{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T18:04:57Z","timestamp":1791396297685,"version":"4.3.3"},"reference-count":146,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2020,7,14]],"date-time":"2020-07-14T00:00:00Z","timestamp":1594684800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003407","name":"Ministero dell\u2019Istruzione, dell\u2019Universit\u00e0 e della Ricerca","doi-asserted-by":"publisher","award":["POC01_00043"],"award-info":[{"award-number":["POC01_00043"]}],"id":[{"id":"10.13039\/501100003407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009448","name":"Universit\u00e0 degli Studi della Campania Luigi Vanvitelli","doi-asserted-by":"publisher","award":["VALERE: Vanvitelli per la Ricerca"],"award-info":[{"award-number":["VALERE: Vanvitelli per la Ricerca"]}],"id":[{"id":"10.13039\/501100009448","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003852","name":"Regione Campania","doi-asserted-by":"publisher","award":["Campania Regional Government Technology Platform Lotta alle Patologie Oncologiche: iCURE"],"award-info":[{"award-number":["Campania Regional Government Technology Platform Lotta alle Patologie Oncologiche: iCURE"]}],"id":[{"id":"10.13039\/501100003852","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cancers"],"abstract":"<jats:p>The ubiquitin proteasome system (UPS) is the main cellular degradation machinery designed for controlling turnover of critical proteins involved in cancer pathogenesis, including hematological malignancies. UPS plays a functional role in regulating turnover of key proteins involved in cell cycle arrest, apoptosis and terminal differentiation. When deregulated, it leads to several disorders, including cancer. Several studies indicate that, in some subtypes of human hematological neoplasms such as multiple myeloma and Burkitt\u2019s lymphoma, abnormalities in the UPS made it an attractive therapeutic target due to pro-cancer activity. In this review, we discuss the aberrant role of UPS evaluating its impact in hematological malignancies. Finally, we also review the most promising therapeutic approaches to target UPS as powerful strategies to improve treatment of blood cancers.<\/jats:p>","DOI":"10.3390\/cancers12071898","type":"journal-article","created":{"date-parts":[[2020,7,14]],"date-time":"2020-07-14T11:03:23Z","timestamp":1594724603000},"page":"1898","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["The Ubiquitin Proteasome System in Hematological Malignancies: New Insight into Its Functional Role and Therapeutic Options"],"prefix":"10.3390","volume":"12","author":[{"given":"Antonella","family":"Di Costanzo","sequence":"first","affiliation":[{"name":"Department of Precision Medicine, University of Campania \"Luigi Vanvitelli\", Vico L. De Crecchio 7, 80138 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nunzio","family":"Del Gaudio","sequence":"additional","affiliation":[{"name":"Department of Precision Medicine, University of Campania \"Luigi Vanvitelli\", Vico L. De Crecchio 7, 80138 Naples, Italy"},{"name":"Center for Genomic Science of IIT@SEMM, Fondazione Istituto Italiano di Tecnologia (IIT), 20139 Milan, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lidio","family":"Conte","sequence":"additional","affiliation":[{"name":"Department of Precision Medicine, University of Campania \"Luigi Vanvitelli\", Vico L. De Crecchio 7, 80138 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7312-5387","authenticated-orcid":false,"given":"Lucia","family":"Altucci","sequence":"additional","affiliation":[{"name":"Department of Precision Medicine, University of Campania \"Luigi Vanvitelli\", Vico L. De Crecchio 7, 80138 Naples, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,7,14]]},"reference":[{"key":"ref_1","first-page":"565","article-title":"The ubiquitin-mediated proteolytic pathway: Mechanisms of action and cellular physiology","volume":"375","author":"Ciechanover","year":"1994","journal-title":"Biol. Chem. Hoppe-Seyler"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","article-title":"The ubiquitin system","volume":"67","author":"Hershko","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2104","DOI":"10.1182\/blood.V95.6.2104","article-title":"c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover","volume":"95","author":"Bahram","year":"2000","journal-title":"Blood"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2559","DOI":"10.1038\/s41388-018-0143-1","article-title":"The HDAC inhibitor SAHA regulates CBX2 stability via a SUMO-triggered ubiquitin-mediated pathway in leukemia","volume":"37","author":"Conte","year":"2018","journal-title":"Oncogene"},{"key":"ref_5","first-page":"31","article-title":"Altered expression of p53 and MDM2 proteins in hematological malignancies","volume":"50","author":"Konikova","year":"2003","journal-title":"Neoplasma"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1152\/physrev.00027.2001","article-title":"The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction","volume":"82","author":"Glickman","year":"2002","journal-title":"Physiol. Rev."