{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,31]],"date-time":"2026-03-31T17:02:41Z","timestamp":1774976561490,"version":"3.50.1"},"update-to":[{"DOI":"10.1371\/journal.pntd.0006180","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2018,2,1]],"date-time":"2018-02-01T00:00:00Z","timestamp":1517443200000}}],"reference-count":91,"publisher":"Public Library of Science (PLoS)","issue":"1","license":[{"start":{"date-parts":[[2018,1,22]],"date-time":"2018-01-22T00:00:00Z","timestamp":1516579200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosntds.org"],"crossmark-restriction":false},"short-container-title":["PLoS Negl Trop Dis"],"DOI":"10.1371\/journal.pntd.0006180","type":"journal-article","created":{"date-parts":[[2018,1,22]],"date-time":"2018-01-22T18:28:48Z","timestamp":1516645728000},"page":"e0006180","update-policy":"https:\/\/doi.org\/10.1371\/journal.pntd.corrections_policy","source":"Crossref","is-referenced-by-count":12,"title":["Inhibitors of Trypanosoma cruzi Sir2 related protein 1 as potential drugs against Chagas disease"],"prefix":"10.1371","volume":"12","author":[{"given":"Lu\u00eds","family":"Gaspar","sequence":"first","affiliation":[]},{"given":"Ross P.","family":"Coron","sequence":"additional","affiliation":[]},{"given":"Paul","family":"KongThoo Lin","sequence":"additional","affiliation":[]},{"given":"David M.","family":"Costa","sequence":"additional","affiliation":[]},{"given":"Bego\u00f1a","family":"Perez-Cabezas","sequence":"additional","affiliation":[]},{"given":"Joana","family":"Tavares","sequence":"additional","affiliation":[]},{"given":"Meritxell","family":"Roura-Ferrer","sequence":"additional","affiliation":[]},{"given":"Isbaal","family":"Ramos","sequence":"additional","affiliation":[]},{"given":"C\u00e9line","family":"Ronin","sequence":"additional","affiliation":[]},{"given":"Louise L.","family":"Major","sequence":"additional","affiliation":[]},{"given":"Fabrice","family":"Ciesielski","sequence":"additional","affiliation":[]},{"given":"Iain K.","family":"Pemberton","sequence":"additional","affiliation":[]},{"given":"Jane","family":"MacDougall","sequence":"additional","affiliation":[]},{"given":"Paola","family":"Ciapetti","sequence":"additional","affiliation":[]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1994-2009","authenticated-orcid":true,"given":"Terry K.","family":"Smith","sequence":"additional","affiliation":[]},{"given":"Anabela","family":"Cordeiro-da-Silva","sequence":"additional","affiliation":[]}],"member":"340","published-online":{"date-parts":[[2018,1,22]]},"reference":[{"issue":"6","key":"ref1","first-page":"33","article-title":"WHO Chagas disease in Latin America: an epidemiological update based on 2010 estimates","volume":"90","year":"2015","journal-title":"Wkly Epidemiol Rec"},{"issue":"2","key":"ref2","doi-asserted-by":"crossref","first-page":"e114","DOI":"10.1371\/journal.pntd.0000114","article-title":"Measuring the burden of neglected tropical diseases: the global burden of disease framework","volume":"1","author":"C. D. Mathers","year":"2007","journal-title":"PLoS Negl Trop Dis"},{"issue":"4","key":"ref3","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/S1473-3099(13)70002-1","article-title":"Global economic burden of Chagas disease: a computational simulation model","volume":"13","author":"B. Y. Lee","year":"2013","journal-title":"Lancet Infect Dis"},{"issue":"11","key":"ref4","doi-asserted-by":"crossref","first-page":"e0003981","DOI":"10.1371\/journal.pntd.0003981","article-title":"Historical Perspectives on the Epidemiology of Human Chagas Disease in Texas and Recommendations for Enhanced Understanding of Clinical Chagas Disease in the Southern United States","volume":"9","author":"MN Garcia","year":"2015","journal-title":"PLoS Negl Trop Dis"},{"issue":"5","key":"ref5","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1056\/NEJMra1410150","article-title":"Chagas&apos; Disease","volume":"373","author":"C. Bern","year":"2015","journal-title":"N Engl J Med"},{"issue":"9723","key":"ref6","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1016\/S0140-6736(10)60061-X","article-title":"Chagas disease","volume":"375","author":"A. Rassi","year":"2010","journal-title":"The Lancet"},{"key":"ref7","unstructured":"WHO Reporte sobre la enfermedade de Chagas. Available at: <ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/whqlibdoc.who.int\/hq\/2007\/TDR_SWG_09_spa.pdf\" xlink:type=\"simple\">http:\/\/whqlibdoc.who.int\/hq\/2007\/TDR_SWG_09_spa.pdf<\/ext-link> (Accessed May 22, 2015)."