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Notably, BKI-1708 does not affect the viability of mammalian cells. Upon exposure to BKI-1708, T. gondii tachyzoites form large multinucleated complexes named baryzoites and remain trapped within host cells. In this study, proteins binding to BKI-1708 were identified in soluble extracts of T. gondii ME49 tachyzoites and human foreskin fibroblasts (HFF) using differential affinity chromatography coupled to mass spectrometry (DAC-MS). Beyond kinases, secondary interactions in T. gondii involved the binding of proteins associated with cell division, cytoskeleton, vesicular trafficking, secretory organelles, and transcriptional and translational regulators. In non-infected HFFs, BKI-1708 interactors included cytoskeletal regulators along with multiple RNA\/DNA-binding proteins. Upon infection, this profile shifted, with cytoskeletal components no longer detected, while nucleic acid-binding proteins remained present, consistent with infection-induced chromatin and transcriptional remodeling. These results suggest that multi-target interference could contribute to the impaired cytokinesis and the formation of multinucleated baryzoites, aligning with the concept that antiprotozoal drugs exert efficacy through coordinated perturbation of multiple cellular processes rather than a single dominant target.<\/jats:p>","DOI":"10.3390\/microorganisms14081608","type":"journal-article","created":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T09:11:26Z","timestamp":1784797886000},"page":"1608","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Affino-Proteomic Analysis of Bumped Kinase Inhibitor BKI-1708 in Toxoplasma gondii and Human Fibroblast Host Cells"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0009-0007-2056-2157","authenticated-orcid":false,"given":"Maria Cristina","family":"Ferreira de Sousa","sequence":"first","affiliation":[{"name":"Institute of Parasitology, Vetsuisse Faculty, University of Bern, 3012 Bern, Switzerland"},{"name":"Graduate School for Cellular and Biomedical Sciences (GCB), University of Bern, 3012 Bern, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8189-9270","authenticated-orcid":false,"given":"Joachim","family":"M\u00fcller","sequence":"additional","affiliation":[{"name":"Institute of Parasitology, Vetsuisse Faculty, University of Bern, 3012 Bern, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6364-7325","authenticated-orcid":false,"given":"Manfred","family":"Heller","sequence":"additional","affiliation":[{"name":"Proteomics and Mass Spectrometry Core Facility, Department for BioMedical Research (DBMR), University of Bern, 3012 Bern, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne-Christine","family":"Uldry","sequence":"additional","affiliation":[{"name":"Proteomics and Mass Spectrometry Core Facility, Department for BioMedical Research (DBMR), University of Bern, 3012 Bern, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sophie","family":"Braga-Lagache","sequence":"additional","affiliation":[{"name":"Proteomics and Mass Spectrometry Core Facility, Department for BioMedical Research (DBMR), University of Bern, 3012 Bern, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kayode K.","family":"Ojo","sequence":"additional","affiliation":[{"name":"Department of Medicine, Center for Emerging and Re-Emerging Infectious Diseases, University of Washington, Seattle, WA 98109-4766, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wesley C. Van","family":"Voorhis","sequence":"additional","affiliation":[{"name":"Department of Medicine, Center for Emerging and Re-Emerging Infectious Diseases, University of Washington, Seattle, WA 98109-4766, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0622-2128","authenticated-orcid":false,"given":"Andrew","family":"Hemphill","sequence":"additional","affiliation":[{"name":"Institute of Parasitology, Vetsuisse Faculty, University of Bern, 3012 Bern, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,7,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Dubey, J.P. (2021). Toxoplasmosis of Animals and Humans, CRC Press.","DOI":"10.1201\/9781003199373"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Martorelli Di Genova, B., Wilson, S.K., Dubey, J.P., and Knoll, L.J. (2019). Intestinal Delta-6-Desaturase Activity Determines Host Range for Toxoplasma Sexual Reproduction. PLoS Biol., 17.","DOI":"10.1101\/688580"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.rvsc.2020.10.019","article-title":"Foodborne Transmission of Toxoplasma gondii Infection in the Last Decade. An Overview","volume":"135","author":"Almeria","year":"2021","journal-title":"Res. Vet. Sci."