{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T23:51:34Z","timestamp":1790898694098,"version":"4.1.0"},"reference-count":221,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2022,5,31]],"date-time":"2022-05-31T00:00:00Z","timestamp":1653955200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"MIUR PRIN","award":["2017RKWNJT"],"award-info":[{"award-number":["2017RKWNJT"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Glycogen synthase kinase-3 (GSK-3) is an evolutionarily conserved, ubiquitously expressed, multifunctional serine\/threonine protein kinase involved in the regulation of a variety of physiological processes. GSK-3 comprises two isoforms (\u03b1 and \u03b2) which were originally discovered in 1980 as enzymes involved in glucose metabolism via inhibitory phosphorylation of glycogen synthase. Differently from other proteins kinases, GSK-3 isoforms are constitutively active in resting cells, and their modulation mainly involves inhibition through upstream regulatory networks. In the early 1990s, GSK-3 isoforms were implicated as key players in cancer cell pathobiology. Active GSK-3 facilitates the destruction of multiple oncogenic proteins which include \u03b2-catenin and Master regulator of cell cycle entry and proliferative metabolism (c-Myc). Therefore, GSK-3 was initially considered to be a tumor suppressor. Consistently, GSK-3 is often inactivated in cancer cells through dysregulated upstream signaling pathways. However, over the past 10\u201315 years, a growing number of studies highlighted that in some cancer settings GSK-3 isoforms inhibit tumor suppressing pathways and therefore act as tumor promoters. In this article, we will discuss the multiple and often enigmatic roles played by GSK-3 isoforms in some chronic hematological malignancies (chronic myelogenous leukemia, chronic lymphocytic leukemia, multiple myeloma, and B-cell non-Hodgkin\u2019s lymphomas) which are among the most common blood cancer cell types. We will also summarize possible novel strategies targeting GSK-3 for innovative therapies of these disorders.<\/jats:p>","DOI":"10.3390\/cells11111812","type":"journal-article","created":{"date-parts":[[2022,6,1]],"date-time":"2022-06-01T03:33:18Z","timestamp":1654054398000},"page":"1812","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Pathobiology and Therapeutic Relevance of GSK-3 in Chronic Hematological Malignancies"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5196-7260","authenticated-orcid":false,"given":"Alberto M.","family":"Martelli","sequence":"first","affiliation":[{"name":"Department of Biomedical and Neuromotor Sciences, University of Bologna, 40126 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesca","family":"Paganelli","sequence":"additional","affiliation":[{"name":"Department of Biomedical and Neuromotor Sciences, University of Bologna, 40126 Bologna, Italy"},{"name":"CNR-Institute of Molecular Genetics \u201cLuigi Luca Cavalli-Sforza\u201d, Unit of Bologna, 40136 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Camilla","family":"Evangelisti","sequence":"additional","affiliation":[{"name":"Department of Biomedical and Neuromotor Sciences, University of Bologna, 40126 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesca","family":"Chiarini","sequence":"additional","affiliation":[{"name":"CNR-Institute of Molecular Genetics \u201cLuigi Luca Cavalli-Sforza\u201d, Unit of Bologna, 40136 Bologna, Italy"},{"name":"IRCCS Istituto Ortopedico Rizzoli, 40136 Bologna, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6027-3156","authenticated-orcid":false,"given":"James A.","family":"McCubrey","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, East Carolina University, Greenville, NC 27834, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,5,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2391","DOI":"10.1182\/blood-2016-03-643544","article-title":"The 2016 revision to the World Health Organization classification of myeloid neoplasms and acute leukemia","volume":"127","author":"Arber","year":"2016","journal-title":"Blood"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"2375","DOI":"10.1182\/blood-2016-01-643569","article-title":"The 2016 revision of the World Health Organization classification of lymphoid neoplasms","volume":"127","author":"Swerdlow","year":"2016","journal-title":"Blood"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1007\/s11899-021-00655-z","article-title":"The Evolving Landscape of Frontline Therapy in Chronic Phase Chronic Myeloid Leukemia (CML)","volume":"16","author":"Wolfe","year":"2021","journal-title":"Curr. Hematol. Malign. Rep."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/s40265-021-01657-0","article-title":"Current Treatment of Chronic Lymphocytic Leukemia: The Diminishing Role of Chemoimmunotherapy","volume":"82","author":"Roeker","year":"2022","journal-title":"Drugs"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1007\/s40265-021-01514-0","article-title":"Evolution of Treatment Paradigms in Newly Diagnosed Multiple Myeloma","volume":"81","author":"Elnair","year":"2021","journal-title":"Drugs"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"a034843","DOI":"10.1101\/cshperspect.a034843","article-title":"Non-Hodgkin Lymphomas: Malignancies Arising from Mature B Cells","volume":"11","author":"Shingleton","year":"2021","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1080\/17474086.2020.1717944","article-title":"What are the considerations for tyrosine kinase inhibitor discontinuation in chronic-phase chronic myeloid leukemia?","volume":"13","author":"Harrington","year":"2020","journal-title":"Expert Rev. Hematol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2205","DOI":"10.3324\/haematol.2019.236000","article-title":"Chronic lymphocytic leukemia: From molecular pathogenesis to novel therapeutic strategies","volume":"105","author":"Delgado","year":"2020","journal-title":"Haematologica"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"114053","DOI":"10.1016\/j.ejmech.2021.114053","article-title":"A review on the treatment of multiple myeloma with small molecular agents in the past five years","volume":"229","author":"Zhang","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Watanabe, T. (2021). Approaches of the Innate Immune System to Ameliorate Adaptive Immunotherapy for B-Cell Non-Hodgkin Lymphoma in Their Microenvironment. Cancers, 14.","DOI":"10.3390\/cancers14010141"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Cho, S.F., Xing, L., Anderson, K.C., and Tai, Y.T. (2021). Promising Antigens for the New Frontier of Targeted Immunotherapy in Multiple Myeloma. Cancers, 13.","DOI":"10.3390\/cancers13236136"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1002\/ajh.26367","article-title":"Chronic lymphocytic leukemia: 2022 update on diagnostic and therapeutic procedures","volume":"96","author":"Hallek","year":"2021","journal-title":"Am. J. Hematol."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Alves, R., Goncalves, A.C., Rutella, S., Almeida, A.M., De Las Rivas, J., Trougakos, I.P., and Sarmento Ribeiro, A.B. (2021). Resistance to Tyrosine Kinase Inhibitors in Chronic Myeloid Leukemia-From Molecular Mechanisms to Clinical Relevance. Cancers, 13.","DOI":"10.3390\/cancers13194820"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"106037","DOI":"10.1016\/j.phrs.2021.106037","article-title":"Properties of FDA-approved small molecule protein kinase inhibitors: A 2022 update","volume":"175","author":"Roskoski","year":"2022","journal-title":"Pharmacol. Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1186\/s12943-018-0804-2","article-title":"Kinase-targeted cancer therapies: Progress, challenges and future directions","volume":"17","author":"Bhullar","year":"2018","journal-title":"Mol. Cancer"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1042\/bst0290537","article-title":"Regulation of glycogen synthesis in human muscle cells","volume":"29","author":"Yeaman","year":"2001","journal-title":"Biochem. Soc. Trans."