{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T11:01:49Z","timestamp":1790420509422,"version":"4.1.0"},"reference-count":23,"publisher":"Springer Science and Business Media LLC","issue":"1-2","license":[{"start":{"date-parts":[[1997,12,1]],"date-time":"1997-12-01T00:00:00Z","timestamp":880934400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[1997,12,1]],"date-time":"1997-12-01T00:00:00Z","timestamp":880934400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Mol Cell Biochem"],"published-print":{"date-parts":[[1997,12]]},"DOI":"10.1023\/a:1006815306876","type":"journal-article","created":{"date-parts":[[2002,12,22]],"date-time":"2002-12-22T02:57:47Z","timestamp":1040525867000},"page":"7-14","source":"Crossref","is-referenced-by-count":6,"title":["Site directed mutagenesis of Histidine residues in Anthrax toxin lethal factor binding domain reduces toxicity"],"prefix":"10.1007","volume":"177","author":[{"given":"Naveen","family":"Arora","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","reference":[{"key":"122091_CR1","first-page":"543","volume-title":"Bacterial toxins and Virulence Factors in disease. Hand book of natural toxins","author":"SH Leppla","year":"1995","unstructured":"Leppla SH: Anthrax toxins. In: J Moss, B Iglewski, M Vaughan, Tu (eds). Bacterial toxins and Virulence Factors in disease. Hand book of natural toxins. Vol 8 New York, Marcel Dekkar, Inc. 1995, pp 543\u2013572"},{"key":"122091_CR2","first-page":"277","volume-title":"Source book of Bacterial protein toxins","author":"SH Leppla","year":"1991","unstructured":"Leppla SH: The Anthrax toxin complex. In: JE Alouf, JH Freer (eds). Source book of Bacterial protein toxins, London, Academic press, 1991, pp 277\u2013302"},{"key":"122091_CR3","volume-title":"Bacterial protein toxins","author":"SH Leppla","year":"1988","unstructured":"Leppla SH, Friedlander AH, Cord E: Proteolytic activation of anthrax toxin bound to Cellular receptors. In: F Fehrenbach, JE Alouf, P Falmagne, W Goebel, J Jeizaszewiez, D Jergen, R Rappouli (eds). Bacterial protein toxins. Gostav Fischer, New York, 1988"},{"key":"122091_CR4","doi-asserted-by":"crossref","first-page":"19103","DOI":"10.1016\/S0021-9258(19)47273-6","volume":"264","author":"Y Singh","year":"1989","unstructured":"Singh Y, Chaudhary VK, Leppla SH: A deleted varient of B. anthracis protective antigen is non-toxic and blocks anthrax toxin action. J Biol Chem 264: 19103\u201319107, 1989","journal-title":"J Biol Chem"},{"key":"122091_CR5","doi-asserted-by":"crossref","first-page":"10277","DOI":"10.1073\/pnas.89.21.10277","volume":"89","author":"KR Klimpel","year":"1992","unstructured":"Klimpel KR, Mallay SS, Thomas G, Leppla SH: Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin. Proc Natl Acad Sci (USA) 89: 10277\u201310287, 1992","journal-title":"Proc Natl Acad Sci (USA)"},{"key":"122091_CR6","doi-asserted-by":"crossref","first-page":"7123","DOI":"10.1016\/S0021-9258(17)38364-3","volume":"261","author":"AM Friedlander","year":"1986","unstructured":"Friedlander AM: Macrophages are sensitive to anthrax lethal toxin through an acid dependent process. J Biol Chem 261: 7123\u20137126, 1986","journal-title":"J Biol Chem"},{"key":"122091_CR7","doi-asserted-by":"crossref","first-page":"20607","DOI":"10.1016\/S0021-9258(17)32036-7","volume":"269","author":"JC Milne","year":"1994","unstructured":"Milne JC, Furlong D, Hauna PC, Wall JS, Collier RJ: Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J Biol Chem 269: 20607\u201320612, 