus containing Bacillus anthracis toxin genes","volume":"44","author":"Avashia","year":"2007","journal-title":"Clin. Infect. Dis."},{"key":"10.1074\/jbc.M112.412809_bib11","doi-asserted-by":"crossref","first-page":"8449","DOI":"10.1073\/pnas.0402414101","article-title":"Identification of anthrax toxin genes in a Bacillus cereus associated with an illness resembling inhalation anthrax","volume":"101","author":"Hoffmaster","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.412809_bib12","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1146\/annurev.micro.62.081307.162848","article-title":"Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins","volume":"62","author":"Deng","year":"2008","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1074\/jbc.M112.412809_bib13","doi-asserted-by":"crossref","first-page":"4579","DOI":"10.1111\/j.1742-4658.2006.05442.x","article-title":"A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins","volume":"273","author":"Holbourn","year":"2006","journal-title":"FEBS J."},{"key":"10.1074\/jbc.M112.412809_bib14","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/j.tibs.2008.08.003","article-title":"Needle in the haystack. Structure-based toxin discovery","volume":"33","author":"Fieldhouse","year":"2008","journal-title":"Trends Biochem. Sci."},{"key":"10.1074\/jbc.M112.412809_bib15","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1038\/322390a0","article-title":"Botulinum C2 toxin ADP-ribosylates actin","volume":"322","author":"Aktories","year":"1986","journal-title":"Nature"},{"key":"10.1074\/jbc.M112.412809_bib16","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/0014-5793(87)81129-8","article-title":"Clostridium perfringens \u03b9-toxin ADP-ribosylates skeletal muscle actin in Arg-177","volume":"225","author":"Vandekerckhove","year":"1987","journal-title":"FEBS Lett."},{"key":"10.1074\/jbc.M112.412809_bib17","doi-asserted-by":"crossref","first-page":"13525","DOI":"10.1074\/jbc.M109.077339","article-title":"Photox, a novel actin-targeting mono-ADP-ribosyltransferase from Photorhabdus luminescens","volume":"285","author":"Visschedyk","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.412809_bib18","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1111\/j.1432-1033.1988.tb13908.x","article-title":"Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes","volume":"172","author":"Aktories","year":"1988","journal-title":"Eur. J. Biochem."},{"key":"10.1074\/jbc.M112.412809_bib19","doi-asserted-by":"crossref","first-page":"19312","DOI":"10.1016\/S0021-9258(18)54999-1","article-title":"Clostridium botulinum C3 ADP-ribosyltransferase gene. Cloning, sequencing, and expression of a functional protein in Escherichia coli","volume":"266","author":"Nemoto","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.412809_bib20","doi-asserted-by":"crossref","first-page":"10274","DOI":"10.1016\/S0021-9258(19)50014-X","article-title":"Purification and characterization of an ADP-ribosyltransferase produced by Clostridium limosum","volume":"267","author":"Just","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.412809_bib21","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1021\/bi015809i","article-title":"Structure-function analysis of the Rho-ADP-ribosylating exoenzyme C3stau2 from Staphylococcus aureus","volume":"41","author":"Wilde","year":"2002","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M112.412809_bib22","doi-asserted-by":"crossref","first-page":"7760","DOI":"10.1128\/IAI.69.12.7760-7771.2001","article-title":"Complete nucleotide sequence of a Staphylococcus aureus exfoliative toxin B plasmid and identification of a novel ADP-ribosyltransferase, EDIN-C","volume":"69","author":"Yamaguchi","year":"2001","journal-title":"Infect. Immun."},{"key":"10.1074\/jbc.M112.412809_bib23","doi-asserted-by":"crossref","first-page":"5835","DOI":"10.1128\/IAI.70.10.5835-5845.2002","article-title":"Identification of the Staphylococcus aureus etd pathogenicity island, which encodes a novel exfoliative toxin, ETD, and EDIN-B","volume":"70","author":"Yamaguchi","year":"2002","journal-title":"Infect. Immun."},{"key":"10.1074\/jbc.M112.412809_bib24","doi-asserted-by":"crossref","first-page":"29506","DOI":"10.1074\/jbc.273.45.29506","article-title":"Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis","volume":"273","author":"Barth","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.412809_bib25","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1038\/13300","article-title":"Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex","volume":"6","author":"Han","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1074\/jbc.M112.412809_bib26","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1038\/embor.2008.90","article-title":"The nature and character of the transition state for the ADP-ribosyltransferase reaction","volume":"9","author":"J\u00f8rgensen","year":"2008","journal-title":"EMBO Rep."},{"key":"10.1074\/jbc.M112.412809_bib27","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/S0065-2571(02)00044-4","article-title":"Clostridium perfringens \u03b9-toxin, ADP-ribosyltransferase. Structure and mechanism of action","volume":"43","author":"Sakurai","year":"2003","journal-title":"Adv. Enzyme Regul."