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.bbamcr.2013.05.026","article-title":"RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination","volume":"1843","author":"Metzger","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"3121","DOI":"10.1007\/s00018-018-2848-2","article-title":"Regulating the human HECT E3 ligases","volume":"75","author":"Sluimer","year":"2018","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1083\/jcb.201005101","article-title":"RAD18-mediated ubiquitination of PCNA activates the Fanconi anemia DNA repair network","volume":"191","author":"Geng","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1146\/annurev-biochem-051810-094654","article-title":"Ubiquitin-binding proteins: Decoders of ubiquitin-mediated cellular functions","volume":"81","author":"Husnjak","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/j.molcel.2006.02.011","article-title":"Differential modification of Ras proteins by ubiquitination","volume":"21","author":"Jura","year":"2006","journal-title":"Mol. Cell"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.cell.2006.04.029","article-title":"Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II","volume":"125","author":"Pavri","year":"2006","journal-title":"Cell"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"ra13","DOI":"10.1126\/scisignal.2001518","article-title":"Ubiquitination of K-Ras enhances activation and facilitates binding to select downstream effectors","volume":"4","author":"Sasaki","year":"2011","journal-title":"Sci. Signal."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1128\/MCB.01146-12","article-title":"Monoubiquitination of filamin B regulates vascular endothelial growth factor-mediated trafficking of histone deacetylase 7","volume":"33","author":"Su","year":"2013","journal-title":"Mol. Cell. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1111\/gtc.12250","article-title":"Protein monoubiquitylation: Targets and diverse functions","volume":"20","author":"Nakagawa","year":"2015","journal-title":"Genes Cells Devoted Mol. Cell. Mech."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/ncb2425","article-title":"APC\/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1","volume":"14","author":"Dimova","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/ncb3358","article-title":"The increasing complexity of the ubiquitin code","volume":"18","author":"Yau","year":"2016","journal-title":"Nat. Cell Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1016\/j.molcel.2015.05.006","article-title":"Quantitative Proteomic Atlas of Ubiquitination and Acetylation in the DNA Damage Response","volume":"59","author":"Elia","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1038\/nsmb.3475","article-title":"Mechanism and regulation of the Lys6-selective deubiquitinase USP30","volume":"24","author":"Gersch","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.molcel.2017.08.020","article-title":"Ubiquitin Linkage-Specific Affimers Reveal Insights into K6-Linked Ubiquitin Signaling","volume":"68","author":"Michel","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_21","first-page":"355","article-title":"Emerging roles for Lys11-linked polyubiquitin in cellular regulation","volume":"36","author":"Bremm","year":"2011","journal-title":"Trends Biochem. Sci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"14274","DOI":"10.1038\/ncomms14274","article-title":"Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains","volume":"8","author":"Liu","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1856","DOI":"10.4049\/jimmunol.1601647","article-title":"TRIM8 Negatively Regulates TLR3\/4-Mediated Innate Immune Response by Blocking TRIF-TBK1 Interaction","volume":"199","author":"Ye","year":"2017","journal-title":"J. Immunol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1200\/JCO.2012.44.0958","article-title":"Role of ubiquitin ligases and the proteasome in oncogenesis: Novel targets for anticancer therapies","volume":"31","author":"Micel","year":"2013","journal-title":"J. Clin. Oncol. Off. J. Am. Soc. Clin. Oncol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1007\/s10555-017-9697-6","article-title":"Proteasome-associated deubiquitinases and cancer","volume":"36","author":"Mofers","year":"2017","journal-title":"Cancer Metastasis Rev."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"7071","DOI":"10.1073\/pnas.87.18.7071","article-title":"Abnormally high expression of proteasomes in human leukemic cells","volume":"87","author":"Kumatori","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2251","DOI":"10.1182\/blood-2009-07-231191","article-title":"The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma","volume":"115","author":"Xu","year":"2010","journal-title":"Blood"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1553","DOI":"10.1182\/blood-2018-03-784116","article-title":"Chronic immune response dysregulation in MDS pathogenesis","volume":"132","author":"Barreyro","year":"2018","journal-title":"Blood"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/cr.2010.178","article-title":"Crosstalk of reactive oxygen species and NF-kappaB signaling","volume":"21","author":"Morgan","year":"2011","journal-title":"Cell Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.molcel.2012.05.045","article-title":"Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks","volume":"47","author":"Panier","year":"2012","journal-title":"Mol. Cell"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"634","DOI":"10.1080\/15384101.2017.1288326","article-title":"The importance of regulatory ubiquitination in cancer and metastasis","volume":"16","author":"Gallo","year":"2017","journal-title":"Cell Cycle"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1111\/j.1365-2559.2009.03296.x","article-title":"UbcH10 expression in human lymphomas","volume":"54","author":"Troncone","year":"2009","journal-title":"Histopathology"},{"key":"ref_33","first-page":"196","article-title":"Expression Status of UBE2Q2 in Colorectal Primary Tumors and Cell Lines","volume":"39","author":"Shafiee","year":"2014","journal-title":"Iran. J. Med. Sci."