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"4032","DOI":"10.4161\/cc.8.24.10111","article-title":"Regulation of protein stability by GSK3 mediated phosphorylation","volume":"8","author":"Xu","year":"2009","journal-title":"Cell Cycle"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2942","DOI":"10.1016\/j.bbamcr.2016.09.004","article-title":"Effects of mutations in Wnt\/\u03b2-catenin, hedgehog, Notch and PI3K pathways on GSK-3 activity-Diverse effects on cell growth, metabolism and cancer","volume":"1863","author":"McCubrey","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"341","DOI":"10.3389\/fcell.2019.00341","article-title":"Signaling Enzymes Required for Sperm Maturation and Fertilization in Mammals","volume":"7","author":"Dey","year":"2019","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1007\/s12035-013-8571-y","article-title":"Glycogen synthase kinase 3 \u03b2 (GSK3\u03b2) at the tip of neuronal development and regeneration","volume":"49","author":"Seira","year":"2014","journal-title":"Mol. Neurobiol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"4209475","DOI":"10.1155\/2019\/4209475","article-title":"GSK-3\u03b2 at the Intersection of Neuronal Plasticity and Neurodegeneration","volume":"2019","author":"Jaworski","year":"2019","journal-title":"Neural Plast."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"167","DOI":"10.12688\/f1000research.10557.1","article-title":"Recent advances in understanding the cellular roles of GSK-3","volume":"6","author":"Cormier","year":"2017","journal-title":"F1000Res"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"663","DOI":"10.2174\/1389200219666171227203737","article-title":"Glycogen Synthase Kinase-3\u03b2 as a Putative Therapeutic Target for Bipolar Disorder","volume":"19","author":"Dandekar","year":"2018","journal-title":"Curr. Drug Metab."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.bcp.2019.02.020","article-title":"Glycogen synthase kinase-3 inhibitor as a multi-targeting anti-rheumatoid drug","volume":"165","author":"Arioka","year":"2019","journal-title":"Biochem. Pharmacol."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Huang, A., Patel, S., McAlpine, C.S., and Werstuck, G.H. (2018). The Role of Endoplasmic Reticulum Stress-Glycogen Synthase Kinase-3 Signaling in Atherogenesis. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19061607"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.semcancer.2017.12.010","article-title":"Glycogen synthase kinases: Moonlighting proteins with theranostic potential in cancer","volume":"56","author":"Nagini","year":"2019","journal-title":"Semin. Cancer Biol."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Demuro, S., Di Martino, R.M.C., Ortega, J.A., and Cavalli, A. (2021). GSK-3\u03b2, FYN, and DYRK1A: Master Regulators in Neurodegenerative Pathways. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22169098"},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"D\u2019Mello, S.R. (2021). When Good Kinases Go Rogue: GSK3, p38 MAPK and CDKs as Therapeutic Targets for Alzheimer\u2019s and Huntington\u2019s Disease. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22115911"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"4629495","DOI":"10.1155\/2017\/4629495","article-title":"Multifaceted Roles of GSK-3 in Cancer and Autophagy-Related Diseases","volume":"2017","author":"Mancinelli","year":"2017","journal-title":"Oxid. Med. Cell Longev."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"118659","DOI":"10.1016\/j.bbamcr.2020.118659","article-title":"GSK-3\u03b2 in DNA repair, apoptosis, and resistance of chemotherapy, radiotherapy of cancer","volume":"1867","author":"Lin","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4","DOI":"10.3389\/fnmol.2012.00004","article-title":"GSK3 as a Sensor Determining Cell Fate in the Brain","volume":"5","author":"Cole","year":"2012","journal-title":"Front. Mol. Neurosci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"44","DOI":"10.3389\/fnmol.2011.00044","article-title":"Functions of GSK-3 Signaling in Development of the Nervous System","volume":"4","author":"Kim","year":"2011","journal-title":"Front. Mol. Neurosci."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0378-1119(02)01092-2","article-title":"Gene structure and alternative splicing of glycogen synthase kinase 3 \u03b2 (GSK-3\u03b2) in neural and non-neural tissues","volume":"302","author":"Schaffer","year":"2003","journal-title":"Gene"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.mcn.2009.07.002","article-title":"An alternatively spliced form of glycogen synthase kinase-3\u03b2 is targeted to growing neurites and growth cones","volume":"42","author":"Kraus","year":"2009","journal-title":"Mol. Cell Neurosci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"29227","DOI":"10.1074\/jbc.M112.372086","article-title":"GSK-3\u03b1 and GSK-3\u03b2 proteins are involved in early stages of chondrocyte differentiation with functional redundancy through RelA protein phosphorylation","volume":"287","author":"Itoh","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1038\/35017574","article-title":"Requirement for glycogen synthase kinase-3\u03b2 in cell survival and NF-\u03baB activation","volume":"406","author":"Hoeflich","year":"2000","journal-title":"Nature"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/nature05557","article-title":"Chemical rescue of cleft palate and midline defects in conditional GSK-3\u03b2 mice","volume":"446","author":"Liu","year":"2007","journal-title":"Nature"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"3609","DOI":"10.1172\/JCI36245","article-title":"Deletion of GSK-3\u03b2 in mice leads to hypertrophic cardiomyopathy secondary to cardiomyoblast hyperproliferation","volume":"118","author":"Kerkela","year":"2008","journal-title":"J. Clin. Investig."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2092","DOI":"10.1128\/MCB.01405-08","article-title":"Subcellular localization of glycogen synthase kinase 3\u03b2 controls embryonic stem cell self-renewal","volume":"29","author":"Bechard","year":"2009","journal-title":"Mol. Cell Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"118635","DOI":"10.1016\/j.bbamcr.2019.118635","article-title":"Crosstalks of GSK3 signaling with the mTOR network and effects on targeted therapy of cancer","volume":"1867","author":"Evangelisti","year":"2019","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"5074","DOI":"10.1158\/1078-0432.CCR-06-0196","article-title":"Aberrant nuclear accumulation of glycogen synthase kinase-3\u03b2 in human pancreatic cancer: Association with kinase activity and tumor dedifferentiation","volume":"12","author":"Ougolkov","year":"2006","journal-title":"Clin. Cancer Res."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"e1142","DOI":"10.1038\/cddis.2014.102","article-title":"Differential activity of GSK-3 isoforms regulates NF-\u03baB and TRAIL- or TNF\u03b1 induced apoptosis in pancreatic cancer cells","volume":"5","author":"Zhang","year":"2014","journal-title":"Cell Death Dis."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.molcel.2006.10.009","article-title":"A chaperone-dependent GSK3\u03b2 transitional intermediate mediates activation-loop autophosphorylation","volume":"24","author":"Lochhead","year":"2006","journal-title":"Mol. Cell"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"775","DOI":"10.18632\/oncotarget.1770","article-title":"Targeting Src-mediated Tyr216 phosphorylation and activation of GSK-3 in prostate cancer cells inhibit prostate cancer progression in vitro and in vivo","volume":"5","author":"Goc","year":"2014","journal-title":"Oncotarget"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.bbrc.2004.02.061","article-title":"Glycogen synthase kinase-3\u03b2 is tyrosine-phosphorylated by MEK1 in human skin fibroblasts","volume":"316","author":"Shiraishi","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/S0092-8674(01)00374-9","article-title":"Crystal structure of glycogen synthase kinase 3 \u03b2: Structural basis for phosphate-primed substrate specificity and autoinhibition","volume":"105","author":"Dajani","year":"2001","journal-title":"Cell"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"758","DOI":"10.4049\/jimmunol.169.2.758","article-title":"The B cell antigen receptor regulates the transcriptional activator \u03b2-catenin via protein kinase C-mediated inhibition of glycogen synthase kinase-3","volume":"169","author":"Christian","year":"2002","journal-title":"J. Immunol."