{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T10:28:17Z","timestamp":1762079297613},"reference-count":38,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2011,12,1]],"date-time":"2011-12-01T00:00:00Z","timestamp":1322697600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Experimental Parasitology"],"published-print":{"date-parts":[[2011,12]]},"DOI":"10.1016\/j.exppara.2011.09.013","type":"journal-article","created":{"date-parts":[[2011,10,2]],"date-time":"2011-10-02T08:11:44Z","timestamp":1317543104000},"page":"323-330","source":"Crossref","is-referenced-by-count":33,"title":["A recombinant thioredoxin-glutathione reductase from Fasciola hepatica induces a protective response in rabbits"],"prefix":"10.1016","volume":"129","author":[{"given":"Gabriela","family":"Maggioli","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fernando","family":"Silveira","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9 M.","family":"Mart\u00edn-Alonso","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gustavo","family":"Salinas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carlos","family":"Carmona","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Francisco","family":"Parra","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.exppara.2011.09.013_b0005","doi-asserted-by":"crossref","first-page":"12920","DOI":"10.1074\/jbc.M209266200","article-title":"Alternative mRNAs arising from trans-splicing code for mitochondrial and cytosolic variants of Echinococcus granulosus thioredoxin Glutathione reductase","volume":"278","author":"Agorio","year":"2003","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/j.exppara.2011.09.013_b0010","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0166-6851(02)00031-2","article-title":"The disulfide redox system of Schistosoma mansoni and the importance of a multifunctional enzyme, thioredoxin glutathione reductase","volume":"121","author":"Alger","year":"2002","journal-title":"Molecular and Biochemical Parasitology"},{"key":"10.1016\/j.exppara.2011.09.013_b0015","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1006\/jmbi.1999.3085","article-title":"High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes","volume":"292","author":"Arner","year":"1999","journal-title":"Journal of Molecular Biology"},{"key":"10.1016\/j.exppara.2011.09.013_b0020","doi-asserted-by":"crossref","first-page":"6102","DOI":"10.1046\/j.1432-1327.2000.01701.x","article-title":"Physiological functions of thioredoxin and thioredoxin reductase","volume":"267","author":"Arner","year":"2000","journal-title":"European Journal of Biochemistry"},{"key":"10.1016\/j.exppara.2011.09.013_b0025","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0891-5849(00)00448-2","article-title":"Overexpression of wild type and SecCys\/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity.","volume":"30","author":"Bar-Noy","year":"2001","journal-title":"Free Radical Biology and Medicine"},{"key":"10.1016\/j.exppara.2011.09.013_b0030","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/S0952-7915(99)00052-7","article-title":"Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity","volume":"12","author":"Bogdan","year":"2000","journal-title":"Current Opinion in Immunology"},{"key":"10.1016\/j.exppara.2011.09.013_b0035","doi-asserted-by":"crossref","first-page":"17898","DOI":"10.1074\/jbc.M710609200","article-title":"Platyhelminth mitochondrial and cytosolic redox homeostasis is controlled by a single thioredoxin glutathione reductase and dependent on selenium and glutathione","volume":"283","author":"Bonilla","year":"2008","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/j.exppara.2011.09.013_b0040","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Analytical Biochemistry"},{"key":"10.1016\/j.exppara.2011.09.013_b0045","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/0169-4758(88)90162-7","article-title":"Helminth anti-oxidant enzymes: a protective mechanism against host oxidants?","volume":"4","author":"Callahan","year":"1988","journal-title":"Parasitology Today"},{"key":"10.1016\/j.exppara.2011.09.013_b0050","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/S0076-6879(85)13062-4","article-title":"Glutathione reductase","volume":"113","author":"Carlberg","year":"1985","journal-title":"Methods in Enzymology"},{"key":"10.1016\/j.exppara.2011.09.013_b0055","unstructured":"Fritsch, E.F., Sambrook, J. and Maniatis, T., 1989. Molecular cloning. A laboratory manual. 