1994","journal-title":"J Biol Chem"},{"key":"122091_CR8","doi-asserted-by":"crossref","first-page":"3162","DOI":"10.1073\/pnas.79.10.3162","volume":"79","author":"SH Leppla","year":"1982","unstructured":"Leppla SH: Anthrax toxin edema factor: a bacterial adenylate-cyclase that increased cAMP concentration in eukaryotic cells. Proc Natl Acad Sci (USA) 79: 3162\u20133166, 1982","journal-title":"Proc Natl Acad Sci (USA)"},{"key":"122091_CR9","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1111\/j.1365-2958.1994.tb00500.x","volume":"13","author":"KR Klimpel","year":"1994","unstructured":"Klimpel KR, Arora N, Leppla SH: Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol Microb 13: 1093\u20131100, 1994","journal-title":"Mol Microb"},{"key":"122091_CR10","doi-asserted-by":"crossref","first-page":"15542","DOI":"10.1016\/S0021-9258(19)49569-0","volume":"267","author":"N Arora","year":"1992","unstructured":"Arora N, Klimpel KR, Singh Y, Leppla SH: Fusions of anthrax toxin lethal factor to the ADP ribosylation domain or Pseudomonas exotoxin A are cytotoxins which are translocated to the cytosol of mammalian cells. J Biol Chem 267: 15542\u201315548, 1992","journal-title":"J Biol Chem"},{"key":"122091_CR11","doi-asserted-by":"crossref","first-page":"3334","DOI":"10.1016\/S0021-9258(18)53698-X","volume":"268","author":"N Arora","year":"1993","unstructured":"Arora N and Leppla SH: Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides. J Biol Chem 268: 3334\u20133341, 1993","journal-title":"J Biol Chem"},{"key":"122091_CR12","doi-asserted-by":"crossref","first-page":"4955","DOI":"10.1128\/iai.62.11.4955-4961.1994","volume":"62","author":"N Arora","year":"1994","unstructured":"Arora N, Leppla SH: Fusions of anthrax toxin lethal factors with Shiga toxin and diphtheria toxin enzymatic domains are toxic to mammalian cells. Infect and Immun 62: 4955\u20134961, 1994","journal-title":"Infect and Immun"},{"key":"122091_CR13","doi-asserted-by":"crossref","first-page":"26165","DOI":"10.1016\/S0021-9258(18)47173-6","volume":"269","author":"N Arora","year":"1994","unstructured":"Arora N, Williamson LC, Leppla SH, Halpern J: Cytotoxic effects of a chimeric protein consisting of tetanus toxin light chain and anthrax toxin lethal factor in non-neuronal cells. J Biol Chem 269: 26165\u201326171, 1994","journal-title":"J Biol Chem"},{"key":"122091_CR14","doi-asserted-by":"crossref","first-page":"20124","DOI":"10.1016\/S0021-9258(18)54899-7","volume":"266","author":"CP Quinn","year":"1991","unstructured":"Quinn CP, Singh Y, Klimpel KR, Leppla SH: Functional mapping of anthrax toxin lethal factor by inframe insertion mutagenesis. J Biol Chem 266: 20124\u201320130, 1991","journal-title":"J Biol Chem"},{"key":"122091_CR15","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1021\/bi00804a010","volume":"9","author":"WB Melchior","year":"1970","unstructured":"Melchior WB, Fahrner D: Formylation of proteins. Reaction with Ethoses formic anhydride with a-chymotrypsin, pepsin and pancreatic ribonuclease at pH4. Biochemistry 9: 256\u2013258, 1970","journal-title":"Biochemistry"},{"key":"122091_CR16","doi-asserted-by":"crossref","first-page":"10583","DOI":"10.1016\/S0021-9258(19)85125-6","volume":"260","author":"P Dominici","year":"1985","unstructured":"Dominici P, Tahoini B, Voltattorni CB: Chemical modification of pig kidney 3-4-dihydrocylphenylalanine decarboxylase with diethyl pyrocarbonate. J Biol Chem 260: 10583\u201310589, 1985","journal-title":"J Biol