{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,20]],"date-time":"2026-02-20T07:01:59Z","timestamp":1771570919758,"version":"3.50.1"},"reference-count":48,"publisher":"Elsevier BV","content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Proteomics"],"published-print":{"date-parts":[[2014,5]]},"DOI":"10.1016\/j.jprot.2014.02.030","type":"journal-article","created":{"date-parts":[[2014,3,15]],"date-time":"2014-03-15T02:00:34Z","timestamp":1394848834000},"page":"44-59","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":25,"special_numbering":"C","title":["A quantitative proteomic screen to identify potential drug resistance mechanism in \u03b1-difluoromethylornithine (DFMO) resistant Leishmania donovani"],"prefix":"10.1016","volume":"102","author":[{"given":"Alok Kumar","family":"Singh","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sigrid","family":"Roberts","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Buddy","family":"Ullman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rentala","family":"Madhubala","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jprot.2014.02.030_bb0005","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.drup.2004.07.002","article-title":"Leishmaniasis: drugs in the clinic, resistance and new developments","volume":"7","author":"Ouellette","year":"2004","journal-title":"Drug Resist Updat"},{"key":"10.1016\/j.jprot.2014.02.030_bb0010","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1086\/318121","article-title":"Failure of pentavalent antimony in visceral leishmaniasis in India: report from the center of the Indian epidemic","volume":"31","author":"Sundar","year":"2000","journal-title":"Clin Infect Dis"},{"key":"10.1016\/j.jprot.2014.02.030_bb0015","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1007\/s00726-010-0630-3","article-title":"Polyamine metabolism in Leishmania: from arginine to trypanothione","volume":"40","author":"Colotti","year":"2011","journal-title":"Amino Acids"},{"key":"10.1016\/j.jprot.2014.02.030_bb0020","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1128\/AAC.01193-06","article-title":"Leishmania donovani polyamine biosynthetic enzyme overproducers as tools to investigate the mode of action of cytotoxic polyamine analogs","volume":"51","author":"Roberts","year":"2007","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.jprot.2014.02.030_bb0025","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 Gen Subj"},{"key":"10.1016\/j.jprot.2014.02.030_bb0030","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.jprot.2014.02.030_bb0035","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1042\/BST0350314","article-title":"Ornithine decarboxylase and S-adenosylmethionine decarboxylase in trypanosomatids","volume":"35","author":"Persson","year":"2007","journal-title":"Biochem Soc Trans"},{"key":"10.1016\/j.jprot.2014.02.030_bb0040","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1128\/IAI.01236-08","article-title":"Leishmania donovani ornithine decarboxylase is indispensable for parasite survival in the mammalian host","volume":"77","author":"Boitz","year":"2009","journal-title":"Infect Immun"},{"key":"10.1016\/j.jprot.2014.02.030_bb0045","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1006\/expr.1998.4237","article-title":"Trypanosoma brucei brucei: characterization of an ODC null bloodstream form mutant and the action of alpha-difluoromethylornithine","volume":"88","author":"Li","year":"1998","journal-title":"Exp Parasitol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0050","doi-asserted-by":"crossref","first-page":"2764","DOI":"10.1128\/IAI.00073-11","article-title":"Spermidine synthase is required for virulence of Leishmania donovani","volume":"79","author":"Gilroy","year":"2011","journal-title":"Infect Immun"},{"key":"10.1016\/j.jprot.2014.02.030_bb0055","doi-asserted-by":"crossref","first-page":"23668","DOI":"10.1074\/jbc.M402042200","article-title":"Arginase plays a pivotal role in polyamine precursor metabolism in Leishmania. Characterization of gene deletion mutants","volume":"279","author":"Roberts","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jprot.2014.02.030_bb0060","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1006\/bbrc.2000.3996","article-title":"Sensitivity of trypanosomatid protozoa to DFMO and metabolic turnover of ornithine decarboxylase","volume":"279","author":"Carrillo","year":"2000","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.jprot.2014.02.030_bb0065","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1126\/science.6775372","article-title":"Polyamine metabolism: a potential therapeutic target in trypanosomes","volume":"210","author":"Bacchi","year":"1980","journal-title":"Science"},{"key":"10.1016\/j.jprot.2014.02.030_bb0070","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1016\/0035-9203(85)90195-6","article-title":"Treatment of gambiense sleeping sickness in the Sudan with oral DFMO (dl-alpha-difluoromethylornithine), an inhibitor of ornithine decarboxylase; first field trial","volume":"79","author":"Van Nieuwenhove","year":"1985","journal-title":"Trans R Soc Trop Med Hyg"},{"key":"10.1016\/j.jprot.2014.02.030_bb0075","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1111\/j.1550-7408.1986.tb05654.x","article-title":"Effects of dl-alpha-difluoromethylornithine on Leishmania donovani