{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T12:54:03Z","timestamp":1789908843796,"version":"4.0.1"},"reference-count":70,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,8,31]],"date-time":"2022-08-31T00:00:00Z","timestamp":1661904000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Mol. Biosci."],"abstract":"<jats:p>The heat shock protein 40 (Hsp40) family, also called J domain proteins (JDPs), regulate their Hsp70 partners by ensuring that they are engaging the right substrate at the right time and in the right location within the cell. A number of JDPs can serve as co-chaperone for a particular Hsp70, and so one generally finds many more JDPs than Hsp70s in the cell. In humans there are 13 Hsp70s and 49 JDPs. The human malaria parasite, <jats:italic>Plasmodium falciparum<\/jats:italic>, has dedicated an unusually large proportion of its genome to molecular chaperones, with a disproportionately high number of JDPs (PfJDPs) of 49 members. Interestingly, just under half of the PfJDPs are exported into the host cell during the asexual stage of the life cycle, when the malaria parasite invades mature red blood cells. Recent evidence suggests that these PfJDPs may be functionalizing both host and parasite Hsp70s within the infected red blood cell, and thereby driving the renovation of the host cell towards pathological ends. PfJDPs have been found to localize to the host cytosol, mobile structures within the host cytosol (so called \u201cJ Dots\u201d), the host plasma membrane, and specialized structures associated with malaria pathology such as the knobs. A number of these exported PfJDPs are essential, and there is growing experimental evidence that they are important for the survival and pathogenesis of the malaria parasite. This review critiques our understanding of the important role these exported PfJDPs play at the host-parasite interface.<\/jats:p>","DOI":"10.3389\/fmolb.2022.978663","type":"journal-article","created":{"date-parts":[[2022,8,31]],"date-time":"2022-08-31T06:23:40Z","timestamp":1661927020000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":13,"title":["Exported J domain proteins of the human malaria parasite"],"prefix":"10.3389","volume":"9","author":[{"given":"Shaikha Y.","family":"Almaazmi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harpreet","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tanima","family":"Dutta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory L.","family":"Blatch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,8,31]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"e44605","DOI":"10.1371\/journal.pone.0044605","article-title":"An exported heat shock protein 40 associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytes","volume":"7","author":"Acharya","year":"2012","journal-title":"PloS ONE"},{"key":"B2","doi-asserted-by":"publisher","first-page":"e1600177","DOI":"10.1002\/prca.201600177","article-title":"Proteome and structural organization of the knob complex on the surface of the Plasmodium infected red blood cell","volume":"12","author":"Alampalli","year":"2018","journal-title":"Proteomics. Clin. Appl."},{"key":"B3","doi-asserted-by":"publisher","first-page":"3902","DOI":"10.1074\/jbc.M110513200","article-title":"Host chaperones are recruited in membrane-bound complexes by Plasmodium falciparum","volume":"277","author":"Banumathy","year":"2002","journal-title":"J. Biol. Chem."},{"key":"B4","doi-asserted-by":"publisher","first-page":"592","DOI":"10.1038\/nature13574","article-title":"PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes","volume":"511","author":"Beck","year":"2014","journal-title":"Nature"},{"key":"B5","doi-asserted-by":"publisher","first-page":"2664","DOI":"10.1038\/s41598-019-39217-y","article-title":"Cholesterol bound Plasmodium falciparum co-chaperone \u2018PFA0660w\u2019 complexes with major virulence factor \u2018PfEMP1\u2019 via chaperone \u2018PfHsp70-x","volume":"9","author":"Behl","year":"2019","journal-title":"Sci. Rep."},{"key":"B6","doi-asserted-by":"publisher","first-page":"107099","DOI":"10.1016\/j.compbiolchem.2019.107099","article-title":"Structural insights into the binding mechanism of Plasmodium falciparum exported Hsp40-Hsp70 chaperone pair","volume":"83","author":"Behl","year":"2019","journal-title":"Comput. Biol. Chem."},{"key":"B7","doi-asserted-by":"publisher","first-page":"15299","DOI":"10.1074\/jbc.272.24.15299","article-title":"Defining the minimal domain of the Plasmodium falciparum protein MESA involved in the interaction with the red cell membrane skeletal protein 4.1","volume":"272","author":"Bennett","year":"1997","journal-title":"J. Biol. Chem."