Chemically induced degradation of CK2 by proteolysis targeting chimeras based on a ubiquitin-proteasome pathway
Abstract
As a ubiquitous, highly pleiotropic and constitutively active serine/threonine protein kinase, casein kinase 2 (CK2) is closely associated with tumorigenesis by its overexpression in cancer cells. Here we report several proteolysis targeting chimeras (PROTACs) via "click reaction" to connect a CK2 inhibitor (CX-4945) and pomalidomide for degradation of CK2 protein. Among them, compound 2 degraded CK2 in a dose and time-dependent manner, and kept CK2 at a low basal level by recruiting ubiquitin-proteasome system. The degradation of CK2 resulted in the reduced phosphorylation of Akt and the up-regulation of p53. As a CK2 protein degrader, 2 showed the analogous cytotoxicity to CX-4945 but with a quite different mechanism of action from the CK2 inhibitor, hinting that degradation of CK2 proteins by PROTACs is a potential way for cancer treatments.
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Reported CK2 degraders were active only at the 24 h time point.
“For example, reported CK2 degraders were active only at the 24 h time point (Chen et al., 2018).”
From Mapping the Degradable Kinome Provides a Resource for Expedited Degrader Development (2020) · cites this paper as Chen et al., 2018
Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,216 · see citing works
Phthalimide conjugation as a strategy for in vivo target protein degradation
Winter, G. E., Buckley, D. L., Paulk, J., Roberts, J. M., Souza, A., Dhe-Paganon, S., & Bradner, J. E. (2015) · Science · doi:10.1126/science.aab1433 · Cited by 1,760 · see citing works
Structural basis of PROTAC cooperative recognition for selective protein degradation
Gadd, M. S., Testa, A., Lucas, X., Chan, K.-H., Chen, W., Lamont, D. J., Zengerle, M., & Ciulli, A. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2329 · Cited by 1,242 · see citing works
Protein kinase CK2: structure, regulation and role in cellular decisions of life and death
Litchfield, D. W. (2002) · Biochemical Journal · doi:10.1042/bj20021469 · Cited by 1,237 · see citing works
Structure of the DDB1–CRBN E3 ubiquitin ligase in complex with thalidomide
Fischer, E. S., Böhm, K., Lydeard, J. R., Yang, H., Stadler, M. B., Cavadini, S., Nagel, J., Serluca, F., Acker, V., Lingaraju, G. M., et al. (2014) · Nature · doi:10.1038/nature13527 · Cited by 1,141 · see citing works
Hijacking the E3 Ubiquitin Ligase Cereblon to Efficiently Target BRD4
Lu, J., Qian, Y., Altieri, M., Dong, H., Wang, J., Raina, K., Hines, J., Winkler, J. D., Crew, A. P., Coleman, K., et al. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.05.009 · Cited by 1,140 · see citing works
Vousden, K. H., & Ryan, K. M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2715 · Cited by 959 · see citing works
Lenalidomide induces ubiquitination and degradation of CK1α in del(5q) MDS
Krönke, J., Fink, E. C., Hollenbach, P. W., MacBeth, K. J., Hurst, S. N., Udeshi, N. D., Chamberlain, P. P., Mani, D. R., Man, H. W., Gandhi, A. K., et al. (2015) · Nature · doi:10.1038/nature14610 · Cited by 863 · see citing works
Small‐Molecule PROTACS: New Approaches to Protein Degradation
Toure, M., & Crews, C. M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201507978 · Cited by 674 · see citing works
Drug discovery in the ubiquitin–proteasome system
Nalepa, G., Rolfe, M., & Harper, J. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2056 · Cited by 619 · see citing works
Modular PROTAC design for the degradation of oncogenic BCR-ABL
Lai, A. C., Toure, M., Hellerschmied, D., Salami, J., Jaime‐Figueroa, S., Ko, E., Hines, J., & Crews, C. M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201507634 · Cited by 618 · see citing works
Targeting the ubiquitin system in cancer therapy
Hoeller, D., & Đikić, I. (2009) · Nature · doi:10.1038/nature07960 · Cited by 595 · see citing works
Protein kinase CK2: a challenge to canons
Pinna, L. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.00074 · Cited by 491 · see citing works
Protac-Induced Protein Degradation in Drug Discovery: Breaking the Rules or Just Making New Ones?