2,"},{"key":"10.1016\/j.exppara.2011.09.013_b0060","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/j.pt.2003.09.005","article-title":"Drugs for the control of parasitic diseases: current status and development in schistosomiasis","volume":"19","author":"Fenwick","year":"2003","journal-title":"Trends in Parasitology"},{"key":"10.1016\/j.exppara.2011.09.013_b0065","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1002\/med.10051","article-title":"The thioredoxin system\u2014from science to clinic","volume":"24","author":"Gromer","year":"2004","journal-title":"Medicinal Research Reviews"},{"key":"10.1016\/j.exppara.2011.09.013_b0070","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.parint.2011.01.005","article-title":"Hysteresis in thioredoxin-glutathione reductase (TGR) from the adult stage of the liver fluke Fasciola hepatica","volume":"60","author":"Guevara-Flores","year":"2011","journal-title":"Parasitology International"},{"key":"10.1016\/j.exppara.2011.09.013_b0075","doi-asserted-by":"crossref","first-page":"9627","DOI":"10.1016\/S0021-9258(19)83562-7","article-title":"Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide","volume":"254","author":"Holmgren","year":"1979","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/j.exppara.2011.09.013_b0080","doi-asserted-by":"crossref","first-page":"13963","DOI":"10.1016\/S0021-9258(18)71625-6","article-title":"Thioredoxin and glutaredoxin systems","volume":"264","author":"Holmgren","year":"1989","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/j.exppara.2011.09.013_b0085","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/0076-6879(95)52031-7","article-title":"Glutaredoxin","volume":"252","author":"Holmgren","year":"1995","journal-title":"Methods in Enzymology"},{"key":"10.1016\/j.exppara.2011.09.013_b0090","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbagen.2005.05.010","article-title":"Selenocysteine in proteins-properties and biotechnological use","volume":"1726","author":"Johansson","year":"2005","journal-title":"Biochimica et Biophysica Acta"},{"key":"10.1016\/j.exppara.2011.09.013_b0095","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1126\/science.291.5504.643","article-title":"Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster","volume":"291","author":"Kanzok","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.exppara.2011.09.013_b0100","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1002\/anie.200300639","article-title":"Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia","volume":"44","author":"Krauth-Siegel","year":"2005","journal-title":"Angewandte Chemie International Edition"},{"key":"10.1016\/j.exppara.2011.09.013_b0195","doi-asserted-by":"crossref","first-page":"e206","DOI":"10.1371\/journal.pmed.0040206","article-title":"Thioredoxin glutathione reductase from Schistosoma mansoni: an essential parasite enzyme and a key drug target","volume":"4","author":"Kuntz","year":"2007","journal-title":"PLoS Medicine"},{"key":"10.1016\/j.exppara.2011.09.013_b0110","doi-asserted-by":"crossref","first-page":"6302","DOI":"10.1128\/JB.182.22.6302-6307.2000","article-title":"The bulged nucleotide in the Escherichia coli minimal selenocysteine insertion sequence participates in interaction with SelB: a genetic approach","volume":"182","author":"Li","year":"2000","journal-title":"Journal of Bacteriology"},{"key":"10.1016\/j.exppara.2011.09.013_b0115","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/0968-0004(96)10025-6","article-title":"Knowing when not to stop: selenocysteine incorporation in eukaryotes","volume":"21","author":"Low","year":"1996","journal-title":"Trends in Biochemical Sciences"},{"key":"10.1016\/j.exppara.2011.09.013_b0120","doi-asserted-by":"crossref","first-page":"2158","DOI":"10.1073\/pnas.76.5.2158","article-title":"Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase","volume":"76","author":"Luthman","year":"1979","journal-title":"Proceedings of the National Academy of Sciences USA"},{"key":"10.1016\/j.exppara.2011.09.013_b0125","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1645\/GE-3247","article-title":"Purification, characterization, and immunolocalization of a thioredoxin reductase from adult Fasciola hepatica","volume":"90","author":"Maggioli","year":"2004","journal-title":"The Journal of Parasitology"},{"key":"10.1016\/j.exppara.2011.09.013_b0130","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/0166-6851(92)90136-8","article-title":"Identification and expression of a Fasciola hepatica gene encoding a gut antigen protein bearing repetitive sequences","volume":"55","author":"Marin","year":"1992","journal-title":"Molecular