{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T02:38:04Z","timestamp":1740105484659,"version":"3.37.3"},"reference-count":37,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,7,1]],"date-time":"2019-07-01T00:00:00Z","timestamp":1561939200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001412","name":"Council of Scientific and Industrial Research, India","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001412","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001501","name":"UGC","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001501","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Protein Expression and Purification"],"published-print":{"date-parts":[[2019,7]]},"DOI":"10.1016\/j.pep.2019.02.018","type":"journal-article","created":{"date-parts":[[2019,3,1]],"date-time":"2019-03-01T17:45:00Z","timestamp":1551462300000},"page":"1-9","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"C","title":["Molecular characterization of recombinant arginase of Leishmania donovani"],"prefix":"10.1016","volume":"159","author":[{"given":"Neha","family":"Gaur","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kishore","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chhedi Lal","family":"Gupta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jitendra Kumar","family":"Saxena","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"4","key":"10.1016\/j.pep.2019.02.018_bib1","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/S1473-3099(10)70320-0","article-title":"Visceral leishmaniasis: elimination with existing interventions","volume":"11","author":"Matlashewski","year":"2011","journal-title":"Lancet Infect. Dis."},{"issue":"3","key":"10.1016\/j.pep.2019.02.018_bib2","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1517\/14728210903153862","article-title":"Developments in the treatment of visceral leishmaniasis","volume":"14","author":"den Boer","year":"2009","journal-title":"Expert Opin. Emerg. Drugs"},{"issue":"9185","key":"10.1016\/j.pep.2019.02.018_bib3","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1016\/S0140-6736(98)10178-2","article-title":"Leishmaniasis","volume":"354","author":"Herwaldt","year":"1999","journal-title":"Lancet"},{"issue":"3","key":"10.1016\/j.pep.2019.02.018_bib4","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/S1201-9712(00)90078-X","article-title":"Treatment of visceral leishmaniasis (kala-azar): a decade of progress and future approaches","volume":"4","author":"Murray","year":"2000","journal-title":"Int. J. Infect. Dis."},{"issue":"2","key":"10.1016\/j.pep.2019.02.018_bib5","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1128\/CMR.14.2.229-243.2001","article-title":"Leishmaniasis: current status of vaccine development","volume":"14","author":"Handman","year":"2001","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.pep.2019.02.018_bib6","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1146\/annurev.bi.53.070184.003533","article-title":"Polyamines","volume":"53","author":"Tabor","year":"1984","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.pep.2019.02.018_bib7","series-title":"Polyamines in Biology and Medicine","first-page":"3","author":"Pegg","year":"1981"},{"key":"10.1016\/j.pep.2019.02.018_bib8","doi-asserted-by":"crossref","first-page":"15174","DOI":"10.1021\/bi9915115","article-title":"X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine","volume":"38","author":"Grishin","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.pep.2019.02.018_bib9","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.pep.2019.02.018_bib10","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.pep.2019.02.018_bib11","doi-asserted-by":"crossref","first-page":"109","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.pep.2019.02.018_bib12","doi-asserted-by":"crossref","first-page":"23668","DOI":"10.1074\/jbc.M402042200","article-title":"Arginase plays a pivotal role in polyamine precursor metabolism in leishmanial","volume":"279","author":"Roberts","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"b","key":"10.1016\/j.pep.2019.02.018_bib13","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.vph.2012.01.001","article-title":"Arginase inhibition alleviates hypertension associated with diabetes: effect on endothelial dependent relaxation and NO production","volume":"57","author":"El-Bassossy","year":"2012","journal-title":"Vasc. Pharmacol."},{"key":"10.1016\/j.pep.2019.02.018_bib14","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1161\/01.HYP.0000146907.82869.f2","article-title":"Upregulation of vascular arginase in hypertension decreases nitric oxide mediated dilation of coronary arterioles","volume":"44","author":"Zhang","year":"2004","journal-title":"Hypertension"},{"key":"10.1016\/j.pep.2019.02.018_bib15","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0009-8981(02)00391-1","article-title":"Arginase in patients with breast cancer","volume":"328","author":"Porembska","year":"2003","journal-title":"Clin. Chim. Acta"},{"issue":"2","key":"10.1016\/j.pep.2019.02.018_bib16","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.abb.2013.03.015","article-title":"Crystal structure of arginase from Leishmania mexicana and implications for the inhibition of polyamine biosynthesis in parasitic infections","volume":"535","author":"D'Antonio","year":"2013","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.pep.2019.02.018_bib17","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":"10.1016\/j.pep.2019.02.018_bib18","doi-asserted-by":"crossref","first-page":"3058","DOI":"10.1073\/pnas.0504027102","article-title":"Crystal structure of human arginase I at 1.29-\u00c5 resolution and exploration of inhibition in the immune response","volume":"102","author":"Di Costanzo","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.pep.2019.02.018_bib19","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.exppara.2014.12.004","article-title":"Arg-265: a critical residue of L. donovani cytosolic SHMT in maintaining the binding of THF and catalysis","volume":"149","author":"Gandhi","year":"2015","journal-title":"Exp. Parasitol."