},{"issue":"1\u20132","key":"ref8","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.actatropica.2009.11.003","article-title":"Chagas disease: a Latin American health problem becoming a world health problem","volume":"115","author":"G. A. Schmunis","year":"2010","journal-title":"Acta Trop"},{"issue":"2","key":"ref9","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1586\/14787210.7.2.157","article-title":"Side effects of benznidazole as treatment in chronic Chagas disease: fears and realities","volume":"7","author":"R. Viotti","year":"2009","journal-title":"Expert Rev Anti Infect Ther"},{"issue":"8","key":"ref10","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1191\/0960327106het653oa","article-title":"Toxic side effects of drugs used to treat Chagas&apos; disease (American trypanosomiasis)","volume":"25","author":"J. A. Castro","year":"2006","journal-title":"Hum Exp Toxicol"},{"issue":"7301","key":"ref11","doi-asserted-by":"crossref","first-page":"S12","DOI":"10.1038\/nature09224","article-title":"Chagas disease: pushing through the pipeline","volume":"465","author":"J. Clayton","year":"2010","journal-title":"Nature"},{"issue":"20","key":"ref12","doi-asserted-by":"crossref","first-page":"1899","DOI":"10.1056\/NEJMoa1313122","article-title":"Randomized trial of posaconazole and benznidazole for chronic Chagas&apos; disease","volume":"370","author":"I. Molina","year":"2014","journal-title":"N Engl J Med"},{"issue":"14","key":"ref13","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1056\/NEJMoa1507574","article-title":"Randomized Trial of Benznidazole for Chronic Chagas&apos; Cardiomyopathy","volume":"373","author":"C. A. Morillo","year":"2015","journal-title":"N Engl J Med"},{"key":"ref14","unstructured":"DNDi, Drug Trial for Leading Parasitic Killer of the Americas Shows Mixed Results but Provides New Evidence for Improved Therapy. Washington D.C., 2013."},{"issue":"2","key":"ref15","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1006\/bbrc.2000.3000","article-title":"Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins","volume":"273","author":"R. A. Frye","year":"2000","journal-title":"Biochem Biophys Res Commun"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1186\/1471-2148-13-60","article-title":"Genealogy of an ancient protein family: the Sirtuins, a family of disordered members","volume":"13","author":"S. Costantini","year":"2013","journal-title":"BMC Evol Biol"},{"issue":"1","key":"ref17","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0968-0004(02)00005-1","article-title":"Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases","volume":"28","author":"J. M. Denu","year":"2003","journal-title":"Trends Biochem Sci"},{"issue":"4","key":"ref18","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.cell.2005.03.035","article-title":"Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation","volume":"121","author":"G. G. Liou","year":"2005","journal-title":"Cell"},{"issue":"5","key":"ref19","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1016\/j.cell.2006.06.057","article-title":"SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells","volume":"126","author":"M. C. Haigis","year":"2006","journal-title":"Cell"},{"issue":"22","key":"ref20","doi-asserted-by":"crossref","first-page":"21313","DOI":"10.1074\/jbc.M413296200","article-title":"Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase","volume":"280","author":"G. Liszt","year":"2005","journal-title":"J Biol Chem"},{"issue":"21","key":"ref21","doi-asserted-by":"crossref","first-page":"5851","DOI":"10.1093\/emboj\/cdg553","article-title":"A