{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T16:01:07Z","timestamp":1792425667706,"version":"4.5.0"},"reference-count":68,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"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":["Biochimie"],"published-print":{"date-parts":[[2023,4]]},"DOI":"10.1016\/j.biochi.2022.11.015","type":"journal-article","created":{"date-parts":[[2022,12,5]],"date-time":"2022-12-05T02:40:57Z","timestamp":1670208057000},"page":"75-82","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"special_numbering":"C","title":["The glycoprotein gp63\u2013 a potential pan drug target for developing new antileishmanial agents"],"prefix":"10.1016","volume":"207","author":[{"given":"Namrata","family":"Devsani","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Divya","family":"Vemula","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1930-1722","authenticated-orcid":false,"given":"Vasundhra","family":"Bhandari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"9185","key":"10.1016\/j.biochi.2022.11.015_bib1","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":"5","key":"10.1016\/j.biochi.2022.11.015_bib2","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0035671","article-title":"WHO Leishmaniasis Control Team. Leishmaniasis worldwide and global estimates of its incidence","volume":"7","author":"Alvar","year":"2012","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.biochi.2022.11.015_bib3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12864-019-5465-z","article-title":"In silico characterization of multiple genes encoding the gp63 virulence protein from Leishmania braziliensis: identification of sources of variation and putative roles in immune evasion","volume":"20","author":"Castro Neto","year":"2019","journal-title":"BMC Genom."},{"issue":"12","key":"10.1016\/j.biochi.2022.11.015_bib4","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0262158","article-title":"The role of Leishmania gp63 in the modulation of the innate inflammatory response to Leishmania major infection","volume":"16","author":"Chan","year":"2021","journal-title":"PLoS One"},{"issue":"6","key":"10.1016\/j.biochi.2022.11.015_bib5","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1016\/j.micinf.2006.01.006","article-title":"Down-regulation of gp63 level in Leishmania amazonensis promastigotes reduces their infectivity in BALB\/c mice","volume":"8","author":"Thiakaki","year":"2006","journal-title":"Microb. Infect."},{"issue":"3","key":"10.1016\/j.biochi.2022.11.015_bib6","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/0014-4894(90)90034-A","article-title":"Leishmania major: expression and gene structure of the glycoprotein 63 molecule in virulent and avirulent clones and strains","volume":"71","author":"Murray","year":"1990","journal-title":"Exp. Parasitol."},{"issue":"7","key":"10.1016\/j.biochi.2022.11.015_bib7","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/ng2053","article-title":"Comparative genomic analysis of three leishmania species that cause diverse human disease","volume":"39","author":"Peacock","year":"2007","journal-title":"Nat. Genet."},{"issue":"14","key":"10.1016\/j.biochi.2022.11.015_bib8","doi-asserted-by":"crossref","first-page":"7903","DOI":"10.1074\/jbc.271.14.7903","volume":"271","author":"McGwire","year":"1996","journal-title":"J.\u00a0Biol. Chem."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib9","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/0166-6851(91)90113-K","article-title":"Heterogeneity of the genes encoding the major surface glycoprotein of Leishmania donovani","volume":"48","author":"Webb","year":"1991","journal-title":"Mol. Biochem. Parasitol."},{"issue":"3","key":"10.1016\/j.biochi.2022.11.015_bib10","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1042\/BST20191142","article-title":"Mammalian GPI-anchor modifications and the enzymes involved","volume":"48","author":"Liu","year":"2020","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.biochi.2022.11.015_bib11","volume":"vol. 4","author":"Stillwell","year":"2016"},{"issue":"S1","key":"10.1016\/j.biochi.2022.11.015_bib12","doi-asserted-by":"crossref","first-page":"S45","DOI":"10.1017\/S0031182000075715","article-title":"Glycosyl-phosphatidylinositol molecules of the parasite and the host","volume":"108","author":"Ferguson","year":"1994","journal-title":"Parasitology"},{"issue":"1","key":"10.1016\/j.biochi.2022.11.015_bib13","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/0166-6851(90)90205-Z","article-title":"The glycoinositolphospholipid profiles of two Leishmania major strains that differ in lipophosphoglycan expression","volume":"38","author":"McConville","year":"1990","journal-title":"Mol. Biochem. Parasitol."