{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T03:29:31Z","timestamp":1767929371960,"version":"3.49.0"},"reference-count":54,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2017,1,1]],"date-time":"2017-01-01T00:00:00Z","timestamp":1483228800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,28]],"date-time":"2020-08-28T00:00:00Z","timestamp":1598572800000},"content-version":"vor","delay-in-days":1335,"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":["R01 GM105947"],"award-info":[{"award-number":["R01 GM105947"]}],"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":["R01 GM104047"],"award-info":[{"award-number":["R01 GM104047"]}],"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":["T32 GM007324"],"award-info":[{"award-number":["T32 GM007324"]}],"id":[{"id":"10.13039\/100000057","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":[[2017,1]]},"DOI":"10.1074\/jbc.m116.761734","type":"journal-article","created":{"date-parts":[[2016,12,2]],"date-time":"2016-12-02T01:15:22Z","timestamp":1480641322000},"page":"814-825","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":14,"title":["Identification of a Substrate-selective Exosite within the Metalloproteinase Anthrax Lethal Factor"],"prefix":"10.1016","volume":"292","author":[{"given":"Allison B.","family":"Goldberg","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eunice","family":"Cho","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chad J.","family":"Miller","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hua Jane","family":"Lou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Benjamin E.","family":"Turk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M116.761734_bib1","first-page":"1","article-title":"Bacterial protein toxins: an overview","volume":"145","author":"Alouf","year":"2000","journal-title":"Methods Mol. Biol"},{"key":"10.1074\/jbc.M116.761734_bib2","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1038\/365160a0","article-title":"Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25","volume":"365","author":"Blasi","year":"1993","journal-title":"Nature"},{"key":"10.1074\/jbc.M116.761734_bib3","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1038\/359832a0","article-title":"Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin","volume":"359","author":"Schiavo","year":"1992","journal-title":"Nature"},{"key":"10.1074\/jbc.M116.761734_bib4","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1042\/BJ20061891","article-title":"Manipulation of host signalling pathways by anthrax toxins","volume":"402","author":"Turk","year":"2007","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M116.761734_bib5","doi-asserted-by":"crossref","first-page":"6313","DOI":"10.1128\/IAI.72.11.6313-6317.2004","article-title":"Functional analysis of Bacillus anthracis protective antigen by using neutralizing monoclonal antibodies","volume":"72","author":"Brossier","year":"2004","journal-title":"Infect. Immun"},{"key":"10.1074\/jbc.M116.761734_bib6","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1042\/bj20031382","article-title":"Anthrax lethal factor-cleavage products of MAPK (mitogen-activated protein kinase) kinases exhibit reduced binding to their cognate MAPKs","volume":"378","author":"Bardwell","year":"2004","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M116.761734_bib7","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.M116.761734_bib8","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-1-60761-795-2_1","article-title":"The MAP kinase signaling cascades: a system of hundreds of components regulates a diverse array of physiological functions","volume":"661","author":"Keshet","year":"2010","journal-title":"Methods. Mol. Biol"},{"key":"10.1074\/jbc.M116.761734_bib9","doi-asserted-by":"crossref","first-page":"6552","DOI":"10.4049\/jimmunol.167.11.6552","article-title":"Role of p38 mitogen-activated protein kinase in chemokine-induced emigration and chemotaxis in vivo","volume":"167","author":"Cara","year":"2001","journal-title":"J. Immunol"},{"key":"10.1074\/jbc.M116.761734_bib10","doi-asserted-by":"crossref","first-page":"27059","DOI":"10.1074\/jbc.M314258200","article-title":"Distinct ligand-dependent roles for p38 MAPK in priming and activation of the neutrophil NADPH oxidase","volume":"279","author":"Brown","year":"2004","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.761734_bib11","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0898-6568(00)00149-2","article-title":"LPS