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1789","DOI":"10.3324\/haematol.2017.179937","article-title":"De novo UBE2A mutations are recurrently acquired during chronic myeloid leukemia progression and interfere with myeloid differentiation pathways","volume":"104","author":"Magistroni","year":"2019","journal-title":"Haematologica"},{"key":"ref_35","first-page":"1657","article-title":"FBW7 in hematological tumors","volume":"19","author":"Zhu","year":"2020","journal-title":"Oncol. Lett."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1101\/gad.1621808","article-title":"Fbxw7 acts as a critical fail-safe against premature loss of hematopoietic stem cells and development of T-ALL","volume":"22","author":"Matsuoka","year":"2008","journal-title":"Genes Dev."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"6731","DOI":"10.1073\/pnas.1601537113","article-title":"Oncogenic mutations in the FBXW7 gene of adult T-cell leukemia patients","volume":"113","author":"Yeh","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"830","DOI":"10.1182\/blood-2018-09-874529","article-title":"FBXW7 mutations reduce binding of NOTCH1, leading to cleaved NOTCH1 accumulation and target gene activation in CLL","volume":"133","author":"Close","year":"2019","journal-title":"Blood"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"3132","DOI":"10.1182\/blood-2011-06-358911","article-title":"F-box protein FBXL2 targets cyclin D2 for ubiquitination and degradation to inhibit leukemic cell proliferation","volume":"119","author":"Chen","year":"2012","journal-title":"Blood"},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Hynes-Smith, R.W., Swenson, S.A., Vahle, H., Wittorf, K.J., Caplan, M., Amador, C., Hyde, R.K., and Buckley, S.M. (2019). Loss of FBXO9 Enhances Proteasome Activity and Promotes Aggressiveness in Acute Myeloid Leukemia. Cancers, 11.","DOI":"10.1101\/732198"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1002\/jcp.20694","article-title":"The Cbl family proteins: Ring leaders in regulation of cell signaling","volume":"209","author":"Swaminathan","year":"2006","journal-title":"J. Cell. Physiol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1002\/cncr.23317","article-title":"Oncogenic properties and prognostic implications of the ubiquitin ligase Skp2 in cancer","volume":"112","author":"Hershko","year":"2008","journal-title":"Cancer"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1002\/ajh.10379","article-title":"Prognostic significance of the F-box protein Skp2 expression in diffuse large B-cell lymphoma","volume":"73","author":"Seki","year":"2003","journal-title":"Am. J. Hematol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"4838","DOI":"10.1172\/JCI41769","article-title":"Loss of nuclear pro-IL-16 facilitates cell cycle progression in human cutaneous T cell lymphoma","volume":"121","author":"Yamasaki","year":"2011","journal-title":"J. Clin. Investig."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3141","DOI":"10.1016\/j.yexcr.2007.04.027","article-title":"Notch signaling induces SKP2 expression and promotes reduction of p27Kip1 in T-cell acute lymphoblastic leukemia cell lines","volume":"313","author":"Dohda","year":"2007","journal-title":"Exp. Cell Res."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1038\/leu.2016.258","article-title":"Pharmacogenomics and chemical library screens reveal a novel SCF(SKP2) inhibitor that overcomes Bortezomib resistance in multiple myeloma","volume":"31","author":"Malek","year":"2017","journal-title":"Leukemia"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1038\/leu.2017.342","article-title":"The E3 ubiquitin ligase WWP1 sustains the growth of acute myeloid leukaemia","volume":"32","author":"Sanarico","year":"2018","journal-title":"Leukemia"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2408","DOI":"10.4049\/jimmunol.1700708","article-title":"Klhl6 Deficiency Impairs Transitional B Cell Survival and Differentiation","volume":"199","author":"Bertocci","year":"2017","journal-title":"J. Immunol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"8531","DOI":"10.1128\/MCB.25.19.8531-8540.2005","article-title":"The BTB-kelch protein KLHL6 is involved in B-lymphocyte antigen receptor signaling and germinal center formation","volume":"25","author":"Kroll","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"43052","DOI":"10.18632\/oncotarget.9678","article-title":"The genetic landscape of dural marginal zone