},{"issue":"13","key":"10.1016\/j.biochi.2022.11.015_bib14","doi-asserted-by":"crossref","first-page":"7385","DOI":"10.1016\/S0021-9258(19)39125-2","article-title":"Structures of the glycoinositolphospholipids from Leishmania major. A family of novel galactofuranose-containing glycolipids","volume":"265","author":"McConville","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"issue":"23","key":"10.1016\/j.biochi.2022.11.015_bib15","doi-asserted-by":"crossref","first-page":"15170","DOI":"10.1016\/S0021-9258(18)98600-X","article-title":"Developmental changes in the glycosylated phosphatidylinositols of Leishmania donovani. Characterization of the promastigote and amastigote glycolipids","volume":"266","author":"McConville","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"issue":"Pt 2","key":"10.1016\/j.biochi.2022.11.015_bib16","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1042\/bj2940305","article-title":"The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes","volume":"294","author":"McConville","year":"1993","journal-title":"Biochem. J."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib17","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1042\/bj2950555","article-title":"Characterization of glycoinositol phospholipids in the amastigote stage of the protozoan parasite Leishmania major","volume":"295","author":"Schneider","year":"1993","journal-title":"Biochem. J."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib18","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1042\/bj3040603","article-title":"Glycoinositol-phospholipid profiles of four serotypically distinct Old World Leishmania strains","volume":"304","author":"Schneider","year":"1994","journal-title":"Biochem. J."},{"issue":"9","key":"10.1016\/j.biochi.2022.11.015_bib19","doi-asserted-by":"crossref","first-page":"2471","DOI":"10.1242\/jcs.107.9.2471","article-title":"Surface antigens of Leishmania mexicana amastigotes: characterization of glycoinositol phospholipids and a macrophage-derived glycosphingolipid","volume":"107","author":"Winter","year":"1994","journal-title":"J.\u00a0Cell Sci."},{"issue":"29","key":"10.1016\/j.biochi.2022.11.015_bib20","doi-asserted-by":"crossref","first-page":"15504","DOI":"10.1016\/S0021-9258(17)36283-X","article-title":"Identification and purification of membrane and soluble forms of the major surface protein of Leishmania promastigotes","volume":"260","author":"Bouvier","year":"1985","journal-title":"J.\u00a0Biol. Chem."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib21","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/0014-4894(92)90179-E","article-title":"Leishmania major: differential regulation of the surface metalloprotease in amastigote and promastigote stages","volume":"75","author":"Schneider","year":"1992","journal-title":"Exp. Parasitol."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib22","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1002\/prot.21009","article-title":"Molecular dynamics simulation of Leishmania major surface metalloprotease gp63 (leishmanolysin)","volume":"64","author":"Bianchini","year":"2006","journal-title":"Proteins Struct. Funct. Genet."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib23","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/0014-4894(91)90137-L","article-title":"The comparative fine structure and surface glycoconjugate expression of three life stages of Leishmania major","volume":"72","author":"Pimenta","year":"1991","journal-title":"Exp. Parasitol."},{"issue":"4","key":"10.1016\/j.biochi.2022.11.015_bib24","doi-asserted-by":"crossref","first-page":"1266","DOI":"10.1007\/s12639-015-0665-1","article-title":"In silico sequence analysis, homology modeling and function annotation of leishmanolysin from Leishmania donovani","volume":"40","author":"Waghmare","year":"2016","journal-title":"J.\u00a0Parasit. Dis."},{"issue":"8","key":"10.1016\/j.biochi.2022.11.015_bib25","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1016\/S0969-2126(98)00104-X","article-title":"The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63)","volume":"6","author":"Schlagenhauf","year":"1998","journal-title":"Structure"},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib26","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/0167-4838(95)00155-5","article-title":"Analysis of the active site and activation mechanism of the Leishmania surface metalloproteinase gp63","volume":"1253","author":"Macdonald","year":"1995","journal-title":"Biochim. Biophys. Acta Protein Struct. Mol. Enzymol."