},{"key":"B70","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/j.molbiopara.2008.04.001","article-title":"In vivo studies support the role of trafficking and cytoskeletal-binding motifs in the interaction of MESA with the membrane skeleton of Plasmodium falciparum-infected red blood cells","volume":"160","author":"Black","year":"2008","journal-title":"Mol. Biochem. Parasitol."},{"key":"B8","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1007\/s12192-010-0250-6","article-title":"Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock","volume":"16","author":"Botha","year":"2011","journal-title":"Cell Stress Chaperones"},{"key":"B9","doi-asserted-by":"publisher","first-page":"1781","DOI":"10.1016\/j.biocel.2007.02.011","article-title":"The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: Regulating chaperone power in the parasite and the host","volume":"39","author":"Botha","year":"2007","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"B10","doi-asserted-by":"publisher","first-page":"E5","DOI":"10.1371\/journal.pbio.0000005","article-title":"The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum","volume":"1","author":"Bozdech","year":"2003","journal-title":"PLoS Biol."},{"key":"B11","doi-asserted-by":"publisher","first-page":"3609","DOI":"10.1016\/j.bmc.2012.03.067","article-title":"Novel inhibitors of heat shock protein Hsp70-mediated luciferase refolding that bind to DnaJ","volume":"20","author":"Cassel","year":"2012","journal-title":"Bioorg. Med. Chem."},{"key":"B12","doi-asserted-by":"publisher","first-page":"1353","DOI":"10.1515\/hsz-2014-0138","article-title":"Selective modulation of plasmodial Hsp70s by small molecules with antimalarial activity","volume":"395","author":"Cockburn","year":"2014","journal-title":"Biol. Chem."},{"key":"B13","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1515\/BC.2011.040","article-title":"Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: Inhibition of the plasmodial chaperone PfHsp70-1","volume":"392","author":"Cockburn","year":"2011","journal-title":"Biol. Chem."},{"key":"B14","doi-asserted-by":"publisher","first-page":"203","DOI":"10.1046\/j.1365-2141.2002.03404.x","article-title":"Assignment of functional roles to parasite proteins in malaria-infected red blood cells by competitive flow-based adhesion assay","volume":"117","author":"Cooke","year":"2002","journal-title":"Br. J. Haematol."},{"key":"B16","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1016\/0166-6851(88)90152-1","article-title":"MESA is a Plasmodium falciparum phosphoprotein associated with the erythrocyte membrane skeleton","volume":"31","author":"Coppel","year":"1988","journal-title":"Mol. Biochem. Parasitol."},{"key":"B17","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1016\/0166-6851(92)90231-8","article-title":"Repeat structures in a Plasmodium falciparum protein (MESA) that binds human erythrocyte protein 4.1","volume":"50","author":"Coppel","year":"1992","journal-title":"Mol. Biochem. Parasitol."},{"key":"B18","doi-asserted-by":"publisher","first-page":"4555","DOI":"10.2174\/1381612823666170124142439","article-title":"Plasmodial Hsp40s: New avenues for antimalarial drug discovery","volume":"23","author":"Daniyan","year":"2017","journal-title":"Curr. Pharm. Des."},{"key":"B19","doi-asserted-by":"publisher","first-page":"e0148517","DOI":"10.1371\/journal.pone.0148517","article-title":"The malarial exported PFA0660w is an Hsp40 co-chaperone of PfHsp70-x","volume":"11","author":"Daniyan","year":"2016","journal-title":"PLoS ONE"},{"key":"B20","doi-asserted-by":"publisher","first-page":"14611","DOI":"10.1096\/fj.201901741R","article-title":"The Plasmodium falciparum Hsp70-x chaperone assists the heat stress response of the malaria parasite","volume":"33","author":"Day","year":"2019","journal-title":"FASEB J."},{"key":"B21","doi-asserted-by":"publisher","first-page":"945","DOI":"10.1038\/nature08104","article-title":"A newly discovered protein export machine in malaria parasites","volume":"459","author":"de Koning-Ward","year":"2009","journal-title":"Nature"},{"key":"B22","doi-asserted-by":"publisher","first-page":"e1009969","DOI":"10.1371\/journal.ppat.1009969","article-title":"Co-chaperone involvement in knob biogenesis implicates host-derived chaperones in malaria virulence","volume":"17","author":"Diehl","year":"2021","journal-title":"PLoS Pathog."