promastigotes","volume":"33","author":"Kaur","year":"1986","journal-title":"J Protozool"},{"key":"10.1016\/j.jprot.2014.02.030_bb0080","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/0024-3205(94)00916-3","article-title":"Fluorinated analogues of l-ornithine are powerful inhibitors of ornithine decarboxylase and cell growth of Leishmania infantum promastigotes","volume":"56","author":"Reguera","year":"1995","journal-title":"Life Sci"},{"key":"10.1016\/j.jprot.2014.02.030_bb0085","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1007\/s00726-007-0537-9","article-title":"Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis","volume":"33","author":"Heby","year":"2007","journal-title":"Amino Acids"},{"key":"10.1016\/j.jprot.2014.02.030_bb0090","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/0166-6851(90)90010-J","article-title":"Alpha-difluoromethylornithine resistance in Leishmania donovani is associated with increased ornithine decarboxylase activity","volume":"39","author":"Coons","year":"1990","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0095","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/0006-2952(93)90524-Z","article-title":"Resistance to dl-alpha-difluoromethylornithine by clinical isolates of Trypanosoma brucei rhodesiense. Role of S-adenosylmethionine","volume":"46","author":"Bacchi","year":"1993","journal-title":"Biochem Pharmacol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0100","doi-asserted-by":"crossref","first-page":"633","DOI":"10.2307\/3281131","article-title":"High efficiency plating method for Leishmania promastigotes in semidefined or completely-defined medium","volume":"69","author":"Iovannisci","year":"1983","journal-title":"J Parasitol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0105","first-page":"9","article-title":"The Bradford method for protein quantitation","volume":"32","author":"Kruger","year":"1994","journal-title":"Methods Mol Biol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0110","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1074\/mcp.M600398-MCP200","article-title":"Quantitative proteomics analysis of human endothelial cell membrane rafts evidence of MARCKS and MRP regulation in the sphingosine 1-phosphate-induced barrier enhancement","volume":"6","author":"Guo","year":"2007","journal-title":"Mol Cell Proteomics"},{"key":"10.1016\/j.jprot.2014.02.030_bb0115","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.molbiopara.2011.06.004","article-title":"Differential expression of proteins in antimony-susceptible and -resistant isolates of Leishmania donovani","volume":"179","author":"Biyani","year":"2011","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0120","doi-asserted-by":"crossref","first-page":"2350","DOI":"10.1016\/S0021-9258(18)45885-1","article-title":"Amplification and molecular cloning of the ornithine decarboxylase gene of Leishmania donovani","volume":"267","author":"Hanson","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jprot.2014.02.030_bb0125","first-page":"1","article-title":"Sulfur-containing amino acid metabolism in parasitic protozoa","volume":"vol. 60","author":"Nozaki","year":"2005"},{"key":"10.1016\/j.jprot.2014.02.030_bb0130","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0166-6851(01)00213-4","article-title":"Pteridine salvage throughout the Leishmania infectious cycle: implications for antifolate chemotherapy","volume":"113","author":"Cunningham","year":"2001","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0135","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":"Irigo\u00edn","year":"2008","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.jprot.2014.02.030_bb0140","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 Gen Subj"},{"key":"10.1016\/j.jprot.2014.02.030_bb0145","doi-asserted-by":"crossref","first-page":"2590","DOI":"10.1093\/emboj\/16.10.2590","article-title":"Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages","volume":"16","author":"Dumas","year":"1997","journal-title":"EMBO J"},{"key":"10.1016\/j.jprot.2014.02.030_bb0150","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.jprot.2014.02.030_bb0155","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1186\/1756-3305-5-160","article-title":"Proteinases as virulence factors in Leishmania spp. infection in mammals","volume":"5","author":"Silva-Almeida","year":"2012","journal-title":"Parasit Vectors"},{"key":"10.1016\/j.jprot.2014.02.030_bb0160","doi-asserted-by":"crossref","first-page":"e1001148","DOI":"10.1371\/journal.ppat.1001148","article-title":"Leishmania-induced inactivation of the macrophage transcription factor AP-1 is mediated by the parasite metalloprotease GP63","volume":"6","author":"Contreras","year":"2010","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.jprot.2014.02.030_bb0165","first-page":"99","article-title":"Heat shock proteins: role in thermotolerance, drug resistance, and relationship to DNA topoisomerases","author":"Li","year":"1987","journal-title":"NCI Monogr"},{"issue":"16","key":"10.1016\/j.jprot.2014.02.030_bb0170","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1093\/carcin\/bgt111","article-title":"The HSP70 family and cancer","volume":"34","author":"Murphy","year":"2013","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.jprot.2014.02.030_bb0175","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/j.ijpara.2007.10.001","article-title":"Functional