{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T20:09:24Z","timestamp":1791662964257,"version":"4.3.4"},"reference-count":258,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Immunopharmacology"],"published-print":{"date-parts":[[2023,2]]},"DOI":"10.1016\/j.intimp.2022.109649","type":"journal-article","created":{"date-parts":[[2023,1,3]],"date-time":"2023-01-03T18:41:51Z","timestamp":1672771311000},"page":"109649","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":15,"special_numbering":"C","title":["Emerging strategies and challenges of molecular therapeutics in antileishmanial drug development"],"prefix":"10.1016","volume":"115","author":[{"given":"Deepak","family":"Gupta","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pankaj K.","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavan K.","family":"Yadav","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tadigoppula","family":"Narender","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Umesh K.","family":"Patil","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanjay K.","family":"Jain","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manish K.","family":"Chourasia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.intimp.2022.109649_b0005","series-title":"Encyclopedia of Cancer","first-page":"2364","article-title":"Molecular therapy","author":"Kausch","year":"2011"},{"key":"10.1016\/j.intimp.2022.109649_b0010","series-title":"Modern Pharmaceutics","first-page":"529","article-title":"Targeted-oriented drug-delivery systems","author":"Kumar","year":"2002"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0015","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.idc.2018.10.005","article-title":"Visceral leishmaniasis: recent advances in diagnostics and treatment regimens","volume":"33","author":"van Griensven","year":"2019","journal-title":"Infect. Dis. Clin. North Am."},{"issue":"1\u20132","key":"10.1016\/j.intimp.2022.109649_b0020","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.ijpharm.2018.06.018","article-title":"Promising nanotherapy in treating leishmaniasis","volume":"547","author":"de Souza","year":"2018","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.intimp.2022.109649_b0025","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2022.993338","article-title":"Meglumine antimoniate was associated with a higher cure rate than liposomal amphotericin B in the treatment of American tegumentary leishmaniasis: a retrospective cohort study from a Leishmania braziliensis-endemic area","volume":"12","author":"Barroso","year":"2022","journal-title":"Front. Cell. Infect. Microbiol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0030","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1517\/14656566.2015.973850","article-title":"An update on pharmacotherapy for leishmaniasis","volume":"16","author":"Sundar","year":"2015","journal-title":"Expert Opin. Pharmacother."},{"key":"10.1016\/j.intimp.2022.109649_b0035","unstructured":"World Health Organization, Leishmaniasis, 2022, January 8. https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/leishmaniasis. (Accessed 17\/11\/2022)."},{"issue":"22","key":"10.1016\/j.intimp.2022.109649_b0040","first-page":"287","article-title":"Leishmaniasis in high-burden countries: an epidemiological update based on data reported in 2014","volume":"91","author":"World Health Organization","year":"2016","journal-title":"Wkly Epidemiol. Rec."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0045","doi-asserted-by":"crossref","DOI":"10.3390\/microorganisms7120695","article-title":"Protective or detrimental? understanding the role of host immunity in leishmaniasis","volume":"7","author":"Dos Santos Meira","year":"2019","journal-title":"Microorganisms"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0050","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.drudis.2017.09.006","article-title":"Molecular targets and pathways for the treatment of visceral leishmaniasis","volume":"23","author":"Jain","year":"2018","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.intimp.2022.109649_b0055","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2022.953785","article-title":"Leishmania infection-induced multinucleated giant cell formation via upregulation of ATP6V0D2 expression","volume":"12","author":"Hong","year":"2022","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/j.intimp.2022.109649_b0060","doi-asserted-by":"crossref","DOI":"10.3389\/fnut.2022.948488","article-title":"Thymus, undernutrition, and infection: Approaching cellular and molecular interactions","volume":"9","author":"Savino","year":"2022","journal-title":"Front. Nutr."},{"key":"10.1016\/j.intimp.2022.109649_b0065","doi-asserted-by":"crossref","unstructured":"E, Torres-Guerrero, M.R. Quintanilla-Cedillo, J. Ruiz-Esmenjaud, R. Arenas, Leishmaniasis: a review, F1000Res 6 (2017) 750.","DOI":"10.12688\/f1000research.11120.1"},{"key":"10.1016\/j.intimp.2022.109649_b0070","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jim.2015.03.017","article-title":"Vaccines for visceral leishmaniasis: a review","volume":"422","author":"Jain","year":"2015","journal-title":"J. Immunol. Methods"},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0075","article-title":"Developing a vaccine for leishmaniasis: how biology shapes policy","volume":"137","author":"M\u00fcller","year":"2017","journal-title":"Tidsskr. Nor. Laegeforen."},{"key":"10.1016\/j.intimp.2022.109649_b0080","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/s40249-016-0112-2","article-title":"Current challenges in treatment options for visceral leishmaniasis in India: a public health perspective","volume":"5","author":"Singh","year":"2016","journal-title":"Infect. Dis. Poverty"},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0085","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1208\/s12249-022-02435-1","article-title":"Evaluation of the Efficacy of Amphotericin B and terbinafine microemulsions and their combination on cutaneous leishmaniasis and comparison with the conventional drug form in BALB\/c Mice","volume":"23","author":"Baharvandi","year":"2022","journal-title":"AAPS PharmSciTech."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0090","first-page":"26","article-title":"Limitations of current therapeutic options, possible drug targets and scope of natural products in control of leishmaniasis","volume":"18","author":"Tiwari","year":"2018","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.intimp.2022.109649_b0095","doi-asserted-by":"crossref","unstructured":"T.R, de Moura, M.L, Santos, J.M, Braz, L.F, Santos, M.T, Arag\u00e3o, F.A, de Oliveira, P.L, Santos, M, da Silva \u00c2, A.R, de Jesus, R.P, de Almeida, Cross-resistance of Leishmania infantum isolates to nitric oxide from patients refractory to antimony treatment, and greater tolerance to antileishmanial responses by macrophages, Parasitol Res 115(2) (2016) 713-721.","DOI":"10.1007\/s00436-015-4793-4"},{"key":"10.1016\/j.intimp.2022.109649_b0100","doi-asserted-by":"crossref","first-page":"1492","DOI":"10.3389\/fimmu.2017.01492","article-title":"Immune checkpoint targets for host-directed therapy to prevent and treat leishmaniasis","volume":"8","author":"Kumar","year":"2017","journal-title":"Front. Immunol."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0105","doi-asserted-by":"crossref","first-page":"e709","DOI":"10.1371\/journal.pntd.0000709","article-title":"Geographical variation in the response of visceral leishmaniasis to paromomycin in East Africa: a multicentre, open-label, randomized trial","volume":"4","author":"Hailu","year":"2010","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0110","doi-asserted-by":"crossref","first-page":"e304","DOI":"10.1016\/S1473-3099(16)30140-2","article-title":"Elimination of visceral leishmaniasis on the Indian subcontinent","volume":"16","author":"Singh","year":"2016","journal-title":"Lancet Infect. Dis."},{"issue":"14","key":"10.1016\/j.intimp.2022.109649_b0115","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.2217\/nnm-2018-0448","article-title":"Envisioning the innovations in nanomedicine to combat visceral leishmaniasis: for future theranostic application","volume":"14","author":"Singh","year":"2019","journal-title":"Nanomedicine (Lond.)"},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0120","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/S0169-4758(00)01692-6","article-title":"Leishmania-host-cell interaction: complexities and alternative views","volume":"16","author":"Rittig","year":"2000","journal-title":"Parasitol. Today"},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0125","doi-asserted-by":"crossref","first-page":"e2675","DOI":"10.1371\/journal.pntd.0002675","article-title":"Significantly lower anti-Leishmania IgG responses in Sudanese versus Indian visceral leishmaniasis","volume":"8","author":"Bhattacharyya","year":"2014","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0130","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1007\/s40291-018-0343-y","article-title":"Molecular diagnosis of visceral leishmaniasis","volume":"22","author":"Sundar","year":"2018","journal-title":"Mol. Diagn. Ther."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0135","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1080\/14728222.2018.1472241","article-title":"Emerging therapeutic targets for treatment of leishmaniasis","volume":"22","author":"Sundar","year":"2018","journal-title":"Expert Opin. Ther. Targets"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0140","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1039\/C5CS00674K","article-title":"New approaches from nanomedicine for treating leishmaniasis","volume":"45","author":"Guti\u00e9rrez","year":"2016","journal-title":"Chem. Soc. Rev."},{"issue":"23\u201324","key":"10.1016\/j.intimp.2022.109649_b0145","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1016\/j.drudis.2013.08.005","article-title":"Novel therapeutic strategies for treatment of visceral leishmaniasis","volume":"18","author":"Jain","year":"2013","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.intimp.2022.109649_b0150","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2022.112016","article-title":"New multifunctional Ru(II) organometallic compounds show activity against Trypanosoma brucei and Leishmania infantum","volume":"237","author":"Rivas","year":"2022","journal-title":"J. Inorg. Biochem."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0155","first-page":"231","article-title":"A molecular and serological study on visceral leishmaniasis in asymptomatic stray dogs in mashhad","volume":"72","author":"Sabzevari","year":"2017","journal-title":"Iran, Arch. Razi. Inst."