{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T13:33:25Z","timestamp":1778765605720,"version":"3.51.4"},"reference-count":54,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2023,3,1]],"date-time":"2023-03-01T00:00:00Z","timestamp":1677628800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"ANPCyT","award":["PICT 2015-1288"],"award-info":[{"award-number":["PICT 2015-1288"]}]},{"name":"ANPCyT","award":["P20GM103449"],"award-info":[{"award-number":["P20GM103449"]}]},{"name":"INBRE Program of the National Institute of General Medical Science (BD)","award":["PICT 2015-1288"],"award-info":[{"award-number":["PICT 2015-1288"]}]},{"name":"INBRE Program of the National Institute of General Medical Science (BD)","award":["P20GM103449"],"award-info":[{"award-number":["P20GM103449"]}]},{"name":"Training Innovations in Parasitologic Studies (TIPS) Fellowships, Center for Tropical &amp; Emerging Global Diseases (CTEGD), University of Georgia","award":["PICT 2015-1288"],"award-info":[{"award-number":["PICT 2015-1288"]}]},{"name":"Training Innovations in Parasitologic Studies (TIPS) Fellowships, Center for Tropical &amp; Emerging Global Diseases (CTEGD), University of Georgia","award":["P20GM103449"],"award-info":[{"award-number":["P20GM103449"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteomes"],"abstract":"<jats:p>Toxoplasma gondii is an obligate intracellular apicomplexan that causes toxoplasmosis in humans and animals. Central to its dissemination and pathogenicity is the ability to rapidly divide in the tachyzoite stage and infect any type of nucleated cell. Adaptation to different cell contexts requires high plasticity in which heat shock proteins (Hsps) could play a fundamental role. Tgj1 is a type I Hsp40 of T. gondii, an ortholog of the DNAJA1 group, which is essential during the tachyzoite lytic cycle. Tgj1 consists of a J-domain, ZFD, and DNAJ_C domains with a CRQQ C-terminal motif, which is usually prone to lipidation. Tgj1 presented a mostly cytosolic subcellular localization overlapping partially with endoplasmic reticulum. Protein\u2013protein Interaction (PPI) analysis showed that Tgj1 could be implicated in various biological pathways, mainly translation, protein folding, energy metabolism, membrane transport and protein translocation, invasion\/pathogenesis, cell signaling, chromatin and transcription regulation, and cell redox homeostasis among others. The combination of Tgj1 and Hsp90 PPIs retrieved only 70 interactors linked to the Tgj1-Hsp90 axis, suggesting that Tgj1 would present specific functions in addition to those of the Hsp70\/Hsp90 cycle, standing out invasion\/pathogenesis, cell shape motility, and energy pathway. Within the Hsp70\/Hsp90 cycle, translation-associated pathways, cell redox homeostasis, and protein folding were highly enriched in the Tgj1-Hsp90 axis. In conclusion, Tgj1 would interact with a wide range of proteins from different biological pathways, which could suggest a relevant role in them.<\/jats:p>","DOI":"10.3390\/proteomes11010009","type":"journal-article","created":{"date-parts":[[2023,3,2]],"date-time":"2023-03-02T03:54:56Z","timestamp":1677729296000},"page":"9","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Analysis of the Interactome of the Toxoplasma gondii Tgj1 HSP40 Chaperone"],"prefix":"10.3390","volume":"11","author":[{"given":"Jonathan","family":"Munera L\u00f3pez","sequence":"first","affiliation":[{"name":"Laboratorio de Parasitolog\u00eda Molecular, INTECH, CONICET-UNSAM, Av. Intendente Marino Km. 8.2, C.C 164, Chascom\u00fas 7130, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2896-7147","authenticated-orcid":false,"given":"Andr\u00e9s Mariano","family":"Alonso","sequence":"additional","affiliation":[{"name":"Laboratorio de Parasitolog\u00eda Molecular, INTECH, CONICET-UNSAM, Av. Intendente Marino Km. 8.2, C.C 164, Chascom\u00fas 7130, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria Julia","family":"Figueras","sequence":"additional","affiliation":[{"name":"Laboratorio de Parasitolog\u00eda Molecular, INTECH, CONICET-UNSAM, Av. Intendente Marino Km. 8.2, C.C 164, Chascom\u00fas 7130, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ana Mar\u00eda","family":"Saldarriaga Cartagena","sequence":"additional","affiliation":[{"name":"Laboratorio de Parasitolog\u00eda Molecular, INTECH, CONICET-UNSAM, Av. Intendente Marino Km. 8.2, C.C 164, Chascom\u00fas 7130, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5964-8512","authenticated-orcid":false,"given":"Miryam A.","family":"Hortua Triana","sequence":"additional","affiliation":[{"name":"Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8052-4880","authenticated-orcid":false,"given":"Luis","family":"Diambra","sequence":"additional","affiliation":[{"name":"Centro Regional de Estudios Gen\u00f3micos, Universidad Nacional de La Plata, La Plata 1900, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4064-2556","authenticated-orcid":false,"given":"Laura","family":"Vanagas","sequence":"additional","affiliation":[{"name":"Laboratorio