},{"key":"10.1016\/j.pep.2019.02.018_bib20","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"issue":"3","key":"10.1016\/j.pep.2019.02.018_bib21","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1016\/j.parint.2008.03.004","article-title":"Molecular cloning and characterization of Brugia malayi hexokinase","volume":"57","author":"Singh","year":"2008","journal-title":"Parasitol. Int."},{"key":"10.1016\/j.pep.2019.02.018_bib22","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.actatropica.2014.02.003","article-title":"Molecular cloning and characterization of Brugia malayi thymidylate kinase","volume":"133","author":"Doharey","year":"2014","journal-title":"Acta Trop."},{"key":"10.1016\/j.pep.2019.02.018_bib23","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1007\/s12539-015-0269-6","article-title":"In silico elucidation and inhibition studies of selected phytoligands against Mitogen activated protein kinases of protozoan parasites","volume":"8","author":"Gupta","year":"2016","journal-title":"Interdiscipl. Sci. Comput. Life Sci."},{"key":"10.1016\/j.pep.2019.02.018_bib24","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":"JAppl Cryst"},{"key":"10.1016\/j.pep.2019.02.018_bib25","doi-asserted-by":"crossref","first-page":"W407","DOI":"10.1093\/nar\/gkm290","article-title":"ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins","volume":"3","author":"Wiederstein","year":"2007","journal-title":"Nucleic Acids Res."},{"issue":"14","key":"10.1016\/j.pep.2019.02.018_bib26","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1002\/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B","article-title":"Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function","volume":"19","author":"Morris","year":"1998","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.pep.2019.02.018_bib27","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.molbiopara.2008.02.011","article-title":"Biochemical and biophysical properties of a highly active recombinant arginase from Leishmania (Leishmania) amazonensis and subcellular localization of native enzyme","volume":"159","author":"da Silva","year":"2008","journal-title":"Mol. Biochem. Parasitol."},{"issue":"6600","key":"10.1016\/j.pep.2019.02.018_bib28","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1038\/383554a0","article-title":"Structure of a unique binuclear manganese cluster in arginase","volume":"383","author":"Kanyo","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.pep.2019.02.018_bib29","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0305-0491(95)02138-8","article-title":"Comparative properties of arginases","volume":"114","author":"Jenkinson","year":"1996","journal-title":"Comp Biochem Physiol B Biochem Mol Bio"},{"key":"10.1016\/j.pep.2019.02.018_bib30","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/0010-406X(70)90563-3","article-title":"Comparative physical- chemical studies of mammalian arginases","volume":"37","author":"Hirsch-Kolb","year":"1970","journal-title":"Comp. Biochem. Physiol."},{"key":"10.1016\/j.pep.2019.02.018_bib31","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1006\/abbi.1994.1276","article-title":"Rat liver arginase: kinetic mechanism, alternate substrates, and inhibitors","volume":"312","author":"Reczkowski","year":"1994","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.pep.2019.02.018_bib32","doi-asserted-by":"crossref","first-page":"5625","DOI":"10.1111\/j.1742-4658.2006.05551.x","article-title":"Mutational analysis of substrate recognition by human arginase type I: agmatinase activity of the N130D variant","volume":"273","author":"Alarcon","year":"2006","journal-title":"FEBS J."},{"key":"10.1016\/j.pep.2019.02.018_bib33","doi-asserted-by":"crossref","first-page":"14242","DOI":"10.1074\/jbc.M010575200","article-title":"Subunit subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid","volume":"276","author":"Lavulo","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2019.02.018_bib34","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1515\/BC.2005.015","article-title":"Structural metal dependency of the arginase from the human malaria parasite Plasmodium falciparum","volume":"386","author":"Muller","year":"2005","journal-title":"Biol. Chem."},{"issue":"10","key":"10.1016\/j.pep.2019.02.018_bib35","doi-asserted-by":"crossref","first-page":"1952","DOI":"10.1111\/j.1432-1033.2004.04105.x","article-title":"Purification and characterization of Helicobacter pylori arginase, RocF: unique features among the arginase superfamily","volume":"271","author":"McGee","year":"2004","journal-title":"Eur. J. Biochem."},{"issue":"2\u20133","key":"10.1016\/j.pep.2019.02.018_bib36","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S0014-5793(01)02650-3","article-title":"Glu-256 is a main structural determinant for oligomerisation of human arginase I","volume":"501","author":"Sabio","year":"2001","journal-title":"FEBS Lett."},{"key":"10.1016\/j.pep.2019.02.018_bib37","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/S0020-7519(02)00002-4","article-title":"Genomic organisation and transcription characterisation of the gene encoding Leishmania (Leishmania) amazonensis arginase and its protein structure prediction","volume":"32","author":"da Silva","year":"2002","journal-title":"Int. J. Parasitol."}],"container-title":["Protein Expression and Purification"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592818306272?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592818306272?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,8,7]],"date-time":"2019-08-07T10:44:12Z","timestamp":1565174652000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1046592818306272"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,7]]},"references-count":37,"alternative-id":["S1046592818306272"],"URL":"https:\/\/doi.org\/10.1016\/j.pep.2019.02.018","relation":{},"ISSN":["1046-5928"],"issn-type":[{"type":"print","value":"1046-5928"}],"subject":[],"published":{"date-parts":[[2019,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Molecular characterization of recombinant arginase of Leishmania donovani","name":"articletitle","label":"Article Title"},{"value":"Protein Expression and Purification","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.pep.2019.02.018","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}