Churcher, I. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01272 · Cited by 491 · see citing works
Casein Kinase IIα Transgene-Induced Murine Lymphoma: Relation to Theileriosis in Cattle
Seldin, D. C., & Leder, P. (1995) · Science · doi:10.1126/science.7846532 · Cited by 400 · see citing works
The Protein Kinase CK2 Facilitates Repair of Chromosomal DNA Single-Strand Breaks
Loizou, J. I., El‐Khamisy, S. F., Zlatanou, A., Moore, D. J., Chan, D. W., Qin, J., Sarno, S., Meggio, F., Pinna, L. A., & Caldecott, K. W. (2004) · Cell · doi:10.1016/s0092-8674(04)00206-5 · Cited by 330 · see citing works
Pierre, F., Chua, P. C., O’Brien, S., Siddiqui-Jain, A., Bourbon, P., Haddach, M., Michaux, J., Nagasawa, J. Y., Schwaebe, M. K., Stefan, E., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm101251q · Cited by 299 · see citing works
Protein kinase CK2 in mammary gland tumorigenesis
Landesman‐Bollag, E., Romieu, R., Song, D. H., Sonenshein, G. E., Cardiff, R. D., & Seldin, D. C. (2001) · Oncogene · doi:10.1038/sj.onc.1204411 · Cited by 290 · see citing works
Waste disposal—An attractive strategy for cancer therapy
Salami, J., & Crews, C. M. (2017) · Science · doi:10.1126/science.aam7340 · Cited by 279 · see citing works
Schiedel, M., Herp, D., Hammelmann, S., Swyter, S., Lehotzky, A., Robaa, D., Oláh, J., Ovádi, J., Sippl, W., & Jung, M. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01872 · Cited by 275 · see citing works
The selectivity of inhibitors of protein kinase CK2: an update
Pagano, M. A., Bain, J., Kazimierczuk, Z., Sarno, S., Ruzzene, M., Maira, G. D., Elliott, M., Orzeszko, A., Cozza, G., Meggio, F., et al. (2008) · Biochemical Journal · doi:10.1042/bj20080309 · Cited by 243 · see citing works
Imaging 26S proteasome activity and inhibition in living mice
Luker, G. D., Pica, C. M., Song, J., Luker, K. E., & Piwnica-Worms, D. R. (2003) · Nature Medicine · doi:10.1038/nm894 · Cited by 175 · see citing works
Structural basis of CX-4945 binding to human protein kinase CK2
Ferguson, A. D., Sheth, P. R., Basso, A. D., Paliwal, S., Gray, K., Fischmann, T. O., & Le, H. V. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.11.019 · Cited by 121 · see citing works
Targeted protein knockdown using small molecule degraders
Raina, K., & Crews, C. M. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.05.016 · Cited by 111 · see citing works
ATP Site-Directed Inhibitors of Protein Kinase CK2: An Update
Sarno, S., Papinutto, E., Franchin, C., Bain, J., Elliott, M., Meggio, F., Kazimierczuk, Z., Orzeszko, A., Zanotti, G., Battistutta, R., et al. (2011) · Current Topics in Medicinal Chemistry · doi:10.2174/156802611795589638 · Cited by 102 · see citing works
Chemical Inducers of Targeted Protein Degradation
Raina, K., & Crews, C. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.078105 · Cited by 64 · see citing works
Izeradjene, K., Douglas, L., Delaney, A. B., & Houghton, J. A. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-0576 · Cited by 64 · see citing works
Two‐Headed PROTAC: An Effective New Tool for Targeted Protein Degradation
Cyrus, K., Wehenkel, M., Choi, E., Swanson, H. I., & Kim, K. (2010) · ChemBioChem · doi:10.1002/cbic.201000222 · Cited by 59 · see citing works
Tubi, L. Q., Gurrieri, C., Brancalion, A., Bonaldi, L., Bertorelle, R., Manni, S., Pavan, L., Lessi, F., Zambello, R., Trentin, L., et al. (2013) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-6-78 · Cited by 56 · see citing works
A CK2-targeted Pt(IV) prodrug to disrupt DNA damage response
Chen, F., Huang, X., Wu, M., Gou, S., & Hu, W. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.10.026 · Cited by 49 · see citing works