},{"key":"ref_48","first-page":"40","article-title":"GSK-3: Functional Insights from Cell Biology and Animal Models","volume":"4","author":"Woodgett","year":"2011","journal-title":"Front. Mol. Neurosci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1126\/science.1156037","article-title":"Phosphorylation by p38 MAPK as an alternative pathway for GSK3\u03b2 inactivation","volume":"320","author":"Thornton","year":"2008","journal-title":"Science"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"16","DOI":"10.3389\/fonc.2013.00016","article-title":"GSK-3 and mitochondria in cancer cells","volume":"3","author":"Chiara","year":"2013","journal-title":"Front. Oncol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.cellsig.2010.09.011","article-title":"SHP-1 inhibits \u03b2-catenin function by inducing its degradation and interfering with its association with TATA-binding protein","volume":"23","author":"Simoneau","year":"2011","journal-title":"Cell Signal."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/j.mce.2016.08.048","article-title":"Protein tyrosine phosphatase SHP-1 modulates osteoblast differentiation through direct association with and dephosphorylation of GSK3\u03b2","volume":"439","author":"Tang","year":"2017","journal-title":"Mol. Cell Endocrinol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.neuron.2007.01.029","article-title":"LTP inhibits LTD in the hippocampus via regulation of GSK3\u03b2","volume":"53","author":"Peineau","year":"2007","journal-title":"Neuron"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1038\/onc.2017.350","article-title":"Loss of protein phosphatase 2A regulatory subunit B56\u03b4 promotes spontaneous tumorigenesis in vivo","volume":"37","author":"Lambrecht","year":"2018","journal-title":"Oncogene"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s11010-010-0544-0","article-title":"Regulation of GSK3 isoforms by phosphatases PP1 and PP2A","volume":"344","author":"Hernandez","year":"2010","journal-title":"Mol. Cell Biochem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1158\/1535-7163.MCT-20-0497","article-title":"The Landscape of Glycogen Synthase Kinase-3 \u03b2 Genomic Alterations in Cancer","volume":"20","author":"Borden","year":"2021","journal-title":"Mol. Cancer Ther."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"118770","DOI":"10.1016\/j.bbamcr.2020.118770","article-title":"GSK-3 and miRs: Master regulators of therapeutic sensitivity of cancer cells","volume":"1867","author":"Duda","year":"2020","journal-title":"Biochim Biophys. Acta Mol. Cell Res."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"112949","DOI":"10.1016\/j.ejmech.2020.112949","article-title":"PROTACs suppression of GSK-3\u03b2, a crucial kinase in neurodegenerative diseases","volume":"210","author":"Jiang","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"14042","DOI":"10.1016\/S0021-9258(18)47901-X","article-title":"Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3","volume":"262","author":"Fiol","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1126\/science.272.5264.1023","article-title":"Binding of GSK3\u03b2 to the APC-\u03b2-catenin complex and regulation of complex assembly","volume":"272","author":"Rubinfeld","year":"1996","journal-title":"Science"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"3499","DOI":"10.1101\/gad.12.22.3499","article-title":"Glycogen synthase kinase-3\u03b2 regulates cyclin D1 proteolysis and subcellular localization","volume":"12","author":"Diehl","year":"1998","journal-title":"Genes Dev."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1002\/mc.10087","article-title":"Expression, localization, and activity of glycogen synthase kinase 3\u03b2 during mouse skin tumorigenesis","volume":"35","author":"Leis","year":"2002","journal-title":"Mol. Carcinog."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2512","DOI":"10.1158\/0008-5472.CAN-16-3242","article-title":"Mcl-1 Degradation Is Required for Targeted Therapeutics to Eradicate Colon Cancer Cells","volume":"77","author":"Tong","year":"2017","journal-title":"Cancer Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1016\/j.cell.2006.06.055","article-title":"TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth","volume":"126","author":"Inoki","year":"2006","journal-title":"Cell"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"14120","DOI":"10.1074\/jbc.M114.633057","article-title":"Rictor Undergoes Glycogen Synthase Kinase 3 (GSK3)-dependent, FBXW7-mediated Ubiquitination and Proteasomal Degradation","volume":"290","author":"Koo","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1042\/BJ20150404","article-title":"GSK3-mediated raptor phosphorylation supports amino-acid-dependent mTORC1-directed signalling","volume":"470","author":"Stretton","year":"2015","journal-title":"Biochem. J."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"E1204","DOI":"10.1073\/pnas.1110195108","article-title":"Glycogen synthase kinase (GSK)-3 promotes p70 ribosomal protein S6 kinase (p70S6K) activity and cell proliferation","volume":"108","author":"Shin","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1690","DOI":"10.1038\/onc.2013.113","article-title":"Glycogen synthase kinase-3\u03b2 positively regulates protein synthesis and cell proliferation through the regulation of translation initiation factor 4E-binding protein 1","volume":"33","author":"Shin","year":"2014","journal-title":"Oncogene"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/j.molcel.2018.04.024","article-title":"mTORC1 Promotes Metabolic Reprogramming by the Suppression of GSK3-Dependent Foxk1 Phosphorylation","volume":"70","author":"He","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"9993","DOI":"10.1523\/JNEUROSCI.2057-04.2004","article-title":"Glycogen synthase kinase-3\u03b2 phosphorylates Bax and promotes its mitochondrial localization during neuronal apoptosis","volume":"24","author":"Linseman","year":"2004","journal-title":"J. Neurosci."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1158\/2159-8290.CD-21-1059","article-title":"Hallmarks of Cancer: New Dimensions","volume":"12","author":"Hanahan","year":"2022","journal-title":"Cancer Discov."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.bcp.2017.10.016","article-title":"A partnership with the proteasome; the destructive nature of GSK3","volume":"147","author":"Robertson","year":"2018","journal-title":"Biochem. Pharmacol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.ccr.2008.10.013","article-title":"Glycogen synthase kinase-3 and cancer: Good cop, bad cop?","volume":"14","author":"Patel","year":"2008","journal-title":"Cancer Cell"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1093\/emboj\/cdg068","article-title":"Structural basis for recruitment of glycogen synthase kinase 3\u03b2 to the axin-APC scaffold complex","volume":"22","author":"Dajani","year":"2003","journal-title":"EMBO J."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"a007898","DOI":"10.1101\/cshperspect.a007898","article-title":"The \u03b2-catenin destruction complex","volume":"5","author":"Stamos","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"2854","DOI":"10.3389\/fimmu.2019.02854","article-title":"WNT Signaling in Tumors: The Way to Evade Drugs and Immunity","volume":"10","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/leu.2013.184","article-title":"Multifaceted roles of GSK-3 and Wnt\/\u03b2-catenin in hematopoiesis and leukemogenesis: Opportunities for therapeutic intervention","volume":"28","author":"McCubrey","year":"2014","journal-title":"Leukemia"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1038\/sj.emboj.7600633","article-title":"Role that phosphorylation of GSK3 plays in insulin and Wnt signalling defined by knockin analysis","volume":"24","author":"McManus","year":"2005","journal-title":"EMBO J."