lymphomas","volume":"7","author":"Ganapathi","year":"2016","journal-title":"Oncotarget"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"370","DOI":"10.3324\/haematol.2014.109777","article-title":"Targeted next-generation sequencing in chronic lymphocytic leukemia: A high-throughput yet tailored approach will facilitate implementation in a clinical setting","volume":"100","author":"Sutton","year":"2015","journal-title":"Haematologica"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1038\/s41556-018-0084-5","article-title":"Loss of KLHL6 promotes diffuse large B-cell lymphoma growth and survival by stabilizing the mRNA decay factor roquin2","volume":"20","author":"Choi","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"4372","DOI":"10.1200\/JCO.2005.07.084","article-title":"Prognostic factors and outcome of human herpesvirus 8-associated primary effusion lymphoma in patients with AIDS","volume":"23","author":"Boulanger","year":"2005","journal-title":"J. Clin. Oncol. Off. J. Am. Soc. Clin. Oncol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2077","DOI":"10.4049\/jimmunol.165.4.2077","article-title":"Impaired CTL recognition of cells latently infected with Kaposi\u2019s sarcoma-associated herpes virus","volume":"165","author":"Brander","year":"2000","journal-title":"J. Immunol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"8051","DOI":"10.1073\/pnas.140129797","article-title":"Kaposi\u2019s sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis","volume":"97","author":"Coscoy","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1128\/JVI.01961-06","article-title":"Downregulation of gamma interferon receptor 1 by Kaposi\u2019s sarcoma-associated herpesvirus K3 and K5","volume":"81","author":"Li","year":"2007","journal-title":"J. Virol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1097\/COH.0000000000000330","article-title":"Kaposi sarcoma herpesvirus-associated cancers and related diseases","volume":"12","author":"Goncalves","year":"2017","journal-title":"Curr. Opin. HIV AIDS"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/35060076","article-title":"c-myc overexpression activates alternative pathways for intracellular proteolysis in lymphoma cells","volume":"3","author":"Gavioli","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2107","DOI":"10.1038\/sj.onc.1207372","article-title":"Epstein-Barr virus oncogenesis and the ubiquitin-proteasome system","volume":"23","author":"Masucci","year":"2004","journal-title":"Oncogene"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1038\/nrc1881","article-title":"Ubiquitin ligases: Cell-cycle control and cancer","volume":"6","author":"Nakayama","year":"2006","journal-title":"Nat. Rev. Cancer"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1038\/nrc2396","article-title":"Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: Tipping the scales of cancer","volume":"8","author":"Frescas","year":"2008","journal-title":"Nat. Rev. Cancer"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1016\/j.cell.2005.11.007","article-title":"A genomic and functional inventory of deubiquitinating enzymes","volume":"123","author":"Nijman","year":"2005","journal-title":"Cell"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/ncb1378","article-title":"Regulation of monoubiquitinated PCNA by DUB autocleavage","volume":"8","author":"Huang","year":"2006","journal-title":"Nat. Cell Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1016\/j.molcel.2007.09.031","article-title":"A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway","volume":"28","author":"Cohn","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2651","DOI":"10.1158\/1535-7163.MCT-13-0103-T","article-title":"Small-molecule inhibitors of USP1 target ID1 degradation in leukemic cells","volume":"12","author":"Mistry","year":"2013","journal-title":"Mol. Cancer Ther."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1016\/j.cell.2011.07.040","article-title":"USP1 deubiquitinates ID proteins to preserve a mesenchymal stem cell program in osteosarcoma","volume":"146","author":"Williams","year":"2011","journal-title":"Cell"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1007\/s12013-011-9185-5","article-title":"The multifaceted roles of USP7: New therapeutic opportunities","volume":"60","author":"Nicholson","year":"2011","journal-title":"Cell Biochem. Biophys."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1182\/blood-2016-12-758219","article-title":"USP7 inhibition alters homologous recombination repair and targets CLL cells independently of ATM\/p53 functional status","volume":"130","author":"Agathanggelou","year":"2017","journal-title":"Blood"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.cell.2009.12.032","article-title":"USP10 regulates p53 localization and stability by deubiquitinating p53","volume":"140","author":"Yuan","year":"2010","journal-title":"Cell"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"18778","DOI":"10.1074\/jbc.M109.001685","article-title":"The deubiquitinating enzyme USP10 regulates the post-endocytic sorting of cystic fibrosis transmembrane conductance regulator in airway epithelial cells","volume":"284","author":"Bomberger","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/j.molcel.2016.01.010","article-title":"Deubiquitination and Activation of AMPK by USP10","volume":"61","author":"Deng","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/s41421-019-0092-z","article-title":"USP10 modulates the SKP2\/Bcr-Abl axis via stabilizing SKP2 in chronic myeloid leukemia","volume":"5","author":"Liao","year":"2019","journal-title":"Cell Discov."