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Holec-G\u0105sior, L., and So\u0142owi\u0144ska, K. (2023). Detection of Toxoplasma gondii Infection in Small Ruminants: Old Problems, and Current Solutions. Animals, 13.","DOI":"10.3390\/ani13172696"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1111\/j.1574-6976.2011.00305.x","article-title":"Mechanisms of Toxoplasma gondii Persistence and Latency","volume":"36","author":"Sullivan","year":"2012","journal-title":"FEMS Microbiol. Rev."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"D391","DOI":"10.2741\/Weiss","article-title":"The development and biology of bradyzoites of Toxoplasma gondii","volume":"5","author":"Weiss","year":"2000","journal-title":"Front. Biosci."},{"key":"ref_7","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_8","doi-asserted-by":"crossref","first-page":"103143","DOI":"10.1016\/j.parint.2025.103143","article-title":"Prevalence, Risk Factors, Diagnosis and Outcomes of Toxoplasma gondii Infection in Pregnancy: A Review","volume":"110","author":"Walana","year":"2026","journal-title":"Parasitol. Int."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"20740","DOI":"10.1021\/acs.jmedchem.4c01733","article-title":"Comprehensive Insights into the Development of Antitoxoplasmosis Drugs: Current Advances, Obstacles, and Future Perspectives","volume":"67","author":"Liu","year":"2024","journal-title":"J. Med. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.ijpara.2020.01.006","article-title":"Bumped Kinase Inhibitors as Therapy for Apicomplexan Parasitic Diseases: Lessons Learned","volume":"50","author":"Choi","year":"2020","journal-title":"Int. J. Parasitol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"3135","DOI":"10.1021\/acs.jmedchem.9b00069","article-title":"Development of 5-Aminopyrazole-4-Carboxamide-Based Bumped-Kinase Inhibitors for Cryptosporidiosis Therapy","volume":"62","author":"Huang","year":"2019","journal-title":"J. Med. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.ijpddr.2021.05.001","article-title":"In Vitro Activity, Safety and in Vivo Efficacy of the Novel Bumped Kinase Inhibitor BKI-1748 in Non-Pregnant and Pregnant Mice Experimentally Infected with Neospora caninum Tachyzoites and Toxoplasma gondii Oocysts","volume":"16","author":"Imhof","year":"2021","journal-title":"Int. J. Parasitol. Drugs Drug Resist."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1021\/cb400115y","article-title":"Exploiting the Unique ATP-Binding Pocket of Toxoplasma Calcium-Dependent Protein Kinase 1 to Identify Its Substrates","volume":"8","author":"Lourido","year":"2013","journal-title":"ACS Chem. Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.ijmm.2012.07.012","article-title":"Does Protein Phosphorylation Govern Host Cell Entry and Egress by the Apicomplexa?","volume":"302","author":"Jacot","year":"2012","journal-title":"Int. J. Med. Microbiol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/nature09022","article-title":"Calcium-Dependent Protein Kinase 1 Is an Essential Regulator of Exocytosis in Toxoplasma","volume":"465","author":"Lourido","year":"2010","journal-title":"Nature"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2121","DOI":"10.1007\/s00436-013-3451-y","article-title":"Protein Kinases of Toxoplasma gondii: Functions and Drug Targets","volume":"112","author":"Wei","year":"2013","journal-title":"Parasitol. Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1021\/acsinfecdis.5c00051","article-title":"Bumped Kinase Inhibitors Inhibit Both Toxoplasma gondii MAPKL1 and CDPK1","volume":"11","author":"Montgomery","year":"2025","journal-title":"ACS Infect. Dis."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ijpddr.2014.12.001","article-title":"A Single Mutation in the Gatekeeper Residue in TgMAPKL-1 Restores the Inhibitory Effect of a Bumped Kinase Inhibitor on the Cell Cycle","volume":"5","author":"Sugi","year":"2014","journal-title":"Int. J. Parasitol. Drugs Drug Resist."