{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T23:47:20Z","timestamp":1777420040622,"version":"3.51.4"},"reference-count":97,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2012,1,1]],"date-time":"2012-01-01T00:00:00Z","timestamp":1325376000000},"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":["Biotechnology Advances"],"published-print":{"date-parts":[[2012,1]]},"DOI":"10.1016\/j.biotechadv.2011.05.012","type":"journal-article","created":{"date-parts":[[2011,5,22]],"date-time":"2011-05-22T15:41:37Z","timestamp":1306078897000},"page":"294-301","source":"Crossref","is-referenced-by-count":40,"title":["The trypanothione system and the opportunities it offers to create drugs for the neglected kinetoplast diseases"],"prefix":"10.1016","volume":"30","author":[{"given":"Leopold","family":"Floh\u00e9","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.biotechadv.2011.05.012_bb0005","doi-asserted-by":"crossref","first-page":"25613","DOI":"10.1074\/jbc.274.36.25613","article-title":"The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-I","volume":"274","author":"Alphey","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0010","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1006\/jmbi.2000.3881","article-title":"The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins","volume":"300","author":"Alphey","year":"2000","journal-title":"J Mol Biol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0015","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1042\/BJ20080889","article-title":"Structural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidases","volume":"414","author":"Alphey","year":"2008","journal-title":"Biochem J"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0020","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1042\/BJ20050911","article-title":"Phenotypic analysis of trypanothione synthetase knockdown in the African trypanosome","volume":"391","author":"Ariyanayagam","year":"2005","journal-title":"Biochem J"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0025","doi-asserted-by":"crossref","first-page":"10816","DOI":"10.1074\/jbc.M212990200","article-title":"Role of peroxidoxins in Leishmania chagasi survival. Evidence of an enzymatic defense against nitrosative stress","volume":"278","author":"Barr","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0030","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1042\/bj1880643","article-title":"Deficient metabolic utilization of hydrogen peroxide in Trypanosoma cruzi","volume":"188","author":"Boveris","year":"1980","journal-title":"Biochem J"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0035","doi-asserted-by":"crossref","DOI":"10.1089\/ars.2010.3534","article-title":"Basic principles and emerging concepts in the redox control of transcription factors","author":"Brigelius-Floh\u00e9","year":"2011","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0040","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0166-6851(93)90160-Y","article-title":"Trypanothione-dependent peroxide metabolism in Trypanosoma cruzi different stages","volume":"61","author":"Carnieri","year":"1993","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0045","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1089\/ars.2008.2050","article-title":"Peroxidases of trypanosomatids","volume":"10","author":"Castro","year":"2008","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0050","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.molbiopara.2004.02.015","article-title":"Two linked genes of Leishmania infantum encode tryparedoxins localised to cytosol and mitochondrion","volume":"136","author":"Castro","year":"2004","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0055","doi-asserted-by":"crossref","first-page":"e12607","DOI":"10.1371\/journal.pone.0012607","article-title":"Mitochondrial redox metabolism in trypanosomatids is independent of tryparedoxin activity","volume":"5","author":"Castro","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0060","unstructured":"Comini M, Menge U, Floh\u00e9 L. Additions and Corrections for K\u00f6nig et al. (1997): J Biol Chem 272, 11908\u201311915. 2005a;280:7407\u20138."},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0065","first-page":"653","article-title":"Biosynthesis of trypanothione in Trypanosoma brucei brucei","volume":"384","author":"Comini","year":"2003","journal-title":"Biol Chem Hoppe Seyler"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0070","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1016\/j.freeradbiomed.2004.02.008","article-title":"Validation of Trypanosoma brucei trypanothione synthetase as drug target","volume":"36","author":"Comini","year":"2004","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0075","doi-asserted-by":"crossref","first-page":"6850","DOI":"10.1074\/jbc.M404486200","article-title":"Trypanothione synthesis in crithidia revisited","volume":"280","author":"Comini","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0080","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1042\/BJ20061341","article-title":"Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes","volume":"402","author":"Comini","year":"2007","journal-title":"Biochem J"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0085","doi-asserted-by":"crossref","first-page":"2976","DOI":"10.1021\/jm000502n","article-title":"QSAR study on the contribution of log P and E(s) to the in vitro antiprotozoal activity of glutathione derivatives","volume":"44","author":"Daunes","year":"2001","journal-title":"J Med Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0090","doi-asserted-by":"crossref","first-page":"10602","DOI":"10.1074\/jbc.M010352200","article-title":"Trypanothione-dependent synthesis of deoxyribonucleotides by Trypanosoma brucei ribonucleotide reductase","volume":"276","author":"Dormeyer","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0095","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0166-6851(95)00098-L","article-title":"cDNA