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1038\/nchembio.2486","article-title":"Inhibition of USP10 induces degradation of oncogenic FLT3","volume":"13","author":"Weisberg","year":"2017","journal-title":"Nat. Chem. Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature08646","article-title":"Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival","volume":"463","author":"Schwickart","year":"2010","journal-title":"Nature"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1046\/j.1365-2443.1999.00297.x","article-title":"The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin","volume":"4","author":"Taya","year":"1999","journal-title":"Genes Cells Devoted Mol. Cell. Mech."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2008.10.051","article-title":"FAM\/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination","volume":"136","author":"Dupont","year":"2009","journal-title":"Cell"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1038\/nature11114","article-title":"The deubiquitinase USP9X suppresses pancreatic ductal adenocarcinoma","volume":"486","author":"Rust","year":"2012","journal-title":"Nature"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"3151","DOI":"10.1182\/blood-2010-03-276477","article-title":"Bcr-Abl ubiquitination and Usp9x inhibition block kinase signaling and promote CML cell apoptosis","volume":"117","author":"Sun","year":"2011","journal-title":"Blood"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.bbrc.2015.02.115","article-title":"Targeting of the deubiquitinase USP9X attenuates B-cell acute lymphoblastic leukemia cell survival and overcomes glucocorticoid resistance","volume":"459","author":"Zhou","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.canlet.2019.03.046","article-title":"Inhibition of USP9X induces apoptosis in FLT3-ITD-positive AML cells cooperatively by inhibiting the mutant kinase through aggresomal translocation and inducing oxidative stress","volume":"453","author":"Akiyama","year":"2019","journal-title":"Cancer Lett."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"9472","DOI":"10.1158\/0008-5472.CAN-07-0568","article-title":"Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics","volume":"67","author":"Yang","year":"2007","journal-title":"Cancer Res."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"4542","DOI":"10.1016\/j.bmcl.2015.10.015","article-title":"A selective inhibitor of the UFM1-activating enzyme, UBA5","volume":"26","author":"Paiva","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1021\/ml2000615","article-title":"Identification of NAE Inhibitors Exhibiting Potent Activity in Leukemia Cells: Exploring the Structural Determinants of NAE Specificity","volume":"2","author":"Lukkarila","year":"2011","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1038\/nature07884","article-title":"An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer","volume":"458","author":"Soucy","year":"2009","journal-title":"Nature"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.molcel.2011.08.025","article-title":"Systematic and quantitative assessment of the ubiquitin-modified proteome","volume":"44","author":"Kim","year":"2011","journal-title":"Mol. Cell"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/nm.4474","article-title":"A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment","volume":"24","author":"Hyer","year":"2018","journal-title":"Nat. Med."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1016\/j.cell.2011.05.039","article-title":"An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme","volume":"145","author":"Ceccarelli","year":"2011","journal-title":"Cell"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1038\/cr.2016.31","article-title":"Drugging the undruggables: Exploring the ubiquitin system for drug development","volume":"26","author":"Huang","year":"2016","journal-title":"Cell Res."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1182\/blood-2012-02-406074","article-title":"Inhibition of proliferation and survival of diffuse large B-cell lymphoma cells by a small-molecule inhibitor of the ubiquitin-conjugating enzyme Ubc13-Uev1A","volume":"120","author":"Pulvino","year":"2012","journal-title":"Blood"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1960","DOI":"10.1182\/blood-2007-09-113860","article-title":"Absence of SKP2 expression attenuates BCR-ABL-induced myeloproliferative disease","volume":"112","author":"Agarwal","year":"2008","journal-title":"Blood"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1016\/j.cell.2013.06.048","article-title":"Pharmacological inactivation of Skp2 SCF ubiquitin ligase restricts cancer stem cell traits and cancer progression","volume":"154","author":"Chan","year":"2013","journal-title":"Cell"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4690","DOI":"10.1182\/blood-2007-09-112904","article-title":"Targeting