and Biochemical Parasitology"},{"key":"10.1016\/j.exppara.2011.09.013_b0135","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0169-4758(97)01211-8","article-title":"Peroxidoxins: a new antioxidant family","volume":"14","author":"McGonigle","year":"1998","journal-title":"Parasitology Today"},{"key":"10.1016\/j.exppara.2011.09.013_b0140","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1016\/S0891-5849(01)00724-9","article-title":"Reactive oxygen species, antioxidants, and the mammalian thioredoxin system","volume":"31","author":"Nordberg","year":"2001","journal-title":"Free Radical Biology and Medicine"},{"key":"10.1016\/j.exppara.2011.09.013_b0200","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.molbiopara.2003.09.003","article-title":"Purification, characterization and kinetic properties of the multifunctional thioredoxin-glutathione reductase from Taenia crassiceps metacestode (cysticerci)","volume":"133","author":"Rendon","year":"2004","journal-title":"Molecular and Biochemical Parasitology"},{"key":"10.1016\/j.exppara.2011.09.013_b0150","doi-asserted-by":"crossref","first-page":"5159","DOI":"10.1128\/AEM.70.9.5159-5167.2004","article-title":"Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis","volume":"70","author":"Rengby","year":"2004","journal-title":"Applied and Environmental Microbiology"},{"key":"10.1016\/j.exppara.2011.09.013_b0155","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.pt.2004.05.002","article-title":"Linked thioredoxin-glutathione systems in platyhelminths","volume":"20","author":"Salinas","year":"2004","journal-title":"Trends in Parasitology"},{"key":"10.1016\/j.exppara.2011.09.013_b0160","doi-asserted-by":"crossref","first-page":"5463","DOI":"10.1073\/pnas.74.12.5463","article-title":"DNA sequencing with chain-terminating inhibitors","volume":"74","author":"Sanger","year":"1977","journal-title":"Proceedings of the National Academy of Sciences USA"},{"key":"10.1016\/j.exppara.2011.09.013_b0165","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1016\/S0020-7519(98)00107-6","article-title":"Resistance of filarial nematode parasites to oxidative stress","volume":"28","author":"Selkirk","year":"1998","journal-title":"International Journal for Parasitology"},{"key":"10.1016\/j.exppara.2011.09.013_b0170","doi-asserted-by":"crossref","first-page":"26491","DOI":"10.1074\/jbc.M503638200","article-title":"Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation","volume":"280","author":"Su","year":"2005","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/j.exppara.2011.09.013_b0175","doi-asserted-by":"crossref","first-page":"3673","DOI":"10.1073\/pnas.051454398","article-title":"Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems","volume":"98","author":"Sun","year":"2001","journal-title":"Proceedings of the National Academy of Sciences USA"},{"key":"10.1016\/j.exppara.2011.09.013_b0180","doi-asserted-by":"crossref","first-page":"24522","DOI":"10.1074\/jbc.274.35.24522","article-title":"Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases","volume":"274","author":"Sun","year":"1999","journal-title":"The Journal of Biological Chemistry"},{"key":"10.1016\/j.exppara.2011.09.013_b0185","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/S0753-3322(03)00043-X","article-title":"The importance of glutathione in human disease","volume":"57","author":"Townsend","year":"2003","journal-title":"Biomedicine & Pharmacotherapy"},{"key":"10.1016\/j.exppara.2011.09.013_b0190","doi-asserted-by":"crossref","first-page":"22953","DOI":"10.1074\/jbc.M604326200","article-title":"Characterization of alternative cytosolic forms and cellular targets of mouse mitochondrial thioredoxin reductase","volume":"281","author":"Turanov","year":"2006","journal-title":"The Journal of Biological Chemistry"}],"container-title":["Experimental Parasitology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014489411002852?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0014489411002852?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,12,8]],"date-time":"2021-12-08T14:29:50Z","timestamp":1638973790000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0014489411002852"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,12]]},"references-count":38,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2011,12]]}},"alternative-id":["S0014489411002852"],"URL":"https:\/\/doi.org\/10.1016\/j.exppara.2011.09.013","relation":{},"ISSN":["0014-4894"],"issn-type":[{"type":"print","value":"0014-4894"}],"subject":[],"published":{"date-parts":[[2011,12]]}}}