},{"key":"10.1074\/jbc.M112.412809_bib28","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.tibs.2005.12.007","article-title":"Stealth and mimicry by deadly bacterial toxins","volume":"31","author":"Yates","year":"2006","journal-title":"Trends Biochem. Sci."},{"key":"10.1074\/jbc.M112.412809_bib29","doi-asserted-by":"crossref","first-page":"e1001029","DOI":"10.1371\/journal.pcbi.1001029","article-title":"Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases","volume":"6","author":"Fieldhouse","year":"2010","journal-title":"PLoS Comput. Biol."},{"key":"10.1074\/jbc.M112.412809_bib30","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1128\/AAC.01164-10","article-title":"Newly discovered and characterized antivirulence compounds inhibit bacterial mono-ADP-ribosyltransferase toxins","volume":"55","author":"Turgeon","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.M112.412809_bib31","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1042\/BJ20041480","article-title":"Structure-function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa","volume":"385","author":"Yates","year":"2005","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M112.412809_bib32","doi-asserted-by":"crossref","first-page":"3099","DOI":"10.1016\/0006-2952(73)90196-2","article-title":"Relationship between the inhibition constant (K1) and the concentration of inhibitor that causes 50 percent inhibition (I50) of an enzymatic reaction","volume":"22","author":"Cheng","year":"1973","journal-title":"Biochem. Pharmacol."},{"key":"10.1074\/jbc.M112.412809_bib33","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1111\/j.1574-6968.2009.01777.x","article-title":"Yeast as a tool for characterizing mono-ADP-ribosyltransferase toxins","volume":"300","author":"Turgeon","year":"2009","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1074\/jbc.M112.412809_bib34","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1107\/S0909049511019431","article-title":"Beamline 08ID-1, the prime beamline of the Canadian Macromolecular Crystallography Facility","volume":"18","author":"Grochulski","year":"2011","journal-title":"J. Synchrotron Radiat."},{"key":"10.1074\/jbc.M112.412809_bib35","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.M112.412809_bib36","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.M112.412809_bib37","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1021\/bi052253g","article-title":"Exchange of glutamine-217 to glutamate of Clostridium limosum exoenzyme C3 turns the asparagine-specific ADP-ribosyltransferase into an arginine-modifying enzyme","volume":"45","author":"Vogelsgesang","year":"2006","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M112.412809_bib38","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1107\/S0021889897006766","article-title":"MOLREP. An automated program for molecular replacement","volume":"30","author":"Vagin","year":"1997","journal-title":"J. Appl. Crystallogr."},{"key":"10.1074\/jbc.M112.412809_bib39","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":"10.1074\/jbc.M112.412809_bib40","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. D Biol. Crystallogr."},{"key":"10.1074\/jbc.M112.412809_bib41","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. D. Biol. Crystallogr."},{"key":"10.1074\/jbc.M112.412809_bib42","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for building protein models in electron density maps and the location of errors in these models","volume":"47","author":"Jones","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1074\/jbc.M112.412809_bib43","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1074\/jbc.M112.412809_bib44","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.M112.412809_bib45","doi-asserted-by":"crossref","first-page":"11099","DOI":"10.1016\/S0021-9258(18)60433-8","article-title":"Internalization and processing of Bacillus anthracis lethal toxin by toxin-sensitive and -resistant cells","volume":"264","author":"Singh","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.412809_bib46","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1038\/385833a0","article-title":"Crystal structure of the anthrax toxin protective antigen","volume":"385","author":"Petosa","year":"1997","journal-title":"Nature"},{"key":"10.1074\/jbc.M112.412809_bib47","doi-asserted-by":"crossref","first-page":"20124","DOI":"10.1016\/S0021-9258(18)54899-7","article-title":"Functional mapping of anthrax toxin lethal factor by in-frame insertion mutagenesis","volume":"266","author":"Quinn","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.412809_bib48","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1111\/j.1462-5822.2010.01480.x","article-title":"Imaging the cell entry of the anthrax edema and lethal toxins with fluorescent protein chimeras","volume":"12","author":"Zornetta","year":"2010","journal-title":"Cell Microbiol."},{"key":"10.1074\/jbc.M112.412809_bib49","doi-asserted-by":"crossref","first-page":"2509","DOI":"10.1111\/j.1462-5822.2008.01226.x","article-title":"Functional interactions between anthrax toxin receptors and the WNT signaling protein LRP6","volume":"10","author":"Abrami","year":"2008","journal-title":"Cell Microbiol."