the p27 E3 ligase SCF(Skp2) results in p27- and Skp2-mediated cell-cycle arrest and activation of autophagy","volume":"111","author":"Chen","year":"2008","journal-title":"Blood"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1126\/science.1092472","article-title":"In vivo activation of the p53 pathway by small-molecule antagonists of MDM2","volume":"303","author":"Vassilev","year":"2004","journal-title":"Science"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1016\/j.cell.2010.11.016","article-title":"Will the ubiquitin system furnish as many drug targets as protein kinases?","volume":"143","author":"Cohen","year":"2010","journal-title":"Cell"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2819","DOI":"10.1021\/acs.jmedchem.6b01665","article-title":"Discovery of 4-((3\u2032R,4\u2032S,5\u2032R)-6\u2033-Chloro-4\u2032-(3-chloro-2-fluorophenyl)-1\u2032-ethyl-2\u2033-oxodispiro[cyclohexane-1,2\u2032-pyrrolidine-3\u2032,3\u2033-indoline]-5\u2032-carboxamido)bicyclo[2.2.2]octane -1-carboxylic Acid (AA-115\/APG-115): A Potent and Orally Active Murine Double Minute 2 (MDM2) Inhibitor in Clinical Development","volume":"60","author":"Aguilar","year":"2017","journal-title":"J. Med. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"eaao3003","DOI":"10.1126\/scitranslmed.aao3003","article-title":"Dual inhibition of MDMX and MDM2 as a therapeutic strategy in leukemia","volume":"10","author":"Carvajal","year":"2018","journal-title":"Sci. Transl. Med."},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Sailo, B.L., Banik, K., Girisa, S., Bordoloi, D., Fan, L., Halim, C.E., Wang, H., Kumar, A.P., Zheng, D., and Mao, X. (2019). FBXW7 in Cancer: What Has Been Unraveled Thus Far?. Cancers, 11.","DOI":"10.3390\/cancers11020246"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"46723","DOI":"10.1074\/jbc.M406537200","article-title":"Pathway for degradation of peptides generated by proteasomes: A key role for thimet oligopeptidase and other metallopeptidases","volume":"279","author":"Saric","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.ejmech.2017.07.048","article-title":"Puromycin based inhibitors of aminopeptidases for the potential treatment of hematologic malignancies","volume":"139","author":"Singh","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1054\/bjoc.2000.1353","article-title":"Single amino acid (arginine) deprivation: Rapid and selective death of cultured transformed and malignant cells","volume":"83","author":"Scott","year":"2000","journal-title":"Br. J. Cancer"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1158\/1535-7163.MCT-08-0735","article-title":"Aminopeptidase inhibition as a targeted treatment strategy in myeloma","volume":"8","author":"Moore","year":"2009","journal-title":"Mol. Cancer Ther."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.4161\/auto.5.7.9510","article-title":"Starving to succeed","volume":"5","author":"Davenport","year":"2009","journal-title":"Autophagy"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.cell.2012.03.017","article-title":"mTOR signaling in growth control and disease","volume":"149","author":"Laplante","year":"2012","journal-title":"Cell"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1987","DOI":"10.1080\/1042819031000122033","article-title":"Aminopeptidase inhibitors inhibit proliferation and induce apoptosis of K562 and STI571-resistant K562 cell lines through the MAPK and GSK-3beta pathways","volume":"44","author":"Sawafuji","year":"2003","journal-title":"Leuk. Lymphoma"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"6669","DOI":"10.1158\/0008-5472.CAN-07-6627","article-title":"CHR-2797: An antiproliferative aminopeptidase inhibitor that leads to amino acid deprivation in human leukemic cells","volume":"68","author":"Krige","year":"2008","journal-title":"Cancer Res."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/j.leukres.2010.10.030","article-title":"Aminopeptidase inhibition by the novel agent CHR-2797 (tosedostat) for the therapy of acute myeloid leukemia","volume":"35","author":"Jenkins","year":"2011","journal-title":"Leuk. Res."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1186\/s13045-017-0463-6","article-title":"Emerging therapies for acute myeloid leukemia","volume":"10","author":"Saygin","year":"2017","journal-title":"J. Hematol. Oncol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"3945","DOI":"10.1182\/blood-2018-99-114447","article-title":"Statins Potentiate Aminopeptidase Inhibitor (pro)Drug Activity in Acute Myeloid Leukemia Cells","volume":"132","author":"Cloos","year":"2018","journal-title":"Blood"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"e503","DOI":"10.1038\/bcj.2016.112","article-title":"The role of the proteasome in AML","volume":"6","author":"Csizmar","year":"2016","journal-title":"Blood Cancer J."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.htct.2018.07.003","article-title":"New proteasome inhibitors in the treatment of multiple myeloma","volume":"41","author":"Hungria","year":"2019","journal-title":"Hematol. Transfus. Cell Ther."