{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T21:21:12Z","timestamp":1780435272957,"version":"3.54.1"},"reference-count":88,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,2,1]],"date-time":"2016-02-01T00:00:00Z","timestamp":1454284800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001411","name":"Indian Council of Medical Research (ICMR)","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001411","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Department of Health Research"},{"DOI":"10.13039\/501100007334","name":"Ministry of Health and Family Welfare","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100007334","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Department of Sciences and Technology","award":["DST\/INT\/JSPS\/P-117-2011"],"award-info":[{"award-number":["DST\/INT\/JSPS\/P-117-2011"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2016,2]]},"DOI":"10.1016\/j.biochi.2015.12.017","type":"journal-article","created":{"date-parts":[[2015,12,30]],"date-time":"2015-12-30T02:32:50Z","timestamp":1451442770000},"page":"312-325","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":41,"special_numbering":"C","title":["Up-regulation of cytosolic tryparedoxin in Amp B resistant isolates of Leishmania donovani and its interaction with cytosolic tryparedoxin peroxidase"],"prefix":"10.1016","volume":"121","author":[{"given":"Shashi S.","family":"Suman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Asif","family":"Equbal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amir","family":"Zaidi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Md. Yousuf","family":"Ansari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Krishn Pratap","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kuljit","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bidyut","family":"Purkait","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ganesh Chandra","family":"Sahoo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanjeeva","family":"Bimal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pradeep","family":"Das","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vahab","family":"Ali","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2015.12.017_bib1","first-page":"1","article-title":"World Health Organization Control of the Leishmaniases","volume":"Xii-Xiii","author":"W.H.O","year":"2010","journal-title":"World Health organ.tech.rep.ser."},{"key":"10.1016\/j.biochi.2015.12.017_bib2","first-page":"197","article-title":"Pre- & post-treatment evaluation of immunological features in Indian visceral leishmaniasis (VL) patients with HIV co-infection","volume":"123","author":"Sinha","year":"2006","journal-title":"Indian J. Med. Res."},{"key":"10.1016\/j.biochi.2015.12.017_bib3","doi-asserted-by":"crossref","first-page":"536","DOI":"10.4269\/ajtmh.1995.52.536","article-title":"Use of amphotericin B in drug-resistant cases of visceral leishmaniasis in north Bihar, India","volume":"52","author":"Jha","year":"1995","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"10.1016\/j.biochi.2015.12.017_bib4","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1128\/AAC.42.2.352","article-title":"Mechanism of amphotericin B resistance in Leishmania donovani promastigotes","volume":"42","author":"Mbongo","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.biochi.2015.12.017_bib5","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1128\/AAC.00030-11","article-title":"Mechanism of amphotericin B resistance in clinical isolates of Leishmania donovani","volume":"56","author":"Purkait","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.biochi.2015.12.017_bib6","doi-asserted-by":"crossref","first-page":"e97600","DOI":"10.1371\/journal.pone.0097600","article-title":"Stage-dependent expression and up-regulation of trypanothione synthetase in amphotericin B resistant Leishmania donovani","volume":"9","author":"Equbal","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2015.12.017_bib7","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1128\/CMR.19.1.111-126.2006","article-title":"Drug resistance in leishmaniasis","volume":"19","author":"Croft","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.biochi.2015.12.017_bib8","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0166-6851(03)00176-2","article-title":"Properties of trypanothione synthetase from Trypanosoma brucei","volume":"131","author":"Oza","year":"2003","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib9","first-page":"617521","article-title":"Drug resistance in visceral leishmaniasis","volume":"2010","author":"Maltezou","year":"2010","journal-title":"J.\u00a0Biomed. Biotechnol."