{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T10:52:07Z","timestamp":1782730327046,"version":"3.54.5"},"reference-count":67,"publisher":"Elsevier BV","issue":"13","license":[{"start":{"date-parts":[[2013,3,1]],"date-time":"2013-03-01T00:00:00Z","timestamp":1362096000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,30]],"date-time":"2020-09-30T00:00:00Z","timestamp":1601424000000},"content-version":"vor","delay-in-days":2770,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,3]]},"DOI":"10.1074\/jbc.m112.431486","type":"journal-article","created":{"date-parts":[[2013,2,13]],"date-time":"2013-02-13T04:56:45Z","timestamp":1360731405000},"page":"8977-8990","source":"Crossref","is-referenced-by-count":33,"title":["Adenylosuccinate Synthetase and Adenylosuccinate Lyase Deficiencies Trigger Growth and Infectivity Deficits in Leishmania donovani"],"prefix":"10.1016","volume":"288","author":[{"given":"Jan M.","family":"Boitz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rona","family":"Strasser","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phillip A.","family":"Yates","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Armando","family":"Jardim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Buddy","family":"Ullman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M112.431486_bib1","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.pt.2003.09.008","article-title":"Leishmaniasis: current chemotherapy and recent advances in the search for novel drugs","volume":"19","author":"Croft","year":"2003","journal-title":"Trends Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib2","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/978-1-4684-8559-2_10","article-title":"Purine salvage enzymes in man and Leishmania donovani","volume":"122B","author":"Krenitsky","year":"1979","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1074\/jbc.M112.431486_bib3","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":"10.1074\/jbc.M112.431486_bib4","doi-asserted-by":"crossref","first-page":"319","DOI":"10.2174\/1381612023396258","article-title":"Chemotherapy of leishmaniasis","volume":"8","author":"Croft","year":"2002","journal-title":"Curr. Pharm. Des."},{"key":"10.1074\/jbc.M112.431486_bib5","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/0304-4165(78)90104-6","article-title":"Purine metabolism in Leishmania donovaniLeishmania braziliensis","volume":"544","author":"Marr","year":"1978","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.M112.431486_bib6","first-page":"89","article-title":"purine and pyrimidine metabolism","author":"Berens","year":"1995"},{"key":"10.1074\/jbc.M112.431486_bib7","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/0166-6851(83)90053-1","article-title":"Purine metabolism in Leishmania donovani amastigotes and promastigotes","volume":"9","author":"Looker","year":"1983","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib8","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/0006-2952(82)90216-7","article-title":"Purine and pyrimidine salvage pathways in Leishmania donovani","volume":"31","author":"LaFon","year":"1982","journal-title":"Biochem. Pharmacol."},{"key":"10.1074\/jbc.M112.431486_bib9","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/S0021-9258(19)86119-7","article-title":"Purine phosphoribosyltransferases from Leishmania donovani","volume":"255","author":"Tuttle","year":"1980","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib10","doi-asserted-by":"crossref","first-page":"5515","DOI":"10.1016\/S0021-9258(18)45602-5","article-title":"Isolation and characterization of adenosine kinase from Leishmania donovani","volume":"262","author":"Datta","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib11","doi-asserted-by":"crossref","first-page":"1534","DOI":"10.1074\/jbc.273.3.1534","article-title":"Localization and targeting of the Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase to the glycosome","volume":"273","author":"Shih","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib12","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.molbiopara.2003.08.016","article-title":"Subcellular localization of adenine and xanthine phosphoribosyltransferases in Leishmania donovani","volume":"134","author":"Zarella-Boitz","year":"2004","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib13","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/S0166-6851(01)00261-4","article-title":"Biogenesis and function of peroxisomes and glycosomes","volume":"115","author":"Parsons","year":"2001","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib14","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/S0169-4758(00)01810-X","article-title":"Metabolic aspects of glycosomes in trypanosomatidae: new data and views","volume":"16","author":"Michels","year":"2000","journal-title":"Parasitol. Today"},{"key":"10.1074\/jbc.M112.431486_bib15","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1111\/j.1365-2958.2004.04203.x","article-title":"Glycosomes: parasites and the divergence of peroxisomal purpose","volume":"53","author":"Parsons","year":"2004","journal-title":"Mol. Microbiol."