expressed sequence tags of Trypanosoma brucei rhodesiense provide new insights into the biology of the parasite","volume":"73","author":"El-Sayed","year":"1995","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0100","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1126\/science.1112181","article-title":"Comparative genomics of trypanosomatid parasitic protozoa","volume":"309","author":"El-Sayed","year":"2005","journal-title":"Science"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0105","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1146\/annurev.mi.46.100192.003403","article-title":"Metabolism and functions of trypanothione in the Kinetoplastida","volume":"46","author":"Fairlamb","year":"1992","journal-title":"Annu Rev Microbiol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0110","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1126\/science.3883489","article-title":"Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids","volume":"227","author":"Fairlamb","year":"1985","journal-title":"Science"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0115","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/0166-6851(86)90130-1","article-title":"The biosynthesis of trypanothione and N1-glutathionylspermidine in Crithidia fasciculata","volume":"21","author":"Fairlamb","year":"1986","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0120","series-title":"R&D Methodologies and Issues","article-title":"Drugs against parsitic diseases","author":"Fairlamb","year":"2003"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0125","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1002\/biof.5520080115","article-title":"The Achilles' heel of trypanosomatids: trypanothione-mediated hydroperoxide metabolism","volume":"8","author":"Floh\u00e9","year":"1998","journal-title":"Biofactors"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0130","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0076-6879(10)73001-9","article-title":"Changing paradigms in thiology from antioxidant defense toward redox regulation","volume":"473","author":"Floh\u00e9","year":"2010","journal-title":"Methods Enzymol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0135","series-title":"Selenium Its Molecular Biology and Role in Human Health","first-page":"161","article-title":"Selenoproteins of the glutathione system","author":"Floh\u00e9","year":"2006"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0140","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1006\/abbi.2001.2688","article-title":"Tryparedoxin peroxidase of Leishmania donovani: molecular cloning, heterologous expression, specificity, and catalytic mechanism","volume":"397","author":"Floh\u00e9","year":"2002","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0145","series-title":"Abstracts10th Drug Design and Development Seminar Abstracts","first-page":"IL33","article-title":"Paullones as drugs for trypanosomatids","author":"Floh\u00e9","year":"2009"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0150","doi-asserted-by":"crossref","first-page":"17672","DOI":"10.1074\/jbc.M801850200","article-title":"Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities","volume":"283","author":"Fyfe","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0155","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1111\/j.1432-1033.1997.t01-1-00913.x","article-title":"Catalytic characteristics of tryparedoxin","volume":"248","author":"Gommel","year":"1997","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0160","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1046\/j.1432-1327.1999.00087.x","article-title":"Sequence, heterologous expression and functional characterization of tryparedoxin1 from Crithidia fasciculata","volume":"259","author":"Guerrero","year":"1999","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0165","doi-asserted-by":"crossref","first-page":"6809","DOI":"10.1074\/jbc.M210392200","article-title":"A second class of peroxidases linked to the trypanothione metabolism","volume":"278","author":"Hillebrand","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0170","first-page":"459","article-title":"Structures of tryparedoxins revealing interaction with trypanothione","volume":"382","author":"Hofmann","year":"2001","journal-title":"Biol Chem Hoppe Seyler"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0175","first-page":"347","article-title":"Peroxiredoxins","volume":"383","author":"Hofmann","year":"2002","journal-title":"Biol Chem Hoppe Seyler"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0180","doi-asserted-by":"crossref","first-page":"2824","DOI":"10.1128\/AAC.01568-08","article-title":"Trypanothione reductase high-throughput screening campaign identifies novel classes of inhibitors with antiparasitic activity","volume":"53","author":"Holloway","year":"2009","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0185","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1146\/annurev.bi.54.070185.001321","article-title":"Thioredoxin","volume":"54","author":"Holmgren","year":"1985","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0190","doi-asserted-by":"crossref","first-page":"4524","DOI":"10.1021\/jm020885k","article-title":"Coupling of a competitive and an irreversible ligand generates mixed type inhibitors of Trypanosoma cruzi trypanothione reductase","volume":"45","author":"Inhoff","year":"2002","journal-title":"J Med Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0195","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1016\/j.freeradbiomed.2008.05.028","article-title":"Insights into the redox biology of Trypanosoma cruzi: trypanothione metabolism and oxidant detoxification","volume":"45","author":"Irigoin","year":"2008","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0200","doi-asserted-by":"crossref","first-page":"22209","DOI":"10.1074\/jbc.M401240200","article-title":"Glyoxalase