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0160","doi-asserted-by":"crossref","first-page":"e0266291","DOI":"10.1371\/journal.pone.0266291","article-title":"Determinants of anthroponotic cutaneous leishmaniasis by case-control study in Morocco","volume":"17","author":"Amane","year":"2022","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0165","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1054\/drup.2000.0177","article-title":"Glycolysis as a target for the design of new anti-trypanosome drugs","volume":"4","author":"Verlinde","year":"2001","journal-title":"Drug Resist. Updat."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0170","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s12639-010-0006-3","article-title":"Drug targets in Leishmania","volume":"34","author":"Chawla","year":"2010","journal-title":"J. Parasit. Dis."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0175","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0166-6851(00)00234-6","article-title":"Putrescine and spermidine transport in Leishmania","volume":"109","author":"Basselin","year":"2000","journal-title":"Mol. Biochem. Parasitol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0180","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1007\/s00436-020-06736-x","article-title":"An overview of biochemically characterized drug targets in metabolic pathways of Leishmania parasite","volume":"119","author":"Raj","year":"2020","journal-title":"Parasitol. Res."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0185","doi-asserted-by":"crossref","first-page":"61","DOI":"10.4155\/fmc-2016-0180","article-title":"Polyamine-trypanothione pathway: an update","volume":"9","author":"Ilari","year":"2017","journal-title":"Future Med. Chem."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0190","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/S1995-7645(12)60084-4","article-title":"Leishmaniasis: Current status of available drugs and new potential drug targets","volume":"5","author":"Singh","year":"2012","journal-title":"Asian Pac. J. Trop. Med."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0195","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."},{"issue":"15","key":"10.1016\/j.intimp.2022.109649_b0200","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.4155\/fmc.13.146","article-title":"Structural insights into the enzymes of the trypanothione pathway: targets for antileishmaniasis drugs","volume":"5","author":"Colotti","year":"2013","journal-title":"Future Med. Chem."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0205","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1186\/s43141-022-00318-3","article-title":"Screening and identification of potential inhibitor for visceral leishmaniasis (VL) through computational analysis","volume":"20","author":"Shaslinah","year":"2022","journal-title":"J. Genet. Eng. Biotechnol."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0210","doi-asserted-by":"crossref","first-page":"1700373","DOI":"10.1002\/ardp.201700373","article-title":"Molecular insights into trypanothione reductase-inhibitor interaction: a structure-based review","volume":"351","author":"Tiwari","year":"2018","journal-title":"Arch. Pharm. Chem. Life Sci."},{"key":"10.1016\/j.intimp.2022.109649_b0215","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1177\/117739280700200007","article-title":"Trypanothione reductase: a viable chemotherapeutic target for antitrypanosomal and antileishmanial drug design","volume":"2","author":"Khan","year":"2007","journal-title":"Drug Target Insights"},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0220","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"},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0225","doi-asserted-by":"crossref","first-page":"e33138","DOI":"10.1371\/journal.pone.0033138","article-title":"A unique modification of the eukaryotic initiation factor 5A shows the presence of the complete hypusine pathway in Leishmania donovani","volume":"7","author":"Chawla","year":"2012","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0230","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1074\/jbc.M109.048850","article-title":"Identification and characterization of a novel deoxyhypusine synthase in Leishmania donovani","volume":"285","author":"Chawla","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0235","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1111\/j.1365-2958.2011.07799.x","article-title":"The Leishmania nicotinamidase is essential for NAD+ production and parasite proliferation","volume":"82","author":"Gazanion","year":"2011","journal-title":"Mol. Microbiol."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0240","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1016\/j.mib.2013.07.018","article-title":"Pathways of iron acquisition and utilization in Leishmania","volume":"16","author":"Flannery","year":"2013","journal-title":"Curr. Opin. Microbiol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0245","doi-asserted-by":"crossref","first-page":"5884","DOI":"10.1074\/jbc.M411845200","article-title":"Hemoglobin receptor in leishmania is a hexokinase located in the flagellar pocket","volume":"280","author":"Krishnamurthy","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b0250","doi-asserted-by":"crossref","first-page":"2758","DOI":"10.1074\/jbc.274.5.2758","article-title":"Hemoglobin Endocytosis in Leishmania Is Mediated through a 46-kDa Protein Located in the Flagellar Pocket","volume":"274","author":"Sengupta","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"21","key":"10.1016\/j.intimp.2022.109649_b0255","doi-asserted-by":"crossref","first-page":"5712","DOI":"10.1093\/emboj\/cdg557","article-title":"Rab5-mediated endosome\u2013endosome fusion regulates hemoglobin endocytosis in Leishmania donovani","volume":"22","author":"Singh","year":"2003","journal-title":"EMBO J."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0260","doi-asserted-by":"crossref","first-page":"3980","DOI":"10.1073\/pnas.0800404105","article-title":"Leishmania requires Rab7-mediated degradation of endocytosed hemoglobin for their growth","volume":"105","author":"Patel","year":"2008","journal-title":"PNAS"},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b0265","first-page":"1065","article-title":"Clathrin-mediated hemoglobin endocytosis is essential for survival of Leishmania","volume":"1833","author":"Agarwal","year":"2013","journal-title":"BBA"},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0270","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1111\/j.1365-2958.2010.07531.x","article-title":"A new ATP-binding cassette protein is involved in intracellular haem trafficking in Leishmania","volume":"79","author":"Campos-Salinas","year":"2011","journal-title":"Mol. Microbiol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0275","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1111\/j.1462-5822.2008.01241.x","article-title":"Leishmania donovani depletes labile iron pool to exploit iron uptake capacity of macrophage for its intracellular growth","volume":"11","author":"Das","year":"2009","journal-title":"Cell. Microbiol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0280","first-page":"298","article-title":"Malaria: autophagy as a potential therapeutic target","volume":"4","author":"Singh","year":"2016","journal-title":"J. Pharm. Pharmacol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0285","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1186\/s13104-018-3354-1","article-title":"Homology modelling, molecular docking, and molecular dynamics simulations reveal the inhibition of Leishmania donovani dihydrofolate reductase-thymidylate synthase enzyme by Withaferin-A","volume":"11","author":"Vadloori","year":"2018","journal-title":"BMC. Res. Notes"},{"issue":"9","key":"10.1016\/j.intimp.2022.109649_b0290","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1007\/s00894-010-0649-0","article-title":"Probing the structure of Leishmania donovani chagasi DHFR-TS: comparative protein modeling and protein\u2013ligand interaction studies","volume":"16","author":"Maganti","year":"2010","journal-title":"J. Mol. Model."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0295","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/S0020-7519(01)00346-0","article-title":"Pterin transport and metabolism in Leishmania and related trypanosomatid parasites","volume":"32","author":"Ouellette","year":"2002","journal-title":"Int. J. Parasitol."},{"key":"10.1016\/j.intimp.2022.109649_b0300","doi-asserted-by":"crossref","first-page":"S101","DOI":"10.1017\/S0031182097001133","article-title":"New approaches to Leishmania chemotherapy: pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity","volume":"114","author":"Nare","year":"1997","journal-title":"Parasitology"},{"key":"10.1016\/j.intimp.2022.109649_b0305","doi-asserted-by":"crossref","DOI":"10.4061\/2011\/278051","article-title":"Bioinformatic analysis of leishmania donovani long-chain fatty acid-coa ligase as a novel drug target","author":"Kaur","year":"2011","journal-title":"Mol. Biol. Int."},{"key":"10.1016\/j.intimp.2022.109649_b0310","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.micpath.2013.11.001","article-title":"Exploring Leishmania donovani 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) as a potential drug target by biochemical, biophysical and inhibition studies","volume":"66","author":"Dinesh","year":"2014","journal-title":"Microb. Pathog."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0315","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1073\/pnas.97.1.406","article-title":"The role of phosphoglycans in Leishmania-sand fly interactions","volume":"97","author":"Sacks","year":"2000","journal-title":"PNAS"},{"key":"10.1016\/j.intimp.2022.109649_b0320","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1146\/annurev.mi.46.100192.000433","article-title":"The lipophosphoglycan of Leishmania parasites","volume":"46","author":"Turco","year":"1992","journal-title":"Annu. Rev. Microbiol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0325","doi-asserted-by":"crossref","first-page":"10","DOI":"10.3390\/proteomes10020010","article-title":"In-depth quantitative proteomics characterization of in vitro selected miltefosine resistance in leishmania infantum","volume":"10","author":"Saboia-Vahia","year":"2022","journal-title":"Proteomes"},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0330","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."