chromosomal SIR2 homologue with both histone NAD-dependent ADP-ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei","volume":"22","author":"J. A. Garcia-Salcedo","year":"2003","journal-title":"EMBO J"},{"issue":"3","key":"ref22","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1042\/BJ20080666","article-title":"The Leishmania infantum cytosolic SIR2-related protein 1 (LiSIR2RP1) is an NAD+ -dependent deacetylase and ADP-ribosyltransferase","volume":"415","author":"J. Tavares","year":"2008","journal-title":"Biochem J"},{"issue":"26","key":"ref23","doi-asserted-by":"crossref","first-page":"14178","DOI":"10.1073\/pnas.250422697","article-title":"Silent information regulator 2 family of NAD- dependent histone\/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose","volume":"97","author":"K. G. Tanner","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6057","key":"ref24","doi-asserted-by":"crossref","first-page":"806","DOI":"10.1126\/science.1207861","article-title":"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase","volume":"334","author":"J. Du","year":"2011","journal-title":"Science"},{"issue":"4","key":"ref25","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/j.cmet.2014.03.014","article-title":"Lysine glutarylation is a protein posttranslational modification regulated by SIRT5","volume":"19","author":"M. Tan","year":"2014","journal-title":"Cell Metab"},{"issue":"9","key":"ref26","doi-asserted-by":"crossref","first-page":"750","DOI":"10.14348\/molcells.2015.0167","article-title":"Sirtuins in Cancer: a Balancing Act between Genome Stability and Metabolism","volume":"38","author":"S. M. Jeong","year":"2015","journal-title":"Mol Cells"},{"key":"ref27","article-title":"Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism","author":"P. Gomes","year":"2015","journal-title":"Trends Pharmacol Sci"},{"issue":"1","key":"ref28","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.advms.2015.09.003","article-title":"The role of sirtuins in aging and age-related diseases","volume":"61","author":"M. Watroba","year":"2015","journal-title":"Adv Med Sci"},{"issue":"10","key":"ref29","doi-asserted-by":"crossref","first-page":"1907","DOI":"10.4161\/cc.9.10.11481","article-title":"At the crossroad of lifespan, calorie restriction, chromatin and disease: meeting on sirtuins","volume":"9","author":"R. Mostoslavsky","year":"2010","journal-title":"Cell Cycle"},{"issue":"4","key":"ref30","doi-asserted-by":"crossref","first-page":"a018713","DOI":"10.1101\/cshperspect.a018713","article-title":"Erasers of histone acetylation: the histone deacetylase enzymes","volume":"6","author":"E. Seto","year":"2014","journal-title":"Cold Spring Harb Perspect Biol"},{"issue":"10","key":"ref31","doi-asserted-by":"crossref","first-page":"4623","DOI":"10.1091\/mbc.E05-01-0033","article-title":"Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins","volume":"16","author":"E. Michishita","year":"2005","journal-title":"Mol Biol Cell"},{"issue":"6","key":"ref32","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1093\/emboj\/20.6.1353","article-title":"Acetylation of TAF(I)68, a subunit of TIF-IB\/SL1, activates RNA polymerase I transcription","volume":"20","author":"V. Muth","year":"2001","journal-title":"EMBO J"},{"issue":"29","key":"ref33","doi-asserted-by":"crossref","first-page":"11800","DOI":"10.1073\/pnas.1200583109","article-title":"Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence","volume":"109","author":"Z. Mao","year":"2012","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6036","key":"ref34","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1126\/science.1202723","article-title":"SIRT6 promotes DNA repair under stress by activating PARP1","volume":"332","author":"Z. Mao","year":"2011","journal-title":"Science"},{"issue":"1","key":"ref35","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/j.bbrc.2013.10.020","article-title":"Inhibition of H3K18 deacetylation of Sirt7 by Myb-binding protein 1a (Mybbp1a)","volume":"441","author":"M. F. Karim","year":"2013","journal-title":"Biochem Biophys Res Commun"},{"issue":"5","key":"ref36","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1074\/mcp.A111.015156","article-title":"Functional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcription","volume":"11","author":"Y. C. Tsai","year":"2012","journal-title":"Mol Cell Proteomics"},{"issue":"8","key":"ref37","doi-asserted-by":"crossref","first-page":"e784","DOI":"10.1371\/journal.pone.0000784","article-title":"Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis","volume":"2","author":"B. J. North","year":"2007","journal-title":"PLoS One"},{"issue":"7285","key":"ref38","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1038\/nature08778","article-title":"SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation","volume":"464","author":"M. D. Hirschey","year":"2010","journal-title":"Nature"},{"issue":"3","key":"ref39","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1016\/j.cell.2009.02.026","article-title":"SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle","volume":"137","author":"T. Nakagawa","year":"2009","journal-title":"Cell"},{"issue":"1","key":"ref40","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.cell.2005.01.037","article-title":"Telomeric heterochromatin propagation and histone acetylation control mutually exclusive expression of antigenic variation genes in malaria parasites","volume":"121","author":"L. H. Freitas-Junior","year":"2005","journal-title":"Cell"},{"issue":"4","key":"ref41","doi-asserted-by":"crossref","first-page":"e84","DOI":"10.1371\/journal.pbio.1000084","article-title":"Sir2 paralogues cooperate to regulate virulence genes and antigenic variation in Plasmodium falciparum","volume":"7","author":"C. J. Tonkin","year":"2009","journal-title":"PLoS Biol"},{"issue":"3","key":"ref42","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1111\/j.1365-2958.2006.05553.x","article-title":"A sirtuin in the African trypanosome is involved in both DNA repair and telomeric gene silencing but is not required for antigenic variation","volume":"63","author":"S. Alsford","year":"2007","journal-title":"Mol Microbiol"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.gene.2005.06.047","article-title":"Targeted disruption of cytosolic SIR2 deacetylase discloses its essential role in Leishmania survival and proliferation","volume":"363","author":"B. Vergnes","year":"2005","journal-title":"Gene"},{"issue":"8","key":"ref44","doi-asserted-by":"crossref","first-page":"4669","DOI":"10.1128\/AAC.04694-14","article-title":"Characterization of Trypanosoma cruzi sirtuins as possible drug targets for Chagas Disease","volume":"59","author":"N. S. Moretti","year":"2015","journal-title":"Antimicrob Agents Chemother"},{"issue":"4","key":"ref45","doi-asserted-by":"crossref","first-page":"e0003725","DOI":"10.1371\/journal.pntd.0003725","article-title":"Overexpression of cytoplasmic TcSIR2RP1 and mitochondrial TcSIR2RP3 impacts on Trypanosoma cruzi growth and cell invasion","volume":"9","author":"C. Ritagliati","year":"2015","journal-title":"PLoS Negl Trop Dis"},{"issue":"1","key":"ref46","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1002\/cmdc.200900367","article-title":"Bisnaphthalimidopropyl derivatives as inhibitors of Leishmania SIR2 related protein 1","volume":"5","author":"J. Tavares","year":"2010","journal-title":"ChemMedChem"},{"issue":"8","key":"ref47","doi-asserted-by":"crossref","first-page":"e1298","DOI":"10.1371\/journal.pntd.0001298","article-title":"Activity in vivo of anti-Trypanosoma cruzi compounds selected from a high throughput screening","volume":"5","author":"G. Andriani","year":"2011","journal-title":"PLoS Negl Trop Dis"},{"issue":"2","key":"ref48","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/S0378-1119(99)00386-8","article-title":"Functional analysis of the intergenic regions of TcP2beta gene loci allowed the construction of an improved Trypanosoma cruzi expression