},{"key":"B23","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1038\/srep00614","article-title":"Pf155\/RESA protein influences the dynamic microcirculatory behavior of ring-stage Plasmodium falciparum infected red blood cells","volume":"2","author":"Diez-Silva","year":"2012","journal-title":"Sci. Rep."},{"key":"B24","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1007\/978-3-030-78397-6_4","article-title":"Role of the J domain protein family in the survival and pathogenesis of Plasmodium falciparum","volume":"1340","author":"Dutta","year":"","journal-title":"Adv. Exp. Med. Biol."},{"key":"B25","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1007\/s12192-020-01181-2","article-title":"Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership","volume":"26","author":"Dutta","year":"","journal-title":"Cell Stress Chaperones"},{"key":"B26","doi-asserted-by":"publisher","first-page":"587","DOI":"10.1038\/nature13555","article-title":"PTEX is an essential nexus for protein export in malaria parasites","volume":"511","author":"Elsworth","year":"2014","journal-title":"Nature"},{"key":"B27","doi-asserted-by":"publisher","first-page":"1551","DOI":"10.1111\/cmi.12596","article-title":"Proteomic analysis reveals novel proteins associated with the Plasmodium protein exporter PTEX and a loss of complex stability upon truncation of the core PTEX component","volume":"18","author":"Elsworth","year":"2016","journal-title":"PTEX150. Cell. Microbiol."},{"key":"B28","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1051\/parasite\/2012002","article-title":"Identification of an exported heat shock protein 70 in Plasmodium falciparum","volume":"20","author":"Grover","year":"2013","journal-title":"Parasite"},{"key":"B71","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1379\/1466-1268(2000)005<0347:AOTLOC>2.0.CO;2","article-title":"Analysis of the levels of conservation of the J domain among the various types of DnaJ-like proteins","volume":"5","author":"Hennessy","year":"2000","journal-title":"Cell Stress Chaperones"},{"key":"B29","doi-asserted-by":"publisher","first-page":"1697","DOI":"10.1110\/ps.051406805","article-title":"Not all J domains are created equal: Implications for the specificity of hsp40-hsp70 interactions","volume":"14","author":"Hennessy","year":"2005","journal-title":"Protein Sci."},{"key":"B30","doi-asserted-by":"publisher","first-page":"1934","DOI":"10.1126\/science.1102737","article-title":"A host-targeting signal in virulence proteins reveals a secretome in malarial infection","volume":"306","author":"Hiller","year":"2004","journal-title":"Science"},{"key":"B31","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1016\/j.molbiopara.2017.03.003","article-title":"Plasmodium Hsp40 and human Hsp70: A potential cochaperone-chaperone complex","volume":"214","author":"Jha","year":"2017","journal-title":"Mol. Biochem. Parasitol."},{"key":"B32","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1007\/978-3-030-78397-6_6","article-title":"The role of malaria parasite heat shock proteins in protein trafficking and remodelling of red blood cells","volume":"1340","author":"Jonsdottir","year":"2021","journal-title":"Adv. Exp. Med. Biol."},{"key":"B33","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1007\/s12192-018-0948-4","article-title":"Function, evolution, and structure of J-domain proteins","volume":"24","author":"Kampinga","year":"2019","journal-title":"Cell Stress Chaperones"},{"key":"B34","doi-asserted-by":"publisher","first-page":"1439","DOI":"10.1128\/EC.05180-11","article-title":"An erythrocyte cytoskeleton-binding motif in exported Plasmodium falciparum proteins","volume":"10","author":"Kilili","year":"2011","journal-title":"Eukaryot. Cell"},{"key":"B35","doi-asserted-by":"publisher","first-page":"1784","DOI":"10.1111\/j.1462-5822.2012.01840.x","article-title":"Plasmodium falciparum-encoded exported hsp70\/hsp40 chaperone\/co-chaperone complexes within the host erythrocyte","volume":"14","author":"K\u00fclzer","year":"2012","journal-title":"Cell. Microbiol."},{"key":"B36","doi-asserted-by":"publisher","first-page":"1398","DOI":"10.1111\/j.1462-5822.2010.01477.x","article-title":"Parasite-encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum-infected erythrocyte","volume":"12","author":"K\u00fclzer","year":"2010","journal-title":"Cell. Microbiol."},{"key":"B37","doi-asserted-by":"publisher","first-page":"2753","DOI":"10.1007\/s00436-019-06420-9","article-title":"Plasmodium helical interspersed subtelomeric family-an enigmatic piece of the Plasmodium biology puzzle","volume":"118","author":"Kumar","year":"2019","journal-title":"Parasitol. Res."