{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T13:32:10Z","timestamp":1790947930584,"version":"4.1.0"},"reference-count":151,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2022,3,8]],"date-time":"2022-03-08T00:00:00Z","timestamp":1646697600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microorganisms"],"abstract":"<jats:p>Parasites belonging to the Apicomplexa phylum still represent a major public health and world-wide socioeconomic burden that is greatly amplified by the spread of resistances against known therapeutic drugs. Therefore, it is essential to provide the scientific and medical communities with innovative strategies specifically targeting these organisms. In this review, we present an overview of the diversity of the phosphatome as well as the variety of functions that phosphatases display throughout the Apicomplexan parasites\u2019 life cycles. We also discuss how this diversity could be used for the design of innovative and specific new drugs\/therapeutic strategies.<\/jats:p>","DOI":"10.3390\/microorganisms10030585","type":"journal-article","created":{"date-parts":[[2022,3,9]],"date-time":"2022-03-09T01:53:54Z","timestamp":1646790834000},"page":"585","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Deciphering the Role of Protein Phosphatases in Apicomplexa: The Future of Innovative Therapeutics?"],"prefix":"10.3390","volume":"10","author":[{"given":"Aline","family":"Fr\u00e9ville","sequence":"first","affiliation":[{"name":"Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019-UMR 9017-CIIL-Centre d\u2019Infection et d\u2019Immunit\u00e9 de Lille, 59000 Lille, France"},{"name":"Department of Infection Biology, Faculty of Infectious and Tropical Diseases, London School of Tropical Medicine and Hygiene, Keppel Street, London WC1E 7HT, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B\u00e9n\u00e9dicte","family":"Gnangnon","sequence":"additional","affiliation":[{"name":"Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019-UMR 9017-CIIL-Centre d\u2019Infection et d\u2019Immunit\u00e9 de Lille, 59000 Lille, France"},{"name":"Department of Epidemiology, Center for Communicable Diseases Dynamics, Harvard TH Chan School of Public Health, Boston, MA 02115, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Asma S.","family":"Khelifa","sequence":"additional","affiliation":[{"name":"Univ. 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Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0166-6851(01)00328-0","article-title":"Apical organelles of Apicomplexa: Biology and isolation by subcellular fractionation","volume":"117","author":"Blackman","year":"2001","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/37132","article-title":"A plastid organelle as a drug target in apicomplexan parasites","volume":"390","author":"Fichera","year":"1997","journal-title":"Nature"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"R262","DOI":"10.1016\/j.cub.2014.01.024","article-title":"Apicoplast","volume":"24","author":"McFadden","year":"2014","journal-title":"Curr. Biol."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Salomaki, E.D., and Kolisko, M. (2019). There Is Treasure Everywhere: Reductive Plastid Evolution in Apicomplexa in Light of Their Close Relatives. Biomolecules, 9.","DOI":"10.3390\/biom9080378"},{"key":"ref_6","unstructured":"World Health, O. (2020). World Malaria Report 2020: 20 Years of Global Progress and Challenges, World Health Organization."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Hajj, R.E., Tawk, L., Itani, S., Hamie, M., Ezzeddine, J., El Sabban, M., and El Hajj, H. (2021). Toxoplasmosis: Current and Emerging Parasite Druggable Targets. Microorganisms, 9.","DOI":"10.3390\/microorganisms9122531"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1016\/S0140-6736(04)16412-X","article-title":"Toxoplasmosis","volume":"363","author":"Montoya","year":"2004","journal-title":"Lancet"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"e00054","DOI":"10.1016\/j.fawpar.2019.e00054","article-title":"Toxoplasmosis: Overview from a One Health perspective","volume":"15","author":"Dubey","year":"2019","journal-title":"Food Waterborne Parasitol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"113293","DOI":"10.1016\/j.psychres.2020.113293","article-title":"Association between schizophrenia and Toxoplasma gondii infection in Algeria","volume":"291","author":"Kezai","year":"2020","journal-title":"Psychiat Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.17219\/acem\/61435","article-title":"Relationship between toxoplasmosis and schizophrenia: A review","volume":"26","author":"Fuglewicz","year":"2017","journal-title":"Adv. Clin. Exp. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.jns.2015.02.028","article-title":"Neurobiological studies on the relationship between toxoplasmosis and neuropsychiatric diseases","volume":"351","author":"Fabiani","year":"2015","journal-title":"J. Neurol. Sci"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Ngoungou, E.B., Bhalla, D., Nzoghe, A., Dard\u00e9, M.-L., and Preux, P.