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"6361","DOI":"10.1128\/AAC.01236-15","article-title":"In Vitro and In Vivo Effects of the Bumped Kinase Inhibitor 1294 in the Related Cyst-Forming Apicomplexans Toxoplasma gondii and Neospora caninum","volume":"59","author":"Winzer","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Winzer, P., Anghel, N., Imhof, D., Balmer, V., Ortega-Mora, L.-M., Ojo, K.K., Van Voorhis, W.C., M\u00fcller, J., and Hemphill, A. (2020). Neospora caninum: Structure and Fate of Multinucleated Complexes Induced by the Bumped Kinase Inhibitor BKI-1294. Pathogens, 9.","DOI":"10.3390\/pathogens9050382"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Winzer, P., M\u00fcller, J., Imhof, D., Ritler, D., Uldry, A.-C., Braga-Lagache, S., Heller, M., Ojo, K.K., Van Voorhis, W.C., and Ortega-Mora, L.-M. (2020). Neospora caninum: Differential Proteome of Multinucleated Complexes Induced by the Bumped Kinase Inhibitor BKI-1294. Microorganisms, 8.","DOI":"10.3390\/microorganisms8060801"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"100553","DOI":"10.1016\/j.ijpddr.2024.100553","article-title":"Efficacy of the Bumped Kinase Inhibitor BKI-1708 against the Cyst-Forming Apicomplexan Parasites Toxoplasma gondii and Neospora caninum in Vitro and in Experimentally Infected Mice","volume":"25","author":"Imhof","year":"2024","journal-title":"Int. J. Parasitol. Drugs Drug Resist."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Choi, R., Hulverson, M.A., Schaefer, D.A., Betzer, D.P., Riggs, M.W., Huang, W., Sun, V., Whitman, G.R., McCloskey, M.C., and Marsh, K. (2025). Anti-Cryptosporidium Efficacy of BKI-1708, an Inhibitor of Cryptosporidium Calcium-Dependent Protein Kinase 1. PLoS Neglected Trop. Dis., 19.","DOI":"10.1371\/journal.pntd.0013263"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"de Sousa, M.C.F., M\u00fcller, J., H\u00e4nggeli, K.P.A., Heller, M., Uldry, A.-C., Braga-Lagache, S., Leitao, A., Ortega-Mora, L.-M., Ojo, K.K., and Van Voorhis, W.C. (2026). Bumped Kinase Inhibitor BKI-1708 Interferes in Cytokinesis and Drives Baryzoite Conversion in the Cyst-Forming Apicomplexan Parasites Toxoplasma gondii, Neospora caninum and Besnoitia besnoiti. Int. J. Mol. Sci., 27.","DOI":"10.1101\/2025.10.22.684074"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"M\u00fcller, J., Boubaker, G., M\u00fcller, N., Uldry, A.-C., Braga-Lagache, S., Heller, M., and Hemphill, A. (2024). Investigating Antiprotozoal Chemotherapies with Novel Proteomic Tools\u2014Chances and Limitations: A Critical Review. Int. J. Mol. Sci., 25.","DOI":"10.20944\/preprints202405.2130.v1"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1002\/ajh.24314","article-title":"Diversity and Severity of Adverse Reactions to Quinine: A Systematic Review","volume":"91","author":"Liles","year":"2016","journal-title":"Am. J. Hematol."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"M\u00fcller, J., Anghel, N., Imhof, D., H\u00e4nggeli, K., Uldry, A.-C., Braga-Lagache, S., Heller, M., Ojo, K.K., Ortega-Mora, L.-M., and Van Voorhis, W.C. (2022). Common Molecular Targets of a Quinolone Based Bumped Kinase Inhibitor in Neospora caninum and Danio rerio. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23042381"},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Ajiboye, J., Uldry, A.-C., Heller, M., Naguleswaran, A., Fan, E., Van Voorhis, W.C., Hemphill, A., and M\u00fcller, J. (2024). Molecular Targets of the 5-Amido-Carboxamide Bumped Kinase Inhibitor BKI-1748 in Cryptosporidium parvum and HCT-8 Host Cells. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25052707"},{"key":"ref_29","first-page":"1","article-title":"Proteomic Characterization of Toxoplasma gondii ME49 Derived Strains Resistant to the Artemisinin Derivatives Artemiside and Artemisone Implies Potential Mode of Action Independent of ROS Formation","volume":"21","author":"Schlange","year":"2023","journal-title":"Int. J. Parasitol. Drugs Drug Resist."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Semeraro, M., Boubaker, G., Scaccaglia, M., M\u00fcller, J., Vigneswaran, A., H\u00e4nggeli, K.P.A., Amdouni, Y., Kramer, L.H., Vismarra, A., and Genchi, M. (2024). Transient Adaptation of Toxoplasma gondii to Exposure by Thiosemicarbazone Drugs That Target Ribosomal Proteins Is Associated with the Upregulated Expression of Tachyzoite Transmembrane Proteins and Transporters. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25169067"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1038\/nmeth.4256","article-title":"MSFragger: Ultrafast and Comprehensive Peptide Identification in Mass Spectrometry\u2013Based Proteomics","volume":"14","author":"Kong","year":"2017","journal-title":"Nat. Methods"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1038\/nature10098","article-title":"Global Quantification of Mammalian Gene Expression Control","volume":"473","author":"Busse","year":"2011","journal-title":"Nature"},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Fereig, R.M., and Nishikawa, Y. (2022). Genetic Disruption of Toxoplasma gondii Peroxiredoxin (TgPrx) 1 and 3 Reveals the Essential Role of TgPrx3 in Protecting Mice from Fatal Consequences of Toxoplasmosis. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23063076"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"115079","DOI":"10.18632\/oncotarget.23023","article-title":"Functional Characterization of a Unique Cytochrome P450 in Toxoplasma gondii","volume":"8","author":"Zhang","year":"2017","journal-title":"Oncotarget"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1186\/1297-9716-42-80","article-title":"Toxoplasma gondii Peroxiredoxin Promotes Altered Macrophage Function, Caspase-1-Dependent IL-1\u03b2 Secretion Enhances Parasite Replication","volume":"42","author":"Marshall","year":"2011","journal-title":"Vet. Res."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1126\/science.1165740","article-title":"Rapid Membrane Disruption by a Perforin-like Protein Facilitates Parasite Exit from Host Cells","volume":"323","author":"Kafsack","year":"2009","journal-title":"Science"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Li, M., Wang, H., Liu, J., Hao, P., Ma, L., and Liu, Q. (2015). The Apoptotic Role of Metacaspase in Toxoplasma gondii. Front. Microbiol., 6.","DOI":"10.3389\/fmicb.2015.01560"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1186\/s13071-021-04878-0","article-title":"Requirement of Toxoplasma gondii Metacaspases for IMC1 Maturation, Endodyogeny and Virulence in Mice","volume":"14","author":"Li","year":"2021","journal-title":"Parasites Vectors"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Radke, J.B., Worth, D., Hong, D., Huang, S., Sullivan, W.J., Wilson, E.H., and White, M.W. (2018). Transcriptional Repression by ApiAP2 Factors Is Central to Chronic Toxoplasmosis. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1007035"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1038\/s41564-025-01980-2","article-title":"An ISWI-Related Chromatin Remodeller Regulates Stage-Specific Gene Expression in Toxoplasma gondii","volume":"10","author":"Pachano","year":"2025","journal-title":"Nat. Microbiol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"20507","DOI":"10.1074\/jbc.M301994200","article-title":"Human PLU-1 Has Transcriptional Repression Properties and Interacts with the Developmental Transcription Factors BF-1 and PAX9","volume":"278","author":"Tan","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1016\/j.molcel.2007.03.001","article-title":"PLU-1 Is an H3K4 Demethylase Involved in Transcriptional Repression and Breast Cancer Cell Proliferation","volume":"25","author":"Yamane","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Delgado, I.L.S., Gon\u00e7alves, J., Fernandes, R., Z\u00faquete, S., Basto, A.P., Leit\u00e3o, A., Soares, H., and Nolasco, S. (2024). Balancing Act: Tubulin Glutamylation and Microtubule Dynamics in Toxoplasma gondii. Microorganisms, 12.","DOI":"10.20944\/preprints202401.0287.v1"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Burette, M., Pezinsky, M., Nguyen, Q., Benharoual, A., Patray, S., Maynadier, M., Delabre, J., Mouveaux, T., Graindorge, A., and Berry, L. (2026). Two Anchoring Proteins Control Daughter Apical Complex Assembly in Toxoplasma gondii. bioRxiv.","DOI":"10.64898\/2026.02.13.705759"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1083\/jcb.200811072","article-title":"A Conserved CCCH-Type Zinc Finger Protein Regulates mRNA Nuclear Adenylation and Export","volume":"185","author":"Hurt","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1091\/mbc.10.1.105","article-title":"Dissociation of the Tubulin-Sequestering and Microtubule Catastrophe-Promoting Activities of Oncoprotein 18\/Stathmin","volume":"10","author":"Howell","year":"1999","journal-title":"Mol. Biol. Cell"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3765","DOI":"10.1016\/S0021-9258(19)84915-3","article-title":"Intracellular Substrates for Extracellular Signaling. Characterization of a Ubiquitous, Neuron-Enriched Phosphoprotein (Stathmin)","volume":"264","author":"Sobel","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1002\/1097-4644(20000915)78:4<558::AID-JCB5>3.0.CO;2-I","article-title":"Interaction of hCLIM1, an Enigma Family Protein, with Alpha-Actinin 2","volume":"78","author":"Kotaka","year":"2000","journal-title":"J. Cell. Biochem."