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0335","first-page":"360","article-title":"Purine metabolism in Leishmania donovani and Leishmania braziliensis","volume":"544","author":"Marr","year":"1978","journal-title":"BBA"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0340","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1111\/j.1365-2958.2010.07327.x","article-title":"Adaptive responses to purine starvation in Leishmania donovani","volume":"78","author":"Carter","year":"2010","journal-title":"Mol. Microbiol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0345","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/j.molbiopara.2006.09.002","article-title":"Functional characterization of nucleoside transporter gene replacements in Leishmania donovani","volume":"150","author":"Liu","year":"2006","journal-title":"Mol. Biochem. Parasitol."},{"issue":"27","key":"10.1016\/j.intimp.2022.109649_b0350","doi-asserted-by":"crossref","first-page":"20935","DOI":"10.1074\/jbc.M002418200","article-title":"Cloning of a novel inosine-guanosine transporter gene from Leishmania donovani by functional rescue of a transport-deficient mutant","volume":"275","author":"Carter","year":"2000","journal-title":"J. Biol. Chem."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0355","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1016\/j.biocel.2005.12.016","article-title":"Point mutations within the LdNT2 nucleoside transporter gene from Leishmania donovani confer drug resistance and transport deficiency","volume":"38","author":"Galazka","year":"2006","journal-title":"Int. J. Biochem. Cell Biol."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0360","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1128\/AAC.46.3.929-931.2002","article-title":"In Vivo Activities of Farnesyl Pyrophosphate Synthase Inhibitors against Leishmania donovani and Toxoplasma gondii","volume":"46","author":"Yardley","year":"2002","journal-title":"Antimicrob. Agents Chemother."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0365","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1021\/jm0002578","article-title":"Bisphosphonates inhibit the growth of Trypanosoma brucei, Trypanosoma cruzi, Leishmania donovani, Toxoplasma gondii, and Plasmodium falciparum: a potential route to chemotherapy","volume":"44","author":"Martin","year":"2001","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0370","doi-asserted-by":"crossref","first-page":"e0003588","DOI":"10.1371\/journal.pntd.0003588","article-title":"Targeting Ergosterol biosynthesis in Leishmania donovani: essentiality of sterol 14 alpha-demethylase","volume":"9","author":"McCall","year":"2015","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0375","doi-asserted-by":"crossref","first-page":"e0004422","DOI":"10.1371\/journal.pntd.0004422","article-title":"Induction of IL-10 and TGF\u03b2 from CD4+CD25+FoxP3+ T Cells Correlates with Parasite Load in indian kala-azar patients infected with leishmania donovani","volume":"10","author":"Bhattacharya","year":"2016","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"9","key":"10.1016\/j.intimp.2022.109649_b0380","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.it.2007.07.004","article-title":"Interleukin-10 and the pathogenesis of human visceral leishmaniasis","volume":"28","author":"Nyl\u00e9n","year":"2007","journal-title":"Trends Immunol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0385","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1590\/S0074-02762000000200013","article-title":"Role of CD8+ T cells in endogenous interleukin-10 secretion associated with visceral leishmaniasis","volume":"95","author":"Holaday","year":"2000","journal-title":"Mem. Inst. Oswaldo Cruz"},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0390","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1084\/jem.20061141","article-title":"Splenic accumulation of IL-10 mRNA in T cells distinct from CD4+CD25+ (Foxp3) regulatory T cells in human visceral leishmaniasis","volume":"204","author":"Nyl\u00e9n","year":"2007","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.intimp.2022.109649_b0395","doi-asserted-by":"crossref","first-page":"296","DOI":"10.3389\/fimmu.2014.00296","article-title":"Immunotherapy and targeted therapies in treatment of visceral leishmaniasis: current status and future prospects","volume":"5","author":"Singh","year":"2014","journal-title":"Front. Immunol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0400","doi-asserted-by":"crossref","first-page":"3977","DOI":"10.4049\/jimmunol.1003588","article-title":"IL-27 and IL-21 are associated with T cell IL-10 responses in human visceral leishmaniasis","volume":"186","author":"Ansari","year":"2011","journal-title":"J. Immunol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0405","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.pt.2005.11.010","article-title":"Chemokines in host-parasite interactions in leishmaniasis","volume":"22","author":"Teixeira","year":"2006","journal-title":"Trends Parasitol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0410","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1002\/(SICI)1521-4141(199901)29:01<203::AID-IMMU203>3.0.CO;2-B","article-title":"Leishmania donovani infection initiates T cell-independent chemokine responses, which are subsequently amplified in a T cell-dependent manner","volume":"29","author":"Cotterell","year":"1999","journal-title":"Eur. J. Immunol."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0415","doi-asserted-by":"crossref","first-page":"8334","DOI":"10.1128\/IAI.73.12.8334-8344.2005","article-title":"Regulation of impaired protein kinase C signaling by chemokines in murine macrophages during visceral leishmaniasis","volume":"73","author":"Dey","year":"2005","journal-title":"Infect. Immun."},{"issue":"8","key":"10.1016\/j.intimp.2022.109649_b0420","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.1086\/605895","article-title":"CXC chemokine-mediated protection against visceral leishmaniasis: involvement of the proinflammatory response","volume":"200","author":"Gupta","year":"2009","journal-title":"J. Infect Dis."},{"issue":"8","key":"10.1016\/j.intimp.2022.109649_b0425","doi-asserted-by":"crossref","first-page":"4177","DOI":"10.1128\/IAI.70.8.4177-4184.2002","article-title":"Leishmania promastigotes release a granulocyte chemotactic factor and induce interleukin-8 release but inhibit gamma interferon-inducible protein 10 production by neutrophil granulocytes","volume":"70","author":"van Zandbergen","year":"2002","journal-title":"Infect. Immun."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0430","first-page":"623","article-title":"Current status and perspectives of the immunotherapy of leishmaniasis","volume":"11","author":"El-On","year":"2009","journal-title":"Isr. Med. Assoc. J."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0435","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1111\/j.1574-6968.2007.01013.x","article-title":"Wild-type Leishmania donovani promastigotes block maturation, increase integrin expression and inhibit detachment of human monocyte-derived dendritic cells \u2013 the influence of phosphoglycans","volume":"279","author":"Tejle","year":"2008","journal-title":"FEMS Microbiol. Lett."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0440","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.4049\/jimmunol.172.2.1186","article-title":"The dendritic cell receptor DC-SIGN discriminates among species and life cycle forms of Leishmania","volume":"172","author":"Colmenares","year":"2004","journal-title":"J. Immunol."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0445","doi-asserted-by":"crossref","first-page":"e47","DOI":"10.1016\/S1473-3099(16)00078-5","article-title":"Host-directed therapies for infectious diseases: current status, recent progress, and future prospects","volume":"16","author":"Zumla","year":"2016","journal-title":"Lancet Infect. Dis."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0450","doi-asserted-by":"crossref","first-page":"e0005480","DOI":"10.1371\/journal.pntd.0005480","article-title":"The enemy within: Targeting host-parasite interaction for antileishmanial drug discovery","volume":"11","author":"Lamotte","year":"2017","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0455","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1017\/S0031182016002031","article-title":"Evaluating drug resistance in visceral leishmaniasis: the challenges","volume":"145","author":"Hendrickx","year":"2016","journal-title":"Parasitology"},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0460","first-page":"411","article-title":"Drug resistance mechanisms in clinical isolates of Leishmania donovani","volume":"123","author":"Singh","year":"2006","journal-title":"Indian J. Med. Res."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0465","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."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0470","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1111\/febs.13601","article-title":"Leishmania hijacking of the macrophage intracellular compartments","volume":"283","author":"Lievin-Le Moal","year":"2016","journal-title":"FEBS J."},{"key":"10.1016\/j.intimp.2022.109649_b0475","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1146\/annurev-micro-090110-102913","article-title":"Metabolic pathways required for the intracellular survival of Leishmania","volume":"65","author":"McConville","year":"2011","journal-title":"Annu. Rev. Microbiol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0480","doi-asserted-by":"crossref","first-page":"111","DOI":"10.2217\/fmb.14.103","article-title":"Leishmania and the macrophage: a multifaceted interaction","volume":"10","author":"Podinovskaia","year":"2015","journal-title":"Future Microbiol."},{"issue":"8","key":"10.1016\/j.intimp.2022.109649_b0485","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1038\/nrmicro2608","article-title":"Leishmaniasis: complexity at the host-pathogen interface","volume":"9","author":"Kaye","year":"2011","journal-title":"Nat. Rev. Microbiol."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0490","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.4049\/jimmunol.1004237","article-title":"Uncoupling protein 2 negatively regulates mitochondrial reactive oxygen species generation and induces phosphatase-mediated anti-inflammatory response in experimental visceral leishmaniasis","volume":"187","author":"Basu Ball","year":"2011","journal-title":"J. Immunol."},{"key":"10.1016\/j.intimp.2022.109649_b0495","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0065-308X(04)58001-6","article-title":"Leishmania spp.: on the interactions they establish with antigen-presenting cells of their mammalian hosts","volume":"58","author":"Antoine","year":"2004","journal-title":"Adv. Parasitol."