},{"key":"10.1074\/jbc.M112.412809_bib50","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1006\/abio.2001.5052","article-title":"Application of a fluorometric assay for characterization of the catalytic competency of a domain III fragment of Pseudomonas aeruginosa exotoxin A","volume":"292","author":"Armstrong","year":"2001","journal-title":"Anal. Biochem."},{"key":"10.1074\/jbc.M112.412809_bib51","doi-asserted-by":"crossref","first-page":"30950","DOI":"10.1074\/jbc.M201844200","article-title":"NAD binding induces conformational changes in Rho ADP-ribosylating Clostridium botulinum C3 exoenzyme","volume":"277","author":"M\u00e9n\u00e9trey","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.412809_bib52","doi-asserted-by":"crossref","first-page":"1630","DOI":"10.1074\/jbc.M511164200","article-title":"Structural determinants for the binding of anthrax lethal factor to oligomeric protective antigen","volume":"281","author":"Melnyk","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.412809_bib53","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1006\/bbrc.2000.4099","article-title":"Involvement of residues 147VYYEIGK153 in binding of lethal factor to protective antigen of Bacillus anthracis","volume":"280","author":"Gupta","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1074\/jbc.M112.412809_bib54","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1006\/jmbi.2000.4292","article-title":"Crystal structure and novel recognition motif of rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum. structural insights for recognition specificity and catalysis","volume":"305","author":"Han","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1074\/jbc.M112.412809_bib55","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/S0022-2836(02)01247-0","article-title":"Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens \u03b9-toxin","volume":"325","author":"Tsuge","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1074\/jbc.M112.412809_bib56","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1007\/s00726-010-0676-2","article-title":"ADP-ribosylation of arginine","volume":"41","author":"Laing","year":"2011","journal-title":"Amino Acids"},{"key":"10.1074\/jbc.M112.412809_bib57","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1021\/bi9520848","article-title":"Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide","volume":"35","author":"Bell","year":"1996","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M112.412809_bib58","doi-asserted-by":"crossref","first-page":"6902","DOI":"10.1073\/pnas.93.14.6902","article-title":"Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog. Implications for the activation process and for ADP ribosylation","volume":"93","author":"Li","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.412809_bib59","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1128\/JB.01313-06","article-title":"Complete sequence analysis of novel plasmids from emetic and periodontal Bacillus cereus isolates reveals a common evolutionary history among the B. cereus group plasmids, including Bacillus anthracis pXO1","volume":"189","author":"Rasko","year":"2007","journal-title":"J. Bacteriol."},{"key":"10.1074\/jbc.M112.412809_bib60","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1111\/j.1365-2958.2011.07582.x","article-title":"Two capsular polysaccharides enable Bacillus cereus G9241 to cause anthrax-like disease","volume":"80","author":"Oh","year":"2011","journal-title":"Mol. Microbiol."},{"key":"10.1074\/jbc.M112.412809_bib61","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.ygeno.2011.03.008","article-title":"Investigating the genome diversity of B. cereus and evolutionary aspects of B. anthracis emergence","volume":"98","author":"Papazisi","year":"2011","journal-title":"Genomics"},{"key":"10.1074\/jbc.M112.412809_bib62","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1111\/j.1574-6976.2008.00112.x","article-title":"From soil to gut. Bacillus cereus and its food poisoning toxins","volume":"32","author":"Stenfors Arnesen","year":"2008","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1074\/jbc.M112.412809_bib63","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/nrmicro2506","article-title":"You cannot B. cereus","volume":"9","author":"Salter","year":"2011","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1074\/jbc.M112.412809_bib64","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/n35101998","article-title":"Crystal structure of the anthrax lethal factor","volume":"414","author":"Pannifer","year":"2001","journal-title":"Nature"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820439110?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820439110?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M112.412809","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T13:13:43Z","timestamp":1641302023000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820439110"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,11]]},"references-count":64,"journal-issue":{"issue":"49","published-print":{"date-parts":[[2012,11]]}},"alternative-id":["S0021925820439110"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m112.412809","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2012,11]]}}}