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"31918","DOI":"10.1074\/jbc.C110.166066","article-title":"Collapsin Response Mediator Protein-2 (Crmp2) Regulates Trafficking by Linking Endocytic Regulatory Proteins to Dynein Motors","volume":"285","author":"Rahajeng","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"13597","DOI":"10.1074\/jbc.275.18.13597","article-title":"Mammalian Homologues of Yeast Sec31p. An Ubiquitously Expressed Form Is Localized to Endoplasmic Reticulum (ER) Exit Sites and Is Essential for ER-Golgi Transport","volume":"275","author":"Tang","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1083\/jcb.201012179","article-title":"SLAIN2 Links Microtubule plus End-Tracking Proteins and Controls Microtubule Growth in Interphase","volume":"193","author":"Manatschal","year":"2011","journal-title":"J. Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1038\/s41422-021-00584-9","article-title":"Regulators of Tubulin Polyglutamylation Control Nuclear Shape and Cilium Disassembly by Balancing Microtubule and Actin Assembly","volume":"32","author":"Wang","year":"2022","journal-title":"Cell Res."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/S0006-8993(99)02294-5","article-title":"Regulation of Phosphorylation of Neuronal Microtubule-Associated Proteins MAP1b and MAP2 by Protein Phosphatase-2A and -2B in Rat Brain","volume":"853","author":"Gong","year":"2000","journal-title":"Brain Res."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1152\/physrev.00030.2001","article-title":"Annexins: From Structure to Function","volume":"82","author":"Gerke","year":"2002","journal-title":"Physiol. Rev."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"168933","DOI":"10.1016\/j.jmb.2024.168933","article-title":"The RNA-Binding Properties of Annexins","volume":"437","author":"Tartaglia","year":"2025","journal-title":"J. Mol. Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2979","DOI":"10.1016\/j.celrep.2017.02.080","article-title":"The Human CCHC-Type Zinc Finger Nucleic Acid-Binding Protein Binds G-Rich Elements in Target mRNA Coding Sequences and Promotes Translation","volume":"18","author":"Benhalevy","year":"2017","journal-title":"Cell Rep."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2083","DOI":"10.1101\/gad.889201","article-title":"Suppression of Cap-Dependent Translation in Mitosis","volume":"15","author":"Pyronnet","year":"2001","journal-title":"Genes Dev."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1038\/nsmb1116","article-title":"Molecular Recognition of Histone H3 by the WD40 Protein WDR5","volume":"13","author":"Couture","year":"2006","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"43285","DOI":"10.1074\/jbc.M108137200","article-title":"Granzyme A Activates an Endoplasmic Reticulum-Associated Caspase-Independent Nuclease to Induce Single-Stranded DNA Nicks","volume":"276","author":"Beresford","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/S0092-8674(03)00150-8","article-title":"Tumor Suppressor NM23-H1 Is a Granzyme A-Activated DNase during CTL-Mediated Apoptosis, and the Nucleosome Assembly Protein SET Is Its Inhibitor","volume":"112","author":"Fan","year":"2003","journal-title":"Cell"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/cyto.1996.0001","article-title":"Partial N-Terminal Amino Acid Sequence of the Anti-Neoplastic Urinary Protein (ANUP) and the Anti-Tumour Effect of the N-Terminal Nonapeptide of the Unique Cytokine Present in Human Granulocytes","volume":"8","author":"Ridge","year":"1996","journal-title":"Cytokine"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"12147","DOI":"10.1073\/pnas.1932773100","article-title":"Identification of a Family of cAMP Response Element-Binding Protein Coactivators by Genome-Scale Functional Analysis in Mammalian Cells","volume":"100","author":"Iourgenko","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.cell.2004.09.015","article-title":"The CREB Coactivator TORC2 Functions as a Calcium- and cAMP-Sensitive Coincidence Detector","volume":"119","author":"Screaton","year":"2004","journal-title":"Cell"},{"key":"ref_64","first-page":"1586","article-title":"A Human Erythrocyte-Derived Growth-Promoting Factor with a Wide Target Cell Spectrum: Identification as Catalase","volume":"55","author":"Takeuchi","year":"1995","journal-title":"Cancer Res."