vector","volume":"239","author":"M. P. Vazquez","year":"1999","journal-title":"Gene"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/1472-6750-6-32","article-title":"pTcINDEX: a stable tetracycline-regulated expression vector for Trypanosoma cruzi","volume":"6","author":"M. C. Taylor","journal-title":"BMC biotechnology"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"2532","DOI":"10.1128\/AAC.02490-15","article-title":"Activity of bisnaphthalimidopropyl derivatives against <italic>Trypanosoma brucei<\/italic>","volume":"60","author":"NAG Gra\u00e7a","year":"2016","journal-title":"Antimicrob Agents Chemother"},{"issue":"14","key":"ref51","doi-asserted-by":"crossref","first-page":"1609","DOI":"10.1016\/S0960-894X(00)00293-6","article-title":"The synthesis and in vitro cytotoxic studies of novel bis-naphthalimidopropyl polyamine derivatives","volume":"10","author":"P. K. Lin","year":"2000","journal-title":"Bioorg Med Chem Lett"},{"issue":"4","key":"ref52","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1016\/j.ejmech.2009.12.047","article-title":"Synthesis, cytotoxicity and DNA-binding of novel bisnaphthalimidopropyl derivatives in breast cancer MDA-MB-231 cells","volume":"45","author":"G. A. Barron","year":"2010","journal-title":"Eur J Med Chem"},{"issue":"3","key":"ref53","first-page":"414","article-title":"Cytotoxicity and Cell Death Mechanisms Induced by a Novel Bisnaphthalimidopropyl Derivative against the NCI-H460 non-small Lung Cancer Cell Line","volume":"13","author":"T. Lima","year":"2013","journal-title":"Anti-Cancer Agents in Medicinal Chemistry"},{"issue":"Pt 2","key":"ref54","first-page":"25","article-title":"XDS. Acta Crystallographica","volume":"66","author":"W. Kabsch","year":"2010","journal-title":"Section D Biological Crystallography"},{"issue":"Pt 4","key":"ref55","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"M.D. Winn","year":"2011","journal-title":"Acta Crystallographica. Section D Biological Crystallography"},{"issue":"Pt 4","key":"ref56","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1107\/S0907444907002661","article-title":"Automated search-model discovery and preparation for structure solution by molecular replacement","volume":"63","author":"R.M. Keegan","year":"2007","journal-title":"Acta Crystallographica. Section D Biological Crystallography"},{"issue":"Pt 4","key":"ref57","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"P. Emsley","year":"2010","journal-title":"Acta Crystallographica. Section D Biological Crystallography"},{"issue":"Pt 4","key":"ref58","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"G.N. Murshudov","year":"2011","journal-title":"Acta Crystallographica. Section D Biological Crystallography"},{"issue":"1","key":"ref59","first-page":"235","article-title":"The Protein Data Bank","volume":"28","author":"H. M. Berman","year":"2000"},{"issue":"23","key":"ref60","doi-asserted-by":"crossref","first-page":"8563","DOI":"10.1073\/pnas.0401057101","article-title":"Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone\/protein deacetylases","volume":"101","author":"K. Zhao","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"ref61","first-page":"136","article-title":"Crystal structure analysis of human Sirt2 and its ADP-ribose complex","volume":"182","author":"S Moniot","year":"2013"},{"key":"ref62","first-page":"6263","article-title":"Selective Sirt2 inhibition by ligand-induced rearrangement of the active site","volume":"6","author":"T. Rumpf","year":"2015"},{"key":"ref63","first-page":"2785","article-title":"Autodock4 and AutoDockTools4: automated docking with selective receptor flexiblity","volume":"16","author":"G. M. Morris","year":"2009"},{"key":"ref64","first-page":"455","article-title":"AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading","volume":"31","author":"O. Trott","year":"2010"},{"key":"ref65","article-title":"The PyMOL Molecular Graphics System, Version 1.5.0.4 Schr\u00f6dinger","author":"Schr\u00f6dinger"},{"key":"ref66","first-page":"237","article-title":"Cancer Cell Culture","volume":"731","author":"J. van Meerloo","year":"2011"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"8026","DOI":"10.1002\/ejoc.201403346","article-title":"Facile Synthesis of Cyclohexanediones and Dialkylresorcinols\u2013Bioactive Natural Products from Entomopathogenic Bacteria","volume":"2014","author":"M. Kronenwerth","year":"2014","journal-title":"Eur. J. Org. Chem."