},{"issue":"9","key":"10.1016\/j.intimp.2022.109649_b0500","doi-asserted-by":"crossref","first-page":"e3202","DOI":"10.1371\/journal.pntd.0003202","article-title":"Impact of Leishmania mexicana infection on dendritic cell signaling and functions","volume":"8","author":"Contreras","year":"2014","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0505","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.chom.2013.06.003","article-title":"Leishmania evades host immunity by inhibiting antigen cross-presentation through direct cleavage of the SNARE VAMP8","volume":"14","author":"Matheoud","year":"2013","journal-title":"Cell Host Microbe"},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0510","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/j.chom.2011.04.014","article-title":"Leishmania promotes its own virulence by inducing expression of the host immune inhibitory ligand CD200","volume":"9","author":"Cortez","year":"2011","journal-title":"Cell Host Microbe"},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b0515","doi-asserted-by":"crossref","first-page":"3214","DOI":"10.4049\/jimmunol.175.5.3214","article-title":"Leishmania donovani affects antigen presentation of macrophage by disrupting lipid rafts","volume":"175","author":"Chakraborty","year":"2005","journal-title":"J. Immunol."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0520","doi-asserted-by":"crossref","first-page":"6706","DOI":"10.4049\/jimmunol.171.12.6706","article-title":"Leishmania-induced inhibition of macrophage antigen presentation analyzed at the single-cell level","volume":"171","author":"Meier","year":"2003","journal-title":"J. Immunol."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0525","doi-asserted-by":"crossref","first-page":"3163","DOI":"10.1002\/eji.1830261249","article-title":"Leishmania-infected macrophages sequester endogenously synthesized parasite antigens from presentation to CD4+ T cells","volume":"26","author":"Kima","year":"1996","journal-title":"Eur. J. Immunol."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0530","doi-asserted-by":"crossref","first-page":"2930","DOI":"10.4049\/jimmunol.152.6.2930","article-title":"Intracellular infection by Leishmania donovani inhibits macrophage apoptosis","volume":"152","author":"Moore","year":"1994","journal-title":"J. Immunol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0535","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1189\/jlb.4A0713-378RR","article-title":"Unmethylated CpG motifs in the L. donovani DNA regulate TLR9-dependent delay of programmed cell death in macrophages","volume":"97","author":"Das","year":"2015","journal-title":"J. Leukoc. Biol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0540","doi-asserted-by":"crossref","first-page":"3496","DOI":"10.1074\/jbc.M115.672873","article-title":"Leishmania donovani Exploits Myeloid Cell Leukemia 1 (MCL-1) Protein to Prevent mitochondria-dependent host cell apoptosis","volume":"291","author":"Giri","year":"2016","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b0545","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1128\/IAI.02833-14","article-title":"Proteomic-based approach to gain insight into reprogramming of THP-1 cells exposed to Leishmania donovani over an early temporal window","volume":"83","author":"Singh","year":"2015","journal-title":"Infect. Immun."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0550","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.chom.2013.02.005","article-title":"Leishmania donovani targets Dicer1 to downregulate miR-122, lower serum cholesterol, and facilitate murine liver infection","volume":"13","author":"Ghosh","year":"2013","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.intimp.2022.109649_b0555","doi-asserted-by":"crossref","first-page":"367","DOI":"10.3389\/fmicb.2016.00367","article-title":"Role of Small RNAs in Trypanosomatid Infections","volume":"7","author":"Linhares-Lacerda","year":"2016","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.intimp.2022.109649_b0560","doi-asserted-by":"crossref","first-page":"272","DOI":"10.3389\/fimmu.2014.00272","article-title":"Immunotherapy and Immunochemotherapy in Visceral Leishmaniasis: promising treatments for this neglected disease","volume":"5","author":"Roatt","year":"2014","journal-title":"Front. Immunol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0565","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nri1391","article-title":"Toll-like receptor signalling","volume":"4","author":"Akira","year":"2004","journal-title":"Nat. Rev. Immunol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0570","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.cyto.2009.08.010","article-title":"Toll-like receptor signaling in cell proliferation and survival","volume":"49","author":"Li","year":"2010","journal-title":"Cytokine"},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0575","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1038\/sj.icb.7100098","article-title":"Coordinating TLR-activated signaling pathways in cells of the immune system","volume":"85","author":"Banerjee","year":"2007","journal-title":"Immunol. Cell Biol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0580","doi-asserted-by":"crossref","first-page":"2318","DOI":"10.1128\/IAI.01468-12","article-title":"Regulatory actions of Toll-like receptor 2 (TLR2) and TLR4 in Leishmania donovani infection in the liver","volume":"81","author":"Murray","year":"2013","journal-title":"Infect. Immun."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0585","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1086\/653210","article-title":"Arabinosylated lipoarabinomannan-mediated protection in visceral leishmaniasis through up-regulation of toll-like receptor 2 signaling: an immunoprophylactic approach","volume":"202","author":"Bhattacharya","year":"2010","journal-title":"J Infect Dis"},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0590","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1002\/eji.200535079","article-title":"RNA interference reveals a role for TLR2 and TLR3 in the recognition of Leishmania donovani promastigotes by interferon-gamma-primed macrophages","volume":"36","author":"Flandin","year":"2006","journal-title":"Eur. J. Immunol."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0595","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.pt.2006.01.003","article-title":"The conundrum of CD40 function: host protection or disease promotion?","volume":"22","author":"Mathur","year":"2006","journal-title":"Trends Parasitol."},{"issue":"11","key":"10.1016\/j.intimp.2022.109649_b0600","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1016\/j.intimp.2011.08.002","article-title":"Immunomodulation by chemotherapeutic agents against Leishmaniasis","volume":"11","author":"Saha","year":"2011","journal-title":"Int. Immunopharmacol."},{"key":"10.1016\/j.intimp.2022.109649_b0605","doi-asserted-by":"crossref","DOI":"10.1155\/2010\/109189","article-title":"Leishmania interferes with host cell signaling to devise a survival strategy","volume":"2010","author":"Bhardwaj","year":"2010","journal-title":"J. Biomed. Biotechnol."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b0610","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1038\/nm1045","article-title":"Reciprocal CD40 signals through p38MAPK and ERK-1\/2 induce counteracting immune responses","volume":"10","author":"Mathur","year":"2004","journal-title":"Nat. Med."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0615","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/ni.1705","article-title":"Cholesterol depletion associated with Leishmania major infection alters macrophage CD40 signalosome composition and effector function","volume":"10","author":"Rub","year":"2009","journal-title":"Nat. Immunol."},{"issue":"1\u20132","key":"10.1016\/j.intimp.2022.109649_b0620","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.cca.2007.04.007","article-title":"Hypocholesterolemia and increased triglyceride in pediatric visceral leishmaniasis","volume":"382","author":"Lal","year":"2007","journal-title":"Clin. Chim. Acta"},{"issue":"11","key":"10.1016\/j.intimp.2022.109649_b0625","doi-asserted-by":"crossref","first-page":"3815","DOI":"10.4049\/jimmunol.147.11.3815","article-title":"IL-10 inhibits cytokine production by activated macrophages","volume":"147","author":"Fiorentino","year":"1991","journal-title":"J. Immunol."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0630","doi-asserted-by":"crossref","first-page":"2101","DOI":"10.1084\/jem.185.12.2101","article-title":"Altered Immune Responses in Interleukin 10 Transgenic Mice","volume":"185","author":"Hagenbaugh","year":"1997","journal-title":"J. Exp. Med."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0635","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1046\/j.1365-3083.2001.00856.x","article-title":"Macrophage heterogeneity, antigen presentation, and membrane fluidity: implications in visceral Leishmaniasis","volume":"53","author":"Sen","year":"2001","journal-title":"Scand. J. Immunol."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0640","doi-asserted-by":"crossref","first-page":"6403","DOI":"10.4049\/jimmunol.163.12.6403","volume":"163","author":"Feng","year":"1999","journal-title":"J. Immunol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0645","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1111\/j.1365-2249.2008.03741.x","article-title":"Leishmania donovani infection down-regulates TLR2-stimulated IL-12p40 and activates IL-10 in cells of macrophage\/monocytic lineage by modulating MAPK pathways through a contact-dependent mechanism","volume":"154","author":"Chandra","year":"2008","journal-title":"Clin. Exp. Immunol."},{"issue":"21","key":"10.1016\/j.intimp.2022.109649_b0650","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1038\/sj.onc.1203485","article-title":"The biology of Stat4 and Stat6","volume":"19","author":"Wurster","year":"2000","journal-title":"Oncogene"},{"key":"10.1016\/j.intimp.2022.109649_b0655","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1146\/annurev.immunol.15.1.749","article-title":"Cellular responses to interferon-gamma","volume":"15","author":"Boehm","year":"1997","journal-title":"Annu. Rev. Immunol."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0660","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1084\/jem.177.6.1779","article-title":"Promoter of the mouse gene encoding calcium-independent nitric oxide synthase confers inducibility by interferon gamma and bacterial lipopolysaccharide","volume":"177","author":"Xie","year":"1993","journal-title":"J. Exp. Med."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0665","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1038\/89769","article-title":"The essential role of MEKK3 in TNF-induced NF-kappaB activation","volume":"2","author":"Yang","year":"2001","journal-title":"Nat. Immunol."