-M. (2015). Toxoplasmosis and epilepsy--systematic review and meta analysis. PLoS Negl. Trop. Dis., 9.","DOI":"10.1371\/journal.pntd.0003525"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2397","DOI":"10.1056\/NEJMra1202018","article-title":"Human Babesiosis","volume":"366","author":"Vannier","year":"2012","journal-title":"N. Eng. J. Med."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/j.pt.2018.07.009","article-title":"Genetic Diversity and Population Structure of Cryptosporidium","volume":"34","author":"Feng","year":"2018","journal-title":"Trends Parasitol"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"e564","DOI":"10.1016\/S2214-109X(15)00151-5","article-title":"Pathogen-specific burdens of community diarrhoea in developing countries: A multisite birth cohort study (MAL-ED)","volume":"3","author":"Babji","year":"2015","journal-title":"Lancet Glob. Health"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0140-6736(13)60844-2","article-title":"Burden and aetiology of diarrhoeal disease in infants and young children in developing countries (the Global Enteric Multicenter Study, GEMS): A prospective, case-control study","volume":"382","author":"Kotloff","year":"2013","journal-title":"Lancet"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1097\/QAD.0b013e3283437e88","article-title":"Cryptosporidiosis in patients with HIV\/AIDS","volume":"25","author":"Shaffie","year":"2011","journal-title":"AIDS"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Sawant, M., Baydoun, M., Creusy, C., Chab\u00e9, M., Viscogliosi, E., Certad, G., and Benamrouz-Vanneste, S. (2020). Cryptosporidium and Colon Cancer: Cause or Consequence?. Microorganisms, 8.","DOI":"10.3390\/microorganisms8111665"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1146\/annurev-micro-092412-155741","article-title":"The Algal Past and Parasite Present of the Apicoplast","volume":"67","author":"Striepen","year":"2013","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"670049","DOI":"10.3389\/fcimb.2021.670049","article-title":"The Modular Circuitry of Apicomplexan Cell Division Plasticity","volume":"11","author":"Gubbels","year":"2021","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1042\/BJ20081986","article-title":"Evolution of protein phosphatases in plants and animals","volume":"417","author":"Moorhead","year":"2009","journal-title":"Biochem. J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1912","DOI":"10.1126\/science.1075762","article-title":"The protein kinase complement of the human genome","volume":"298","author":"Manning","year":"2002","journal-title":"Science"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"eaag1796","DOI":"10.1126\/scisignal.aag1796","article-title":"Genomics and evolution of protein phosphatases","volume":"10","author":"Chen","year":"2017","journal-title":"Sci. Signal."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1016\/j.micinf.2012.04.007","article-title":"The kinomes of apicomplexan parasites","volume":"14","author":"Barton","year":"2012","journal-title":"Microbes Infect."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1002\/prot.21444","article-title":"Classification and functional annotation of eukaryotic protein kinases","volume":"68","author":"Barton","year":"2007","journal-title":"Proteins"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/mmi.13715","article-title":"The serine\/threonine phosphatases of apicomplexan parasites","volume":"106","author":"Yang","year":"2017","journal-title":"Mol. Microbiol."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Wilkes, J.M., and Doerig, C. (2008). The protein-phosphatome of the human malaria parasite Plasmodium falciparum. BMC Genom., 9.","DOI":"10.1186\/1471-2164-9-412"},{"key":"ref_29","unstructured":"(2021, September 01). Phosphatase Wiki\u2014Protein Phosphatase Classification and Evolution. Available online: http:\/\/phosphatome.net\/wiki."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1016\/j.chom.2011.09.004","article-title":"The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites\u2019 boundaries","volume":"10","author":"Treeck","year":"2011","journal-title":"Cell Host Microbe"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"a020644","DOI":"10.1101\/cshperspect.a020644","article-title":"The genesis of tyrosine phosphorylation","volume":"6","author":"Hunter","year":"2014","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.1080\/15548627.2017.1341453","article-title":"PTPN22 regulates NLRP3-mediated IL1B secretion in an autophagy-dependent manner","volume":"13","author":"Spalinger","year":"2017","journal-title":"Autophagy"},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Yoshimura, A. (2017). Mining the Complex Family of Protein Tyrosine Phosphatases for Checkpoint Regulators in Immunity. Emerging Concepts Targeting Immune Checkpoints in Cancer and Autoimmunity, Springer International Publishing.","DOI":"10.1007\/978-3-319-68929-6"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1007\/s10741-018-9676-1","article-title":"Protein tyrosine phosphatases in cardiac physiology and pathophysiology","volume":"23","author":"Wade","year":"2018","journal-title":"Heart Fail. Rev."