},{"issue":"9","key":"ref68","doi-asserted-by":"crossref","first-page":"5317","DOI":"10.1074\/jbc.M707613200","article-title":"Acetylation-dependent ADP-ribosylation by Trypanosoma brucei Sir2","volume":"283","author":"T. M. Kowieski","year":"2008","journal-title":"J Biol Chem"},{"issue":"30","key":"ref69","doi-asserted-by":"crossref","first-page":"9877","DOI":"10.1021\/bi049592e","article-title":"Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone\/protein deacetylases","volume":"43","author":"M. T. Borra","year":"2004","journal-title":"Biochemistry"},{"issue":"2","key":"ref70","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/S1097-2765(03)00038-8","article-title":"The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase","volume":"11","author":"B. J. North","year":"2003","journal-title":"Molecular Cell"},{"issue":"6","key":"ref71","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.molcel.2005.02.022","article-title":"Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme","volume":"17","author":"J. L. Avalos","year":"2005","journal-title":"Mol Cell"},{"issue":"2","key":"ref72","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.molbiopara.2007.12.003","article-title":"Biochemical characterization of Plasmodium falciparum Sir2, a NAD+-dependent deacetylase","volume":"158","author":"S. P. Chakrabarty","year":"2008","journal-title":"Mol Biochem Parasitol"},{"issue":"2","key":"ref73","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.actatropica.2012.01.001","article-title":"Anti-Trypanosoma cruzi activity of nicotinamide","volume":"122","author":"M. B. Soares","year":"2012","journal-title":"Acta Trop"},{"issue":"2","key":"ref74","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.parint.2011.11.005","article-title":"Anti-leishmanial activity of the bisnaphthalimidopropyl derivatives","volume":"61","author":"J. Tavares","year":"2012","journal-title":"Parasitol Int"},{"issue":"2","key":"ref75","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1177\/108705719900400206","article-title":"A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays","volume":"4","author":"J. H. Zhang","year":"1999","journal-title":"J Biomol Screen"},{"key":"ref76","doi-asserted-by":"crossref","DOI":"10.1038\/srep04703","article-title":"Nitroheterocyclic compounds are more efficacious than CYP51 inhibitors against Trypanosoma cruzi: implications for Chagas disease drug discovery and development","volume":"4","author":"C. B. Moraes","year":"2014","journal-title":"Sci Rep"},{"issue":"2","key":"ref77","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1124\/jpet.102.038620","article-title":"The critical role of mitochondrial energetic impairment in the toxicity of nimesulide to hepatocytes","volume":"303","author":"F. E. Mingatto","year":"2002","journal-title":"J Pharmacol Exp Ther"},{"issue":"3","key":"ref78","doi-asserted-by":"crossref","first-page":"255","DOI":"10.3109\/01480545.2013.838779","article-title":"The genotoxic and cytotoxic effects of nimesulide in the mouse bone marrow","volume":"37","author":"R. Tripathi","year":"2014","journal-title":"Drug Chem Toxicol"},{"issue":"2","key":"ref79","doi-asserted-by":"crossref","first-page":"178","DOI":"10.3109\/01480545.2013.834357","article-title":"Genotoxicity of nimesulide in Wistar rats","volume":"37","author":"D. Borkotoky","year":"2014","journal-title":"Drug Chem Toxicol"},{"issue":"2","key":"ref80","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.molbiopara.2012.08.003","article-title":"Sirtuins of parasitic protozoa: in search of function(s)","volume":"185","author":"A. A. Religa","year":"2012","journal-title":"Mol Biochem Parasitol"},{"key":"ref81","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.ejmech.2012.11.014","article-title":"Sirtuins