Chem"},{"key":"122091_CR17","first-page":"528","volume":"8","author":"RM Horton","year":"1990","unstructured":"Horton RM, Lai ZL, Ho SN, Pease LR: Gene splicing by overlap extrusion:tailor made genes used the polymerase chain reaction. Biotechniques 8: 528\u2013535, 1990","journal-title":"Biotechniques"},{"key":"122091_CR18","doi-asserted-by":"crossref","first-page":"29039","DOI":"10.1016\/S0021-9258(19)62010-7","volume":"269","author":"Y Singh","year":"1994","unstructured":"Singh Y, Klimpel KR, Arora N, Sharma M, Leppla SH: The chymotrypsin sensitive site, FFD, in anthrax toxin protective antigen is required for translocation of lethal factor. J Biol Chem 269: 29039\u201329046, 1994","journal-title":"J Biol Chem"},{"key":"122091_CR19","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1021\/bc00001a001","volume":"1","author":"GE Means","year":"1990","unstructured":"Means GE, Feema RE: Chemical modification of proteins: History and Applications. Bioconjugate Chem. 1: 2\u201312, 1990","journal-title":"Bioconjugate Chem."},{"key":"122091_CR20","doi-asserted-by":"crossref","first-page":"13203","DOI":"10.1016\/S0021-9258(18)37692-0","volume":"263","author":"Y Jinno","year":"1988","unstructured":"Jinno Y, Chaudhary VK, Kondo T, Adhya S, Fikgerald DJ, Pastan l: Mutational analysis of domain 1 of Pseudomonas exotoxin. J Biol Chem 263: 13203\u201313207, 1988","journal-title":"J Biol Chem"},{"key":"122091_CR21","doi-asserted-by":"crossref","first-page":"1843","DOI":"10.1128\/iai.62.5.1843-1847.1994","volume":"62","author":"BE Menzies","year":"1994","unstructured":"Menzies BE, Kernodle DS: Site directed mutagenesis of the alpha-toxin gel of Staphylococcus aureas: Role of histidine in toxin activity invitro and murine model. Infection and immunity 62: 1843\u20131847, 1994","journal-title":"Infection and immunity"},{"key":"122091_CR22","first-page":"18625","volume":"270","author":"J Zhao","year":"1995","unstructured":"Zhao J, Mline JC and Collier RJ: Effect of anthrax toxin lethal factor on ion channels formed by protective antigen. J Biol Chem 270: 18625\u201318630, 1995","journal-title":"J Biol Chem"},{"key":"122091_CR23","doi-asserted-by":"crossref","first-page":"6122","DOI":"10.1074\/jbc.271.11.6122","volume":"271","author":"AG Zdanovsky","year":"1996","unstructured":"Zdanovsky AG, Zdanovskaia MV, Strickland D and Fikgerald DJ: Lig-and-toxin hybrids directed to the \u03b12-macroglobulin receptor\/low den-sity lipoprotein receptor-related protein exhibit lower toxicity than native Pseudomonas exotoxin. J Biol Chem 271: 6122\u20136128, 1996","journal-title":"J Biol Chem"}],"container-title":["Molecular and Cellular Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1023\/A:1006815306876.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1023\/A:1006815306876\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1023\/A:1006815306876.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,7,10]],"date-time":"2025-07-10T13:34:59Z","timestamp":1752154499000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1023\/A:1006815306876"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,12]]},"references-count":23,"journal-issue":{"issue":"1-2","published-print":{"date-parts":[[1997,12]]}},"alternative-id":["122091"],"URL":"https:\/\/doi.org\/10.1023\/a:1006815306876","relation":{},"ISSN":["0300-8177","1573-4919"],"issn-type":[{"value":"0300-8177","type":"print"},{"value":"1573-4919","type":"electronic"}],"subject":[],"published":{"date-parts":[[1997,12]]}}}