},{"issue":"5","key":"10.1016\/j.biochi.2022.11.015_bib27","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1002\/pro.5560040502","article-title":"The metzincins\u2014topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc-peptidases","volume":"4","author":"St\u00f6cker","year":"1995","journal-title":"Protein Sci."},{"issue":"12","key":"10.1016\/j.biochi.2022.11.015_bib28","doi-asserted-by":"crossref","first-page":"1876","DOI":"10.1016\/j.biochi.2010.07.014","article-title":"The effect of C-terminal domain deletion on the catalytic activity of Leishmania donovani surface proteinase gp63: role of Ser446 in proteolysis","volume":"92","author":"Mazumder","year":"2010","journal-title":"Biochimie"},{"issue":"3","key":"10.1016\/j.biochi.2022.11.015_bib29","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/0959-440X(95)80101-4","article-title":"Structural features of a superfamily of zinc-endopeptidases: the metzincins","volume":"5","author":"St\u00f6cker","year":"1995","journal-title":"Curr. Opin. Struct. Biol."},{"issue":"6382","key":"10.1016\/j.biochi.2022.11.015_bib30","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1038\/358164a0","article-title":"Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases","volume":"358","author":"Bode","year":"1992","journal-title":"Nature"},{"issue":"10","key":"10.1016\/j.biochi.2022.11.015_bib31","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.pt.2012.07.002","article-title":"Sink or swim: lipid rafts in parasite pathogenesis","volume":"28","author":"Goldston","year":"2012","journal-title":"Trends Parasitol."},{"key":"10.1016\/j.biochi.2022.11.015_bib32","series-title":"Essentials of Glycobiology","first-page":"137","article-title":"Glycosylphosphatidylinositol","author":"Ferguson","year":"2015"},{"issue":"9","key":"10.1016\/j.biochi.2022.11.015_bib33","doi-asserted-by":"crossref","first-page":"4477","DOI":"10.1128\/IAI.67.9.4477-4484.1999","article-title":"Interaction of Leishmania gp63 with cellular receptors for fibronectin","volume":"67","author":"Brittingham","year":"1999","journal-title":"Infect. Immun."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib34","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/0166-6851(91)90113-K","article-title":"Heterogeneity of the genes encoding the major surface glycoprotein of Leishmania donovani","volume":"48","author":"Webb","year":"1991","journal-title":"Mol. Biochem. Parasitol."},{"issue":"4","key":"10.1016\/j.biochi.2022.11.015_bib35","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/j.micpath.2004.11.002","article-title":"Immunopathogenesis of infection with the visceralizing Leishmania species","volume":"38","author":"Wilson","year":"2005","journal-title":"Microb. Pathog."},{"issue":"6","key":"10.1016\/j.biochi.2022.11.015_bib36","doi-asserted-by":"crossref","first-page":"1926","DOI":"10.4049\/jimmunol.138.6.1926","article-title":"Parasite-accessory cell interactions in murine leishmaniasis. II. Leishmania donovani suppresses macrophage expression of class I and class II major histocompatibility complex gene products","volume":"138","author":"Reiner","year":"1987","journal-title":"J.\u00a0Immunol."},{"issue":"6","key":"10.1016\/j.biochi.2022.11.015_bib37","doi-asserted-by":"crossref","first-page":"1914","DOI":"10.1172\/JCI114654","volume":"85","author":"Reiner","year":"1990","journal-title":"J.\u00a0Clin. Investig."},{"issue":"6","key":"10.1016\/j.biochi.2022.11.015_bib38","doi-asserted-by":"crossref","first-page":"3102","DOI":"10.4049\/jimmunol.155.6.3102","article-title":"Role of the Leishmania surface protease gp63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis","volume":"155","author":"Brittingham","year":"1995","journal-title":"J.\u00a0Immunol."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib39","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.jaci.2005.05.036","article-title":"Innate immune responses to infection","volume":"116","author":"Tosi","year":"2005","journal-title":"J.\u00a0Allergy Clin. Immunol."},{"issue":"1","key":"10.1016\/j.biochi.2022.11.015_bib40","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":"5","key":"10.1016\/j.biochi.2022.11.015_bib41","doi-asserted-by":"crossref","first-page":"2582","DOI":"10.1128\/IAI.72.5.2582-2589.2004","article-title":"Leishmania major amastigotes induce p50\/c-Rel NF-\u03ba\u0392 transcription factor in human macrophages: involvement in cytokine synthesis","volume":"72","author":"Guizani-Tabbane","year":"2004","journal-title":"Infect. Immun."