},{"key":"10.1074\/jbc.M112.431486_bib16","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.molbiopara.2006.02.015","article-title":"Leishmania donovani singly deficient in HGPRT, APRT, or XPRT are viable in vitro and within mammalian macrophages","volume":"148","author":"Boitz","year":"2006","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib17","doi-asserted-by":"crossref","first-page":"30840","DOI":"10.1074\/jbc.271.48.30840","article-title":"Creation of homozygous mutants of Leishmania donovani with single targeting constructs","volume":"271","author":"Hwang","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib18","doi-asserted-by":"crossref","first-page":"19488","DOI":"10.1074\/jbc.272.31.19488","article-title":"Genetic analysis of purine metabolism in Leishmania donovani","volume":"272","author":"Hwang","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib19","doi-asserted-by":"crossref","first-page":"14617","DOI":"10.1016\/S0021-9258(17)42646-9","article-title":"Genetic analysis of adenine metabolism in Leishmania donovani promastigotes. Evidence for diploidy at the adenine phosphoribosyltransferase locus","volume":"259","author":"Iovannisci","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib20","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0166-6851(84)90131-2","article-title":"Characterization of a mutant Leishmania donovani deficient in adenosine kinase activity","volume":"12","author":"Iovannisci","year":"1984","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib21","doi-asserted-by":"crossref","first-page":"16084","DOI":"10.1074\/jbc.M600188200","article-title":"A conditional mutant deficient in hypoxanthine-guanine phosphoribosyltransferase and xanthine phosphoribosyltransferase validates the purine salvage pathway of Leishmania donovani","volume":"281","author":"Boitz","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib22","doi-asserted-by":"crossref","first-page":"3891","DOI":"10.1016\/0006-2952(82)90307-0","article-title":"Guanosine 5\u2032-monophosphate reductase from Leishmania donovani. A possible chemotherapeutic target","volume":"31","author":"Spector","year":"1982","journal-title":"Biochem. Pharmacol."},{"key":"10.1074\/jbc.M112.431486_bib23","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0006-2952(82)90203-9","article-title":"Antileishmanial action of 4-thiopyrazolo (3.4-d) pyrimidine and its ribonucleoside. Biological effects and metabolism","volume":"31","author":"Marr","year":"1982","journal-title":"Biochem. Pharmacol."},{"key":"10.1074\/jbc.M112.431486_bib24","doi-asserted-by":"crossref","first-page":"8422","DOI":"10.1016\/S0021-9258(19)86908-9","article-title":"Specificity of adenylosuccinate synthetase and adenylosuccinate lyase from Leishmania donovani. Selective amination of an antiprotozoal agent","volume":"254","author":"Spector","year":"1979","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib25","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1016\/0006-2952(84)90282-X","article-title":"Monophosphates of formycin B and allopurinol riboside. Interactions with leishmanial and mammalian succino-AMP synthetase and GMP reductase","volume":"33","author":"Spector","year":"1984","journal-title":"Biochem. Pharmacol."},{"key":"10.1074\/jbc.M112.431486_bib26","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1007\/BF00269424","article-title":"Location on the chromosome of Escherichia coli of genes governing purine metabolism. Adenosine deaminase (add), guanosine kinase (gsk), and hypoxanthine phosphoribosyltransferase (hpt)","volume":"143","author":"Jochimsen","year":"1975","journal-title":"Mol. Gen. Genet."},{"key":"10.1074\/jbc.M112.431486_bib27","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.molbiopara.2006.11.007","article-title":"Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani","volume":"152","author":"Dobie","year":"2007","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib28","doi-asserted-by":"crossref","first-page":"7170","DOI":"10.1073\/pnas.88.16.7170","article-title":"Double targeted gene replacement for creating null mutants","volume":"88","author":"Cruz","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.431486_bib29","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0166-6851(00)00210-3","article-title":"Blasticidin resistance: a new independent marker for stable transfection of Leishmania","volume":"108","author":"Goyard","year":"2000","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib30","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/373663b0","article-title":"Improved green fluorescence","volume":"373","author":"Heim","year":"1995","journal-title":"Nature"},{"key":"10.1074\/jbc.M112.431486_bib31","doi-asserted-by":"crossref","first-page":"847","DOI":"10.2307\/3278338","article-title":"A monophasic medium for cultivating Leishmania donovani in large numbers","volume":"58","author":"Dwyer","year":"1972","journal-title":"J. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib32","doi-asserted-by":"crossref","first-page":"704","DOI":"10.4269\/ajtmh.1975.24.704","article-title":"Comparison of two geographic strains of Leishmania donovani by resistance of mice to superinfection","volume":"24","author":"Holbrook","year":"1975","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"10.1074\/jbc.M112.431486_bib33","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/j.ijpara.2003.10.011","article-title":"Generation of Leishmania donovani axenic amastigotes: their growth and biological characteristics","volume":"34","author":"Debrabant","year":"2004","journal-title":"Int. J. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib34","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0166-6851(03)00142-7","article-title":"An in vitro system for developmental and genetic studies of Leishmania donovani phosphoglycans","volume":"130","author":"Goyard","year":"2003","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib35","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":"10.1074\/jbc.M112.431486_bib36","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1007\/978-1-4684-4553-4_46","article-title":"Single cell cloning of Leishmania parasites in purine-defined medium: isolation of drug-resistant variants","volume":"165","author":"Iovannisci","year":"1984","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1074\/jbc.M112.431486_bib37","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1093\/nar\/20.5.1083","article-title":"Stable propagation of cosmid sized human DNA inserts in an F factor-based vector","volume":"20","author":"Kim","year":"1992","journal-title":"Nucleic Acids Res."},{"key":"10.1074\/jbc.M112.431486_bib38","doi-asserted-by":"crossref","first-page":"D457","DOI":"10.1093\/nar\/gkp851","article-title":"TriTrypDB: a functional genomic resource for the Trypanosomatidae","volume":"38","author":"Aslett","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"10.1074\/jbc.M112.431486_bib39","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1101\/SQB.1986.051.01.032","article-title":"Specific enzymatic amplification of DNA in vitro: the polymerase chain reaction","volume":"51","author":"Mullis","year":"1986","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"10.1074\/jbc.M112.431486_bib40","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1126\/science.2999980","article-title":"Enzymatic amplification of \u03b2-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia","volume":"230","author":"Saiki","year":"1985","journal-title":"Science"},{"key":"10.1074\/jbc.M112.431486_bib41","doi-asserted-by":"crossref","first-page":"7341","DOI":"10.1093\/nar\/14.18.7341","article-title":"Cloning and characterization of a Leishmania gene encoding a RNA-spliced leader sequence","volume":"14","author":"Miller","year":"1986","journal-title":"Nucleic Acids Res."},{"key":"10.1074\/jbc.M112.431486_bib42","doi-asserted-by":"crossref","first-page":"7626","DOI":"10.1074\/jbc.M111.307884","article-title":"Adenine aminohydrolase from Leishmania donovani: unique enzyme in parasite purine metabolism","volume":"287","author":"Boitz","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib43","series-title":"Molecular Cloning: A Laboratory Manual","first-page":"7.35","author":"Sambrook","year":"2001"},{"key":"10.1074\/jbc.M112.431486_bib44","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1021\/jm00247a002","article-title":"Enzyme inhibitors. 26. Bridging hydrophobic and hydrophilic regions on adenosine deaminase with some 9-(2-hydroxy-3-alkyl)adenines","volume":"17","author":"Schaeffer","year":"1974","journal-title":"J. Med. Chem."},{"key":"10.1074\/jbc.M112.431486_bib45","doi-asserted-by":"crossref","first-page":"3211","DOI":"10.1016\/S0021-9258(19)81097-9","article-title":"Immunoreactive protein in adenosine deaminase-deficient human lymphoblast cell lines","volume":"257","author":"Wiginton","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib46","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/0003-9861(77)90412-X","article-title":"Adenine deaminase of a eukaryotic animal cell, Crithidia fasciculata","volume":"183","author":"Kidder","year":"1977","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1074\/jbc.M112.431486_bib47","doi-asserted-by":"crossref","first-page":"3605","DOI":"10.1046\/j.1432-1327.2001.02271.x","article-title":"Poly(A) polymerase from Escherichia coli adenylylates the 3\u2032-hydroxyl residue of nucleosides, nucleoside 5\u2032-phosphates, and nucleoside(5\u2032)oligophospho(5\u2032)nucleosides (NpnN)","volume":"268","author":"Sillero","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1074\/jbc.M112.431486_bib48","doi-asserted-by":"crossref","first-page":"18555","DOI":"10.1074\/jbc.M110.125393","article-title":"Amplification of adenine phosphoribosyltransferase suppresses the conditionally lethal growth and virulence phenotype of Leishmania donovani mutants lacking both hypoxanthine-guanine and xanthine phosphoribosyltransferases","volume":"285","author":"Boitz","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib49","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":"10.1074\/jbc.M112.431486_bib50","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1128\/AAC.39.9.2167","article-title":"Culture microtitration: a sensitive method for quantifying Leishmania infantum in tissues of infected mice","volume":"39","author":"Buffet","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.M112.431486_bib51","doi-asserted-by":"crossref","first-page":"2500","DOI":"10.1073\/pnas.88.6.2500","article-title":"High level expression in Escherichia coli of soluble, enzymatically active schistosomal hypoxanthine\/guanine phosphoribosyltransferase and trypanosomal ornithine decarboxylase","volume":"88","author":"Craig","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.431486_bib52","doi-asserted-by":"crossref","first-page":"19147","DOI":"10.1016\/S0021-9258(18)37402-7","article-title":"Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12","volume":"263","author":"Wolfe","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib53","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1006\/prep.2001.1610","article-title":"Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli","volume":"25","author":"Jayalakshmi","year":"2002","journal-title":"Protein Expr. Purif."