},{"key":"ref_35","first-page":"188562","article-title":"The emerging roles of dual-specificity phosphatases and their specific characteristics in human cancer","volume":"1876","author":"Gao","year":"2021","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2571","DOI":"10.1007\/s00018-019-03095-4","article-title":"Protein tyrosine phosphatases: Promising targets in pancreatic ductal adenocarcinoma","volume":"76","author":"Ruckert","year":"2019","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"5701","DOI":"10.1158\/0008-5472.CAN-17-1510","article-title":"Therapeutic Targeting of Oncogenic Tyrosine Phosphatases","volume":"77","author":"Frankson","year":"2017","journal-title":"Cancer Res."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.cell.2004.05.018","article-title":"Protein tyrosine phosphatases in the human genome","volume":"117","author":"Alonso","year":"2004","journal-title":"Cell"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molbiopara.2007.11.006","article-title":"Characterization of a PRL protein tyrosine phosphatase from Plasmodium falciparum","volume":"158","author":"Pendyala","year":"2008","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.molbiopara.2003.11.005","article-title":"A zinc-binding dual-specificity YVH1 phosphatase in the malaria parasite, Plasm.modium falciparum, and its interaction with the nuclear protein, pescadillo","volume":"133","author":"Kumar","year":"2004","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1128\/EC.00028-13","article-title":"Atypical mitogen-activated protein kinase phosphatase implicated in regulating transition from pre-S-Phase asexual intraerythrocytic development of Plasmodium falciparum","volume":"12","author":"Balu","year":"2013","journal-title":"Eukaryot. Cell"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"e202000879","DOI":"10.26508\/lsa.202000879","article-title":"Plasmodium DEH is ER-localized and crucial for oocyst mitotic division during malaria transmission","volume":"3","author":"Guttery","year":"2020","journal-title":"Life Sci. Alliance"},{"key":"ref_43","doi-asserted-by":"crossref","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"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.cell.2017.06.030","article-title":"Functional Profiling of a Plasmodium Genome Reveals an Abundance of Essential Genes","volume":"170","author":"Bushell","year":"2017","journal-title":"Cell"},{"key":"ref_45","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_46","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1152\/physrev.00013.2003","article-title":"Functional diversity of protein phosphatase-1, a cellular economizer and reset button","volume":"84","author":"Ceulemans","year":"2004","journal-title":"Physiol. Rev."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1042\/BST20160154","article-title":"Biogenesis and activity regulation of protein phosphatase 1","volume":"45","author":"Verbinnen","year":"2017","journal-title":"Biochem. Soc. Trans."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1111\/j.1365-2958.2006.05119.x","article-title":"Regulation of protein phosphatase type 1 and cell cycle progression by PfLRR1, a novel leucine-rich repeat protein of the human malaria parasite Plasmodium falciparum","volume":"60","author":"Daher","year":"2006","journal-title":"Mol. Microbiol."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Hollin, T., De Witte, C., Freville, A., Guerrera, I.C., Chhuon, C., Saliou, J.M., Herbert, F., Pierrot, C., and Khalife, J. (2019). Essential role of GEXP15, a specific Protein Phosphatase type 1 partner, in Plasmodium berghei in asexual erythrocytic proliferation and transmission. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1007973"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"3532","DOI":"10.1038\/s41467-020-17306-1","article-title":"Co-option of Plasmodium falciparum PP1 for egress from host erythrocytes","volume":"11","author":"Paul","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1111\/j.1462-5822.2005.00650.x","article-title":"Protein phosphatase 1, a Plasmodium falciparum essential enzyme, is exported to the host cell and implicated in the release of infectious merozoites","volume":"8","author":"Blisnick","year":"2006","journal-title":"Cell. Microbiol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/S0020-7519(02)00007-3","article-title":"Plasmodium falciparum protein phosphatase type 1 functionally complements a glc7 mutant in Saccharomyces cerevisiae","volume":"32","author":"Bhattacharyya","year":"2002","journal-title":"Int. J. Parasitol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1038\/s42003-021-02273-0","article-title":"Protein phosphatase 1 regulates atypical mitotic and meiotic division in Plasmodium sexual stages","volume":"4","author":"Zeeshan","year":"2021","journal-title":"Commun. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/j.chom.2009.03.008","article-title":"Clonal Conditional Mutagenesis in Malaria Parasites","volume":"5","author":"Combe","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Hollin, T., De Witte, C., Lenne, A., Pierrot, C., and Khalife, J. (2016). Analysis of the interactome of the Ser\/Thr Protein Phosphatase type 1 in Plasmodium falciparum. BMC Genom., 17.","DOI":"10.1186\/s12864-016-2571-z"},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Freville, A., Cailliau-Maggio, K., Pierrot, C., Tellier, G., Kalamou, H., Lafitte, S., Martoriati, A., Pierce, R.J., Bodart, J.F., and Khalife, J. (2013). Plasmodium falciparum encodes a conserved active inhibitor-2 for Protein Phosphatase type 1: Perspectives for novel anti-plasmodial therapy. BMC Biol., 11.","DOI":"10.1186\/1741-7007-11-80"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1074\/jbc.M111.276865","article-title":"Plasmodium falciparum inhib.bitor-3 homolog increases protein phosphatase type 1 activity and is essential for parasitic survival","volume":"287","author":"Freville","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"4519","DOI":"10.1111\/febs.12960","article-title":"Identification of a Plasmodium falciparum inhibitor-2 motif involved in the binding and regulation activity of protein phosphatase type 1","volume":"281","author":"Freville","year":"2014","journal-title":"FEBS J."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"8120","DOI":"10.1038\/s41598-019-44542-3","article-title":"Plasmodium pseudo-Tyrosine Kinase-like binds PP1 and SERA5 and is exported to host erythrocytes","volume":"9","author":"Gnangnon","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.3389\/fmicb.2018.02617","article-title":"Characterization of a Protein Phosphatase Type-1 and a Kinase Anchoring Protein in Plasmodium falciparum","volume":"9","author":"Lenne","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"85","DOI":"10.2147\/DDDT.S153095","article-title":"Peptides derived from Plasmodium falciparum leucine-rich repeat 1 bind to serine\/threonine phosphatase type 1 and inhibit parasite growth in vitro","volume":"12","author":"Pierrot","year":"2018","journal-title":"Drug Des. Dev. Ther."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"777","DOI":"10.3389\/fmicb.2016.00777","article-title":"Identification of Plasmodium falciparum Translation Initiation eIF2beta Subunit: Direct Interaction with Protein Phosphatase Type 1","volume":"7","author":"Tellier","year":"2016","journal-title":"Front. Microbiol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.pt.2020.09.003","article-title":"The Multifaceted Role of Protein Phosphatase 1 in Plasmodium","volume":"37","author":"Khalife","year":"2021","journal-title":"Trends Parasitol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1483","DOI":"10.1152\/physrev.2000.80.4.1483","article-title":"Calcineurin: Form and Function","volume":"80","author":"Rusnak","year":"2000","journal-title":"Physiol. Rev."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"13367","DOI":"10.1074\/jbc.273.22.13367","article-title":"Regulation of the Calmodulin-stimulated Protein Phosphatase, Calcineurin","volume":"273","author":"Klee","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/S0166-6851(99)00010-9","article-title":"Characterization of protein Ser\/Thr phosphatases of the malaria parasite, Plasmodium falciparum: Inhibition of the parasitic calcineurin by cyclophilin-cyclosporin complex","volume":"99","author":"Dobson","year":"1999","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/0092-8674(91)90124-H","article-title":"Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes","volume":"66","author":"Liu","year":"1991","journal-title":"Cell"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1111\/cmi.12177","article-title":"Role of calcineurin and actin dynamics in regulated secretion of microneme proteins in Plasmodium falciparum merozoites during erythrocyte invasion","volume":"16","author":"Singh","year":"2014","journal-title":"Cell. Microbiol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.chom.2015.06.003","article-title":"Parasite Calcineurin Regulates Host Cell Recognition and Attachment by Apicomplexans","volume":"18","author":"Paul","year":"2015","journal-title":"Cell Host Microbe"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/j.chom.2015.05.018","article-title":"Conditional Degradation of Plasmodium Calcineurin Reveals Functions in Parasite Colonization of both Host and Vector","volume":"18","author":"Philip","year":"2015","journal-title":"Cell Host Microbe"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"11075","DOI":"10.1073\/pnas.91.23.11075","article-title":"Targeting of a distinctive protein-serine phosphatase to the protein kinase-like domain of the atrial natriuretic peptide receptor","volume":"91","author":"Chinkers","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"22586","DOI":"10.1016\/S0021-9258(17)31686-1","article-title":"Molecular cloning of a protein serine\/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain","volume":"269","author":"Becker","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"2358","DOI":"10.1016\/j.biocel.2007.08.010","article-title":"Protein phosphatase 5","volume":"40","author":"Hinds","year":"2008","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Dobson, S., Kar, B., Kumar, R., Adams, B., and Barik, S. (2001). A novel tetratricopeptide repeat (TPR) containing PP5 serine\/threonine protein phosphatase in the malaria parasite, Plasmodium falciparum. BMC Microbiol., 1.","DOI":"10.1016\/S0166-6851(01)00260-2"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0166-6851(02)00007-5","article-title":"Identification and biochemical characterisation of a protein phosphatase 5 homologue from