},{"key":"10.1016\/j.biochi.2015.12.017_bib10","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/S0966-842X(98)01433-4","article-title":"Recent advances in identifying and validating drug targets in trypanosomes and leishmanias","volume":"7","author":"Barrett","year":"1999","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.biochi.2015.12.017_bib11","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.exppara.2012.12.007","article-title":"Release of the cytosolic tryparedoxin peroxidase into the incubation medium and a different profile of cytosolic and mitochondrial peroxiredoxin expression in H2O2-treated Trypanosoma cruzi tissue culture-derived trypomastigotes","volume":"133","author":"Gadelha","year":"2013","journal-title":"Exp. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib12","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.ijpddr.2014.05.002","article-title":"Quantitative proteomic analysis of amphotericin B resistance in Leishmania infantum","volume":"4","author":"Brotherton","year":"2014","journal-title":"Int. J. Parasitol. Drugs Drug Resist"},{"key":"10.1016\/j.biochi.2015.12.017_bib13","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.mam.2004.02.021","article-title":"Oxidative stress and antioxidant defenses: a target for the treatment of diseases caused by parasitic protozoa","volume":"25","author":"Turrens","year":"2004","journal-title":"Mol. Asp. Med."},{"key":"10.1016\/j.biochi.2015.12.017_bib14","doi-asserted-by":"crossref","first-page":"3199","DOI":"10.1016\/j.bbagen.2013.01.013","article-title":"Trypanothione: A unique bis-glutathionyl derivative in trypanosomatids","volume":"1830","author":"Manta","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2015.12.017_bib15","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.biochi.2015.12.017_bib16","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib17","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/35025109","article-title":"Peroxynitrite reductase activity of bacterial peroxiredoxins","volume":"407","author":"Bryk","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2015.12.017_bib18","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.biochi.2015.12.017_bib19","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.biochi.2015.12.017_bib20","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.4155\/fmc.13.146","article-title":"Structural insights into the enzymes of the trypanothione pathway: targets for antileishmaniasis drugs","volume":"5","author":"Colotti","year":"2013","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib21","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.biochi.2015.12.017_bib22","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":"Ludemann","year":"1998","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2015.12.017_bib23","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1002\/biof.5520110121","article-title":"Crystallisation of tryparedoxin I from Crithidia fasciculata","volume":"11","author":"Kalisz","year":"2000","journal-title":"Biofactors"},{"key":"10.1016\/j.biochi.2015.12.017_bib24","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1002\/biof.5520110119","article-title":"Cloning and expression of tryparedoxin I from Crithidia fasciculata","volume":"11","author":"Guerrero","year":"2000","journal-title":"Biofactors"},{"key":"10.1016\/j.biochi.2015.12.017_bib25","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1002\/biof.5520110120","article-title":"Tryparedoxin and tryparedoxin peroxidase","volume":"11","author":"Montemartini","year":"2000","journal-title":"Biofactors"},{"key":"10.1016\/j.biochi.2015.12.017_bib26","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.exppara.2008.09.002","article-title":"Leishmania infantum: provision of reducing equivalents to the mitochondrial tryparedoxin\/tryparedoxin peroxidase system","volume":"120","author":"Castro","year":"2008","journal-title":"Exp. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib27","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.biochi.2015.12.017_bib28","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.biochi.2015.12.017_bib29","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.biochi.2015.12.017_bib30","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1016\/S0891-5849(02)01088-2","article-title":"Specificity and kinetics of a mitochondrial peroxiredoxin of Leishmania infantum","volume":"33","author":"Castro","year":"2002","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.biochi.2015.12.017_bib31","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib32","doi-asserted-by":"crossref","first-page":"e1781","DOI":"10.1371\/journal.pntd.0001781","article-title":"The crystal structures of the tryparedoxin-tryparedoxin peroxidase couple unveil the structural determinants of Leishmania detoxification pathway","volume":"6","author":"Fiorillo","year":"2012","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.biochi.2015.12.017_bib33","doi-asserted-by":"crossref","first-page":"9705","DOI":"10.1038\/srep09705","article-title":"Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking","volume":"5","author":"Brindisi","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.biochi.2015.12.017_bib34","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.biochi.2015.12.017_bib35","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.biochi.2015.12.017_bib36","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib37","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1016\/j.jprot.2011.04.006","article-title":"Molecular characterization and interactome analysis of Trypanosoma cruzi tryparedoxin 1","volume":"74","author":"Pineyro","year":"2011","journal-title":"J.