},{"key":"10.1074\/jbc.M112.431486_bib54","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.molbiopara.2006.06.001","article-title":"Adenosine kinase from Cryptosporidium parvum","volume":"149","author":"Galazka","year":"2006","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib55","doi-asserted-by":"crossref","first-page":"13637","DOI":"10.1016\/S0021-9258(18)67068-1","article-title":"Metabolism of threo-\u03b2-fluoroaspartate by H4 cells. Inhibition of adenylosuccinate lyase by fluoro analogs of its substrates","volume":"261","author":"Casey","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.431486_bib56","first-page":"333","article-title":"The kinetics of invertase activity","volume":"49","author":"Michealis","year":"1913","journal-title":"Biochem. Z."},{"key":"10.1074\/jbc.M112.431486_bib57","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0166-6851(02)00164-0","article-title":"Peroxisomal targeting protein 14 (PEX14) from Leishmania donovani. Molecular, biochemical, and immunocytochemical characterization","volume":"124","author":"Jardim","year":"2002","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib58","first-page":"197","article-title":"Purine and pyrimidine transport and metabolism","author":"Carter","year":"2003"},{"key":"10.1074\/jbc.M112.431486_bib59","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1016\/j.jmb.2003.11.036","article-title":"Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum","volume":"335","author":"Eaazhisai","year":"2004","journal-title":"J. Mol. Biol."},{"key":"10.1074\/jbc.M112.431486_bib60","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1006\/jmbi.1996.0693","article-title":"Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3\u2212, and Mg2+","volume":"264","author":"Poland","year":"1996","journal-title":"J. Mol. Biol."},{"key":"10.1074\/jbc.M112.431486_bib61","doi-asserted-by":"crossref","first-page":"3670","DOI":"10.1073\/pnas.76.8.3670","article-title":"Adenine aminohydrolase: occurrence and possible significance in trypanosomid flagellates","volume":"76","author":"Kidder","year":"1979","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.431486_bib62","doi-asserted-by":"crossref","first-page":"2722","DOI":"10.1128\/AAC.42.10.2722","article-title":"Visceral leishmaniasis in the BALB\/c mouse: a comparison of the efficacy of a nonionic surfactant formulation of sodium stibogluconate with those of three proprietary formulations of amphotericin B","volume":"42","author":"Mullen","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1074\/jbc.M112.431486_bib63","first-page":"439","article-title":"Animal models for vaccine studies for visceral leishmaniasis","volume":"123","author":"Garg","year":"2006","journal-title":"Indian J. Med. Res."},{"key":"10.1074\/jbc.M112.431486_bib64","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/j.micpath.2004.11.002","article-title":"Immunopathogenesis of infection with the visceralizing Leishmania species","volume":"38","author":"Wilson","year":"2005","journal-title":"Microb. Pathog."},{"key":"10.1074\/jbc.M112.431486_bib65","doi-asserted-by":"crossref","first-page":"3643","DOI":"10.1093\/emboj\/18.13.3643","article-title":"Glycosylphosphatidylinositol biosynthetic enzymes are localized to a stable tubular subcompartment of the endoplasmic reticulum in Leishmania mexicana","volume":"18","author":"Ilgoutz","year":"1999","journal-title":"EMBO J."},{"key":"10.1074\/jbc.M112.431486_bib66","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.molbiopara.2007.11.013","article-title":"Interaction of Leishmania PTS2 receptor peroxin 7 with the glycosomal protein import machinery","volume":"158","author":"Pilar","year":"2008","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1074\/jbc.M112.431486_bib67","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.molbiopara.2006.02.010","article-title":"In silico prediction of the glycosomal enzymes of Leishmania major and trypanosomes","volume":"147","author":"Opperdoes","year":"2006","journal-title":"Mol. Biochem. Parasitol."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925819350586?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925819350586?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M112.431486","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,6,24]],"date-time":"2021-06-24T23:16:24Z","timestamp":1624576584000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925819350586"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,3]]},"references-count":67,"journal-issue":{"issue":"13","published-print":{"date-parts":[[2013,3]]}},"alternative-id":["S0021925819350586"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m112.431486","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,3]]}}}