Plasmodium falciparum","volume":"120","author":"Lindenthal","year":"2002","journal-title":"Mol. Biochem. Parasitol"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.chom.2014.05.020","article-title":"Genome-wide functional analysis of Plasmodium protein phosphatases reveals key regulators of parasite development and differentiation","volume":"16","author":"Guttery","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/j.ijpara.2019.03.007","article-title":"Plasmodium berghei serine\/threonine protein phosphatase PP5 plays a critical role in male gamete fertility","volume":"49","author":"Zhu","year":"2019","journal-title":"Int. J. Parasitol Drug"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/S0898-6568(02)00018-9","article-title":"Protein Ser\/Thr phosphatases with kelch-like repeat domains","volume":"14","author":"Kutuzov","year":"2002","journal-title":"Cell. Signal."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0166-6851(98)00106-6","article-title":"A putative protein serine\/threonine phosphatase from Plasmodium falciparum contains a large N-terminal extension and five unique inserts in the catalytic domain","volume":"95","author":"Li","year":"1998","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Philip, N., Vaikkinen, H.J., Tetley, L., and Waters, A.P. (2012). A unique Kelch domain phosphatase in Plasmodium regulates ookinete morphology, motility and invasion. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0044617"},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Guttery, D.S., Poulin, B., Ferguson, D.J., Szoor, B., Wickstead, B., Carroll, P.L., Ramakrishnan, C., Brady, D., Patzewitz, E.M., and Straschil, U. (2012). A unique protein phosphatase with kelch-like domains (PPKL) in Plasmodium modulates ookinete differentiation, motility and invasion. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1002948"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/1471-2148-4-47","article-title":"Widespread presence of \u201cbacterial-like\u201d PPP phosphatases in eukaryotes","volume":"4","author":"Andreeva","year":"2004","journal-title":"BMC Evol. Biol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1016\/j.celrep.2013.01.032","article-title":"An ancient protein phosphatase, SHLP1, is critical to microneme development in Plasmodium ookinetes and parasite transmission","volume":"3","author":"Patzewitz","year":"2013","journal-title":"Cell Rep."},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Miliu, A., Lebrun, M., Braun-Breton, C., and Lamarque, M.H. (2017). Shelph2, a bacterial-like phosphatase of the malaria parasite Plasmodium falciparum, is dispensable during asexual blood stage. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0187073"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1128\/EC.00027-13","article-title":"A bacterial phosphatase-like enzyme of the malaria parasite Plasmodium falciparum possesses tyrosine phosphatase activity and is implicated in the regulation of band 3 dynamics during parasite invasion","volume":"12","author":"Slouka","year":"2013","journal-title":"Eukaryot. Cell"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1051\/parasite\/2008153197","article-title":"Molecular dissection of host cell invasion by the Apicomplexans: The glideosome","volume":"15","year":"2008","journal-title":"Parasite"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"5197","DOI":"10.1074\/jbc.M509807200","article-title":"A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites","volume":"281","author":"Baum","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1128\/EC.00244-10","article-title":"Tracking Glideosome-associated protein 50 reveals the development and organization of the inner membrane complex of Plasmodium falciparum","volume":"10","author":"Yeoman","year":"2011","journal-title":"Eukaryot. Cell"},{"key":"ref_89","first-page":"2053","article-title":"Origin, composition, organization and function of the inner membrane complex of Plasmodium falciparum gametocytes","volume":"125","author":"Dearnley","year":"2012","journal-title":"J. Cell Sci."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.chom.2012.11.013","article-title":"Malaria Parasites Co-opt Human Factor H to Prevent Complement-Mediated Lysis in the Mosquito Midgut","volume":"13","author":"Simon","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.jsb.2012.02.009","article-title":"Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum","volume":"178","author":"Bosch","year":"2012","journal-title":"J. Struct. Biol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1111\/j.1462-5822.2010.01426.x","article-title":"Secretion of an acid phosphatase provides a possible mechanism to acquire host nutrients by Plasmodium falciparum","volume":"12","author":"Muller","year":"2010","journal-title":"Cell. Microbiol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1832","DOI":"10.1073\/pnas.0809632106","article-title":"Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development","volume":"106","author":"Harding","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Zhang, M., Mishra, S., Sakthivel, R., Fontoura, B.M., and Nussenzweig, V. (2016). UIS2: A Unique Phosphatase Required for the Development of Plasmodium Liver Stages. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005370"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"11241","DOI":"10.1074\/jbc.273.18.11241","article-title":"Identification and characterization of an unusual double serine\/threonine protein phosphatase 2C in the malaria parasite Plasmodium falciparum","volume":"273","author":"Mamoun","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1046\/j.1365-2958.2001.02289.x","article-title":"Plasmodium protein phosphatase 2C dephosphorylates translation elongation factor 1beta and inhibits its PKC-mediated nucleotide exchange activity in vitro","volume":"39","author":"Mamoun","year":"2001","journal-title":"Mol. Microbiol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1016\/j.bbamcr.2006.12.002","article-title":"Regulation of MAP kinases by MAP kinase phosphatases","volume":"1773","author":"Kondoh","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S1097-2765(01)00186-1","article-title":"Solution Structure of ERK2 Binding Domain of MAPK Phosphatase MKP-3: Structural Insights into MKP-3 Activation by ERK2","volume":"7","author":"Farooq","year":"2001","journal-title":"Mol. Cell"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3009.3001","DOI":"10.1186\/gb-2002-3-7-reviews3009","article-title":"MAP kinase phosphatases","volume":"3","author":"Theodosiou","year":"2002","journal-title":"Genome Biol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1016\/j.cellsig.2003.12.008","article-title":"Structure and regulation of MAPK phosphatases","volume":"16","author":"Farooq","year":"2004","journal-title":"Cell. Signal."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/S1286-4579(02)01538-1","article-title":"A role for Toxoplasma gondii type 1 ser\/thr protein phosphatase in host cell invasion","volume":"4","author":"Delorme","year":"2002","journal-title":"Microbes Infect."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.1128\/EC.00260-07","article-title":"A Toxoplasma gondii leucine-rich repeat protein binds phosphatase type 1 protein and negatively regulates its activity","volume":"6","author":"Daher","year":"2007","journal-title":"Eukaryot. Cell"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"2417","DOI":"10.1007\/s00436-017-5543-6","article-title":"The Toxoplasma gondii inhibitor-2 regulates protein phosphatase 1 activity through multiple motifs","volume":"116","author":"Deveuve","year":"2017","journal-title":"Parasitol. Res."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1128\/MMBR.00049-05","article-title":"Regulation of the cell cycle by protein phosphatase 2A in Saccharomyces cerevisiae","volume":"70","author":"Jiang","year":"2006","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Harding, C.R., Egarter, S., Gow, M., Jim\u00e9nez-Ruiz, E., Ferguson, D.J.P., and Meissner, M. (2016). Gliding Associated Proteins Play Essential Roles during the Formation of the Inner Membrane Complex of Toxoplasma gondii. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005403"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"e00877-00819","DOI":"10.1128\/mSphere.00877-19","article-title":"The Secreted Acid Phosphatase Domain-Containing GRA44 from Toxoplasma gondii Is Required for c-Myc Induction in Infected Cells","volume":"5","author":"Blakely","year":"2020","journal-title":"mSphere"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"5924","DOI":"10.1038\/s41598-019-42441-1","article-title":"A plasma membrane localized protein phosphatase in Toxoplasma gondii, PPM5C, regulates attachment to host cells","volume":"9","author":"Yang","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"e00858-00819","DOI":"10.1128\/mSphere.00858-19","article-title":"Coimmunoprecipitation with MYR1 Identifies Three Additional Proteins within the Toxoplasma gondii Parasitophorous Vacuole Required for Translocation of Dense Granule Effectors into Host Cells","volume":"5","author":"Cygan","year":"2020","journal-title":"mSphere"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"e1008771","DOI":"10.1371\/journal.ppat.1008771","article-title":"Toxoplasma gondii PPM3C, a secreted protein phosphatase, affects parasitophorous vacuole effector export","volume":"16","author":"Mayoral","year":"2020","journal-title":"PLoS Pathog."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/j.micinf.2009.06.002","article-title":"A Toxoplasma type 2C serine-threonine phosphatase is involved in parasite growth in the mammalian host cell","volume":"11","author":"Jan","year":"2009","journal-title":"Microbes Infect."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1091\/mbc.e02-08-0462","article-title":"Actin dynamics is controlled by a casein kinase II and phosphatase 2C interplay on Toxoplasma gondii Toxofilin","volume":"14","author":"Delorme","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"ref_112","first-page":"4333","article-title":"Toxofilin upregulates the host cortical actin cytoskeleton dynamics, facilitating Toxoplasma invasion","volume":"125","author":"Abrivard","year":"2012","journal-title":"J. Cell Sci."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1042\/BJ20061324","article-title":"The toxofilin-actin-PP2C complex of Toxoplasma: Identification of interacting domains","volume":"401","author":"Jan","year":"2007","journal-title":"Biochem. J."