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The success of kinase inhibitors for oncological treatments has paved the way for the exploitation of protein kinases as drug targets in various diseases, including malaria. Casein kinases are ubiquitous serine\/threonine kinases involved in a wide range of cellular processes such as mitotic checkpoint signaling, DNA damage response, and circadian rhythm. In\n            <jats:italic>Plasmodium<\/jats:italic>\n            , it is suggested that these protein kinases are essential for both asexual and sexual blood-stage parasites, reinforcing their potential as targets for multi-stage antimalarials. To identify new putative\n            <jats:italic>Pf<\/jats:italic>\n            CK2\u03b1 inhibitors, we utilized an\n            <jats:italic>in silico<\/jats:italic>\n            chemogenomic strategy involving virtual screening with docking simulations and quantitative structure-activity relationship predictions. Our investigation resulted in the discovery of a new quinazoline molecule (\n            <jats:bold>542<\/jats:bold>\n            ), which exhibited potent activity against asexual blood stages and a high selectivity index (&gt;100). Subsequently, we conducted chemical-genetic interaction analysis on yeasts with mutations in casein kinases. Our chemical-genetic interaction results are consistent with the hypothesis that\n            <jats:bold>542<\/jats:bold>\n            inhibits yeast Cka1, which has a hinge region with high similarity to\n            <jats:italic>Pf<\/jats:italic>\n            CK2\u03b1. This finding is in agreement with our\n            <jats:italic>in silico<\/jats:italic>\n            results suggesting that\n            <jats:bold>542<\/jats:bold>\n            inhibits\n            <jats:italic>Pf<\/jats:italic>\n            CK2\u03b1 via hinge region interaction.\n          <\/jats:p>","DOI":"10.1128\/aac.00589-23","type":"journal-article","created":{"date-parts":[[2023,10,11]],"date-time":"2023-10-11T13:01:48Z","timestamp":1697029308000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Identification of potential inhibitors of casein kinase 2 alpha of\n            <i>Plasmodium falciparum<\/i>\n            with potent\n            <i>in vitro<\/i>\n            activity"],"prefix":"10.1128","volume":"67","author":[{"given":"Kaira C. P.","family":"Tomaz","sequence":"first","affiliation":[{"name":"Laboratory of Tropical Diseases (LDT), Institute of Biology, University of Campinas , Campinas, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tatyana A.","family":"Tavella","sequence":"additional","affiliation":[{"name":"Laboratory of Tropical Diseases (LDT), Institute of Biology, University of Campinas , Campinas, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joyce V. B.","family":"Borba","sequence":"additional","affiliation":[{"name":"Laboratory of Tropical Diseases (LDT), Institute of Biology, University of Campinas , Campinas, Brazil"},{"name":"Laboratory of Molecular Modeling and Drug Design (LabMol), Faculty of Pharmacy, Universidade Federal de Goi\u00e1s (UFG) , Goi\u00e2nia, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luis C.","family":"Salazar-Alvarez","sequence":"additional","affiliation":[{"name":"Laboratory of Tropical Diseases (LDT), Institute of Biology, University of Campinas , Campinas, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jo\u00e3o E.","family":"Levandoski","sequence":"additional","affiliation":[{"name":"Department of Materials and Bioprocesses Engineering, School of Chemical Engineering, University of Campinas , Campinas, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Melina","family":"Mottin","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Modeling and Drug Design (LabMol), Faculty of Pharmacy, Universidade Federal de Goi\u00e1s (UFG) , Goi\u00e2nia, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bruna K. 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