},{"key":"B38","doi-asserted-by":"publisher","first-page":"2778","DOI":"10.1021\/ci200227u","article-title":"LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery","volume":"51","author":"Laskowski","year":"2011","journal-title":"J. Chem. Inf. Model."},{"key":"B39","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1016\/j.cell.2008.04.051","article-title":"Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes","volume":"134","author":"Maier","year":"2008","journal-title":"Cell"},{"key":"B40","doi-asserted-by":"publisher","first-page":"1930","DOI":"10.1126\/science.1102452","article-title":"Targeting malaria virulence and remodeling proteins to the host erythrocyte","volume":"306","author":"Marti","year":"2004","journal-title":"Science"},{"key":"B41","doi-asserted-by":"publisher","first-page":"9213","DOI":"10.1073\/pnas.0703433104","article-title":"Effect of plasmodial RESA protein on deformability of human red blood cells harboring Plasmodium falciparum","volume":"104","author":"Mills","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B42","doi-asserted-by":"publisher","first-page":"1492","DOI":"10.1128\/EC.05155-11","article-title":"Functional analysis of the exported type IV HSP40 protein PfGECO in Plasmodium falciparum gametocytes","volume":"10","author":"Morahan","year":"2011","journal-title":"Eukaryot. Cell"},{"key":"B43","doi-asserted-by":"publisher","first-page":"4022","DOI":"10.1158\/0008-5472.CAN-17-3728","article-title":"Targeting the Hsp40\/Hsp70 chaperone axis as a novel strategy to treat castration-resistant prostate cancer","volume":"78","author":"Moses","year":"2018","journal-title":"Cancer Res."},{"key":"B44","doi-asserted-by":"publisher","first-page":"387","DOI":"10.2174\/138161213804143734","article-title":"Hsp70s and J proteins of Plasmodium parasites infecting rodents and primates: Structure, function, clinical relevance, and drug targets","volume":"19","author":"Njunge","year":"2013","journal-title":"Curr. Pharm. Des."},{"key":"B45","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1016\/j.pt.2011.06.004","article-title":"Clinical and molecular aspects of malaria fever","volume":"27","author":"Oakley","year":"2011","journal-title":"Trends Parasitol."},{"key":"B46","doi-asserted-by":"publisher","first-page":"2012","DOI":"10.1128\/IAI.01236-06","article-title":"Molecular factors and biochemical pathways induced by febrile temperature in intraerythrocytic Plasmodium falciparum parasites","volume":"75","author":"Oakley","year":"2007","journal-title":"Infect. Immun."},{"key":"B47","doi-asserted-by":"publisher","first-page":"791","DOI":"10.1182\/blood-2005-11-007799","article-title":"In-depth analysis of the membrane and cytosolic proteome of red blood cells","volume":"108","author":"Pasini","year":"2006","journal-title":"Blood"},{"key":"B48","doi-asserted-by":"publisher","first-page":"1036","DOI":"10.1182\/blood-2007-02-076919","article-title":"The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion","volume":"110","author":"Pei","year":"2007","journal-title":"Blood"},{"key":"B49","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1007\/7355_2015_92","article-title":"Hsp40 co-chaperones as drug targets: Towards the development of specific inhibitors","volume":"19","author":"Pesce","year":"2016","journal-title":"Top. Med. Chem."},{"key":"B50","doi-asserted-by":"publisher","first-page":"1167","DOI":"10.1017\/S003118201300228X","article-title":"Plasmodial Hsp40 and Hsp70 chaperones: Current and future perspectives","volume":"141","author":"Pesce","year":"2014","journal-title":"Parasitology"},{"key":"B51","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1016\/0166-6851(89)90200-4","article-title":"The mature erythrocyte surface antigen of Plasmodium falciparum is not required for knobs or cytoadherence","volume":"36","author":"Petersen","year":"1989","journal-title":"Mol. Biochem. Parasitol."},{"key":"B52","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/j.ijpara.2016.03.005","article-title":"J-dot targeting of an exported HSP40 in Plasmodium falciparum-infected erythrocytes","volume":"46","author":"Petersen","year":"2016","journal-title":"Int. J. Parasitol."},{"key":"B53","doi-asserted-by":"publisher","first-page":"34","DOI":"10.3389\/fmolb.2015.00034","article-title":"Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle","volume":"2","author":"Przyborski","year":"2015","journal-title":"Front. Mol. Biosci."},{"key":"B54","doi-asserted-by":"publisher","first-page":"112215","DOI":"10.1016\/j.ejmech.2020.112215","article-title":"Chalcone hybrids as privileged scaffolds in antimalarial drug discovery: A key review","volume":"193","author":"Qin","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"B55","doi-asserted-by":"publisher","first-page":"36174","DOI":"10.1038\/srep36174","article-title":"Trafficking of the exported P. falciparum chaperone PfHsp70x","volume":"6","author":"Rhiel","year":"2016","journal-title":"Sci. Rep."