analysis of Leishmania major cyclophilin","volume":"38","author":"Yurchenko","year":"2008","journal-title":"Int J Parasitol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0180","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1128\/CMR.18.2.293-305.2005","article-title":"Subversion mechanisms by which Leishmania parasites can escape the host immune response: a signaling point of view","volume":"18","author":"Olivier","year":"2005","journal-title":"Clin Microbiol Rev"},{"key":"10.1016\/j.jprot.2014.02.030_bb0185","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1111\/j.1600-0854.2004.00229.x","article-title":"LdARF1 in trafficking and structural maintenance of the trans-Golgi cisternal network in the protozoan pathogen Leishmania donovani","volume":"5","author":"Porter-Kelley","year":"2004","journal-title":"Traffic"},{"key":"10.1016\/j.jprot.2014.02.030_bb0190","first-page":"281","article-title":"Role of 14-3-3 proteins in eukaryotic signaling and development","volume":"vol. 68","author":"Darling","year":"2005"},{"key":"10.1016\/j.jprot.2014.02.030_bb0195","doi-asserted-by":"crossref","first-page":"11539","DOI":"10.1073\/pnas.92.25.11539","article-title":"14-3-3 proteins: potential roles in vesicular transport and Ras signaling in Saccharomyces cerevisiae","volume":"92","author":"Gelperin","year":"1995","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jprot.2014.02.030_bb0200","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1016\/j.ijpara.2006.06.013","article-title":"Inhibitors of casein kinase 1 block the growth of Leishmania major promastigotes in vitro","volume":"36","author":"Allocco","year":"2006","journal-title":"Int J Parasitol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0205","first-page":"103","article-title":"Nucleoside monophosphate kinases: structure, mechanism, and substrate specificity","volume":"73","author":"Yan","year":"1999","journal-title":"Adv Enzymol Relat Areas Mol Biol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0210","doi-asserted-by":"crossref","first-page":"4339","DOI":"10.1046\/j.1432-1033.2003.03826.x","article-title":"Molecular and functional characterization of adenylate kinase 2 gene from Leishmania donovani","volume":"270","author":"Villa","year":"2003","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.jprot.2014.02.030_bb0215","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1007\/s00018-010-0612-3","article-title":"Adenine nucleotide transporters in organelles: novel genes and functions","volume":"68","author":"Traba","year":"2011","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.jprot.2014.02.030_bb0220","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/j.cub.2005.02.068","article-title":"A novel ADP\/ATP transporter in the mitosome of the microaerophilic human parasite Entamoeba histolytica","volume":"15","author":"Chan","year":"2005","journal-title":"Curr Biol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0225","doi-asserted-by":"crossref","first-page":"1978","DOI":"10.1016\/j.bbamem.2008.04.011","article-title":"The ADP and ATP transport in mitochondria and its carrier","volume":"1778","author":"Klingenberg","year":"2008","journal-title":"Biochim Biophys Acta Biomembr"},{"key":"10.1016\/j.jprot.2014.02.030_bb0230","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1021\/pr0501158","article-title":"Proteomic evidence for roles for nucleolin and poly[ADP-ribosyl] transferase in drug resistance","volume":"4","author":"Fu","year":"2005","journal-title":"J Proteome Res"},{"key":"10.1016\/j.jprot.2014.02.030_bb0235","doi-asserted-by":"crossref","first-page":"2251","DOI":"10.1016\/j.biocel.2009.04.021","article-title":"Identification of proteins whose synthesis is preferentially enhanced by polyamines at the level of translation in mammalian cells","volume":"41","author":"Nishimura","year":"2009","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1016\/j.jprot.2014.02.030_bb0240","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1042\/BST20060330","article-title":"S-adenosylmethionine: jack of all trades and master of everything?","volume":"34","author":"Loenen","year":"2006","journal-title":"Biochem Soc Trans"}],"container-title":["Journal of Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391914001031?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391914001031?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,3,29]],"date-time":"2022-03-29T20:21:06Z","timestamp":1648585266000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874391914001031"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,5]]},"references-count":48,"alternative-id":["S1874391914001031"],"URL":"https:\/\/doi.org\/10.1016\/j.jprot.2014.02.030","relation":{},"ISSN":["1874-3919"],"issn-type":[{"value":"1874-3919","type":"print"}],"subject":[],"published":{"date-parts":[[2014,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"A quantitative proteomic screen to identify potential drug resistance mechanism in \u03b1-difluoromethylornithine (DFMO) resistant Leishmania donovani","name":"articletitle","label":"Article Title"},{"value":"Journal of Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jprot.2014.02.030","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier B.V. Published by Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}