{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T16:24:03Z","timestamp":1777566243163,"version":"3.51.4"},"reference-count":35,"publisher":"Elsevier BV","issue":"22","license":[{"start":{"date-parts":[[2016,5,1]],"date-time":"2016-05-01T00:00:00Z","timestamp":1462060800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,31]],"date-time":"2020-08-31T00:00:00Z","timestamp":1598832000000},"content-version":"vor","delay-in-days":1583,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Vetenskapsr\u00e5det","doi-asserted-by":"publisher","award":["2012-1932"],"award-info":[{"award-number":["2012-1932"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007067","name":"Kempestiftelserna","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007067","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004441","name":"Styrelsen f\u00f6r Internationellt Utvecklingssamarbete","doi-asserted-by":"publisher","award":["2008-069"],"award-info":[{"award-number":["2008-069"]}],"id":[{"id":"10.13039\/100004441","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2016,5]]},"DOI":"10.1074\/jbc.m116.715615","type":"journal-article","created":{"date-parts":[[2016,4,2]],"date-time":"2016-04-02T00:07:40Z","timestamp":1459555660000},"page":"11717-11726","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"title":["Trypanosoma brucei Methylthioadenosine Phosphorylase Protects the Parasite from the Antitrypanosomal Effect of Deoxyadenosine"],"prefix":"10.1016","volume":"291","author":[{"given":"Munender","family":"Vodnala","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Farahnaz","family":"Ranjbarian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anna","family":"Pavlova","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Harry P.","family":"de Koning","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anders","family":"Hofer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M116.715615_bib1","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1111\/j.1469-0691.2011.03536.x","article-title":"Sleeping sickness","volume":"17","author":"Malvy","year":"2011","journal-title":"Clin. Microbiol. Infect"},{"issue":"suppl.","key":"10.1074\/jbc.M116.715615_bib2","doi-asserted-by":"crossref","first-page":"S11","DOI":"10.1016\/j.jip.2012.07.014","article-title":"Tsetse-transmitted trypanosomes\u2014their biology, disease impact and control","volume":"112","author":"Holmes","year":"2013","journal-title":"J. Invertebr. Pathol"},{"key":"10.1074\/jbc.M116.715615_bib3","doi-asserted-by":"crossref","first-page":"948","DOI":"10.2174\/156802611795347582","article-title":"Molecular biology of nucleoside transporters and their distributions and functions in the brain","volume":"11","author":"Parkinson","year":"2011","journal-title":"Curr. Top. Med. Chem"},{"key":"10.1074\/jbc.M116.715615_bib4","doi-asserted-by":"crossref","first-page":"17628","DOI":"10.1074\/jbc.M112.340059","article-title":"Trypanosoma brucei thymidine kinase is tandem protein consisting of two homologous parts, which together enable efficient substrate binding","volume":"287","author":"Ranjbarian","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715615_bib5","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/0305-0491(72)90138-1","article-title":"Comparative properties of trypanosomal and mammalian thymidine kinases","volume":"43","author":"Chello","year":"1972","journal-title":"Comp. Biochem. Physiol. B"},{"key":"10.1074\/jbc.M116.715615_bib6","doi-asserted-by":"crossref","first-page":"5380","DOI":"10.1074\/jbc.M705603200","article-title":"Adenosine kinase mediates high affinity adenosine salvage in Trypanosoma brucei","volume":"283","author":"Vodnala","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715615_bib7","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0163-7258(03)00071-8","article-title":"Potential chemotherapeutic targets in the purine metabolism of parasites","volume":"99","author":"el Kouni","year":"2003","journal-title":"Pharmacol. Ther"},{"key":"10.1074\/jbc.M116.715615_bib8","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/0003-2697(82)90376-1","article-title":"The determination of purine levels in human and mouse plasma","volume":"125","author":"Slowiaczek","year":"1982","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M116.715615_bib9","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1124\/mol.56.6.1162","article-title":"Adenosine transporters in bloodstream forms of Trypanosoma brucei brucei: substrate recognition motifs and affinity for trypanocidal drugs","volume":"56","author":"de