II of African trypanosomes is trypanothione-dependent","volume":"279","author":"Irsch","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0205","doi-asserted-by":"crossref","first-page":"e658","DOI":"10.1371\/journal.pntd.0000658","article-title":"The genome sequence of Trypanosoma brucei gambiense, causative agent of chronic human african trypanosomiasis","volume":"4","author":"Jackson","year":"2010","journal-title":"PLoS Negl Trop Dis"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0210","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1002\/(SICI)1097-0134(199601)24:1<73::AID-PROT5>3.0.CO;2-P","article-title":"Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complex","volume":"24","author":"Jacoby","year":"1996","journal-title":"Proteins"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0215","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.pt.2006.04.002","article-title":"A tale of three genomes: the kinetoplastids have arrived","volume":"22","author":"Kissinger","year":"2006","journal-title":"Trends Parasitol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0220","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1189\/jlb.1204697","article-title":"Myeloperoxidase: friend and foe","volume":"77","author":"Klebanoff","year":"2005","journal-title":"J Leukoc Biol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0225","series-title":"Abstracts10th Drug Design and Development Seminar","first-page":"L34","article-title":"What makes the difference? A computational approach to explain varying paullone inhibition activity on trypanothione synthetase from different species","author":"Koch","year":"2009"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0230","doi-asserted-by":"crossref","first-page":"11908","DOI":"10.1074\/jbc.272.18.11908","article-title":"Convenient isolation and kinetic mechanism of glutathionylspermidine synthetase from Crithidia fasciculata","volume":"272","author":"Koenig","year":"1997","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0235","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1016\/j.bbagen.2008.03.006","article-title":"Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism","volume":"1780","author":"Krauth-Siegel","year":"2008","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0240","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1007\/978-1-4020-6051-9_11","article-title":"The trypanothione system","volume":"44","author":"Krauth-Siegel","year":"2007","journal-title":"Subcell Biochem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0245","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1046\/j.1365-2958.2000.01721.x","article-title":"Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress","volume":"35","author":"Krieger","year":"2000","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0250","doi-asserted-by":"crossref","first-page":"14720","DOI":"10.1021\/bi030112d","article-title":"NMR studies of the interaction of tryparedoxin with redox-inactive substrate homologues","volume":"42","author":"Krumme","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0255","doi-asserted-by":"crossref","first-page":"181","DOI":"10.2174\/1381612805666230109214720","article-title":"Fused azepinones with antitumor activity","volume":"5","author":"Kunick","year":"1999","journal-title":"Curr Pharm Des"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0260","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.bmcl.2003.10.062","article-title":"1-Azakenpaullone is a selective inhibitor of glycogen synthase kinase-3 beta","volume":"14","author":"Kunick","year":"2004","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0265","doi-asserted-by":"crossref","first-page":"7400","DOI":"10.1021\/jm0504860","article-title":"Irreversible inactivation of trypanothione reductase by unsaturated Mannich bases: a divinyl ketone as key intermediate","volume":"48","author":"Lee","year":"2005","journal-title":"J Med Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0270","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S0166-6851(98)00122-4","article-title":"Identification and characterisation of a functional peroxidoxin from Leishmania major","volume":"96","author":"Levick","year":"1998","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0275","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/S0891-5849(00)00159-3","article-title":"Evidence for a trypanothione-dependent peroxidase system in Trypanosoma cruzi","volume":"28","author":"Lopez","year":"2000","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0280","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S0014-5793(98)00793-5","article-title":"Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes","volume":"431","author":"L\u00fcdemann","year":"1998","journal-title":"FEBS Lett"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0285","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1080\/07391102.2005.10531227","article-title":"Homology model of the CDK1\/cyclin B complex","volume":"22","author":"McGrath","year":"2005","journal-title":"J Biomol Struct Dyn"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0290","doi-asserted-by":"crossref","first-page":"4793","DOI":"10.1021\/jm050027z","article-title":"Inhibitors of Trypanosoma cruzi trypanothione reductase revealed by virtual screening and parallel synthesis","volume":"48","author":"Meiering","year":"2005","journal-title":"J Med Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0295","first-page":"1137","article-title":"Sequence, heterologous expression and functional characterization of a novel tryparedoxin from Crithidia fasciculata","volume":"379","author":"Montemartini","year":"1998","journal-title":"Biol Chem Hoppe