},{"issue":"26","key":"10.1016\/j.intimp.2022.109649_b0670","doi-asserted-by":"crossref","first-page":"11924","DOI":"10.1073\/pnas.0913179107","article-title":"IkappaBeta, a nuclear IkappaB protein, positively regulates the NF-kappaB-mediated expression of proinflammatory cytokines","volume":"107","author":"Yamauchi","year":"2010","journal-title":"PNAS"},{"issue":"8","key":"10.1016\/j.intimp.2022.109649_b0675","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.1002\/1521-4141(2000)30:8<2235::AID-IMMU2235>3.0.CO;2-9","article-title":"Leishmania donovani promastigotes evade the activation of mitogen-activated protein kinases p38, c-Jun N-terminal kinase, and extracellular signal-regulated kinase-1\/2 during infection of naive macrophages","volume":"30","author":"Priv\u00e9","year":"2000","journal-title":"Eur. J. Immunol."},{"issue":"Pt 2) (Pt 2","key":"10.1016\/j.intimp.2022.109649_b0680","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1042\/bj3320281","article-title":"The extended protein kinase C superfamily","volume":"332","author":"Mellor","year":"1998","journal-title":"Biochem. J"},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0685","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1128\/IAI.69.3.1499-1507.2001","article-title":"Immunomodulatory role of interleukin-10 in visceral leishmaniasis: defective activation of protein kinase C-mediated signal transduction events","volume":"69","author":"Bhattacharyya","year":"2001","journal-title":"Infect. Immun."},{"issue":"16","key":"10.1016\/j.intimp.2022.109649_b0690","doi-asserted-by":"crossref","first-page":"7481","DOI":"10.1073\/pnas.89.16.7481","article-title":"Defective stimulus-response coupling in human monocytes infected with Leishmania donovani is associated with altered activation and translocation of protein kinase C","volume":"89","author":"Olivier","year":"1992","journal-title":"PNAS"},{"issue":"9","key":"10.1016\/j.intimp.2022.109649_b0695","doi-asserted-by":"crossref","first-page":"3008","DOI":"10.4049\/jimmunol.149.9.3008","article-title":"Inhibition of macrophage protein kinase C-mediated protein phosphorylation by Leishmania donovani lipophosphoglycan","volume":"149","author":"Descoteaux","year":"1992","journal-title":"J. Immunol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0700","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1006\/exmp.2002.2418","article-title":"Parasitic adaptive mechanisms in infection by leishmania","volume":"72","author":"Cunningham","year":"2002","journal-title":"Exp. Mol. Pathol."},{"issue":"1\u20132","key":"10.1016\/j.intimp.2022.109649_b0705","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1023\/A:1011048210691","article-title":"Selective impairment of protein kinase C isotypes in murine macrophage by Leishmania donovani","volume":"216","author":"Bhattacharyya","year":"2001","journal-title":"Mol. Cell. Biochem."},{"issue":"1\u20132","key":"10.1016\/j.intimp.2022.109649_b0710","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1023\/A:1017996609928","article-title":"Generation of ceramide in murine macrophages infected with Leishmania donovani alters macrophage signaling events and aids intracellular parasitic survival","volume":"223","author":"Ghosh","year":"2001","journal-title":"Mol. Cell. Biochem."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0715","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1189\/jlb.0210088","article-title":"Editorial: leishmania survival mechanisms: the role of host phosphatases","volume":"88","author":"Shio","year":"2010","journal-title":"J. Leukoc. Biol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0720","doi-asserted-by":"crossref","first-page":"367","DOI":"10.4049\/jimmunol.1100076","article-title":"Myeloid Cell IL-10 Production in Response to Leishmania Involves Inactivation of Glycogen Synthase Kinase-3\u03b2 Downstream of Phosphatidylinositol-3 Kinase","volume":"188","author":"Nandan","year":"2012","journal-title":"J. Immunol."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b0725","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1189\/jlb.0611326","article-title":"Secreted virulence factors and immune evasion in visceral leishmaniasis","volume":"91","author":"Lambertz","year":"2012","journal-title":"J. Leukoc. Biol."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b0730","doi-asserted-by":"crossref","first-page":"3416","DOI":"10.4049\/jimmunol.166.5.3416","article-title":"General suppression of macrophage gene expression during leishmania donovani infection","volume":"166","author":"Buates","year":"2001","journal-title":"J. Immunol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0735","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1111\/j.1462-5822.2006.00769.x","article-title":"Leishmania promastigotes activate PI3K\/Akt signalling to confer host cell resistance to apoptosis","volume":"9","author":"Ruhland","year":"2007","journal-title":"Cell. Microbiol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0740","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1046\/j.1462-5822.2001.00127.x","article-title":"Leishmania donovani lipophosphoglycan causes periphagosomal actin accumulation: correlation with impaired translocation of PKC\u03b1 and defective phagosome maturation","volume":"3","author":"Holm","year":"2001","journal-title":"Cell. Microbiol."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0745","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/S0006-291X(03)00231-6","article-title":"Role of protein kinase C \u03b1 for uptake of unopsonized prey and phagosomal maturation in macrophages","volume":"302","author":"Holm","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"24","key":"10.1016\/j.intimp.2022.109649_b0750","doi-asserted-by":"crossref","first-page":"16782","DOI":"10.1074\/jbc.274.24.16782","article-title":"Down-regulation of MARCKS-related Protein (MRP) in Macrophages Infected with Leishmania","volume":"274","author":"Corradin","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0755","doi-asserted-by":"crossref","first-page":"1922","DOI":"10.1111\/j.1462-5822.2006.00758.x","article-title":"Leishmania donovani lipophosphoglycan blocks NADPH oxidase assembly at the phagosome membrane","volume":"8","author":"Lodge","year":"2006","journal-title":"Cell. Microbiol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0760","first-page":"341","article-title":"Glycoconjugates in Leishmania infectivity","volume":"1455","author":"Descoteaux","year":"1999","journal-title":"BBA"},{"issue":"31","key":"10.1016\/j.intimp.2022.109649_b0765","doi-asserted-by":"crossref","first-page":"18179","DOI":"10.1074\/jbc.270.31.18179","article-title":"Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase","volume":"270","author":"Yetter","year":"1995","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.intimp.2022.109649_b0770","doi-asserted-by":"crossref","first-page":"4495","DOI":"10.1128\/iai.63.11.4495-4500.1995","article-title":"Attenuation of gamma interferon-induced tyrosine phosphorylation in mononuclear phagocytes infected with Leishmania donovani: selective inhibition of signaling through Janus kinases and Stat 1","volume":"63","author":"Nandan","year":"1995","journal-title":"Infect. Immun."},{"key":"10.1016\/j.intimp.2022.109649_b0775","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1146\/annurev.iy.11.040193.001203","article-title":"The role of the CD28 receptor during T cell responses to antigen","volume":"11","author":"Linsley","year":"1993","journal-title":"Annu. Rev. Immunol."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0780","doi-asserted-by":"crossref","first-page":"2001","DOI":"10.4049\/jimmunol.164.4.2001","article-title":"TGF-\u03b2 mediates CTLA-4 suppression of cellular immunity in murine kalaazar","volume":"164","author":"Gomes","year":"2000","journal-title":"J. Immunol."},{"issue":"9","key":"10.1016\/j.intimp.2022.109649_b0785","doi-asserted-by":"crossref","first-page":"2492","DOI":"10.1002\/eji.1830250913","article-title":"Macrophage-T cell interaction in experimental visceral leishmaniasis: failure to express costimulatory molecules on Leishmania-infected macrophages and its implication in the suppression of cell-mediated immunity","volume":"25","author":"Saha","year":"1995","journal-title":"Eur. J. Immunol."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0790","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1128\/AAC.02022-13","article-title":"Pharmacological assessment defines Leishmania donovani casein kinase 1 as a drug target and reveals important functions in parasite viability and intracellular infection","volume":"58","author":"Rachidi","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.intimp.2022.109649_b0795","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.exppara.2014.08.009","article-title":"In vitro anti-leishmanial efficacy of potato tuber extract (PTEx): leishmanial serine protease(s) as putative target","volume":"146","author":"Paik","year":"2014","journal-title":"Exp. Parasitol."},{"key":"10.1016\/j.intimp.2022.109649_b0800","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1016\/j.biopha.2016.08.046","article-title":"Protective inflammatory response against visceral leishmaniasis with potato tuber extract: a new approach of successful therapy","volume":"83","author":"Paik","year":"2016","journal-title":"Biomed. Pharmacother."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0805","doi-asserted-by":"crossref","DOI":"10.1128\/MCB.00344-16","article-title":"Phosphorylation of Translation Initiation Factor 2-Alpha in leishmania donovani under stress is necessary for parasite survival","volume":"37","author":"Abhishek","year":"2017","journal-title":"Mol. Cell Biol."},{"issue":"9","key":"10.1016\/j.intimp.2022.109649_b0810","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/S0020-7519(02)00067-X","article-title":"Effect of pH and temperature on protein kinase release by Leishmania donovani","volume":"32","author":"Vieira","year":"2002","journal-title":"Int. J. Parasitol."},{"key":"10.1016\/j.intimp.2022.109649_b0815","doi-asserted-by":"crossref","first-page":"492","DOI":"10.3389\/fimmu.2019.00492","article-title":"Leishmania-Host Interactions\u2014an epigenetic paradigm","volume":"10","author":"Afrin","year":"2019","journal-title":"Front. Immunol."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0820","doi-asserted-by":"crossref","first-page":"e1004419","DOI":"10.1371\/journal.ppat.1004419","article-title":"Leishmania donovani infection causes distinct epigenetic DNA methylation changes in host macrophages","volume":"10","author":"Marr","year":"2014","journal-title":"PLoS Pathog."