de Parasitolog\u00eda Molecular, INTECH, CONICET-UNSAM, Av. Intendente Marino Km. 8.2, C.C 164, Chascom\u00fas 7130, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bin","family":"Deng","sequence":"additional","affiliation":[{"name":"Department of Biology and VBRN, University of Vermont, Burlington, VT 05405, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2041-6295","authenticated-orcid":false,"given":"Silvia N. J.","family":"Moreno","sequence":"additional","affiliation":[{"name":"Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602, USA"},{"name":"Department of Cellular Biology, University of Georgia, Athens, GA 30602, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4871-3408","authenticated-orcid":false,"given":"Sergio Oscar","family":"Angel","sequence":"additional","affiliation":[{"name":"Laboratorio de Parasitolog\u00eda Molecular, INTECH, CONICET-UNSAM, Av. Intendente Marino Km. 8.2, C.C 164, Chascom\u00fas 7130, Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2023,3,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1128\/CMR.11.2.267","article-title":"Structures of Toxoplasma gondii Tachyzoites, Bradyzoites, and Sporozoites and Biology and Development of Tissue Cysts","volume":"11","author":"Dubey","year":"1998","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1016\/S0020-7519(00)00124-7","article-title":"Toxoplasma gondii: From animals to humans","volume":"30","author":"Tenter","year":"2000","journal-title":"Int. J. Parasitol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1586\/eri.12.58","article-title":"Toxoplasmosis in the fetus and newborn: An update on prevalence, diagnosis and treatment","volume":"10","author":"Moncada","year":"2012","journal-title":"Expert Rev. Anti-Infect. Ther."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1084\/jem.132.4.636","article-title":"The toxoplasma gondii oocyst from cat feces","volume":"132","author":"Dubey","year":"1970","journal-title":"J. Exp. Med."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0166-6851(01)00284-5","article-title":"Defining the cell cycle for the tachyzoite stage of Toxoplasma gondii","volume":"115","author":"Radke","year":"2001","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1016\/j.cell.2016.08.019","article-title":"A Genome-wide CRISPR Screen in Toxoplasma Identifies Essential Apicomplexan Genes","volume":"166","author":"Sidik","year":"2016","journal-title":"Cell"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1091\/mbc.e03-03-0146","article-title":"Exchangeable Chaperone Modules Contribute to Specification of Type I and Type II Hsp40 Cellular Function","volume":"15","author":"Fan","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"704","DOI":"10.3390\/biom4030704","article-title":"Chaperoning Proteins for Destruction: Diverse Roles of Hsp70 Chaperones and their Co-Chaperones in Targeting Misfolded Proteins to the Proteasome","volume":"4","author":"Shiber","year":"2014","journal-title":"Biomolecules"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1038\/s41388-019-1016-y","article-title":"Heat-shock proteins: Chaperoning DNA repair","volume":"39","author":"Dubrez","year":"2019","journal-title":"Oncogene"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/sj.embor.7400172","article-title":"The J-protein family: Modulating protein assembly, disassembly and translocation","volume":"5","author":"Walsh","year":"2004","journal-title":"EMBO Rep."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2560","DOI":"10.1007\/s00018-006-6192-6","article-title":"The diversity of the DnaJ\/Hsp40 family, the crucial partners for Hsp70 chaperones","volume":"63","author":"Qiu","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1083\/jcb.114.4.609","article-title":"Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein","volume":"114","author":"Caplan","year":"1991","journal-title":"J. Cell Biol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"18890","DOI":"10.1016\/S0021-9258(19)37044-9","article-title":"Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae","volume":"267","author":"Caplan","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"6756","DOI":"10.1158\/0008-5472.CAN-06-0185","article-title":"HDJ-2 as a Target for Radiosensitization of Glioblastoma Multiforme Cells by the Farnesyltransferase Inhibitor R115777 and the Role of the p53\/p21 Pathway","volume":"66","author":"Wang","year":"2006","journal-title":"Cancer Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1492","DOI":"10.1093\/emboj\/18.6.1492","article-title":"The Hdj-2\/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis","volume":"18","author":"Meacham","year":"1999","journal-title":"EMBO J."