Koning","year":"1999","journal-title":"Mol. Pharmacol"},{"key":"10.1074\/jbc.M116.715615_bib10","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/j.femsre.2005.03.004","article-title":"Purine and pyrimidine transport in pathogenic protozoa: from biology to therapy","volume":"29","author":"de Koning","year":"2005","journal-title":"FEMS Microbiol. Rev"},{"key":"10.1074\/jbc.M116.715615_bib11","doi-asserted-by":"crossref","first-page":"2118","DOI":"10.1074\/jbc.273.4.2118","article-title":"Molecular cloning and expression of a purine-specific N-ribohydrolase from Trypanosoma brucei brucei. Sequence, expression, and molecular analysis","volume":"273","author":"Pell\u00e9","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715615_bib12","doi-asserted-by":"crossref","first-page":"34098","DOI":"10.1074\/jbc.273.51.34098","article-title":"Allosteric regulation of Trypanosoma brucei ribonucleotide reductase studied in vitro and in vivo","volume":"273","author":"Hofer","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715615_bib13","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1124\/mol.104.010298","article-title":"Molecular pharmacology of adenosine transport in Trypanosoma brucei: P1\/P2 revisited","volume":"68","author":"Geiser","year":"2005","journal-title":"Mol. Pharmacol"},{"key":"10.1074\/jbc.M116.715615_bib14","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1086\/496896","article-title":"Treatment of African trypanosomiasis with cordycepin and adenosine deaminase inhibitors in a mouse model","volume":"192","author":"Rottenberg","year":"2005","journal-title":"J. Infect. Dis"},{"key":"10.1074\/jbc.M116.715615_bib15","doi-asserted-by":"crossref","first-page":"9861","DOI":"10.1021\/jm401530a","article-title":"Structure-activity relationships of synthetic cordycepin analogues as experimental therapeutics for African trypanosomiasis","volume":"56","author":"Vodnala","year":"2013","journal-title":"J. Med. Chem"},{"key":"10.1074\/jbc.M116.715615_bib16","doi-asserted-by":"crossref","first-page":"985","DOI":"10.2307\/3282883","article-title":"Continuous cultivation of Trypanosoma brucei blood stream forms in a medium containing a low concentration of serum protein without feeder cell layers","volume":"75","author":"Hirumi","year":"1989","journal-title":"J. Parasitol"},{"key":"10.1074\/jbc.M116.715615_bib17","first-page":"289","article-title":"Cultivation and in vitro cloning or procyclic culture forms of Trypanosoma brucei in a semi-defined medium. Short communication","volume":"36","author":"Brun","year":"1979","journal-title":"Acta Trop"},{"key":"10.1074\/jbc.M116.715615_bib18","doi-asserted-by":"crossref","first-page":"7834","DOI":"10.1074\/jbc.M512894200","article-title":"Regulation of mammalian ribonucleotide reduction and dNTP pools after DNA damage and in resting cells","volume":"281","author":"H\u00e5kansson","year":"2006","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715615_bib19","doi-asserted-by":"crossref","first-page":"40174","DOI":"10.1074\/jbc.M008405200","article-title":"Inhibition of Trypanosoma brucei gene expression by RNA interference using an integratable vector with opposing T7 promoters","volume":"275","author":"Wang","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715615_bib20","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0166-6851(99)00002-X","article-title":"A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei","volume":"99","author":"Wirtz","year":"1999","journal-title":"Mol. Biochem. Parasitol"},{"key":"10.1074\/jbc.M116.715615_bib21","doi-asserted-by":"crossref","first-page":"50","DOI":"10.3109\/10409238.2011.630372","article-title":"DNA building blocks: keeping control of manufacture","volume":"47","author":"Hofer","year":"2012","journal-title":"Crit. Rev. Biochem. Mol. Biol"},{"key":"10.1074\/jbc.M116.715615_bib22","doi-asserted-by":"crossref","first-page":"6959","DOI":"10.1073\/pnas.94.13.6959","article-title":"Cloning and characterization of the R1 and R2 subunits of ribonucleotide reductase from Trypanosoma brucei","volume":"94","author":"Hofer","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.715615_bib23","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.1093\/nar\/gkq829","article-title":"Mechanisms of mutagenesis in vivo due to imbalanced dNTP pools","volume":"39","author":"Kumar","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.M116.715615_bib24","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1124\/mol.106.031559","article-title":"Molecular interactions underlying the unusually high adenosine affinity of a novel Trypanosoma brucei nucleoside