},{"issue":"4","key":"10.1016\/j.biochi.2022.11.015_bib42","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1002\/eji.200737586","article-title":"A\u00a0novel form of NF-\u03baB is induced by Leishmania infection: involvement in macrophage gene expression","volume":"38","author":"Gregory","year":"2008","journal-title":"Eur. J. Immunol."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib43","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":"2","key":"10.1016\/j.biochi.2022.11.015_bib44","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":"12","key":"10.1016\/j.biochi.2022.11.015_bib45","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1016\/0169-4758(93)90105-O","article-title":"The lipophosphoglycan of Leishmania and macrophage protein kinase C","volume":"9","author":"Descoteaux","year":"1993","journal-title":"Parasitol. today"},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib46","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/0006-291X(87)90926-0","article-title":"Inhibition of protein kinase C activity by the Leishmania donovani lipophosphoglycan","volume":"148","author":"McNeely","year":"1987","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"12","key":"10.1016\/j.biochi.2022.11.015_bib47","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1371\/journal.pntd.0000305","article-title":"Leishmania-induced IRAK-1 inactivation is mediated by SHP-1 interacting with an evolutionarily conserved KTIM motif","volume":"2","author":"Abu-Dayyeh","year":"2008","journal-title":"PLoS Neglected Trop. Dis."},{"issue":"10","key":"10.1016\/j.biochi.2022.11.015_bib48","doi-asserted-by":"crossref","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":"11","key":"10.1016\/j.biochi.2022.11.015_bib49","doi-asserted-by":"crossref","first-page":"6893","DOI":"10.1074\/jbc.M805861200","article-title":"The Leishmania surface protease gp63 cleaves multiple intracellular proteins and actively participates in p38 mitogen-activated protein kinase inactivation","volume":"284","author":"Hall\u00e9","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"issue":"1","key":"10.1016\/j.biochi.2022.11.015_bib50","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1017\/S0031182000007125","article-title":"gp63 gene polymorphism and population structure of Leishmania donovani. complex: influence of the host selection pressure?","volume":"122","author":"Guerbouj","year":"2001","journal-title":"Parasitology"},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib51","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0014644","article-title":"Potency, efficacy and durability of DNA\/DNA, DNA\/protein and protein\/protein based vaccination using gp63 against Leishmania donovani in BALB\/c mice","volume":"6","author":"Mazumder","year":"2011","journal-title":"PLoS One"},{"issue":"6","key":"10.1016\/j.biochi.2022.11.015_bib52","doi-asserted-by":"crossref","first-page":"541","DOI":"10.2174\/1574893613666180828095737","article-title":"A\u00a0therapeutic approach against leishmania donovani by predicting RNAi molecules against the surface protein, gp63","volume":"14","author":"Chowdhury","year":"2019","journal-title":"Curr. Bioinf."},{"issue":"3","key":"10.1016\/j.biochi.2022.11.015_bib53","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1128\/IAI.00611-07","article-title":"gp63 in stable cationic liposomes confers sustained vaccine immunity to susceptible BALB\/c mice infected with Leishmania donovani","volume":"76","author":"Bhowmick","year":"2008","journal-title":"Infect. Immun."},{"issue":"8","key":"10.1016\/j.biochi.2022.11.015_bib54","doi-asserted-by":"crossref","first-page":"320","DOI":"10.6026\/97320630005320","article-title":"A\u00a0gp63 based vaccine candidate against visceral leishmaniasis","volume":"5","author":"Sinha","year":"2011","journal-title":"Bioinformation"},{"issue":"12","key":"10.1016\/j.biochi.2022.11.015_bib55","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.4161\/hv.21881","article-title":"Immunogenicity and immune modulatory effects of in silico predicted L. donovani candidate peptide vaccines","volume":"8","author":"Elfaki","year":"2012","journal-title":"Hum. Vaccines Immunother."},{"key":"10.1016\/j.biochi.2022.11.015_bib56","first-page":"1031","article-title":"Use of natural products in leishmaniasis chemotherapy: an overview","author":"Gervazoni","year":"2020","journal-title":"Front. Chem."