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1016\/S0092-8674(05)80063-7","article-title":"YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism","volume":"71","author":"Caplan","year":"1992","journal-title":"Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"5249","DOI":"10.1091\/mbc.e08-04-0435","article-title":"Farnesylation of Ydj1 Is Required for In Vivo Interaction with Hsp90 Client Proteins","volume":"19","author":"Flom","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"3091","DOI":"10.1083\/jcb.201712029","article-title":"Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial \u03b2-barrel proteins","volume":"217","author":"Jores","year":"2018","journal-title":"J. Cell Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2901","DOI":"10.1039\/c2mb25248a","article-title":"Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones","volume":"8","author":"Gillies","year":"2012","journal-title":"Mol. Biosyst."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1016\/j.ijbiomac.2011.12.012","article-title":"Toxoplasma gondii Sis1-like J-domain protein is a cytosolic chaperone associated to HSP90\/HSP70 complex","volume":"50","author":"Figueras","year":"2012","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S0166-6851(97)00210-7","article-title":"Gene knock-outs and allelic replacements in Toxoplasma gondii: HXGPRT as a selectable marker for hit-and-run mutagenesis","volume":"91","author":"Donald","year":"1998","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1016\/S0002-9440(10)65025-0","article-title":"Genetic and Epigenetic Changes in Human Epithelial Cells Immortalized by Telomerase","volume":"156","author":"Farwell","year":"2000","journal-title":"Am. J. Pathol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.jmb.2005.05.031","article-title":"Toxoplasma gondii Hsp90 is a Potential Drug Target Whose Expression and Subcellular Localization are Developmentally Regulated","volume":"350","author":"Echeverria","year":"2005","journal-title":"J. Mol. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2147","DOI":"10.1128\/EC.00262-07","article-title":"Artemisinin Induces Calcium-Dependent Protein Secretion in the Protozoan Parasite Toxoplasma gondii","volume":"6","author":"Nagamune","year":"2007","journal-title":"Eukaryot. Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"2380","DOI":"10.1016\/j.jprot.2011.05.039","article-title":"Proteomic profiling of acrolein adducts in human lung epithelial cells","volume":"74","author":"Spiess","year":"2011","journal-title":"J. Proteom."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1016\/j.chom.2020.09.011","article-title":"A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions","volume":"28","author":"Barylyuk","year":"2020","journal-title":"Cell Host Microbe"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1093\/molbev\/mst008","article-title":"Sequential Duplications of an Ancient Member of the DnaJ-Family Expanded the Functional Chaperone Network in the Eukaryotic Cytosol","volume":"30","author":"Sahi","year":"2013","journal-title":"Mol. Biol. Evol."},{"key":"ref_28","doi-asserted-by":"crossref","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":"2010","journal-title":"Cell Stress Chaperon."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"S54","DOI":"10.1074\/mcp.M116.064550","article-title":"The Prenylated Proteome of Plasmodium falciparum Reveals Pathogen-specific Prenylation Activity and Drug Mechanism-of-action","volume":"16","author":"Gisselberg","year":"2017","journal-title":"Mol. Cell. Proteom."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1016\/j.jmb.2004.12.040","article-title":"The Crystal Structure of the C-terminal Fragment of Yeast Hsp40 Ydj1 Reveals Novel Dimerization Motif for Hsp40","volume":"346","author":"Wu","year":"2005","journal-title":"J. Mol. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","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":"ref_32","doi-asserted-by":"crossref","first-page":"26235","DOI":"10.1074\/jbc.M605417200","article-title":"Defining the Requirements for Hsp40 and Hsp70 in the Hsp90 Chaperone Pathway","volume":"281","author":"Cintron","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"245","DOI":"10.2174\/1389203715666140331114233","article-title":"Protozoan HSP90-heterocomplex: Molecular interaction network and biological significance","volume":"15","author":"Figueras","year":"2014","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1007\/s12192-016-0697-1","article-title":"J domain independent functions of J proteins","volume":"21","author":"Tamadaddi","year":"2016","journal-title":"Cell Stress Chaperon."},{"key":"ref_35","first-page":"489","article-title":"HSP40 proteins use class-specific regulation to drive HSP70 functional diversity","volume":"587","author":"Faust","year":"2020","journal-title":"Nat. Cell Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"20927","DOI":"10.1016\/S0021-9258(19)36777-8","article-title":"Regulation of Hsp70 function by a eukaryotic DnaJ homolog","volume":"267","author":"Cyr","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1379\/1466-1268(2003)008<0309:MFROHF>2.0.CO;2","article-title":"Mechanisms for regulation of Hsp70 function by Hsp40","volume":"8","author":"Fan","year":"2003","journal-title":"Cell Stress Chaperon."