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1128\/EC.00309-06","article-title":"Toxoplasma gondii targets a protein phosphatase 2C to the nuclei of infected host cells","volume":"6","author":"Gilbert","year":"2007","journal-title":"Eukaryot. Cell"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1645\/18-210","article-title":"Epitope Analysis and Efficacy Evaluation of Phosphatase 2C (PP2C) DNA Vaccine Against Toxoplasma gondii Infection","volume":"106","author":"Song","year":"2020","journal-title":"J. Parasitol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1128\/EC.3.3.735-740.2004","article-title":"Functional unit of the RNA polymerase II C-terminal domain lies within heptapeptide pairs","volume":"3","author":"Stiller","year":"2004","journal-title":"Eukaryot. Cell"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.1074\/mcp.R700001-MCP200","article-title":"The annotation of both human and mouse kinomes in UniProtKB\/Swiss-Prot: One small step in manual annotation, one giant leap for full comprehension of genomes","volume":"7","author":"Orchard","year":"2008","journal-title":"Mol. Cell. Proteom. MCP"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"4739","DOI":"10.1111\/febs.12481","article-title":"Viewing serine\/threonine protein phosphatases through the eyes of drug designers","volume":"280","author":"Zhang","year":"2013","journal-title":"FEBS J."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1111\/febs.12000","article-title":"Protein tyrosine phosphatases in health and disease","volume":"280","author":"Hendriks","year":"2013","journal-title":"FEBS J."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"603","DOI":"10.2217\/fmb-2016-0029","article-title":"Phosphatases are emerging as novel druggable targets in Plasmodium","volume":"11","author":"Khalife","year":"2016","journal-title":"Future Microbiol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1021\/acscentsci.9b00909","article-title":"Turn and Face the Strange: A New View on Phosphatases","volume":"6","year":"2020","journal-title":"ACS Cent. Sci."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/nature18621","article-title":"Allosteric inhibition of SHP2 phosphatase inhibits cancers driven by receptor tyrosine kinases","volume":"535","author":"Chen","year":"2016","journal-title":"Nature"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1016\/j.cell.2018.06.030","article-title":"Target-Based Discovery of an Inhibitor of the Regulatory Phosphatase PPP1R15B","volume":"174","author":"Krzyzosiak","year":"2018","journal-title":"Cell"},{"key":"ref_124","unstructured":"(2021, September 01). Anavo Therapeutics. Available online: https:\/\/www.anavotx.com\/."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"4028","DOI":"10.1021\/pr400394g","article-title":"Global analysis of protein expression and phosphorylation of three stages of Plasmodium falciparum intraerythrocytic development","volume":"12","author":"Pease","year":"2013","journal-title":"J. Proteome Res."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"3996","DOI":"10.2174\/092986710793205363","article-title":"The physiological relevance of protein phosphatase 1 and its interacting proteins to health and disease","volume":"17","author":"Fardilha","year":"2010","journal-title":"Curr. Med. Chem."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1016\/j.cell.2009.10.006","article-title":"Serine\/Threonine Phosphatases: Mechanism through Structure","volume":"139","author":"Shi","year":"2009","journal-title":"Cell"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1038\/nature02582","article-title":"Structural basis of protein phosphatase 1 regulation","volume":"429","author":"Terrak","year":"2004","journal-title":"Nature"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s12576-017-0556-6","article-title":"Protein phosphatases 1 and 2A and their naturally occurring inhibitors: Current topics in smooth muscle physiology and chemical biology","volume":"68","author":"Takai","year":"2018","journal-title":"J. Physiol. Sci"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1006\/bbrc.1998.8730","article-title":"Modulation of the growth of Plasmodium falciparum in vitro by protein serine\/threonine phosphatase inhibitors","volume":"247","author":"Yokoyama","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.cbpa.2013.04.008","article-title":"Targeting the untargetable: Recent advances in the selective chemical modulation of protein phosphatase-1 activity","volume":"17","author":"Chatterjee","year":"2013","journal-title":"Curr. Opin. Chem. Biol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1016\/j.bmc.2017.08.040","article-title":"Microcystins: Synthesis and structure\u2013activity relationship studies toward PP1 and PP2A","volume":"26","author":"Fontanillo","year":"2018","journal-title":"Bioorg Med. Chem."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1002\/cmdc.202000801","article-title":"Tautomycetin Synthetic Analogues: Selective Inhibitors of Protein Phosphatase I","volume":"16","author":"Woydziak","year":"2021","journal-title":"ChemMedChem"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"5059","DOI":"10.1111\/bph.12863","article-title":"1E7-03, a low MW compound targeting host protein phosphatase-1, inhibits HIV-1 transcription","volume":"171","author":"Ammosova","year":"2014","journal-title":"Br. J. Pharm."