},{"issue":"1","key":"10.1016\/j.biochi.2022.11.015_bib57","doi-asserted-by":"crossref","first-page":"58","DOI":"10.3390\/molecules22010058","article-title":"The role of natural products in drug discovery and development against neglected tropical diseases","volume":"22","author":"Cheuka","year":"2016","journal-title":"Molecules"},{"issue":"4","key":"10.1016\/j.biochi.2022.11.015_bib58","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1128\/AAC.50.4.1352-1364.2006","article-title":"Antitrypanosomal and antileishmanial activities of flavonoids and their analogues: in\u00a0vitro, in\u00a0vivo, structure-activity relationship, and quantitative structure-activity relationship studies","volume":"50","author":"Tasdemir","year":"2006","journal-title":"Antimicrob. Agents Chemother."},{"issue":"24","key":"10.1016\/j.biochi.2022.11.015_bib59","doi-asserted-by":"crossref","first-page":"14741","DOI":"10.1021\/acsomega.0c01584","article-title":"Homology modeling of leishmanolysin (gp63) from Leishmania panamensis and molecular docking of flavonoids","volume":"5","author":"Mercado-Camargo","year":"2020","journal-title":"ACS Omega"},{"issue":"3","key":"10.1016\/j.biochi.2022.11.015_bib60","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.phymed.2004.10.008","article-title":"Comparative antiplasmodial, leishmanicidal and antitrypanosomal activities of several biflavonoids","volume":"13","author":"Weniger","year":"2006","journal-title":"Phytomedicine"},{"key":"10.1016\/j.biochi.2022.11.015_bib61","first-page":"394","article-title":"Metalloprotease gp63-targeting novel glycoside exhibits potential antileishmanial activity","author":"Chakrabarti","year":"2022","journal-title":"Front. Cell. Infect. Microbiol."},{"issue":"3","key":"10.1016\/j.biochi.2022.11.015_bib62","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1007\/s00436-003-0960-0","article-title":"Extracellular release of the surface metalloprotease, gp63, from Leishmania and insect trypanosomatids","volume":"91","author":"Jaffe","year":"2003","journal-title":"Parasitol. Res."},{"issue":"1","key":"10.1016\/j.biochi.2022.11.015_bib63","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/0166-6851(89)90043-1","article-title":"Molecular interactions of Leishmania promastigote surface protease with human \u03b12-macroglobulin","volume":"33","author":"Heumann","year":"1989","journal-title":"Mol. Biochem. Parasitol."},{"issue":"43","key":"10.1016\/j.biochi.2022.11.015_bib64","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":"12","key":"10.1016\/j.biochi.2022.11.015_bib65","doi-asserted-by":"crossref","first-page":"5129","DOI":"10.1128\/iai.64.12.5129-5137.1996","article-title":"Surface Zn-proteinase as a molecule for defense of Leishmania mexicana amazonensis promastigotes against cytolysis inside macrophage phagolysosomes","volume":"64","author":"Seay","year":"1996","journal-title":"Infect. Immun."},{"issue":"2","key":"10.1016\/j.biochi.2022.11.015_bib66","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1006\/excr.1997.3909","article-title":"Micromolar zinc affects endonucleolytic activity in hydrogen peroxide-mediated apoptosis","volume":"239","author":"Marini","year":"1998","journal-title":"Exp. Cell Res."},{"issue":"8","key":"10.1016\/j.biochi.2022.11.015_bib67","doi-asserted-by":"crossref","first-page":"3606","DOI":"10.1007\/s00044-012-0375-5","article-title":"Benzimidazole derivatives: synthesis, leishmanicidal effectiveness, and molecular docking studies","volume":"22","author":"Shaukat","year":"2013","journal-title":"Med. Chem. Res."},{"issue":"15","key":"10.1016\/j.biochi.2022.11.015_bib68","doi-asserted-by":"crossref","first-page":"8553","DOI":"10.3390\/ijms23158553","article-title":"Quantum biochemistry screening and in\u00a0vitro evaluation of leishmania metalloproteinase inhibitors","volume":"23","author":"Moreno","year":"2022","journal-title":"Int. J. Mol. Sci."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908422003133?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908422003133?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:24:55Z","timestamp":1759541095000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908422003133"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,4]]},"references-count":68,"alternative-id":["S0300908422003133"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2022.11.015","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2023,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The glycoprotein gp63\u2013 a potential pan drug target for developing new antileishmanial agents","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2022.11.015","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}