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b0825","first-page":"e01079","volume":"11","author":"Saha","year":"2020","journal-title":"Histone Modifications and Other Facets of Epigenetic Regulation in Trypanosomatids: Leaving Their Mark, mBio"},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0830","doi-asserted-by":"crossref","first-page":"2762","DOI":"10.4049\/jimmunol.1900251","article-title":"Leishmania donovani Subverts host immune response by epigenetic reprogramming of macrophage M(Lipopolysaccharides + IFN-\u03b3)\/M(IL-10) Polarization","volume":"204","author":"Parmar","year":"2020","journal-title":"J. Immunol."},{"key":"10.1016\/j.intimp.2022.109649_b0835","series-title":"Extracellular Vesicles - Role in Diseases","article-title":"The role of extracellular vesicles in immunomodulation and pathogenesis of leishmania and other protozoan infections","author":"Islek","year":"2022"},{"key":"10.1016\/j.intimp.2022.109649_b0840","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.cellimm.2016.07.013","article-title":"Leishmania exosomes and other virulence factors: impact on innate immune response and macrophage functions","volume":"309","author":"Atayde","year":"2016","journal-title":"Cell. Immunol."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b0845","doi-asserted-by":"crossref","first-page":"2061","DOI":"10.1084\/jem.185.12.2061","article-title":"Inhibition of phagolysosomal biogenesis by the Leishmania lipophosphoglycan","volume":"185","author":"Desjardins","year":"1997","journal-title":"J. Exp. Med."},{"issue":"14","key":"10.1016\/j.intimp.2022.109649_b0850","doi-asserted-by":"crossref","first-page":"4676","DOI":"10.1021\/bi00014a022","article-title":"Potent inhibition of viral fusion by the lipophosphoglycan of Leishmania donovani","volume":"34","author":"Miao","year":"1995","journal-title":"Biochemistry"},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0855","doi-asserted-by":"crossref","first-page":"e1000628","DOI":"10.1371\/journal.ppat.1000628","article-title":"The Leishmania donovani lipophosphoglycan excludes the vesicular proton-ATPase from phagosomes by impairing the recruitment of synaptotagmin V","volume":"5","author":"Vinet","year":"2009","journal-title":"PLoS Pathog."},{"issue":"11","key":"10.1016\/j.intimp.2022.109649_b0860","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.1111\/j.1462-5822.2005.00582.x","article-title":"Leishmania donovani promastigotes induce periphagosomal F-actin accumulation through retention of the GTPase Cdc42","volume":"7","author":"Lodge","year":"2005","journal-title":"Cell. Microbiol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0865","doi-asserted-by":"crossref","first-page":"2745","DOI":"10.4049\/jimmunol.144.7.2745","article-title":"Requirement of lipophosphoglycan for intracellular survival of Leishmania donovani within human monocytes","volume":"144","author":"McNeely","year":"1990","journal-title":"J. Immunol."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b0870","doi-asserted-by":"crossref","first-page":"2453","DOI":"10.1073\/pnas.86.7.2453","article-title":"Microbial glycolipids: possible virulence factors that scavenge oxygen radicals","volume":"86","author":"Chan","year":"1989","journal-title":"PNAS"},{"key":"10.1016\/j.intimp.2022.109649_b0875","doi-asserted-by":"crossref","DOI":"10.1016\/j.parint.2021.102373","article-title":"The roles of parasite-derived extracellular vesicles in disease and host-parasite communication","volume":"83","author":"Carrera-Bravo","year":"2021","journal-title":"Parasitol. Int."},{"issue":"43","key":"10.1016\/j.intimp.2022.109649_b0880","doi-asserted-by":"crossref","first-page":"10113","DOI":"10.1021\/bi00495a015","article-title":"Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania","volume":"29","author":"Bouvier","year":"1990","journal-title":"Biochemistry"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0885","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1111\/j.1432-1033.1987.tb11013.x","article-title":"The macrophage-attachment glycoprotein gp63 is the predominant C3-acceptor site on Leishmania mexicana promastigotes","volume":"164","author":"Russell","year":"1987","journal-title":"Eur. J. Biochem."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0890","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1128\/IAI.71.2.1008-1010.2003","article-title":"Migration through the extracellular matrix by the parasitic protozoan leishmania is enhanced by surface metalloprotease gp63","volume":"71","author":"McGwire Bradford","year":"2003","journal-title":"Infect. Immun."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0895","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1111\/j.1365-2249.2008.03687.x","article-title":"Leishmania surface protein gp63 binds directly to human natural killer cells and inhibits proliferation","volume":"153","author":"Lieke","year":"2008","journal-title":"Clin. Exp. Immunol."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0900","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S0166-6851(02)00030-0","article-title":"Biosynthesis of the major surface protease GP63 of Leishmania chagasi","volume":"121","author":"Yao","year":"2002","journal-title":"Mol. Biochem. Parasitol."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0905","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1002\/eji.1830270430","article-title":"Epitope cleavage by Leishmania endopeptidase(s) limits the efficiency of the exogenous pathway of major histocompatibility complex class I-associated antigen presentation","volume":"27","author":"Garcia","year":"1997","journal-title":"Eur. J. Immunol."},{"issue":"36","key":"10.1016\/j.intimp.2022.109649_b0910","doi-asserted-by":"crossref","first-page":"25411","DOI":"10.1074\/jbc.274.36.25411","article-title":"MARCKS-related protein (MRP) is a substrate for the Leishmania major surface protease leishmanolysin (gp63)","volume":"274","author":"Corradin","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0915","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."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0920","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1002\/eji.200737586","article-title":"A novel form of NF-kappaB is induced by Leishmania infection: involvement in macrophage gene expression","volume":"38","author":"Gregory","year":"2008","journal-title":"Eur. J. Immunol."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0925","doi-asserted-by":"crossref","first-page":"e1004776","DOI":"10.1371\/journal.ppat.1004776","article-title":"Impact of Leishmania infection on host macrophage nuclear physiology and nucleopore complex integrity","volume":"11","author":"Isnard","year":"2015","journal-title":"PLoS Pathog."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0930","doi-asserted-by":"crossref","first-page":"33","DOI":"10.3390\/vetsci8020033","article-title":"Insights into leishmania molecules and their potential contribution to the virulence of the parasite","volume":"8","author":"Elmahallawy","year":"2021","journal-title":"Veterinary sci."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0935","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1475-9292-1-1","article-title":"Molecular determinants and regulation of Leishmania virulence","volume":"1","author":"Chang","year":"2002","journal-title":"Kinetoplastid biol. Dis."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0940","doi-asserted-by":"crossref","first-page":"e1543","DOI":"10.1371\/journal.pntd.0001543","article-title":"Glycoinositolphospholipids from Leishmania braziliensis and L. infantum: modulation of innate immune system and variations in carbohydrate structure","volume":"6","author":"Assis","year":"2012","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0945","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1194\/jlr.M200296-JLR200","article-title":"Alkylacylglycerolipid domain of GPI molecules of Leishmania is responsible for inhibition of PKC-mediated c-fos expression","volume":"44","author":"Chawla","year":"2003","journal-title":"J. Lipid Res."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b0950","doi-asserted-by":"crossref","first-page":"470","DOI":"10.4049\/jimmunol.0900265","article-title":"Immunization with the DNA-Encoding N-Terminal Domain of Proteophosphoglycan of Leishmania donovani Generates Th1-Type immunoprotective response against experimental visceral leishmaniasis","volume":"183","author":"Samant","year":"2009","journal-title":"J. Immunol."},{"issue":"9","key":"10.1016\/j.intimp.2022.109649_b0955","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1017\/S0031182007002569","article-title":"Proteophosphoglycan is differentially expressed in sodium stibogluconate-sensitive and resistant Indian clinical isolates of Leishmania donovani","volume":"134","author":"Samant","year":"2007","journal-title":"Parasitology"},{"key":"10.1016\/j.intimp.2022.109649_b0960","doi-asserted-by":"crossref","DOI":"10.1155\/2012\/650874","article-title":"Adenosine and Immune Imbalance in Visceral Leishmaniasis: the Possible Role of Ectonucleotidases","volume":"2012","author":"Paletta-Silva","year":"2012","journal-title":"J. Trop. Med."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b0965","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.bj.2016.08.004","article-title":"Purinergic signaling and infection by Leishmania: a new approach to evasion of the immune response","volume":"39","author":"Figueiredo","year":"2016","journal-title":"Biomed. J."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0970","doi-asserted-by":"crossref","first-page":"5910","DOI":"10.1128\/IAI.71.10.5910-5920.2003","article-title":"Iron superoxide dismutases targeted to the glycosomes of Leishmania chagasi are important for survival","volume":"71","author":"Plewes","year":"2003","journal-title":"Infect. Immun."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b0975","doi-asserted-by":"crossref","first-page":"e0006921","DOI":"10.1371\/journal.pntd.0006921","article-title":"SODB1 is essential for Leishmania major infection of macrophages and pathogenesis in mice","volume":"12","author":"Davenport","year":"2018","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"51","key":"10.1016\/j.intimp.2022.109649_b0980","doi-asserted-by":"crossref","first-page":"50190","DOI":"10.1074\/jbc.M209210200","article-title":"Leishmania EF-1\u03b1 Activates the Src Homology 2 domain containing tyrosine phosphatase SHP-1 Leading to Macrophage Deactivation","volume":"277","author":"Nandan","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0985","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.bbrc.2007.10.065","article-title":"Identification of leishmania fructose-1,6-bisphosphate aldolase as a novel activator of host macrophage Src homology 2 domain containing protein tyrosine phosphatase SHP-1","volume":"364","author":"Nandan","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b0990","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/0014-4894(89)90115-X","article-title":"Leishmania donovani: immunochemical localization and secretory mechanism of soluble acid phosphatase","volume":"68","author":"Bates","year":"1989","journal-title":"Exp. Parasitol."