\u00a0Proteomics"},{"key":"10.1016\/j.biochi.2015.12.017_bib38","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.freeradbiomed.2013.04.036","article-title":"Redox metabolism in Trypanosoma cruzi: functional characterization of tryparedoxins revisited","volume":"63","author":"Arias","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.biochi.2015.12.017_bib39","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.jprot.2015.03.001","article-title":"Molecular characterization and interactome analysis of Trypanosoma cruzi tryparedoxin II","volume":"120","author":"Arias","year":"2015","journal-title":"J.\u00a0Proteomics"},{"key":"10.1016\/j.biochi.2015.12.017_bib40","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.biochi.2015.05.016","article-title":"Interaction of frataxin, an iron binding protein, with IscU of Fe-S clusters biogenesis pathway and its upregulation in AmpB resistant Leishmania donovani","volume":"115","author":"Zaidi","year":"2015","journal-title":"Biochimie"},{"key":"10.1016\/j.biochi.2015.12.017_bib41","series-title":"Molecular Cloning: a Laboratory Manual","author":"Sambrook","year":"2001"},{"key":"10.1016\/j.biochi.2015.12.017_bib42","doi-asserted-by":"crossref","first-page":"2371","DOI":"10.1128\/IAI.65.6.2371-2377.1997","article-title":"Adjuvanticity and protective immunity elicited by Leishmania donovani antigens encapsulated in positively charged liposomes","volume":"65","author":"Afrin","year":"1997","journal-title":"Infect. Immun."},{"key":"10.1016\/j.biochi.2015.12.017_bib43","doi-asserted-by":"crossref","first-page":"e108971","DOI":"10.1371\/journal.pone.0108971","article-title":"Interaction between Nbp35 and Cfd1 Proteins of Cytosolic Fe-S Cluster Assembly Reveals a Stable Complex Formation in Entamoeba histolytica","volume":"9","author":"Anwar","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2015.12.017_bib44","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A\u00a0rapid 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":"Anal. Biochem."},{"key":"10.1016\/j.biochi.2015.12.017_bib45","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1111\/j.1432-1033.1972.tb01711.x","article-title":"Hepatic microsomal ethanol oxidation. Hydrogen peroxide formation and the role of catalase","volume":"25","author":"Thurman","year":"1972","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.biochi.2015.12.017_bib46","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1111\/j.1365-2958.2008.06154.x","article-title":"Crucial role of cytosolic tryparedoxin peroxidase in Leishmania donovani survival, drug response and virulence","volume":"68","author":"Iyer","year":"2008","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.biochi.2015.12.017_bib47","first-page":"659","article-title":"Molecular cloning and characterization of a peroxiredoxin from Phanerochaete chrysosporium","volume":"10","author":"Jiang","year":"2005","journal-title":"Cell Mol. Biol. Lett."},{"key":"10.1016\/j.biochi.2015.12.017_bib48","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/0166-6851(87)90113-7","article-title":"Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brucei","volume":"24","author":"Henderson","year":"1987","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib49","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0022-2836(05)80360-2","article-title":"Basic local alignment search tool","volume":"215","author":"Altschul","year":"1990","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2015.12.017_bib50","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.biochi.2015.12.017_bib51","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1006\/jmbi.1993.1626","article-title":"Comparative protein modelling by satisfaction of spatial restraints","volume":"234","author":"Sali","year":"1993","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2015.12.017_bib52","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1002\/prot.340230306","article-title":"Evaluation of comparative protein modeling by MODELLER","volume":"23","author":"Sali","year":"1995","journal-title":"Proteins"},{"key":"10.1016\/j.biochi.2015.12.017_bib53","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.ijbiomac.2012.01.010","article-title":"Comparative modeling of HGPRT enzyme of L.