},{"key":"B56","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1002\/1873-3468.14255","article-title":"Plasmodium falciparum HSP40 protein eCiJp traffics to the erythrocyte cytoskeleton and interacts with the human HSP70 chaperone HSPA1","volume":"596","author":"Sahu","year":"2022","journal-title":"FEBS Lett."},{"key":"B57","doi-asserted-by":"publisher","first-page":"R12","DOI":"10.1186\/gb-2006-7-2-r12","article-title":"Lineage-specific expansion of proteins exported to erythrocytes in malaria parasites","volume":"7","author":"Sargeant","year":"2006","journal-title":"Genome Biol."},{"key":"B58","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1107\/S2053230X2001208X","article-title":"Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x","volume":"76","author":"Schmidt","year":"2020","journal-title":"Acta Crystallogr. F. Struct. Biol. Commun."},{"key":"B59","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1007\/978-3-030-78397-6_10","article-title":"Heat shock proteins of malaria: Highlights and future prospects","volume":"1340","author":"Shonhai","year":"2021","journal-title":"Adv. Exp. Med. Biol."},{"key":"B60","doi-asserted-by":"publisher","first-page":"1803","DOI":"10.1110\/ps.072918107","article-title":"The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum","volume":"16","author":"Shonhai","year":"2007","journal-title":"Protein Sci."},{"key":"B61","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1002\/pro.3290","article-title":"Clustal Omega for making accurate alignments of many protein sequences","volume":"27","author":"Sievers","year":"2018","journal-title":"Protein Sci."},{"key":"B62","doi-asserted-by":"publisher","first-page":"990","DOI":"10.1111\/j.1365-2958.2005.04603.x","article-title":"A role for the Plasmodium falciparum RESA protein in resistance against heat shock demonstrated using gene disruption","volume":"56","author":"Silva","year":"2005","journal-title":"Mol. Microbiol."},{"key":"B63","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1186\/s12936-019-3060-z","article-title":"In vitro anti-malarial efficacy of chalcones: Cytotoxicity profile, mechanism of action and their effect on erythrocytes","volume":"18","author":"Sinha","year":"2019","journal-title":"Malar. J."},{"key":"B64","doi-asserted-by":"publisher","first-page":"1102","DOI":"10.2144\/00286ir01","article-title":"The sequence manipulation suite: JavaScript programs for analyzing and formatting protein and DNA sequences","volume":"28","author":"Stothard","year":"2000","journal-title":"BioTechniques"},{"key":"B65","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"B66","doi-asserted-by":"publisher","first-page":"456","DOI":"10.1016\/j.jprot.2009.08.010","article-title":"Quantitative erythrocyte membrane proteome analysis with Blue-native\/SDS PAGE","author":"van Gestel","year":"2010","journal-title":"J. Proteomics"},{"key":"B67","doi-asserted-by":"publisher","first-page":"1911","DOI":"10.1182\/blood-2002-11-3513","article-title":"Mature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells","volume":"102","author":"Waller","year":"2003","journal-title":"Blood"},{"key":"B68","doi-asserted-by":"publisher","first-page":"W296","DOI":"10.1093\/nar\/gky427","article-title":"SWISS-MODEL: Homology modelling of protein structures and complexes","volume":"46","author":"Waterhouse","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"B69","doi-asserted-by":"publisher","first-page":"eaap7847","DOI":"10.1126\/science.aap7847","article-title":"Uncovering the essential genes of the human malaria parasite Plasmodium falciparum by saturation mutagenesis","volume":"360","author":"Zhang","year":"2018","journal-title":"Science"}],"container-title":["Frontiers in Molecular Biosciences"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmolb.2022.978663\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,8,31]],"date-time":"2022-08-31T06:23:43Z","timestamp":1661927023000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmolb.2022.978663\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,8,31]]},"references-count":70,"alternative-id":["10.3389\/fmolb.2022.978663"],"URL":"https:\/\/doi.org\/10.3389\/fmolb.2022.978663","relation":{},"ISSN":["2296-889X"],"issn-type":[{"value":"2296-889X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,8,31]]},"article-number":"978663"}}