induction of gene expression in human monocytes","volume":"13","author":"Guha","year":"2001","journal-title":"Cell. Signal"},{"key":"10.1074\/jbc.M116.761734_bib12","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1089\/jir.2013.0146","article-title":"The role of mammalian MAPK signaling in regulation of cytokine mRNA stability and translation","volume":"34","author":"Tiedje","year":"2014","journal-title":"J. Interferon Cytokine Res"},{"key":"10.1074\/jbc.M116.761734_bib13","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1126\/science.1073163","article-title":"Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition","volume":"297","author":"Park","year":"2002","journal-title":"Science"},{"key":"10.1074\/jbc.M116.761734_bib14","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1038\/nature12510","article-title":"Key tissue targets responsible for anthrax-toxin-induced lethality","volume":"501","author":"Liu","year":"2013","journal-title":"Nature"},{"key":"10.1074\/jbc.M116.761734_bib15","doi-asserted-by":"crossref","first-page":"e13335","DOI":"10.1371\/journal.pone.0013335","article-title":"Anthrax lethal toxin suppresses murine cardiomyocyte contractile function and intracellular Ca2+ handling via a NADPH oxidase-dependent mechanism","volume":"5","author":"Kandadi","year":"2010","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M116.761734_bib16","doi-asserted-by":"crossref","first-page":"3884","DOI":"10.1016\/j.ijcard.2013.06.050","article-title":"Anthrax lethal toxin induces acute diastolic dysfunction in rats through disruption of the phospholamban signaling network","volume":"168","author":"Golden","year":"2013","journal-title":"Int. J. Cardiol"},{"key":"10.1074\/jbc.M116.761734_bib17","doi-asserted-by":"crossref","first-page":"e49741","DOI":"10.1371\/journal.pone.0049741","article-title":"Anthrax lethal factor cleaves mouse Nlrp1b in both toxin-sensitive and toxin-resistant macrophages","volume":"7","author":"Hellmich","year":"2012","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M116.761734_bib18","doi-asserted-by":"crossref","first-page":"e1003452","DOI":"10.1371\/journal.ppat.1003452","article-title":"Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor","volume":"9","author":"Chavarr\u00eda-Smith","year":"2013","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.M116.761734_bib19","doi-asserted-by":"crossref","first-page":"e1002638","DOI":"10.1371\/journal.ppat.1002638","article-title":"Anthrax lethal factor cleavage of Nlrp1 is required for activation of the inflammasome","volume":"8","author":"Levinsohn","year":"2012","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.M116.761734_bib20","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1038\/nsmb708","article-title":"The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor","volume":"11","author":"Turk","year":"2004","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M116.761734_bib21","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.M116.761734_bib22","doi-asserted-by":"crossref","first-page":"9402","DOI":"10.1074\/jbc.M211262200","article-title":"Anthrax lethal factor proteolysis and inactivation of MAPK kinase","volume":"278","author":"Chopra","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.761734_bib23","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1016\/j.chembiol.2012.05.013","article-title":"Identification of exosite-targeting inhibitors of anthrax lethal factor by high throughput screening","volume":"19","author":"Bannwarth","year":"2012","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.M116.761734_bib24","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"},{"key":"10.1074\/jbc.M116.761734_bib25","doi-asserted-by":"crossref","first-page":"2987","DOI":"10.1128\/JB.00038-12","article-title":"The structure of Mlc titration factor A (MtfA\/YeeI) reveals a prototypical zinc metallopeptidase related to anthrax lethal factor","volume":"194","author":"Xu","year":"2012","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.M116.761734_bib26","doi-asserted-by":"crossref","first-page":"e81306","DOI":"10.1371\/journal.pone.0081306","article-title":"Identification of a novel zinc metalloprotease through a global analysis of Clostridium difficile extracellular proteins","volume":"8","author":"Cafardi","year":"2013","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M116.761734_bib27","doi-asserted-by":"crossref","first-page":"7958","DOI":"10.1073\/pnas.0502159102","article-title":"Anthrax