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b0995","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0166-6851(86)90026-5","article-title":"Hydrolysis of phosphoproteins and inositol phosphates by cell surface phosphatase of Leishmania donovani","volume":"20","author":"Das","year":"1986","journal-title":"Mol. Biochem. Parasitol."},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b1000","first-page":"10816","article-title":"Role of peroxidoxins in Leishmania chagasi survival","volume":"278","author":"Barr","year":"2003","journal-title":"Evidence of an enzymatic defense against nitrosative stress, J. Biol. Chem."},{"issue":"36","key":"10.1016\/j.intimp.2022.109649_b1005","first-page":"34279","article-title":"Cloning and characterization of three differentially expressed peroxidoxin genes from Leishmania chagasi","volume":"276","author":"Barr","year":"2001","journal-title":"Evidence for an enzymatic detoxification of hydroxyl radicals, J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.intimp.2022.109649_b1010","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."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b1015","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1111\/j.1365-2958.2008.06154.x","article-title":"Crucial role of cytosolic tryparedoxin peroxidase in Leishmania donovani survival, drug response and virulence","volume":"68","author":"Iyer","year":"2008","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.intimp.2022.109649_b1020","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1042\/bj3050307","article-title":"Isolation and structural characterization of the Leishmania donovani kinetoplastid membrane protein-11, a major immunoreactive membrane glycoprotein","volume":"305","author":"Jardim","year":"1995","journal-title":"Biochem. J."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b1025","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1074\/jbc.M110.138313","article-title":"The oligopeptidase B of Leishmania regulates parasite enolase and immune evasion","volume":"286","author":"Swenerton","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"41","key":"10.1016\/j.intimp.2022.109649_b1030","doi-asserted-by":"crossref","first-page":"31120","DOI":"10.1074\/jbc.M110.114462","article-title":"Leishmania subtilisin is a maturase for the trypanothione reductase system and contributes to disease pathology","volume":"285","author":"Swenerton","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b1035","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1128\/CVI.00358-09","article-title":"In situ immunolocalization and stage-dependent expression of a secretory serine protease in Leishmania donovani and its role as a vaccine candidate","volume":"17","author":"Choudhury","year":"2010","journal-title":"Clin. vaccine immunol. CVI"},{"issue":"11","key":"10.1016\/j.intimp.2022.109649_b1040","doi-asserted-by":"crossref","first-page":"e79951","DOI":"10.1371\/journal.pone.0079951","article-title":"Cathepsin B gene disruption induced Leishmania donovani proteome remodeling implies cathepsin B role in secretome regulation","volume":"8","author":"Gerbaba","year":"2013","journal-title":"PLoS One"},{"issue":"28","key":"10.1016\/j.intimp.2022.109649_b1045","first-page":"25305","article-title":"Functional analysis of cathepsin B-like cysteine proteases from Leishmania donovani complex","volume":"277","author":"Somanna","year":"2002","journal-title":"Evidence for the activation of latent transforming growth factor beta, J. Biol. Chem."},{"key":"10.1016\/j.intimp.2022.109649_b1050","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1146\/annurev.mi.44.100190.002435","article-title":"Molecular determinants of Leishmania virulence","volume":"44","author":"Chang","year":"1990","journal-title":"Annu. Rev. Microbiol."},{"issue":"11","key":"10.1016\/j.intimp.2022.109649_b1055","doi-asserted-by":"crossref","first-page":"5625","DOI":"10.4049\/jimmunol.170.11.5625","article-title":"Dendritic cell-based immunotherapy combined with antimony-based chemotherapy cures established murine visceral leishmaniasis","volume":"170","author":"Ghosh","year":"2003","journal-title":"J. Immunol."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b1060","doi-asserted-by":"crossref","first-page":"666","DOI":"10.4269\/ajtmh.1993.48.666","article-title":"Immunochemotherapy for visceral leishmaniasis: a controlled pilot trial of antimony versus antimony plus interferon-gamma","volume":"48","author":"Squires","year":"1993","journal-title":"Am. J. Trop. Med. Hyg."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b1065","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1056\/NEJM199001043220104","article-title":"Treatment of visceral leishmaniasis with pentavalent antimony and interferon gamma","volume":"322","author":"Badaro","year":"1990","journal-title":"N. Engl. J. Med."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b1070","doi-asserted-by":"crossref","first-page":"1627","DOI":"10.1093\/infdis\/172.6.1627","article-title":"Effect of treatment with interferon-gamma alone in visceral leishmaniasis","volume":"172","author":"Sundar","year":"1995","journal-title":"J. Infect. Dis."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b1075","doi-asserted-by":"crossref","first-page":"3903","DOI":"10.1128\/IAI.73.7.3903-3911.2005","article-title":"Antagonizing deactivating cytokines to enhance host defense and chemotherapy in experimental visceral leishmaniasis","volume":"73","author":"Murray","year":"2005","journal-title":"Infect. Immun."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b1080","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1084\/jem.181.1.387","article-title":"Interleukin 12 is effective treatment for an established systemic intracellular infection: experimental visceral leishmaniasis","volume":"181","author":"Murray","year":"1995","journal-title":"J. Exp. Med."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b1085","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1086\/315890","article-title":"Interleukin-12 regulates the response to chemotherapy in experimental visceral leishmaniasis","volume":"182","author":"Murray","year":"2000","journal-title":"J. Infect Dis."},{"key":"10.1016\/j.intimp.2022.109649_b1090","doi-asserted-by":"crossref","unstructured":"R.P, Almeida, J, Brito, P.L, Machado, D.E.J, AR, A, Schriefer, L.H, Guimar\u00e3es, E.M, Carvalho, Successful treatment of refractory cutaneous leishmaniasis with GM-CSF and antimonials, Am J Trop Med Hyg 73(1) (2005) 79-81.","DOI":"10.4269\/ajtmh.2005.73.79"},{"key":"10.1016\/j.intimp.2022.109649_b1095","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1146\/annurev.immunol.19.1.683","article-title":"Interleukin-10 and the interleukin-10 receptor","volume":"19","author":"Moore","year":"2001","journal-title":"Annu. Rev. Immunol."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b1100","doi-asserted-by":"crossref","first-page":"2848","DOI":"10.1002\/1521-4141(2001010)31:10<2848::AID-IMMU2848>3.0.CO;2-T","article-title":"IL-10 mediates susceptibility to Leishmania donovani infection","volume":"31","author":"Murphy","year":"2001","journal-title":"Eur. J. Immunol."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b1105","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/j.actatropica.2004.11.008","article-title":"Interleukin 10 receptor blockade\u2013pentavalent antimony treatment in experimental visceral leishmaniasis","volume":"93","author":"Murray","year":"2005","journal-title":"Acta Trop."},{"issue":"8","key":"10.1016\/j.intimp.2022.109649_b1110","doi-asserted-by":"crossref","first-page":"2513","DOI":"10.1128\/AAC.47.8.2513-2517.2003","article-title":"Immunoenhancement combined with amphotericin B as treatment for experimental visceral leishmaniasis","volume":"47","author":"Murray","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"issue":"7","key":"10.1016\/j.intimp.2022.109649_b1115","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1093\/infdis\/jir461","article-title":"IL-10 neutralization promotes parasite clearance in splenic aspirate cells from patients with visceral leishmaniasis","volume":"204","author":"Gautam","year":"2011","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.intimp.2022.109649_b1120","unstructured":"M.O, Emeje, I.C, Obidike, E.I, Akpabio, S.I, Ofoefule, Nanotechnology in Drug Delivery, in: A.D. Sezer (Ed.), Recent Advances in Novel Drug Carrier Systems, IntechOpen 2012, pp. 69-106."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b1125","doi-asserted-by":"crossref","first-page":"387","DOI":"10.2217\/nnm.14.116","article-title":"Surface functionalization of polymeric nanospheres modulates macrophage activation: relevance in leishmaniasis therapy","volume":"10","author":"Barros","year":"2015","journal-title":"Nanomedicine (Lond.)"},{"key":"10.1016\/j.intimp.2022.109649_b1130","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.colsurfb.2015.04.013","article-title":"Therapeutic efficacy of artemisinin-loaded nanoparticles in experimental visceral leishmaniasis","volume":"130","author":"Want","year":"2015","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"10.1016\/j.intimp.2022.109649_b1135","doi-asserted-by":"crossref","first-page":"2189","DOI":"10.2147\/IJN.S106548","article-title":"Nanoliposomal artemisinin for the treatment of murine visceral leishmaniasis","volume":"12","author":"Want","year":"2017","journal-title":"Int. J. Nanomed."},{"key":"10.1016\/j.intimp.2022.109649_b1140","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.ijbiomac.2015.04.043","article-title":"Chondroitin nanocapsules enhanced doxorubicin induced apoptosis against leishmaniasis via Th1 immune response","volume":"79","author":"Chaurasia","year":"2015","journal-title":"Int. J. Biol. Macromol."},{"issue":"8","key":"10.1016\/j.intimp.2022.109649_b1145","first-page":"2663","article-title":"Overexpressed macrophage mannose receptor targeted nanocapsules- mediated cargo delivery approach for eradication of resident parasite","volume":"32","author":"Asthana","year":"2015","journal-title":"In Vitro and In Vivo Studies, Pharm. Res."