as emerging anti-parasitic targets","volume":"59","author":"W. Zheng","year":"2013","journal-title":"Eur J Med Chem"},{"issue":"8","key":"ref82","doi-asserted-by":"crossref","first-page":"883","DOI":"10.2174\/092986706776361058","article-title":"Cell Life versus cell longevity: the mysteries surrounding the NAD+ precursor nicotinamide","volume":"13","author":"F. Li","year":"2006","journal-title":"Curr Med Chem"},{"issue":"2","key":"ref83","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1111\/j.1574-6968.2008.01135.x","article-title":"Nicotinamide inhibits Plasmodium falciparum Sir2 activity in vitro and parasite growth","volume":"282","author":"D. Prusty","year":"2008","journal-title":"FEMS Microbiol Lett"},{"issue":"2","key":"ref84","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1128\/AAC.49.2.808-812.2005","article-title":"In vitro antileishmanial activity of nicotinamide","volume":"49","author":"D. Sereno","year":"2005","journal-title":"Antimicrob Agents Chemother"},{"issue":"15","key":"ref85","doi-asserted-by":"crossref","first-page":"10548","DOI":"10.1074\/jbc.M112.449207","article-title":"Nicotinamide inhibits the lysosomal cathepsin b-like protease and kills African trypanosomes","volume":"288","author":"J. D. Unciti-Broceta","year":"2013","journal-title":"J Biol Chem"},{"issue":"3","key":"ref86","doi-asserted-by":"crossref","first-page":"179","DOI":"10.2174\/157340707781695497","article-title":"Polyamine Analogues and Derivatives as Potential Anticancer Agents","volume":"3","author":"L. Ralton","year":"2007","journal-title":"Current Bioactive Compounds"},{"issue":"3","key":"ref87","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/0223-5234(96)88230-4","article-title":"Bis-naphthalimides. 2. Synthesis and biological activity of 5,6-acenaphthalimidoalkyl-1,8-naphthalimidoalkyl amines","volume":"30","author":"M. F. Bra\u00f1a","year":"1995","journal-title":"European Journal of Medicinal Chemistry"},{"issue":"12","key":"ref88","doi-asserted-by":"crossref","first-page":"e1001226","DOI":"10.1371\/journal.ppat.1001226","article-title":"The killing of African trypanosomes by ethidium bromide","volume":"6","author":"A. Roy Chowdhury","year":"2010","journal-title":"PLoS Pathog"},{"issue":"9","key":"ref89","doi-asserted-by":"crossref","first-page":"1220","DOI":"10.1093\/bioinformatics\/btu016","article-title":"Prediction of nuclear export signals using weighted regular expressions (Wregex)","volume":"30","author":"G. Prieto","year":"2014","journal-title":"Bioinformatics"},{"issue":"25","key":"ref90","doi-asserted-by":"crossref","first-page":"10171","DOI":"10.1073\/pnas.0900604106","article-title":"Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs","volume":"106","author":"S. Kosugi","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"3","key":"ref91","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1038\/nrd2275","article-title":"Determining druggability","volume":"6","author":"J. Owens","year":"2007","journal-title":"Nat Rev Drug Discov"}],"updated-by":[{"DOI":"10.1371\/journal.pntd.0006180","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2018,2,1]],"date-time":"2018-02-01T00:00:00Z","timestamp":1517443200000}}],"container-title":["PLOS Neglected Tropical Diseases"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pntd.0006180","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,8,31]],"date-time":"2023-08-31T17:09:03Z","timestamp":1693501743000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pntd.0006180"}},"subtitle":[],"editor":[{"given":"Igor C.","family":"Almeida","sequence":"first","affiliation":[]}],"short-title":[],"issued":{"date-parts":[[2018,1,22]]},"references-count":91,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2018,1,22]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pntd.0006180","relation":{"new_version":[{"id-type":"doi","id":"10.1371\/journal.pntd.0006180","asserted-by":"object"}]},"ISSN":["1935-2735"],"issn-type":[{"value":"1935-2735","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,1,22]]}}}