lethal factor inhibition","volume":"102","author":"Shoop","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.761734_bib28","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1021\/acschembio.6b00169","article-title":"Delivery of non-native cargo into mammalian cells using anthrax lethal toxin","volume":"11","author":"Rabideau","year":"2016","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/jbc.M116.761734_bib29","doi-asserted-by":"crossref","first-page":"2813","DOI":"10.1107\/S1399004714018161","article-title":"Anthrax toxin lethal factor domain 3 is highly mobile and responsive to ligand binding","volume":"70","author":"Maize","year":"2014","journal-title":"Acta Crystallogr. D"},{"key":"10.1074\/jbc.M116.761734_bib30","doi-asserted-by":"crossref","first-page":"52473","DOI":"10.1074\/jbc.M409105200","article-title":"Involvement of domain II in toxicity of anthrax lethal factor","volume":"279","author":"Liang","year":"2004","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.761734_bib31","doi-asserted-by":"crossref","first-page":"e17695","DOI":"10.1371\/journal.pone.0017695","article-title":"CPORT: a consensus interface predictor and its performance in prediction-driven docking with HADDOCK","volume":"6","author":"de Vries","year":"2011","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M116.761734_bib32","doi-asserted-by":"crossref","first-page":"2207","DOI":"10.1002\/prot.24110","article-title":"Scoring protein interaction decoys using exposed residues (SPIDER): a novel multibody interaction scoring function based on frequent geometric patterns of interfacial residues","volume":"80","author":"Khashan","year":"2012","journal-title":"Proteins"},{"key":"10.1074\/jbc.M116.761734_bib33","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1002\/prot.21233","article-title":"PIER: protein interface recognition for structural proteomics","volume":"67","author":"Kufareva","year":"2007","journal-title":"Proteins"},{"key":"10.1074\/jbc.M116.761734_bib34","doi-asserted-by":"crossref","first-page":"3698","DOI":"10.1093\/nar\/gkl454","article-title":"Protein binding site prediction using an empirical scoring function","volume":"34","author":"Liang","year":"2006","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M116.761734_bib35","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1101\/gad.191999.112","article-title":"Melanoma: from mutations to medicine","volume":"26","author":"Tsao","year":"2012","journal-title":"Genes Dev"},{"key":"10.1074\/jbc.M116.761734_bib36","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1158\/1535-7163.MCT-05-0145","article-title":"BRAF status and mitogen-activated protein\/extracellular signal-regulated kinase kinase 1\/2 activity indicate sensitivity of melanoma cells to anthrax lethal toxin","volume":"4","author":"Abi-Habib","year":"2005","journal-title":"Mol. Cancer Ther"},{"key":"10.1074\/jbc.M116.761734_bib37","doi-asserted-by":"crossref","first-page":"e17165","DOI":"10.1371\/journal.pone.0017165","article-title":"MEK2 is sufficient but not necessary for proliferation and anchorage-independent growth of SK-MEL-28 melanoma cells","volume":"6","author":"Lee","year":"2011","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M116.761734_bib38","doi-asserted-by":"crossref","first-page":"3052","DOI":"10.1073\/pnas.052707699","article-title":"Apoptosis and melanogenesis in human melanoma cells induced by anthrax lethal factor inactivation of mitogen-activated protein kinase kinase","volume":"99","author":"Koo","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.761734_bib39","doi-asserted-by":"crossref","first-page":"12461","DOI":"10.1073\/pnas.0404781101","article-title":"Discovery of an allosteric site in the caspases","volume":"101","author":"Hardy","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.761734_bib40","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1515\/hsz-2012-0162","article-title":"Identification of protease exosite-interacting peptides that enhance substrate cleavage kinetics","volume":"393","author":"Jabaiah","year":"2012","journal-title":"Biol. Chem"},{"key":"10.1074\/jbc.M116.761734_bib41","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1126\/science.1083917","article-title":"Crystal structure of the GpIb\u03b1-thrombin complex essential for platelet aggregation","volume":"301","author":"Dumas","year":"2003","journal-title":"Science"},{"key":"10.1074\/jbc.M116.761734_bib42","doi-asserted-by":"crossref","first-page":"3352","DOI":"10.1128\/JCM.00561-06","article-title":"Characterization