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"172458","DOI":"10.1155\/2015\/172458","article-title":"Mechanism of Action of Bortezomib and the New Proteasome Inhibitors on Myeloma Cells and the Bone Microenvironment: Impact on Myeloma-Induced Alterations of Bone Remodeling","volume":"2015","author":"Accardi","year":"2015","journal-title":"BioMed Res. Int."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1530","DOI":"10.1182\/blood-2002-08-2543","article-title":"Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341","volume":"101","author":"Hideshima","year":"2003","journal-title":"Blood"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/nrclinonc.2016.206","article-title":"Proteasome inhibitors in cancer therapy","volume":"14","author":"Manasanch","year":"2017","journal-title":"Nat. Rev. Clin. Oncol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"E291","DOI":"10.1002\/ajh.25605","article-title":"A phase II study of bortezomib in combination with pegylated liposomal doxorubicin for acute myeloid leukemia","volume":"94","author":"Tomlinson","year":"2019","journal-title":"Am. J. Hematol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"4830","DOI":"10.1158\/1078-0432.CCR-11-3007","article-title":"A phase I single-agent study of twice-weekly consecutive-day dosing of the proteasome inhibitor carfilzomib in patients with relapsed or refractory multiple myeloma or lymphoma","volume":"18","author":"Alsina","year":"2012","journal-title":"Clin. Cancer Res. Off. J. Am. Assoc. Cancer Res."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"5311","DOI":"10.1158\/1078-0432.CCR-11-0476","article-title":"In vitro and in vivo selective antitumor activity of a novel orally bioavailable proteasome inhibitor MLN9708 against multiple myeloma cells","volume":"17","author":"Chauhan","year":"2011","journal-title":"Clin. Cancer Res. Off. J. Am. Assoc. Cancer Res."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1007\/s10555-017-9699-4","article-title":"(Immuno)proteasomes as therapeutic target in acute leukemia","volume":"36","author":"Cloos","year":"2017","journal-title":"Cancer Metastasis Rev."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1446","DOI":"10.1158\/1078-0432.CCR-07-4626","article-title":"Phase I and pharmacokinetic study of bortezomib in combination with idarubicin and cytarabine in patients with acute myelogenous leukemia","volume":"14","author":"Attar","year":"2008","journal-title":"Clin. Cancer Res. Off. J. Am. Assoc. Cancer Res."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1200\/JCO.2012.45.2177","article-title":"Bortezomib added to daunorubicin and cytarabine during induction therapy and to intermediate-dose cytarabine for consolidation in patients with previously untreated acute myeloid leukemia age 60 to 75 years: CALGB (Alliance) study 10502","volume":"31","author":"Attar","year":"2013","journal-title":"J. Clin. Oncol. Off. J. Am. Soc. Clin. Oncol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"6025","DOI":"10.1182\/blood-2012-03-413898","article-title":"Clinical and pharmacodynamic activity of bortezomib and decitabine in acute myeloid leukemia","volume":"119","author":"Blum","year":"2012","journal-title":"Blood"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1007\/s11523-018-0603-0","article-title":"Targeting the Proteasome in Refractory Pediatric Leukemia Cells: Characterization of Effective Cytotoxicity of Carfilzomib","volume":"13","author":"Swift","year":"2018","journal-title":"Target. Oncol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1586\/era.13.4","article-title":"Proteasome inhibitors in acute leukemia","volume":"13","author":"Niewerth","year":"2013","journal-title":"Expert Rev. Anticancer Ther."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"12793","DOI":"10.1038\/srep12793","article-title":"HAUSP-nucleolin interaction is regulated by p53-Mdm2 complex in response to DNA damage response","volume":"5","author":"Lim","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.ccr.2012.08.007","article-title":"A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance","volume":"22","author":"Chauhan","year":"2012","journal-title":"Cancer Cell"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"3588","DOI":"10.1182\/blood-2014-10-605584","article-title":"Targeting deubiquitinase activity with a novel small-molecule inhibitor as therapy for B-cell malignancies","volume":"125","author":"Peterson","year":"2015","journal-title":"Blood"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"26979","DOI":"10.1038\/srep26979","article-title":"The proteasome deubiquitinase inhibitor VLX1570 shows selectivity for ubiquitin-specific protease-14 and induces apoptosis of multiple myeloma cells","volume":"6","author":"Wang","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1636","DOI":"10.1038\/nm.2536","article-title":"Inhibition of proteasome deubiquitinating activity as a new cancer therapy","volume":"17","author":"Brnjic","year":"2011","journal-title":"Nat. Med."