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1016\/j.devcel.2007.04.001","article-title":"Functional redundancy of GSK-3\u03b1 and GSK-3\u03b2 in Wnt\/\u03b2-catenin signaling shown by using an allelic series of embryonic stem cell lines","volume":"12","author":"Doble","year":"2007","journal-title":"Dev. Cell"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1146\/annurev.cellbio.20.010403.092805","article-title":"Signaling pathways in intestinal development and cancer","volume":"20","author":"Sancho","year":"2004","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/s12276-020-0380-6","article-title":"Wnt signaling in cancer: Therapeutic targeting of Wnt signaling beyond \u03b2-catenin and the destruction complex","volume":"52","author":"Jung","year":"2020","journal-title":"Exp. Mol. Med."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"aam8460","DOI":"10.1126\/scitranslmed.aam8460","article-title":"Exploiting an Asp-Glu \u201cswitch\u201d in glycogen synthase kinase 3 to design paralog-selective inhibitors for use in acute myeloid leukemia","volume":"10","author":"Wagner","year":"2018","journal-title":"Sci. Transl. Med."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S1074-7613(00)00004-2","article-title":"Wnt signaling regulates B lymphocyte proliferation through a LEF-1 dependent mechanism","volume":"13","author":"Reya","year":"2000","journal-title":"Immunity"},{"key":"ref_84","first-page":"587809","article-title":"Germinal Center Cells Turning to the Dark Side: Neoplasms of B Cells, Follicular Helper T Cells, and Follicular Dendritic Cells","volume":"10","year":"2020","journal-title":"Front. Oncol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"e582","DOI":"10.1097\/HS9.0000000000000582","article-title":"Biology of Germinal Center B Cells Relating to Lymphomagenesis","volume":"5","author":"Basso","year":"2021","journal-title":"Hemasphere"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1128\/MCB.00650-10","article-title":"Cyclin D3 is selectively required for proliferative expansion of germinal center B cells","volume":"31","author":"Cato","year":"2011","journal-title":"Mol. Cell Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"481","DOI":"10.4049\/jimmunol.2000908","article-title":"GSK3 Restrains Germinal Center B Cells to Form Plasma Cells","volume":"206","author":"Lee","year":"2021","journal-title":"J. Immunol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1038\/ni.3664","article-title":"Gsk3 is a metabolic checkpoint regulator in B cells","volume":"18","author":"Jellusova","year":"2017","journal-title":"Nat. Immunol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"129","DOI":"10.3389\/fendo.2018.00129","article-title":"The Role for Myc in Coordinating Glycolysis, Oxidative Phosphorylation, Glutaminolysis, and Fatty Acid Metabolism in Normal and Neoplastic Tissues","volume":"9","author":"Goetzman","year":"2018","journal-title":"Front. Endocrinol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1002\/ajh.25011","article-title":"Chronic myeloid leukemia: 2018 update on diagnosis, therapy and monitoring","volume":"93","author":"Jabbour","year":"2018","journal-title":"Am. J. Hematol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/243290a0","article-title":"Letter: A new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining","volume":"243","author":"Rowley","year":"1973","journal-title":"Nature"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1158\/1078-0432.CCR-09-3314","article-title":"Targeting the BCR-ABL Signaling Pathway in Therapy-Resistant Philadelphia Chromosome-Positive Leukemia","volume":"17","author":"Deininger","year":"2011","journal-title":"Clin. Cancer Res."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1111\/cas.12655","article-title":"Targeting the canonical Wnt\/-catenin pathway in hematological malignancies","volume":"106","author":"Ashihara","year":"2015","journal-title":"Cancer Sci."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1038\/nature08255","article-title":"Hedgehog signalling is essential for maintenance of cancer stem cells in myeloid leukaemia","volume":"460","author":"Zhao","year":"2009","journal-title":"Nature"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1186\/s12943-018-0780-6","article-title":"Chronic myeloid leukemia: The paradigm of targeting oncogenic tyrosine kinase signaling and counteracting resistance for successful cancer therapy","volume":"17","author":"Soverini","year":"2018","journal-title":"Mol. Cancer"},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Bavaro, L., Martelli, M., Cavo, M., and Soverini, S. (2019). Mechanisms of Disease Progression and Resistance to Tyrosine Kinase Inhibitor Therapy in Chronic Myeloid Leukemia: An Update. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20246141"},{"key":"ref_97","first-page":"1517","article-title":"An evidence-based analysis of the effect of busulfan, hydroxyurea, interferon, and allogeneic bone marrow transplantation in treating the chronic phase of chronic myeloid leukemia: Developed for the American Society of Hematology","volume":"94","author":"Silver","year":"1999","journal-title":"Blood"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"S177","DOI":"10.1007\/s00277-015-2313-3","article-title":"The role of hematopoietic stem cell transplantation in chronic myeloid leukemia","volume":"94","author":"Gratwohl","year":"2015","journal-title":"Ann. Hematol."},{"key":"ref_99","first-page":"935","article-title":"Approval summary for imatinib mesylate capsules in the treatment of chronic myelogenous leukemia","volume":"8","author":"Cohen","year":"2002","journal-title":"Clin. Cancer Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1182\/blood-2012-03-380147","article-title":"How I treat CML blast crisis","volume":"120","author":"Hehlmann","year":"2012","journal-title":"Blood"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"4391","DOI":"10.1002\/cncr.30864","article-title":"Prognostic factors and survival outcomes in patients with chronic myeloid leukemia in blast phase in the tyrosine kinase inhibitor era: Cohort study of 477 patients","volume":"123","author":"Jain","year":"2017","journal-title":"Cancer"},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Mostazo, M.G.C., Kurrle, N., Casado, M., Fuhrmann, D., Alshamleh, I., Haupl, B., Martin-Sanz, P., Brune, B., Serve, H., and Schwalbe, H. (2020). Metabolic Plasticity Is an Essential Requirement of Acquired Tyrosine Kinase Inhibitor Resistance in Chronic Myeloid Leukemia. Cancers, 12.","DOI":"10.3390\/cancers12113443"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1007\/s12185-010-0615-8","article-title":"Molecular pathways to CML stem cells","volume":"91","author":"Rice","year":"2010","journal-title":"Int. J. Hematol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1517\/14712598.2014.867323","article-title":"Kinase-inhibitor-insensitive cancer stem cells in chronic myeloid leukemia","volume":"14","author":"Morotti","year":"2014","journal-title":"Expert Opin. Biol. Ther."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1589","DOI":"10.3324\/haematol.2018.205054","article-title":"Observational study of chronic myeloid leukemia Italian patients who discontinued tyrosine kinase inhibitors in clinical practice","volume":"104","author":"Fava","year":"2019","journal-title":"Haematologica"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1056\/NEJMoa040258","article-title":"Granulocyte-macrophage progenitors as candidate leukemic stem cells in blast-crisis CML","volume":"351","author":"Jamieson","year":"2004","journal-title":"N. Engl. J. Med."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"3925","DOI":"10.1073\/pnas.0900189106","article-title":"Glycogen synthase kinase 3\u03b2 missplicing contributes to leukemia stem cell generation","volume":"106","author":"Abrahamsson","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1038\/sj.emboj.7601485","article-title":"Bcr-Abl stabilizes \u03b2-catenin in chronic myeloid leukemia through its tyrosine phosphorylation","volume":"26","author":"Coluccia","year":"2007","journal-title":"EMBO J."