},{"key":"10.1016\/j.intimp.2022.109649_b1150","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1016\/j.carbpol.2013.10.044","article-title":"Mannose-conjugated chitosan nanoparticles loaded with rifampicin for the treatment of visceral leishmaniasis","volume":"101","author":"Chaubey","year":"2014","journal-title":"Carbohydr. Polym."},{"key":"10.1016\/j.intimp.2022.109649_b1155","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.ijbiomac.2017.12.143","article-title":"Mannose-conjugated curcumin-chitosan nanoparticles: Efficacy and toxicity assessments against Leishmania donovani","volume":"111","author":"Chaubey","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"issue":"10","key":"10.1016\/j.intimp.2022.109649_b1160","doi-asserted-by":"crossref","first-page":"4608","DOI":"10.1128\/AAC.02343-12","article-title":"Antileishmanial activity, uptake, and biodistribution of an amphotericin B and poly(\u03b1-Glutamic Acid) complex","volume":"57","author":"Mohamed-Ahmed","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b1165","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1093\/jac\/dkt320","article-title":"Liposomal resiquimod for the treatment of Leishmania donovani infection","volume":"69","author":"Peine","year":"2014","journal-title":"J. Antimicrob. Chemother."},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b1170","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1021\/mp3005098","article-title":"Electrospray encapsulation of toll-like receptor agonist resiquimod in polymer microparticles for the treatment of visceral leishmaniasis","volume":"10","author":"Duong","year":"2013","journal-title":"Mol. Pharm."},{"issue":"4","key":"10.1016\/j.intimp.2022.109649_b1175","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1166\/jbn.2012.1414","article-title":"Evaluating the potential of polyester nanoparticles for per oral delivery of amphotericin B in treating visceral leishmaniasis","volume":"8","author":"Italia","year":"2012","journal-title":"J. Biomed. Nanotechnol."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b1180","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1016\/j.nano.2013.12.013","article-title":"Crucial CD8(+) T-lymphocyte cytotoxic role in amphotericin B nanospheres efficacy against experimental visceral leishmaniasis","volume":"10","author":"Costa Lima","year":"2014","journal-title":"Nanomedicine"},{"issue":"12","key":"10.1016\/j.intimp.2022.109649_b1185","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.2217\/nnm.12.74","article-title":"Characterization and evaluation of BNIPDaoct-loaded PLGA nanoparticles for visceral leishmaniasis: in vitro and in vivo studies","volume":"7","author":"Costa Lima","year":"2012","journal-title":"Nanomedicine (Lond.)"},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b1190","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1517\/17425247.2014.889678","article-title":"Development of targeted 1,2-diacyl-sn-glycero-3-phospho-l-serine-coated gelatin nanoparticles loaded with amphotericin B for improved in vitro and in vivo effect in leishmaniasis","volume":"11","author":"Khatik","year":"2014","journal-title":"Expert Opin. Drug Deliv."},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b1195","doi-asserted-by":"crossref","first-page":"2479","DOI":"10.1128\/AAC.04213-14","article-title":"Surface-engineered dendrimeric nanoconjugates for macrophage-targeted delivery of amphotericin B: formulation development and in vitro and in vivo evaluation","volume":"59","author":"Jain","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"issue":"2","key":"10.1016\/j.intimp.2022.109649_b1200","doi-asserted-by":"crossref","first-page":"99","DOI":"10.2217\/nnm-2016-0325","article-title":"Development of mannose-anchored thiolated amphotericin B nanocarriers for treatment of visceral leishmaniasis","volume":"12","author":"Shahnaz","year":"2017","journal-title":"Nanomedicine (Lond.)"},{"issue":"5","key":"10.1016\/j.intimp.2022.109649_b1205","doi-asserted-by":"crossref","first-page":"e0177372","DOI":"10.1371\/journal.pone.0177372","article-title":"HAT2 mediates histone H4K4 acetylation and affects micrococcal nuclease sensitivity of chromatin in Leishmania donovani","volume":"12","author":"Jha","year":"2017","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b1210","doi-asserted-by":"crossref","first-page":"27510","DOI":"10.1038\/srep27510","article-title":"Histone acetyltransferase HAT4 modulates navigation across G2\/M and re-entry into G1 in Leishmania donovani","volume":"6","author":"Yadav","year":"2016","journal-title":"Sci. Rep."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b1215","doi-asserted-by":"crossref","first-page":"25","DOI":"10.2217\/nnm-2017-0255","article-title":"Mannosylated thiolated polyethylenimine nanoparticles for the enhanced efficacy of antimonial drug against Leishmaniasis","volume":"13","author":"Sarwar","year":"2018","journal-title":"Nanomedicine (Lond.)"},{"issue":"3","key":"10.1016\/j.intimp.2022.109649_b1220","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1021\/ml1002629","article-title":"Inhibitory effect of silver nanoparticles on trypanothione reductase activity and leishmania infantum proliferation","volume":"2","author":"Baiocco","year":"2011","journal-title":"ACS Med. Chem. Lett."},{"issue":"47","key":"10.1016\/j.intimp.2022.109649_b1225","doi-asserted-by":"crossref","first-page":"20055","DOI":"10.1039\/C5NR06630A","article-title":"A novel self-assembled sandwich nanomedicine for NIR-responsive release of NO","volume":"7","author":"Fan","year":"2015","journal-title":"Nanoscale"},{"key":"10.1016\/j.intimp.2022.109649_b1230","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.intimp.2018.03.012","article-title":"Enhancement of Th1 immune response against Leishmania cysteine peptidase A, B by PLGA nanoparticle","volume":"59","author":"Noormehr","year":"2018","journal-title":"Int. Immunopharmacol."},{"key":"10.1016\/j.intimp.2022.109649_b1235","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.biomaterials.2016.09.004","article-title":"Immunomodulatory nanoparticles ameliorate disease in the Leishmania (Viannia) panamensis mouse model","volume":"108","author":"Siefert","year":"2016","journal-title":"Biomaterials"},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b1240","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1039\/c2ib20117h","article-title":"Common pitfalls in nanotechnology: lessons learned from NCI's Nanotechnology Characterization Laboratory","volume":"5","author":"Crist","year":"2013","journal-title":"Integr Biol (Camb)"},{"key":"10.1016\/j.intimp.2022.109649_b1245","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.taap.2016.02.014","article-title":"Nanotoxicology ten years later: Lights and shadows","volume":"299","author":"Shvedova","year":"2016","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.intimp.2022.109649_b1250","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.taap.2016.01.002","article-title":"Kagan, Enzymatic oxidative biodegradation of nanoparticles: Mechanisms, significance and applications","volume":"299","author":"Vlasova","year":"2016","journal-title":"Toxicol. Appl. Pharmacol."},{"issue":"22","key":"10.1016\/j.intimp.2022.109649_b1255","doi-asserted-by":"crossref","first-page":"11305","DOI":"10.1021\/cr500365f","article-title":"Recent developments in drug discovery for leishmaniasis and human African trypanosomiasis","volume":"114","author":"Nagle","year":"2014","journal-title":"Chem. Rev."},{"issue":"119","key":"10.1016\/j.intimp.2022.109649_b1260","doi-asserted-by":"crossref","first-page":"119re111","DOI":"10.1126\/scitranslmed.3003326","article-title":"The anti-trypanosome drug fexinidazole shows potential for treating visceral leishmaniasis","volume":"4","author":"Wyllie","year":"2012","journal-title":"Sci. Transl. Med."},{"issue":"7619","key":"10.1016\/j.intimp.2022.109649_b1265","first-page":"229","article-title":"Proteasome inhibition for treatment of leishmaniasis","volume":"537","author":"Khare","year":"2016","journal-title":"Chagas dis. sleeping sickness, Nat."},{"key":"10.1016\/j.intimp.2022.109649_b1270","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2020.579891","article-title":"Use of natural products in leishmaniasis chemotherapy: an overview","volume":"8","author":"Gervazoni","year":"2020","journal-title":"Front. Chem."},{"key":"10.1016\/j.intimp.2022.109649_b1275","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2021.655584","article-title":"Green Approach: \u201ca Forwarding Step for Curing Leishmaniasis-A Neglected Tropical Disease\u201d","volume":"8","author":"Sharma","year":"2021","journal-title":"Front. Mol. Biosci."},{"issue":"6","key":"10.1016\/j.intimp.2022.109649_b1280","doi-asserted-by":"crossref","first-page":"780","DOI":"10.4103\/ijmr.IJMR_959_16","article-title":"Cedrus deodara: In vitro antileishmanial efficacy & immumomodulatory activity","volume":"146","author":"Narayan","year":"2017","journal-title":"Indian J. Med. Res."},{"issue":"1","key":"10.1016\/j.intimp.2022.109649_b1285","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s40249-021-00796-6","article-title":"Potentials of marine natural products against malaria, leishmaniasis, and trypanosomiasis parasites: a review of recent articles","volume":"10","author":"Nweze","year":"2021","journal-title":"Infect. Dis. Poverty"},{"key":"10.1016\/j.intimp.2022.109649_b1290","doi-asserted-by":"crossref","DOI":"10.1016\/j.intimp.2022.109281","article-title":"Oceanimonas sp. BPMS22-derived protein protease inhibitor induces anti-leishmanial immune responses through macrophage M2 to M1 repolarization","volume":"112","author":"Jayaraman","year":"2022","journal-title":"Int. Immunopharmacol."}],"container-title":["International Immunopharmacology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1567576922011341?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1567576922011341?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,1,9]],"date-time":"2025-01-09T14:08:05Z","timestamp":1736431685000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1567576922011341"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,2]]},"references-count":258,"alternative-id":["S1567576922011341"],"URL":"https:\/\/doi.org\/10.1016\/j.intimp.2022.109649","relation":{},"ISSN":["1567-5769"],"issn-type":[{"value":"1567-5769","type":"print"}],"subject":[],"published":{"date-parts":[[2023,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Emerging strategies and challenges of molecular therapeutics in antileishmanial drug development","name":"articletitle","label":"Article Title"},{"value":"International Immunopharmacology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.intimp.2022.109649","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"109649"}}