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"eaat0572","DOI":"10.1126\/science.aat0572","article-title":"Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN","volume":"362","author":"Sievers","year":"2018","journal-title":"Science"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1182\/blood-2013-07-517276","article-title":"A phase 2 trial of lenalidomide, bortezomib, and dexamethasone in patients with relapsed and relapsed\/refractory myeloma","volume":"123","author":"Richardson","year":"2014","journal-title":"Blood"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1126\/science.1244851","article-title":"Lenalidomide causes selective degradation of IKZF1 and IKZF3 in multiple myeloma cells","volume":"343","author":"Kronke","year":"2014","journal-title":"Science"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1158\/1078-0432.CCR-18-1203","article-title":"A First-in-Human Study of Novel Cereblon Modulator Avadomide (CC-122) in Advanced Malignancies","volume":"25","author":"Rasco","year":"2019","journal-title":"Clin. Cancer Res. Off. J. Am. Assoc. Cancer Res."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/s41589-019-0378-3","article-title":"Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15","volume":"16","author":"Faust","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"eaal3755","DOI":"10.1126\/science.aal3755","article-title":"Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15","volume":"356","author":"Han","year":"2017","journal-title":"Science"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1016\/j.molcel.2020.01.010","article-title":"Harnessing the Power of Proteolysis for Targeted Protein Inactivation","volume":"77","author":"Verma","year":"2020","journal-title":"Mol. Cell"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"e1700247","DOI":"10.1002\/bies.201700247","article-title":"PROTACs: An Emerging Targeting Technique for Protein Degradation in Drug Discovery","volume":"40","author":"Gu","year":"2018","journal-title":"BioEssays News Rev. Mol. Cell. Dev. Biol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"8554","DOI":"10.1073\/pnas.141230798","article-title":"Protacs: Chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation","volume":"98","author":"Sakamoto","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1002\/anie.201507634","article-title":"Modular PROTAC Design for the Degradation of Oncogenic BCR-ABL","volume":"55","author":"Lai","year":"2016","journal-title":"Angew. Chem."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1021\/acsmedchemlett.7b00247","article-title":"Targeting the Allosteric Site of Oncoprotein BCR-ABL as an Alternative Strategy for Effective Target Protein Degradation","volume":"8","author":"Shimokawa","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1038\/nature10334","article-title":"RNAi screen identifies Brd4 as a therapeutic target in acute myeloid leukaemia","volume":"478","author":"Zuber","year":"2011","journal-title":"Nature"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1126\/science.aab1433","article-title":"Phthalimide conjugation as a strategy for in vivo target protein degradation","volume":"348","author":"Winter","year":"2015","journal-title":"Science"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1016\/j.chembiol.2015.05.009","article-title":"Hijacking the E3 Ubiquitin Ligase Cereblon to Efficiently Target BRD4","volume":"22","author":"Lu","year":"2015","journal-title":"Chem. Biol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1038\/s41419-019-1570-9","article-title":"BRD9 binds cell type-specific chromatin regions regulating leukemic cell survival via STAT5 inhibition","volume":"10","author":"Liu","year":"2019","journal-title":"Cell Death Dis."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1021\/acs.jmedchem.8b01413","article-title":"Iterative Design and Optimization of Initially Inactive Proteolysis Targeting Chimeras (PROTACs) Identify VZ185 as a Potent, Fast, and Selective von Hippel-Lindau (VHL) Based Dual Degrader Probe of BRD9 and BRD7","volume":"62","author":"Zoppi","year":"2019","journal-title":"J. Med. Chem."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1016\/j.ccell.2019.10.010","article-title":"Inhibit versus Destroy: Are PROTAC Degraders the Solution to Targeting STAT3?","volume":"36","author":"Heppler","year":"2019","journal-title":"Cancer Cell"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1021\/acs.jmedchem.7b00635","article-title":"Identification and Characterization of Von Hippel-Lindau-Recruiting Proteolysis Targeting Chimeras (PROTACs) of TANK-Binding Kinase 1","volume":"61","author":"Crew","year":"2018","journal-title":"J. Med. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1158\/1535-7163.MCT-18-1129","article-title":"Acquired Resistance to BET-PROTACs (Proteolysis-Targeting Chimeras) Caused by Genomic Alterations in Core Components of E3 Ligase Complexes","volume":"18","author":"Zhang","year":"2019","journal-title":"Mol. Cancer Ther."}],"container-title":["Cancers"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6694\/12\/7\/1898\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:51:24Z","timestamp":1760176284000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6694\/12\/7\/1898"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,7,14]]},"references-count":146,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2020,7]]}},"alternative-id":["cancers12071898"],"URL":"https:\/\/doi.org\/10.3390\/cancers12071898","relation":{},"ISSN":["2072-6694"],"issn-type":[{"value":"2072-6694","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,7,14]]}}}