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"110580","DOI":"10.1016\/j.jbc.2025.110580","article-title":"In-Depth Analysis of the Tear Fluid Glycoproteome Reveals Diverse Lacritin Glycosylation and Spliceoforms","volume":"301","author":"Chang","year":"2025","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1101\/gad.212308.112","article-title":"PQBP1, a Factor Linked to Intellectual Disability, Affects Alternative Splicing Associated with Neurite Outgrowth","volume":"27","author":"Wang","year":"2013","journal-title":"Genes Dev."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1093\/hmg\/8.6.977","article-title":"PQBP-1, a Novel Polyglutamine Tract-Binding Protein, Inhibits Transcription Activation by Brn-2 and Affects Cell Survival","volume":"8","author":"Waragai","year":"1999","journal-title":"Hum. Mol. Genet."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1038\/nchembio.2172","article-title":"Lactate Metabolism Is Associated with Mammalian Mitochondria","volume":"12","author":"Chen","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1093\/nar\/gkl1058","article-title":"The BRCT Domain of Mammalian Pes1 Is Crucial for Nucleolar Localization and rRNA Processing","volume":"35","author":"Grimm","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"3682","DOI":"10.1128\/MCB.00172-07","article-title":"Interdependence of Pes1, Bop1, and WDR12 Controls Nucleolar Localization and Assembly of the PeBoW Complex Required for Maturation of the 60S Ribosomal Subunit","volume":"27","author":"Rohrmoser","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.devcel.2017.09.022","article-title":"PWP1 Mediates Nutrient-Dependent Growth Control through Nucleolar Regulation of Ribosomal Gene Expression","volume":"43","author":"Liu","year":"2017","journal-title":"Dev. Cell"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1038\/nature18610","article-title":"Ki-67 Acts as a Biological Surfactant to Disperse Mitotic Chromosomes","volume":"535","author":"Cuylen","year":"2016","journal-title":"Nature"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"F1000 Faculty Rev-1719","DOI":"10.12688\/f1000research.16021.1","article-title":"Metabolic Interactions between Toxoplasma gondii and Its Host","volume":"7","author":"Blume","year":"2018","journal-title":"F1000Res"},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Sun, H., Li, J., Wang, L., Yin, K., Xu, C., Liu, G., Xiao, T., Huang, B., Wei, Q., and Gong, M. (2021). Comparative Proteomics Analysis for Elucidating the Interaction Between Host Cells and Toxoplasma gondii. Front. Cell. Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.643001"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Wu, S.-Z., Wei, H.-X., Jiang, D., Li, S.-M., Zou, W.-H., and Peng, H.-J. (2020). Genome-Wide CRISPR Screen Identifies Host Factors Required by Toxoplasma gondii Infection. Front. Cell. Infect. Microbiol., 9.","DOI":"10.3389\/fcimb.2019.00460"},{"key":"ref_76","first-page":"794","article-title":"Mammalian Splicing Factor SF1 Is Encoded by Variant cDNAs and Binds to RNA","volume":"2","author":"Arning","year":"1996","journal-title":"RNA"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"4549","DOI":"10.1093\/emboj\/18.16.4549","article-title":"Phosphorylation of Splicing Factor SF1 on Ser20 by cGMP-Dependent Protein Kinase Regulates Spliceosome Assembly","volume":"18","author":"Wang","year":"1999","journal-title":"EMBO J."}],"container-title":["Microorganisms"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-2607\/14\/8\/1608\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,25]],"date-time":"2026-07-25T04:21:37Z","timestamp":1784953297000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-2607\/14\/8\/1608"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,23]]},"references-count":77,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2026,8]]}},"alternative-id":["microorganisms14081608"],"URL":"https:\/\/doi.org\/10.3390\/microorganisms14081608","relation":{},"ISSN":["2076-2607"],"issn-type":[{"value":"2076-2607","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,23]]}}}