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"342","DOI":"10.15698\/mic2017.10.594","article-title":"Ydj1 governs fungal morphogenesis and stress response, and facilitates mitochondrial protein import via Mas1 and Mas2","volume":"4","author":"Xie","year":"2017","journal-title":"Microb. Cell"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2735","DOI":"10.1016\/j.celrep.2017.08.074","article-title":"Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping","volume":"20","author":"Rizzolo","year":"2017","journal-title":"Cell Rep."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"18045","DOI":"10.1021\/bi980900g","article-title":"Mutations in the Cytosolic DnaJ Homologue, YDJ1, Delay and Compromise the Efficient Translation of Heterologous Proteins in Yeast","volume":"37","author":"Brodsky","year":"1998","journal-title":"Biochemistry"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"4434","DOI":"10.1128\/MCB.00543-08","article-title":"Ydj1 Protects Nascent Protein Kinases from Degradation and Controls the Rate of Their Maturation","volume":"28","author":"Mandal","year":"2008","journal-title":"Mol. Cell. Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"e38131","DOI":"10.7554\/eLife.38131","article-title":"Elucidating the mitochondrial proteome of Toxoplasma gondii reveals the presence of a divergent cytochrome c oxidase","volume":"7","author":"Seidi","year":"2018","journal-title":"eLife"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1002\/pmic.201600477","article-title":"Proteomic profiling of extracellular vesicles secreted from Toxoplasma gondii","volume":"17","author":"Wowk","year":"2017","journal-title":"Proteomics"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"11548","DOI":"10.1016\/S0021-9258(19)50235-6","article-title":"The carboxyl-terminal CXXX sequence of Gi alpha, but not Rab5 or Rab11, supports Ras processing and transforming activity","volume":"268","author":"Cox","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"30608","DOI":"10.1074\/jbc.M103928200","article-title":"Conserved Cysteine and Tryptophan Residues of the Endothelin-converting Enzyme-1 CXAW Motif Are Critical for Protein Maturation and Enzyme Activity","volume":"276","author":"MacLeod","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/S0006-291X(02)00675-7","article-title":"Two C-terminal cysteines are necessary for proper folding of the peptidase neprilysin\/CD10","volume":"295","author":"Santos","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_47","unstructured":"Fewell, S.W., and Brodsky, J.L. (2009). Trafficking Inside Cells, Springer."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1111\/mmi.14661","article-title":"Environmental sensing and regulation of motility in Toxoplasma","volume":"115","author":"Uboldi","year":"2020","journal-title":"Mol. Microbiol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1146\/annurev-micro-041320-021425","article-title":"How Apicomplexa Parasites Secrete and Build Their Invasion Machinery","volume":"76","author":"Cova","year":"2022","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1128\/CMR.00005-17","article-title":"Toxoplasma Effectors Targeting Host Signaling and Transcription","volume":"30","author":"Hakimi","year":"2017","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.chom.2020.01.002","article-title":"Functional and Computational Genomics Reveal Unprecedented Flexibility in Stage-Specific Toxoplasma Metabolism","volume":"27","author":"Krishnan","year":"2020","journal-title":"Cell Host Microbe"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/j.pt.2022.06.001","article-title":"Toxoplasma metabolic flexibility in different growth conditions","volume":"38","author":"Walsh","year":"2022","journal-title":"Trends Parasitol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"16591","DOI":"10.1074\/jbc.M800681200","article-title":"Translation Regulation by Eukaryotic Initiation Factor-2 Kinases in the Development of Latent Cysts in Toxoplasma gondii","volume":"283","author":"Narasimhan","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"e03160-20","DOI":"10.1128\/mBio.03160-20","article-title":"TgIF2K-B Is an eIF2\u03b1 Kinase in Toxoplasma gondii That Responds to Oxidative Stress and Optimizes Pathogenicity","volume":"12","author":"Augusto","year":"2021","journal-title":"Mbio"}],"container-title":["Proteomes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2227-7382\/11\/1\/9\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T18:45:13Z","timestamp":1760121913000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2227-7382\/11\/1\/9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,3,1]]},"references-count":54,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2023,3]]}},"alternative-id":["proteomes11010009"],"URL":"https:\/\/doi.org\/10.3390\/proteomes11010009","relation":{},"ISSN":["2227-7382"],"issn-type":[{"value":"2227-7382","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,3,1]]}}}