Seyler"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0300","doi-asserted-by":"crossref","first-page":"4864","DOI":"10.1074\/jbc.273.9.4864","article-title":"Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli","volume":"273","author":"Montemartini","year":"1998","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0305","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1111\/j.1365-2958.2009.06907.x","article-title":"The gamma-glutamylcysteine synthetase gene of Leishmania is essential and involved in response to oxidants","volume":"74","author":"Mukherjee","year":"2009","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0310","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/978-0-387-77570-8_11","article-title":"Searching the Tritryp genomes for drug targets","volume":"625","author":"Myler","year":"2008","journal-title":"Adv Exp Med Biol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0315","series-title":"Leishmania after the genome","author":"Myler","year":"2008"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0320","first-page":"827","article-title":"A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata","volume":"378","author":"Nogoceke","year":"1997","journal-title":"Biol Chem Hoppe Seyler"},{"issue":"Pt 1","key":"10.1016\/j.biotechadv.2011.05.012_bb0325","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1111\/j.1470-8744.1999.tb01158.x","article-title":"Entamoeba histolytica: a eukaryote with trypanothione metabolism instead of glutathione metabolism","volume":"30","author":"Ondarza","year":"1999","journal-title":"Biotechnol Appl Biochem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0330","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.exppara.2006.03.001","article-title":"Naegleria fowleri: a free-living highly pathogenic amoeba contains trypanothione\/trypanothione reductase and glutathione\/glutathione reductase systems","volume":"114","author":"Ondarza","year":"2006","journal-title":"Exp Parasitol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0335","doi-asserted-by":"crossref","first-page":"3322","DOI":"10.1021\/jm0512241","article-title":"Novel antitrypanosomal agents based on palladium nitrofurylthiosemicarbazone complexes: DNA and redox metabolism as potential therapeutic targets","volume":"49","author":"Otero","year":"2006","journal-title":"J Med Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0340","doi-asserted-by":"crossref","first-page":"35853","DOI":"10.1074\/jbc.M204403200","article-title":"A single enzyme catalyses formation of Trypanothione from glutathione and spermidine in Trypanosoma cruzi","volume":"277","author":"Oza","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0345","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1042\/BJ20050948","article-title":"Characterization of the gene encoding glyoxalase II from Leishmania donovani: a potential target for anti-parasite drugs","volume":"393","author":"Padmanabhan","year":"2006","journal-title":"Biochem J"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0350","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1042\/BJ20071138","article-title":"Peroxiredoxins play a major role in protecting Trypanosoma cruzi against macrophage- and endogenously-derived peroxynitrite","volume":"410","author":"Piacenza","year":"2008","journal-title":"Biochem J"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0355","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.actatropica.2005.10.005","article-title":"On the occurrence of thioredoxin in Trypanosoma cruzi","volume":"97","author":"Piattoni","year":"2006","journal-title":"Acta Trop"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0360","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.jsb.2004.12.005","article-title":"Crystal structure of the tryparedoxin peroxidase from the human parasite Trypanosoma cruzi","volume":"150","author":"Pineyro","year":"2005","journal-title":"J Struct Biol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0365","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1021\/jm050922i","article-title":"Design, synthesis, and biological evaluation of phosphinopeptides against Trypanosoma cruzi targeting trypanothione biosynthesis","volume":"49","author":"Ravaschino","year":"2006","journal-title":"J Med Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0370","doi-asserted-by":"crossref","first-page":"7547","DOI":"10.1074\/jbc.275.11.7547","article-title":"Identification and functional characterization of thioredoxin from Trypanosoma brucei brucei","volume":"275","author":"Reckenfelderb\u00e4umer","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0375","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1002\/cmdc.200900097","article-title":"Improved tricyclic inhibitors of trypanothione reductase by screening and chemical synthesis","volume":"4","author":"Richardson","year":"2009","journal-title":"ChemMedChem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0380","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.ijpara.2008.11.009","article-title":"The cytosolic tryparedoxin of Leishmania infantum is essential for parasite survival","volume":"39","author":"Romao","year":"2009","journal-title":"Int J Parasitol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0385","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1021\/jm001079l","article-title":"2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity","volume":"44","author":"Salmon-Chemin","year":"2001","journal-title":"J Med Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0390","doi-asserted-by":"crossref","first-page":"14385","DOI":"10.1074\/jbc.M413338200","article-title":"Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei","volume":"280","author":"Schlecker","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0395","doi-asserted-by":"crossref","first-page":"3519","DOI":"10.1021\/bi00360a007","article-title":"Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases","volume":"25","author":"Shames","year":"1986","journal-title":"Biochemistry"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0400","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1089\/ars.2009.3029","article-title":"Redox