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1073\/pnas.1213021110","article-title":"ADAR1 promotes malignant progenitor reprogramming in chronic myeloid leukemia","volume":"110","author":"Jiang","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"4603","DOI":"10.3892\/mmr.2017.7215","article-title":"PIM-1 kinase inhibitor SMI-4a exerts antitumor effects in chronic myeloid leukemia cells by enhancing the activity of glycogen synthase kinase 3beta","volume":"16","author":"Fan","year":"2017","journal-title":"Mol. Med. Rep."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1016\/j.bbrc.2020.02.165","article-title":"Involvement of MCL1, c-myc, and cyclin D2 protein degradation in ponatinib-induced cytotoxicity against T315I(+) Ph+leukemia cells","volume":"525","author":"Inoue","year":"2020","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1182\/blood-2011-06-361261","article-title":"Targeting of GSK3\u03b2 promotes imatinib-mediated apoptosis in quiescent CD34+ chronic myeloid leukemia progenitors, preserving normal stem cells","volume":"119","author":"Reddiconto","year":"2012","journal-title":"Blood"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"9624","DOI":"10.1158\/0008-5472.CAN-08-1131","article-title":"Effects of dasatinib on SRC kinase activity and downstream intracellular signaling in primitive chronic myelogenous leukemia hematopoietic cells","volume":"68","author":"Konig","year":"2008","journal-title":"Cancer Res."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"6468","DOI":"10.1158\/0008-5472.CAN-06-0025","article-title":"Janus kinase 2: A critical target in chronic myelogenous leukemia","volume":"66","author":"Samanta","year":"2006","journal-title":"Cancer Res."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1056\/NEJMoa075290","article-title":"Monoclonal B-cell lymphocytosis and chronic lymphocytic leukemia","volume":"359","author":"Rawstron","year":"2008","journal-title":"N. Engl. J. Med."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"2745","DOI":"10.1182\/blood-2017-09-806398","article-title":"iwCLL guidelines for diagnosis, indications for treatment, response assessment, and supportive management of CLL","volume":"131","author":"Hallek","year":"2018","journal-title":"Blood"},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Pula, B., Golos, A., Gorniak, P., and Jamroziak, K. (2019). Overcoming Ibrutinib Resistance in Chronic Lymphocytic Leukemia. Cancers, 11.","DOI":"10.3390\/cancers11121834"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1186\/s40164-019-0139-8","article-title":"Frontline therapies for untreated chronic lymphoid leukemia","volume":"8","author":"Liu","year":"2019","journal-title":"Exp. Hematol. Oncol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1080\/14728214.2020.1724282","article-title":"Emerging bruton tyrosine kinase inhibitors for chronic lymphocytic leukaemia: One step ahead ibrutinib","volume":"25","author":"Molica","year":"2020","journal-title":"Expert Opin. Emerg. Drugs"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1796","DOI":"10.1182\/blood.2019001321","article-title":"Treatment-naive CLL: Lessons from phase 2 and phase 3 clinical trials","volume":"134","author":"Woyach","year":"2019","journal-title":"Blood"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1097\/PPO.0000000000000414","article-title":"Phosphatidylinositol 3 Kinase \u03b4 Inhibitors: Present and Future","volume":"25","author":"Brown","year":"2019","journal-title":"Cancer J."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"2899","DOI":"10.2147\/DDDT.S212500","article-title":"Clinical application of obinutuzumab for treating chronic lymphocytic leukemia","volume":"13","author":"Luan","year":"2019","journal-title":"Drug Des. Devel. Ther."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1200\/EDBK_238735","article-title":"Tailored Treatment Strategies for Chronic Lymphocytic Leukemia in a Rapidly Changing Era","volume":"39","author":"Brander","year":"2019","journal-title":"Am. Soc. Clin. Oncol. Educ. Book"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1097\/PPO.0000000000000406","article-title":"Resistance Mechanisms to Targeted Agents in Chronic Lymphocytic Leukemia","volume":"25","author":"Kittai","year":"2019","journal-title":"Cancer J."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s10020-018-0001-1","article-title":"Critical molecular pathways in CLL therapy","volume":"24","author":"Ferrer","year":"2018","journal-title":"Mol. Med."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"3118","DOI":"10.1073\/pnas.0308648100","article-title":"Activation of the Wnt signaling pathway in chronic lymphocytic leukemia","volume":"101","author":"Lu","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"3839","DOI":"10.1038\/s41467-018-06069-5","article-title":"Notch2 controls non-autonomous Wnt-signalling in chronic lymphocytic leukaemia","volume":"9","author":"Mangolini","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1182\/blood-2006-12-060947","article-title":"Inhibition of glycogen synthase kinase-3 activity leads to epigenetic silencing of nuclear factor kappaB target genes and induction of apoptosis in chronic lymphocytic leukemia B cells","volume":"110","author":"Ougolkov","year":"2007","journal-title":"Blood"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"e1406","DOI":"10.1634\/theoncologist.2020-0141","article-title":"Multiple Myeloma Incidence and Mortality Around the Globe; Interrelations Between Health Access and Quality, Economic Resources, and Patient Empowerment","volume":"25","author":"Ludwig","year":"2020","journal-title":"Oncologist"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1001\/jamaoncol.2018.2128","article-title":"Global Burden of Multiple Myeloma: A Systematic Analysis for the Global Burden of Disease Study 2016","volume":"4","author":"Cowan","year":"2018","journal-title":"JAMA Oncol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1007\/s10555-017-9698-5","article-title":"Emerging small molecule approaches to enhance the antimyeloma benefit of proteasome inhibitors","volume":"36","author":"Driscoll","year":"2017","journal-title":"Cancer Metastasis Rev."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1945","DOI":"10.1080\/10428190802304966","article-title":"Growth control of multiple myeloma cells through inhibition of glycogen synthase kinase-3","volume":"49","author":"Zhou","year":"2008","journal-title":"Leuk. Lymphoma"},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Piazza, F., Manni, S., Tubi, L.Q., Montini, B., Pavan, L., Colpo, A., Gnoato, M., Cabrelle, A., Adami, F., and Zambello, R. (2010). Glycogen Synthase Kinase-3 regulates multiple myeloma cell growth and bortezomib-induced cell death. BMC Cancer, 10.","DOI":"10.1186\/1471-2407-10-526"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.bcp.2013.04.022","article-title":"Activator or inhibitor? GSK-3 as a new drug target","volume":"86","year":"2013","journal-title":"Biochem. Pharmacol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1074\/jbc.M002466200","article-title":"Indirubins inhibit glycogen synthase kinase-3 beta and CDK5\/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer\u2019s disease. A property common to most cyclin-dependent kinase inhibitors?","volume":"276","author":"Leclerc","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2325","DOI":"10.1038\/onc.2009.510","article-title":"AT7519, A novel small molecule multi-cyclin-dependent kinase inhibitor, induces apoptosis in multiple myeloma via GSK-3beta activation and RNA polymerase II inhibition","volume":"29","author":"Santo","year":"2010","journal-title":"Oncogene"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1038\/nri.2017.52","article-title":"The non-canonical NF-\u03baB pathway in immunity and inflammation","volume":"17","author":"Sun","year":"2017","journal-title":"Nat. Rev. Immunol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"188449","DOI":"10.1016\/j.bbcan.2020.188449","article-title":"Pharmacological significance of the non-canonical NF-\u03baB pathway in tumorigenesis","volume":"1874","author":"Morgan","year":"2020","journal-title":"Biochim. Biophys. Acta Rev. Cancer"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1038\/ncb2463","article-title":"Fbxw7\u03b1- and GSK3-mediated degradation of p100 is a pro-survival mechanism in multiple myeloma","volume":"14","author":"Busino","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"e00104-20","DOI":"10.1128\/MCB.00104-20","article-title":"Looking Down on NF-\u03baB","volume":"40","author":"Williams","year":"2020","journal-title":"Mol. Cell Biol."