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2145","DOI":"10.3389\/fmicb.2019.02145","article-title":"Targeting the Non-catalytic RVxF Site of Protein Phosphatase-1 With Small Molecules for Ebola Virus Inhibition","volume":"10","author":"Lin","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"76749","DOI":"10.18632\/oncotarget.19999","article-title":"Inhibition of HIV-1 infection in humanized mice and metabolic stability of protein phosphatase-1-targeting small molecule 1E7-03","volume":"8","author":"Lin","year":"2017","journal-title":"Oncotarget"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"3190","DOI":"10.1021\/acsinfecdis.0c00511","article-title":"Structural Optimization of 2,3-Dihydro-1H-cyclopenta[b]quinolines Targeting the Noncatalytic RVxF Site of Protein Phosphatase 1 for HIV-1 Inhibition","volume":"6","author":"Lin","year":"2020","journal-title":"ACS Infect. Dis."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1712","DOI":"10.1021\/acs.joc.9b02548","article-title":"Development of a Photoactivatable Protein Phosphatase-1-Disrupting Peptide","volume":"85","author":"Trebacz","year":"2020","journal-title":"J. Org. Chem."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.molbiopara.2005.01.012","article-title":"Plasmodium falciparum calcineurin and its association with heat shock protein 90: Mechanisms for the antimalarial activity of cyclosporin A and synergism with geldanamycin","volume":"141","author":"Kumar","year":"2005","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_140","first-page":"1","article-title":"Antimalarial effect of cyclosporin-A on murine P. berghei and human P. falciparum","volume":"28","author":"Biswas","year":"1991","journal-title":"Indian J. Malariol."},{"key":"ref_141","first-page":"47","article-title":"Antimalarial activity of cyclosporins A, C and D","volume":"23","author":"Uadia","year":"1994","journal-title":"Afr. J. Med. Med. Sci."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1007\/BF01978803","article-title":"Antimalarial activity of cyclosporin A","volume":"11","year":"1981","journal-title":"Agents Actions"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1016\/j.bbrc.2008.09.005","article-title":"Effect of cyclosporine on parasitemia and survival of Plasmodium berghei infected mice","volume":"376","author":"Bobbala","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"O3","DOI":"10.1186\/1475-2875-9-S2-O3","article-title":"Identification and characterization of novel Plasmodium falciparum cyclophilins and their roles in the antimalarial actions of cyclosporin A and derivatives","volume":"9","author":"Bell","year":"2010","journal-title":"Malar. J."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1038\/s41467-017-01638-6","article-title":"Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum","volume":"8","author":"Prakash","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1186\/s12936-021-03865-1","article-title":"Analysing the essential proteins set of Plasmodium falciparum PF3D7 for novel drug targets identification against malaria","volume":"20","author":"Ali","year":"2021","journal-title":"Malar. J."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"3531","DOI":"10.1080\/07391102.2017.1392365","article-title":"High throughput in silico identification and characterization of Plasmodium falciparum PRL phosphatase inhibitors","volume":"36","author":"Pandey","year":"2018","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1002\/2211-5463.13171","article-title":"A Plasmodium falciparum protein tyrosine phosphatase inhibitor identified from the ChEMBL-NTD database blocks parasite growth","volume":"11","author":"Pandey","year":"2021","journal-title":"FEBS Open Bio."},{"key":"ref_149","unstructured":"(2021, September 01). PubChem\u2014CID 2928525, Available online: https:\/\/pubchem.ncbi.nlm.nih.gov\/compound\/2928525."},{"key":"ref_150","unstructured":"(2021, September 01). RCSB Protein Data Bank\u2014Crystal Structure of PYST1 (MKP3). Available online: https:\/\/www.rcsb.org\/structure\/1MKP."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1111\/cbdd.12315","article-title":"In silico characterization of an atypical MAPK phosphatase of Plasmodium falciparum as a suitable target for drug discovery","volume":"84","author":"Campbell","year":"2014","journal-title":"Chem. Biol. Drug Des."}],"container-title":["Microorganisms"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-2607\/10\/3\/585\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T22:33:57Z","timestamp":1760135637000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-2607\/10\/3\/585"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,3,8]]},"references-count":151,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2022,3]]}},"alternative-id":["microorganisms10030585"],"URL":"https:\/\/doi.org\/10.3390\/microorganisms10030585","relation":{},"ISSN":["2076-2607"],"issn-type":[{"value":"2076-2607","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,3,8]]}}}