\u00a0donovani and binding affinities of different analogs of GMP","volume":"50","author":"Ansari","year":"2012","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.biochi.2015.12.017_bib54","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1002\/prot.10286","article-title":"Structure validation by C-alpha geometry: phi, psi and C-beta deviation","volume":"50","author":"Lovell","year":"2003","journal-title":"Proteins"},{"key":"10.1016\/j.biochi.2015.12.017_bib55","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.ijbiomac.2015.11.051","article-title":"Establishment of Correlation between In-Silico &In-Vitro Test Analysis against Leishmania HGPRT to inhibitors","volume":"83","author":"Ansari","year":"2016","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.biochi.2015.12.017_bib56","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.biochi.2015.12.017_bib57","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1002\/pro.5560020916","article-title":"Verification of protein structures: patterns of nonbonded atomic interactions","volume":"2","author":"Colovos","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/j.biochi.2015.12.017_bib58","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1002\/prot.340170404","article-title":"Recognition of errors in three-dimensional structures of proteins","volume":"17","author":"Sippl","year":"1993","journal-title":"Proteins"},{"key":"10.1016\/j.biochi.2015.12.017_bib59","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1002\/prot.10389","article-title":"ZDOCK: an initial-stage protein-docking algorithm","volume":"52","author":"Chen","year":"2003","journal-title":"Proteins"},{"key":"10.1016\/j.biochi.2015.12.017_bib60","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1002\/jcc.21287","article-title":"CHARMM: the biomolecular simulation program","volume":"30","author":"Brooks","year":"2009","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib61","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1002\/prot.10092","article-title":"Docking unbound proteins using shape complementarity, desolvation, and electrostatics","volume":"47","author":"Chen","year":"2002","journal-title":"Proteins"},{"key":"10.1016\/j.biochi.2015.12.017_bib62","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1002\/prot.20559","article-title":"ZDOCK and RDOCK performance in CAPRI rounds 3, 4, and 5","volume":"60","author":"Wiehe","year":"2005","journal-title":"Proteins"},{"key":"10.1016\/j.biochi.2015.12.017_bib63","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":"Parasitol. Today"},{"key":"10.1016\/j.biochi.2015.12.017_bib64","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/0035-9203(89)90642-1","article-title":"Reversal of drug resistance in Trypanosoma cruzi and Leishmania donovani by verapamil","volume":"83","author":"Neal","year":"1989","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"10.1016\/j.biochi.2015.12.017_bib65","first-page":"99","article-title":"The mutual sparing effects of selenium and vitamin E in animal nutrition may be further explained by the discovery that mammalian thioredoxin reductase is a selenoenzyme","volume":"5","author":"Tamura","year":"1995","journal-title":"Biofactors"},{"key":"10.1016\/j.biochi.2015.12.017_bib66","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.molbiopara.2007.11.002","article-title":"Divergence of trypanothione-dependent tryparedoxin cascade into cytosolic and mitochondrial pathways in arsenite-resistant variants of Leishmania amazonensis","volume":"157","author":"Hsu","year":"2008","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib67","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.molbiopara.2013.06.006","article-title":"Comparative proteomic analysis of antimony-resistant and -susceptible Leishmania braziliensis and Leishmania infantum chagasi lines","volume":"190","author":"Matrangolo","year":"2013","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib68","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1093\/emboj\/21.8.1881","article-title":"Life without transcriptional control? From fly to man and back again","volume":"21","author":"Clayton","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.biochi.2015.12.017_bib69","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.molbiopara.2007.07.007","article-title":"Post-transcriptional regulation of gene expression in trypanosomes and leishmanias","volume":"156","author":"Clayton","year":"2007","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib70","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.molbiopara.2011.10.002","article-title":"Developmental regulation of gene expression in the absence of transcriptional control: the case of kinetoplastids","volume":"181","author":"Kramer","year":"2012","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib71","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.mib.2009.06.011","article-title":"Fighting the oxidative assault: the Trypanosoma cruzi journey to infection","volume":"12","author":"Piacenza","year":"2009","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.biochi.2015.12.017_bib72","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":"Flohe","year":"2002","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.biochi.2015.12.017_bib73","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.biochi.2015.12.017_bib74","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1515\/bchm.1997.378.8.827","article-title":"A\u00a0unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata","volume":"378","author":"Nogoceke","year":"1997","journal-title":"Biol. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib75","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1016\/S0891-5849(98)00263-9","article-title":"Cytoplasmic localization of the trypanothione peroxidase system in Crithidia fasciculata","volume":"26","author":"Steinert","year":"1999","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.biochi.2015.12.017_bib76","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0166-6851(01)00320-6","article-title":"Molecular characterisation of mitochondrial and cytosolic trypanothione-dependent tryparedoxin peroxidases in Trypanosoma brucei","volume":"116","author":"Tetaud","year":"2001","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.biochi.2015.12.017_bib77","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.biochi.2015.12.017_bib78","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1128\/AAC.01563-07","article-title":"Roles of trypanothione S-transferase and tryparedoxin peroxidase in resistance to antimonials","volume":"52","author":"Wyllie","year":"2008","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.biochi.2015.12.017_bib79","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.molbiopara.2010.05.015","article-title":"Elevated levels of tryparedoxin peroxidase in antimony unresponsive Leishmania donovani field isolates","volume":"173","author":"Wyllie","year":"2010","journal-title":"Mol. Biochem. Parasitol."},{"issue":"3","key":"10.1016\/j.biochi.2015.12.017_bib80","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1042\/bj3520755","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.biochi.2015.12.017_bib81","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.biochi.2015.12.017_bib82","doi-asserted-by":"crossref","first-page":"6627","DOI":"10.1074\/jbc.M110.167247","article-title":"Intraphagosomal peroxynitrite as a macrophage-derived cytotoxin against internalized Trypanosoma cruzi: consequences for oxidative killing and role of microbial peroxiredoxins in infectivity","volume":"286","author":"Alvarez","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib83","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.jprot.2013.01.011","article-title":"Proteome changes associated with Leishmania donovani promastigote adaptation to oxidative and nitrosative stresses","volume":"81","author":"Sardar","year":"2013","journal-title":"J.\u00a0Proteomics"},{"key":"10.1016\/j.biochi.2015.12.017_bib84","doi-asserted-by":"crossref","first-page":"4807","DOI":"10.1111\/febs.12449","article-title":"Miltefosine-unresponsive Leishmania donovani has a greater ability than miltefosine-responsive L.\u00a0donovani to resist reactive oxygen species","volume":"280","author":"Das","year":"2013","journal-title":"FEBS J."},{"key":"10.1016\/j.biochi.2015.12.017_bib85","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1515\/BC.2003.146","article-title":"Verification of the interaction of a tryparedoxin peroxidase with tryparedoxin by ESI-MS\/MS","volume":"384","author":"Budde","year":"2003","journal-title":"Biol. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib86","doi-asserted-by":"crossref","first-page":"25919","DOI":"10.1074\/jbc.M301526200","article-title":"Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function","volume":"278","author":"Alphey","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2015.12.017_bib87","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.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2015.12.017_bib88","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.jprot.2009.08.006","article-title":"Proteomic characterization of the released\/secreted proteins of Leishmania (Viannia) braziliensis promastigotes","volume":"73","author":"Cuervo","year":"2009","journal-title":"J.\u00a0Proteomics"}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908415004319?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908415004319?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,9,13]],"date-time":"2020-09-13T10:05:47Z","timestamp":1599991547000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908415004319"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,2]]},"references-count":88,"alternative-id":["S0300908415004319"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2015.12.017","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2016,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Up-regulation of cytosolic tryparedoxin in Amp B resistant isolates of Leishmania donovani and its interaction with cytosolic tryparedoxin peroxidase","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2015.12.017","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM). All rights reserved.","name":"copyright","label":"Copyright"}]}}