of Bacillus cereus isolates associated with fatal pneumonias: strains are closely related to Bacillus anthracis and harbor B. anthracis virulence genes","volume":"44","author":"Hoffmaster","year":"2006","journal-title":"J. Clin. Microbiol"},{"key":"10.1074\/jbc.M116.761734_bib43","doi-asserted-by":"crossref","first-page":"9499","DOI":"10.1073\/pnas.0502733102","article-title":"Efficient synthetic inhibitors of anthrax lethal factor","volume":"102","author":"Forino","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.761734_bib44","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1038\/nsmb711","article-title":"Identification of small molecule inhibitors of anthrax lethal factor","volume":"11","author":"Panchal","year":"2004","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M116.761734_bib45","doi-asserted-by":"crossref","first-page":"15542","DOI":"10.1016\/S0021-9258(19)49569-0","article-title":"Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells","volume":"267","author":"Arora","year":"1992","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.761734_bib46","doi-asserted-by":"crossref","first-page":"3334","DOI":"10.1016\/S0021-9258(18)53698-X","article-title":"Residues 1\u2013254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides","volume":"268","author":"Arora","year":"1993","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.761734_bib47","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1111\/j.1742-4658.2009.07458.x","article-title":"An anthrax lethal factor mutant that is defective at causing pyroptosis retains proapoptotic activity","volume":"277","author":"Ngai","year":"2010","journal-title":"FEBS J"},{"key":"10.1074\/jbc.M116.761734_bib48","doi-asserted-by":"crossref","first-page":"e1375","DOI":"10.1371\/journal.pone.0001375","article-title":"Structural requirements for Yersinia YopJ inhibition of MAP kinase pathways","volume":"3","author":"Hao","year":"2008","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M116.761734_bib49","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1016\/j.ccr.2014.07.007","article-title":"Structure of the BRAF-MEK complex reveals a kinase activity independent role for BRAF in MAPK signaling","volume":"26","author":"Haling","year":"2014","journal-title":"Cancer Cell"},{"key":"10.1074\/jbc.M116.761734_bib50","doi-asserted-by":"crossref","first-page":"e00969","DOI":"10.7554\/eLife.00969","article-title":"BRAF inhibitors suppress apoptosis through off-target inhibition of JNK signaling","volume":"2","author":"Vin","year":"2013","journal-title":"eLife"},{"key":"10.1074\/jbc.M116.761734_bib51","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1126\/science.1207203","article-title":"Expanding the genetic code of Escherichia coli with phosphoserine","volume":"333","author":"Park","year":"2011","journal-title":"Science"},{"key":"10.1074\/jbc.M116.761734_bib52","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1093\/oxfordjournals.jbchem.a124524","article-title":"Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis","volume":"116","author":"Mansour","year":"1994","journal-title":"J. Biochem"},{"key":"10.1074\/jbc.M116.761734_bib53","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1006\/jtbi.1997.0425","article-title":"Closed form solution for time-dependent enzyme kinetics","volume":"187","author":"Schnell","year":"1997","journal-title":"J. Theor. Biol"},{"key":"10.1074\/jbc.M116.761734_bib54","series-title":"The PyMOL Molecular Graphics System","author":"DeLano","year":"2015"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820402625?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820402625?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M116.761734","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T10:28:02Z","timestamp":1641292082000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820402625"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,1]]},"references-count":54,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2017,1]]}},"alternative-id":["S0021925820402625"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m116.761734","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2017,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Identification of a Substrate-selective Exosite within the Metalloproteinase Anthrax Lethal Factor","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M116.761734","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}