transporter","volume":"71","author":"Al-Salabi","year":"2007","journal-title":"Mol. Pharmacol"},{"key":"10.1074\/jbc.M116.715615_bib25","doi-asserted-by":"crossref","first-page":"9486","DOI":"10.1074\/jbc.273.16.9486","article-title":"Characterization of a nucleoside\/proton symporter in procyclic Trypanosoma brucei brucei","volume":"273","author":"de Koning","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.715615_bib26","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.ijpddr.2013.12.001","article-title":"Trypanosoma brucei adenine-phosphoribosyltransferases mediate adenine salvage and aminopurinol susceptibility but not adenine toxicity","volume":"4","author":"L\u00fcscher","year":"2014","journal-title":"Int. J. Parasitol. Drugs Drug Resist"},{"key":"10.1074\/jbc.M116.715615_bib27","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/0166-6851(88)90030-8","article-title":"Substrate specificities of 5\u2032-deoxy-5\u2032-methylthioadenosine phosphorylase from Trypanosoma brucei brucei and mammalian cells","volume":"27","author":"Ghoda","year":"1988","journal-title":"Mol. Biochem. Parasitol"},{"key":"10.1074\/jbc.M116.715615_bib28","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0065-2776(04)86001-2","article-title":"Adenosine deaminase deficiency: metabolic basis of immune deficiency and pulmonary inflammation","volume":"86","author":"Blackburn","year":"2005","journal-title":"Adv. Immunol"},{"key":"10.1074\/jbc.M116.715615_bib29","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1017\/S0031182000052574","article-title":"The enzymes of purine salvage in Trypanosoma cruzi, Trypanosoma brucei and Leishmania mexicana","volume":"87","author":"Davies","year":"1983","journal-title":"Parasitology"},{"key":"10.1074\/jbc.M116.715615_bib30","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1080\/00034983.1985.11811883","article-title":"Adenosine cycle in African trypanosomes","volume":"79","author":"Ogbunude","year":"1985","journal-title":"Ann. Trop. Med. Parasitol"},{"key":"10.1074\/jbc.M116.715615_bib31","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1128\/AAC.01787-09","article-title":"Evaluation of nucleoside hydrolase inhibitors for treatment of African trypanosomiasis","volume":"54","author":"Berg","year":"2010","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.M116.715615_bib32","doi-asserted-by":"crossref","first-page":"2352","DOI":"10.1128\/AAC.01551-10","article-title":"Trypanocidal furamidine analogues: influence of pyridine nitrogens on trypanocidal activity, transport kinetics, and resistance patterns","volume":"55","author":"Ward","year":"2011","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.M116.715615_bib33","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/S0166-6851(99)00203-0","article-title":"Differential regulation of nucleoside and nucleobase transporters in Crithidia fasciculata and Trypanosoma brucei brucei","volume":"106","author":"de Koning","year":"2000","journal-title":"Mol. Biochem. Parasitol"},{"key":"10.1074\/jbc.M116.715615_bib34","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1017\/S003118201000123X","article-title":"Activity of the enzyme adenosine deaminase in serum, erythrocytes and lymphocytes of rats infected with Trypanosoma evansi","volume":"138","author":"da Silva","year":"2011","journal-title":"Parasitology"},{"key":"10.1074\/jbc.M116.715615_bib35","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.exppara.2010.07.010","article-title":"Trypanosoma evansi: adenosine deaminase activity in the brain of infected rats","volume":"127","author":"Da Silva","year":"2011","journal-title":"Exp. Parasitol"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820432028?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820432028?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M116.715615","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T12:33:09Z","timestamp":1641299589000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820432028"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,5]]},"references-count":35,"journal-issue":{"issue":"22","published-print":{"date-parts":[[2016,5]]}},"alternative-id":["S0021925820432028"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m116.715615","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2016,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Trypanosoma brucei Methylthioadenosine Phosphorylase Protects the Parasite from the Antitrypanosomal Effect of Deoxyadenosine","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M116.715615","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}