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Franic, D., Zubcic, K., and Boban, M. (2021). Nuclear Ubiquitin-Proteasome Pathways in Proteostasis Maintenance. Biomolecules, 11.","DOI":"10.3390\/biom11010054"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1136","DOI":"10.1210\/me.2009-0466","article-title":"Glycogen synthase kinase-3 plays a central role in mediating glucocorticoid-induced apoptosis","volume":"24","author":"Spokoini","year":"2010","journal-title":"Mol. Endocrinol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.brainres.2009.08.034","article-title":"Efficacy of a novel, orally active GSK-3 inhibitor 6-Methyl-N-[3-[[3-(1-methylethoxy)propyl]carbamoyl]-1H-pyrazol-4-yl]pyridine-3-ca rboxamide in tau transgenic mice","volume":"1296","author":"Uno","year":"2009","journal-title":"Brain Res."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1538\/expanim.21-0027","article-title":"Functional analysis of large MAF transcription factors and elucidation of their relationships with human diseases","volume":"70","author":"Takahashi","year":"2021","journal-title":"Exp. Anim."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1182\/asheducation-2011.1.344","article-title":"Many multiple myelomas: Making more of the molecular mayhem","volume":"2011","author":"Chesi","year":"2011","journal-title":"Hematology Am. Soc. Hematol. Edu. Program"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"e175","DOI":"10.1038\/bcj.2013.67","article-title":"GSK3-mediated MAF phosphorylation in multiple myeloma as a potential therapeutic target","volume":"4","author":"Herath","year":"2014","journal-title":"Blood Cancer J."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2396","DOI":"10.1182\/blood-2010-04-278788","article-title":"A mechanistic rationale for MEK inhibitor therapy in myeloma based on blockade of MAF oncogene expression","volume":"117","author":"Annunziata","year":"2011","journal-title":"Blood"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S1535-6108(04)00019-4","article-title":"Overexpression of c-maf is a frequent oncogenic event in multiple myeloma that promotes proliferation and pathological interactions with bone marrow stroma","volume":"5","author":"Hurt","year":"2004","journal-title":"Cancer Cell"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"6936","DOI":"10.1038\/sj.onc.1208844","article-title":"ARK5 is transcriptionally regulated by the Large-MAF family and mediates IGF-1-induced cell invasion in multiple myeloma: ARK5 as a new molecular determinant of malignant multiple myeloma","volume":"24","author":"Suzuki","year":"2005","journal-title":"Oncogene"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/j.cell.2009.03.046","article-title":"DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival","volume":"137","author":"Peterson","year":"2009","journal-title":"Cell"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"3176","DOI":"10.3324\/haematol.2020.253526","article-title":"Expression of the chemokine receptor CCR1 promotes the dissemination of multiple myeloma plasma cells in vivo","volume":"106","author":"Zeissig","year":"2021","journal-title":"Haematologica"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1016\/j.molcel.2007.11.009","article-title":"GSK-3-mediated phosphorylation enhances Maf-transforming activity","volume":"28","author":"Rocques","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"2919","DOI":"10.1182\/blood-2016-03-706077","article-title":"MAF protein mediates innate resistance to proteasome inhibition therapy in multiple myeloma","volume":"128","author":"Qiang","year":"2016","journal-title":"Blood"},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Qiang, Y.W., Ye, S., Huang, Y., Chen, Y., Van Rhee, F., Epstein, J., Walker, B.A., Morgan, G.J., and Davies, F.E. (2018). MAFb protein confers intrinsic resistance to proteasome inhibitors in multiple myeloma. BMC Cancer, 18.","DOI":"10.1186\/s12885-018-4602-4"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"275","DOI":"10.2147\/NDT.S123612","article-title":"A fully integrated new paradigm for lithium\u2019s mode of action\u2014Lithium utilizes latent cellular fail-safe mechanisms","volume":"13","year":"2017","journal-title":"Neuropsychiatr. Dis. Treat."},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Snitow, M.E., Bhansali, R.S., and Klein, P.S. (2021). Lithium and Therapeutic Targeting of GSK-3. Cells, 10.","DOI":"10.3390\/cells10020255"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"4151","DOI":"10.1182\/bloodadvances.2019001393","article-title":"AKT signaling restrains tumor suppressive functions of FOXO transcription factors and GSK3 kinase in multiple myeloma","volume":"4","author":"Bloedjes","year":"2020","journal-title":"Blood Adv."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.3892\/or.2021.7934","article-title":"JMJD2C triggers the growth of multiple myeloma cells via activation of betacatenin","volume":"45","author":"Lv","year":"2021","journal-title":"Oncol. Rep."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/ajh.26512","article-title":"Current Approaches to Management of Newly Diagnosed Multiple Myeloma","volume":"97","author":"Goel","year":"2022","journal-title":"Am. J. Hematol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"11009","DOI":"10.1074\/jbc.M110.180208","article-title":"Evidence of a role for activation of Wnt\/\u03b2-catenin signaling in the resistance of plasma cells to lenalidomide","volume":"286","author":"Bjorklund","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"2060","DOI":"10.1002\/ijc.29670","article-title":"Cancer Incidence in Five Continents: Inclusion criteria, highlights from Volume X and the global status of cancer registration","volume":"137","author":"Bray","year":"2015","journal-title":"Int. J. Cancer"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/35000501","article-title":"Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling","volume":"403","author":"Alizadeh","year":"2000","journal-title":"Nature"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1182\/blood-2018-09-871418","article-title":"Genome-wide discovery of somatic coding and noncoding mutations in pediatric endemic and sporadic Burkitt lymphoma","volume":"133","author":"Grande","year":"2019","journal-title":"Blood"},{"key":"ref_164","doi-asserted-by":"crossref","unstructured":"Robaina, M.C., Mazzoccoli, L., and Klumb, C.E. (2019). Germinal Centre B Cell Functions and Lymphomagenesis: Circuits Involving MYC and MicroRNAs. Cells, 8.","DOI":"10.3390\/cells8111365"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"604685","DOI":"10.3389\/fonc.2020.604685","article-title":"Role of Specific B-Cell Receptor Antigens in Lymphomagenesis","volume":"10","author":"Thurner","year":"2020","journal-title":"Front. Oncol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1053\/j.seminhematol.2015.01.008","article-title":"B-cell receptor signaling in diffuse large B-cell lymphoma","volume":"52","author":"Young","year":"2015","journal-title":"Semin. Hematol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/nature22353","article-title":"The B-cell receptor controls fitness of MYC-driven lymphoma cells via GSK3\u03b2 inhibition","volume":"546","author":"Varano","year":"2017","journal-title":"Nature"},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Vecchio, E., Nistico, N., Golino, G., Iaccino, E., Maisano, D., Mimmi, S., Aloisio, A., Renna, M., Avagliano, A., and Arcucci, A. (2022). IBtkalpha Activates the beta-Catenin-Dependent Transcription of MYC through Ubiquitylation and Proteasomal Degradation of GSK3\u03b2 in Cancerous B Cells. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23042044"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"114924","DOI":"10.18632\/oncotarget.22414","article-title":"GSK-3\u03b2 inhibitor, 9-ING-41, reduces cell viability and halts proliferation of B-cell lymphoma cell lines as a single agent and in combination with novel agents","volume":"8","author":"Karmali","year":"2017","journal-title":"Oncotarget"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1182\/blood.2018874560","article-title":"Targeting glycogen synthase kinase 3 for therapeutic benefit in lymphoma","volume":"134","author":"Wu","year":"2019","journal-title":"Blood"},{"key":"ref_171","first-page":"315","article-title":"Clinically relevant GSK3\u03b2 inhibitor 9ING41 is active as a single agent and in combination with other antitumor therapies in human renal cancer","volume":"45","author":"Anraku","year":"2020","journal-title":"Int. J. Mol. Med."},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Park, R., Coveler, A.L., Cavalcante, L., and Saeed, A. (2021). GSK-3beta in Pancreatic Cancer: Spotlight on 9-ING-41, Its Therapeutic Potential and Immune Modulatory Properties. Biology, 10.","DOI":"10.3390\/biology10070610"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"2429","DOI":"10.1038\/s41375-019-0454-4","article-title":"Transient stabilization, rather than inhibition, of MYC amplifies extrinsic apoptosis and therapeutic responses in refractory B-cell lymphoma","volume":"33","author":"Harrington","year":"2019","journal-title":"Leukemia"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1080\/15384047.2019.1595283","article-title":"Glycogen synthase kinase-3 \u03b2 inhibitors as novel cancer treatments and modulators of antitumor immune responses","volume":"20","author":"Sahin","year":"2019","journal-title":"Cancer Biol. Ther."},{"key":"ref_175","doi-asserted-by":"crossref","unstructured":"Augello, G., Emma, M.R., Cusimano, A., Azzolina, A., Montalto, G., McCubrey, J.A., and Cervello, M. (2020). The Role of GSK-3 in Cancer Immunotherapy: GSK-3 Inhibitors as a New Frontier in Cancer Treatment. Cells, 9.","DOI":"10.3390\/cells9061427"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"1653","DOI":"10.3389\/fimmu.2017.01653","article-title":"Glycogen Synthase Kinase 3 Inactivation Compensates for the Lack of CD28 in the Priming of CD8+ Cytotoxic T-Cells: Implications for anti-PD-1 Immunotherapy","volume":"8","author":"Taylor","year":"2017","journal-title":"Front. Immunol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1158\/0008-5472.CAN-17-0491","article-title":"Small-Molecule Inhibition of PD-1 Transcription Is an Effective Alternative to Antibody Blockade in Cancer Therapy","volume":"78","author":"Taylor","year":"2018","journal-title":"Cancer Res."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"120635","DOI":"10.1016\/j.biomaterials.2020.120635","article-title":"Immune checkpoint inhibition in syngeneic mouse cancer models by a silicasome nanocarrier delivering a GSK3 inhibitor","volume":"269","author":"Allen","year":"2021","journal-title":"Biomaterials"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"2729","DOI":"10.4049\/jimmunol.168.6.2729","article-title":"CD28 costimulation mediates down-regulation of p27kip1 and cell cycle progression by activation of the PI3K\/PKB signaling pathway in primary human T cells","volume":"168","author":"Appleman","year":"2002","journal-title":"J. Immunol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.canlet.2018.06.035","article-title":"Glycogen synthase kinase 3 inhibition lowers PD-1 expression, promotes long-term survival and memory generation in antigen-specific CAR-T cells","volume":"433","author":"Sengupta","year":"2018","journal-title":"Cancer Lett."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"5664","DOI":"10.1158\/0008-5472.CAN-17-0799","article-title":"GSK3 Inhibition Drives Maturation of NK Cells and Enhances Their Antitumor Activity","volume":"77","author":"Cichocki","year":"2017","journal-title":"Cancer Res."},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Kim, N., Kim, M.Y., Choi, W.S., Yi, E., Lee, H.J., and Kim, H.S. (2021). GSK-3alpha Inhibition in Drug-Resistant CML Cells Promotes Susceptibility to NK Cell-Mediated Lysis in an NKG2D- and NKp30-Dependent Manner. Cancers, 13.","DOI":"10.3390\/cancers13081802"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1007\/s40291-021-00550-6","article-title":"Bi-specific and Tri-specific NK Cell Engagers: The New Avenue of Targeted NK Cell Immunotherapy","volume":"25","author":"Phung","year":"2021","journal-title":"Mol. Diagn. Ther."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"e1065368","DOI":"10.1080\/2162402X.2015.1065368","article-title":"Interferon gamma modulates sensitivity of CML cells to tyrosine kinase inhibitors","volume":"5","author":"Held","year":"2016","journal-title":"Oncoimmunology"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"106464","DOI":"10.1016\/j.leukres.2020.106464","article-title":"Evidence that knock down of GSK-3beta in Chronic Myelogenous Leukemia cells augments IFN-\u03b3-induced apoptosis","volume":"99","author":"Kauffman","year":"2020","journal-title":"Leuk. Res."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"6662","DOI":"10.4049\/jimmunol.1201426","article-title":"Inhibition of glycogen synthase kinase-3 increases NKG2D ligand MICA expression and sensitivity to NK cell-mediated cytotoxicity in multiple myeloma cells: Role of STAT3","volume":"190","author":"Fionda","year":"2013","journal-title":"J. Immunol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1800","DOI":"10.1128\/MCB.00034-14","article-title":"Signal integration and gene induction by a functionally distinct STAT3 phosphoform","volume":"34","author":"Waitkus","year":"2014","journal-title":"Mol. Cell Biol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"2301","DOI":"10.1002\/mc.22685","article-title":"Inhibition of glycogen synthase kinase 3 \u03b2 (GSK3\u03b2) suppresses the progression of esophageal squamous cell carcinoma by modifying STAT3 activity","volume":"56","author":"Gao","year":"2017","journal-title":"Mol. Carcinog."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.chom.2019.11.002","article-title":"Salmonella Effector SteE Converts the Mammalian Serine\/Threonine Kinase GSK3 into a Tyrosine Kinase to Direct Macrophage Polarization","volume":"27","author":"Panagi","year":"2020","journal-title":"Cell Host Microbe"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"118616","DOI":"10.1016\/j.bbamcr.2019.118616","article-title":"Emerging roles of GSK-3\u03b1 in pathophysiology: Emphasis on cardio-metabolic disorders","volume":"1867","author":"Ahmad","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"8907","DOI":"10.1021\/acs.jmedchem.5b01200","article-title":"Evaluation of Improved Glycogen Synthase Kinase-3\u03b1 Inhibitors in Models of Acute Myeloid Leukemia","volume":"58","author":"Neumann","year":"2015","journal-title":"J. Med. Chem."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/j.ejmech.2019.03.039","article-title":"Discovery of novel glycogen synthase kinase-3\u03b1 inhibitors: Structure-based virtual screening, preliminary SAR and biological evaluation for treatment of acute myeloid leukemia","volume":"171","author":"Wang","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"7632","DOI":"10.1073\/pnas.0732087100","article-title":"Synthetic small molecules that control stem cell fate","volume":"100","author":"Ding","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"1829","DOI":"10.1038\/s41375-021-01243-z","article-title":"GSK-3: A multifaceted player in acute leukemias","volume":"35","author":"Martelli","year":"2021","journal-title":"Leukemia"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1021\/acs.jmedchem.1c01719","article-title":"Discovery of Cysteine-targeting Covalent Protein Kinase Inhibitors","volume":"65","author":"Lu","year":"2022","journal-title":"J. Med. Chem."