control of protein-DNA interactions: from molecular mechanisms to significance in signal transduction, gene expression, and DNA replication","volume":"13","author":"Shlomai","year":"2010","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0405","doi-asserted-by":"crossref","first-page":"2060","DOI":"10.1002\/cmdc.200900262","article-title":"Investigation of trypanothione reductase as a drug target in Trypanosoma brucei","volume":"4","author":"Spinks","year":"2009","journal-title":"ChemMedChem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0410","series-title":"N-substituted 2-(6-oxo-6,7-dihydro-5H-benzo[2,3]azepino[4,5-b]indol-5-yl)-acetamides for treating tropical diseases","author":"Stuhlmann","year":"2005"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0415","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1002\/cbic.200800565","article-title":"Pentafluorosulfanyl as a novel building block for enzyme inhibitors: trypanothione reductase inhibition and antiprotozoal activities of diarylamines","volume":"10","author":"Stump","year":"2009","journal-title":"Chembiochem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0420","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/S0076-6879(83)94078-8","article-title":"Glutathionylspermidine","volume":"94","author":"Tabor","year":"1983","journal-title":"Methods Enzymol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0425","series-title":"Innovation for health: research that makes a difference: TDR annual report 2009","author":"TDR","year":"2010"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0430","doi-asserted-by":"crossref","first-page":"36137","DOI":"10.1074\/jbc.M109.045336","article-title":"Chemical validation of trypanothione synthetase: a potential drug target for human trypanosomiasis","volume":"284","author":"Torrie","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0435","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1046\/j.1365-2958.1998.00968.x","article-title":"Evidence that trypanothione reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus","volume":"29","author":"Tovar","year":"1998","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0440","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1007\/978-1-4020-6051-9_5","article-title":"Kinetics of peroxiredoxins and their role in the decomposition of peroxynitrite","volume":"44","author":"Trujillo","year":"2007","journal-title":"Subcell Biochem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0445","doi-asserted-by":"crossref","first-page":"27246","DOI":"10.1074\/jbc.M311039200","article-title":"Trypanothione S-transferase activity in a trypanosomatid ribosomal elongation factor 1B","volume":"279","author":"Vickers","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0450","doi-asserted-by":"crossref","first-page":"13186","DOI":"10.1073\/pnas.0402918101","article-title":"A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major","volume":"101","author":"Vickers","year":"2004","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0455","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.molbiopara.2008.09.005","article-title":"Glyoxalase II does not support methylglyoxal detoxification but serves as a general trypanothione thioesterase in African trypanosomes","volume":"163","author":"Wendler","year":"2009","journal-title":"Mol Biochem Parasitol"},{"issue":"Pt 3","key":"10.1016\/j.biotechadv.2011.05.012_bb0460","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1042\/0264-6021:3520755","article-title":"Biochemical characterization of a trypanosome enzyme with glutathione-dependent peroxidase activity","volume":"352","author":"Wilkinson","year":"2000","journal-title":"Biochem J"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0465","doi-asserted-by":"crossref","first-page":"8220","DOI":"10.1074\/jbc.275.11.8220","article-title":"Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi","volume":"275","author":"Wilkinson","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0470","doi-asserted-by":"crossref","first-page":"17062","DOI":"10.1074\/jbc.M111126200","article-title":"The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin","volume":"277","author":"Wilkinson","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0475","doi-asserted-by":"crossref","first-page":"13453","DOI":"10.1073\/pnas.202422899","article-title":"Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulum","volume":"99","author":"Wilkinson","year":"2002","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0480","doi-asserted-by":"crossref","first-page":"31640","DOI":"10.1074\/jbc.M303035200","article-title":"RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the African trypanosome","volume":"278","author":"Wilkinson","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biotechadv.2011.05.012_bb0485","first-page":"2566","article-title":"Discovery and initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases","volume":"59","author":"Zaharevitz","year":"1999","journal-title":"Cancer Res"}],"container-title":["Biotechnology Advances"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S073497501100067X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S073497501100067X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,4,6]],"date-time":"2024-04-06T19:50:10Z","timestamp":1712433010000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S073497501100067X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,1]]},"references-count":97,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2012,1]]}},"alternative-id":["S073497501100067X"],"URL":"https:\/\/doi.org\/10.1016\/j.biotechadv.2011.05.012","relation":{},"ISSN":["0734-9750"],"issn-type":[{"value":"0734-9750","type":"print"}],"subject":[],"published":{"date-parts":[[2012,1]]}}}