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"193","DOI":"10.4155\/fmc-2020-0236","article-title":"10 years into the resurgence of covalent drugs","volume":"13","year":"2021","journal-title":"Future Med. Chem."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/d41586-022-00692-5","article-title":"Promising reversible protein inhibitors kept on target","volume":"603","author":"Hacker","year":"2022","journal-title":"Nature"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1038\/nchembio.925","article-title":"Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles","volume":"8","author":"Serafimova","year":"2012","journal-title":"Nat. Chem. Biol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"1841","DOI":"10.1002\/cbic.202000870","article-title":"SP3-FAIMS Chemoproteomics for High-Coverage Profiling of the Human Cysteinome*","volume":"22","author":"Yan","year":"2021","journal-title":"Chembiochem"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1038\/s41557-021-00765-4","article-title":"A proteome-wide atlas of lysine-reactive chemistry","volume":"13","author":"Abbasov","year":"2021","journal-title":"Nat. Chem."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1021\/jacs.1c12702","article-title":"Lysine-Targeting Reversible Covalent Inhibitors with Long Residence Time","volume":"144","author":"Reja","year":"2022","journal-title":"J. Am. Chem. Soc."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"391","DOI":"10.6026\/97320630012391","article-title":"Pharmacophore feature-based virtual screening for finding potent GSK-3 inhibitors using molecular docking and dynamics simulations","volume":"12","author":"Chauhan","year":"2016","journal-title":"Bioinformation"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1016\/j.bmcl.2019.04.049","article-title":"1-Aryl-3-(4-methoxybenzyl)ureas as potentially irreversible glycogen synthase kinase 3 inhibitors: Synthesis and biological evaluation","volume":"29","author":"Venter","year":"2019","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"7341","DOI":"10.1021\/acs.jmedchem.0c02254","article-title":"Discovery of Novel Benzothiazepinones as Irreversible Covalent Glycogen Synthase Kinase 3\u03b2 Inhibitors for the Treatment of Acute Promyelocytic Leukemia","volume":"64","author":"Zhang","year":"2021","journal-title":"J. Med. Chem."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"4983","DOI":"10.1021\/acs.jmedchem.7b00395","article-title":"Subtly Modulating Glycogen Synthase Kinase 3 \u03b2: Allosteric Inhibitor Development and Their Potential for the Treatment of Chronic Diseases","volume":"60","author":"Palomo","year":"2017","journal-title":"J. Med. Chem."},{"key":"ref_206","doi-asserted-by":"crossref","unstructured":"Silva, G.M., Borges, R.S., Santos, K.L.B., Federico, L.B., Francischini, I.A.G., Gomes, S.Q., Barcelos, M.P., Silva, R.C., Santos, C.B.R., and Silva, C. (2021). Revisiting the Proposition of Binding Pockets and Bioactive Poses for GSK-3\u03b2 Allosteric Modulators Addressed to Neurodegenerative Diseases. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22158252"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1186\/s13045-021-01146-7","article-title":"Protein degradation technology: A strategic paradigm shift in drug discovery","volume":"14","author":"Li","year":"2021","journal-title":"J. Hematol. Oncol."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"2250","DOI":"10.1002\/cbic.202000113","article-title":"Optochemical Control of Protein Degradation","volume":"21","author":"Wu","year":"2020","journal-title":"ChemBioChem"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"113889","DOI":"10.1016\/j.ejmech.2021.113889","article-title":"Discovery of PT-65 as a highly potent and selective Proteolysis-targeting chimera degrader of GSK3 for treating Alzheimer\u2019s disease","volume":"226","author":"Qu","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"ref_210","doi-asserted-by":"crossref","unstructured":"Kenchegowda, M., Rahamathulla, M., Hani, U., Begum, M.Y., Guruswamy, S., Osmani, R.A.M., Gowrav, M.P., Alshehri, S., Ghoneim, M.M., and Alshlowi, A. (2021). Smart Nanocarriers as an Emerging Platform for Cancer Therapy: A Review. Molecules, 27.","DOI":"10.3390\/molecules27010146"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1038\/mt.2014.96","article-title":"Nano-polypharmacy to treat tumors: Coencapsulation of drug combinations using nanoparticle technology","volume":"22","author":"Alexis","year":"2014","journal-title":"Mol. Ther."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"5767","DOI":"10.2147\/IJN.S254574","article-title":"Nanotechnology-Based Targeting of mTOR Signaling in Cancer","volume":"15","author":"Yoon","year":"2020","journal-title":"Int. J. Nanomed."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"9445","DOI":"10.1021\/acsnano.7b05103","article-title":"Fracture-Targeted Delivery of beta-Catenin Agonists via Peptide-Functionalized Nanoparticles Augments Fracture Healing","volume":"11","author":"Wang","year":"2017","journal-title":"ACS Nano"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1983","DOI":"10.1182\/blood.2019001037","article-title":"Donor cell engineering with GSK3 inhibitor-loaded nanoparticles enhances engraftment after in utero transplantation","volume":"134","author":"Loukogeorgakis","year":"2019","journal-title":"Blood"},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"2893","DOI":"10.1021\/acsbiomaterials.9b01820","article-title":"Glycogen Synthase Kinase 3\u03b2 Inhibitor Delivered by Chitosan Nanocapsules Promotes Safe, Fast, and Efficient Activation of Wnt Signaling In Vivo","volume":"6","author":"Ambrosone","year":"2020","journal-title":"ACS Biomater. Sci. Eng."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1007\/s11095-022-03214-0","article-title":"Targeted Drug Delivery for Chronic Lymphocytic Leukemia","volume":"39","author":"Zoulikha","year":"2022","journal-title":"Pharm. Res."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"S547","DOI":"10.3233\/JAD-179934","article-title":"The Conundrum of GSK3 Inhibitors: Is it the Dawn of a New Beginning?","volume":"64","author":"Bhat","year":"2018","journal-title":"J. Alzheimers Dis."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"1800","DOI":"10.3109\/10428194.2015.1122781","article-title":"An open-label phase 2 study of glycogen synthase kinase-3 inhibitor LY2090314 in patients with acute leukemia","volume":"57","author":"Rizzieri","year":"2016","journal-title":"Leuk. Lymphoma."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"e003975","DOI":"10.1136\/jitc-2021-003975","article-title":"Tumor-associated macrophages in multiple myeloma: Advances in biology and therapy","volume":"10","author":"Sun","year":"2022","journal-title":"J. Immunother. Cancer"},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1002\/mc.23268","article-title":"M2-like tumor-associated macrophages-secreted Wnt1 and Wnt3a promotes dedifferentiation and metastasis via activating \u03b2-catenin pathway in thyroid cancer","volume":"60","author":"Lv","year":"2021","journal-title":"Mol. Carcinog."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"4198","DOI":"10.1111\/cas.15101","article-title":"Tumor-associated macrophage-derived transforming growth factor-\u03b2 promotes colorectal cancer progression through HIF1-TRIB3 signaling","volume":"112","author":"Liu","year":"2021","journal-title":"Cancer Sci."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/11\/11\/1812\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T23:23:02Z","timestamp":1760138582000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/11\/11\/1812"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,5,31]]},"references-count":221,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2022,6]]}},"alternative-id":["cells11111812"],"URL":"https:\/\/doi.org\/10.3390\/cells11111812","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,5,31]]}}}