Self-citationLiu, H., Wang, X., Wang, J., Wang, J., Li, Y., Yang, L., & Li, G. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12107004 · Cited by 15 · see citing works
Self-citationNew synthesis route for the preparation of pomalidomide
Huang, D., Shen, C., Wang, W., Huang, L., Ni, F., & Li, J. (2016) · Synthetic Communications · doi:10.1080/00397911.2016.1189574 · Cited by 12 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
PROteolysis TArgeting Chimeras (PROTACs) — Past, present and future
Pettersson, M., & Crews, C. M. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2019.01.002 · Cited by 818 · see citing works
PROTACs: great opportunities for academia and industry
Sun, X., Gao, H., Yang, Y., He, M., Wu, Y., Song, Y.-G., Tong, Y., & Rao, Y. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0101-6 · Cited by 651 · see citing works
Targeted protein degradation: elements of PROTAC design
Paiva, S.-L., & Crews, C. M. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.02.022 · Cited by 586 · see citing works
Current strategies for the design of PROTAC linkers: a critical review
Troup, R. I., Fallan, C., & Baud, M. G. J. (2020) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2020.00018 · Cited by 424 · see citing works
Proteolysis-targeting chimeras (PROTACs) in cancer therapy
Li, X., Pu, W., Zheng, Q., Ai, M., Chen, S., & Peng, Y. (2022) · Molecular Cancer · doi:10.1186/s12943-021-01434-3 · Cited by 374 · see citing works
Mapping the Degradable Kinome Provides a Resource for Expedited Degrader Development
Donovan, K. A., Ferguson, F. M., Bushman, J. W., Eleuteri, N. A., Bhunia, D., Ryu, S., Tan, L., Shi, K., Yue, H., Liu, X., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.038 · Cited by 359 · see citing works
Degradation of proteins by PROTACs and other strategies
Wang, Y., Jiang, X., Feng, F., Liu, W., & Sun, H. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.08.001 · Cited by 335 · see citing works
The PROTAC technology in drug development
Zou, Y., Ma, D., & Wang, Y. (2019) · Cell Biochemistry and Function · doi:10.1002/cbf.3369 · Cited by 307 · see citing works
Targeted protein degradation: A promise for undruggable proteins
Samarasinghe, K. T. G., & Crews, C. M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.011 · Cited by 291 · see citing works
Zeng, S., Huang, W., Zheng, X., Cheng, L., Zhang, Z., Wang, J., & Shen, Z. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112981 · Cited by 262 · see citing works
E3 Ligase Ligands in Successful PROTACs: An Overview of Syntheses and Linker Attachment Points
Bricelj, A., Steinebach, C., Kuchta, R. D., Gütschow, M., & Sosič, I. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.707317 · Cited by 226 · see citing works
E3 ligase ligand chemistries: from building blocks to protein degraders
Sosič, I., Bricelj, A., & Steinebach, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00148a · Cited by 173 · see citing works
Rationalizing PROTAC-Mediated Ternary Complex Formation Using Rosetta
Bai, N., Miller, S. A., Andrianov, G. V., Yates, M., Kirubakaran, P., & Karanicolas, J. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01451 · Cited by 157 · see citing works
Developments of CRBN-based PROTACs as potential therapeutic agents
Wang, C., Zhang, Y., Wu, Y., & Xing, D. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113749 · Cited by 152 · see citing works
Bivalent Ligands for Protein Degradation in Drug Discovery
Scheepstra, M., Hekking, K. F. W., Hijfte, L. V., & Folmer, R. H. A. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.01.006 · Cited by 120 · see citing works
Novel approaches for the rational design of PROTAC linkers
Zagidullin, A. A., Milyukov, V. A., Rizvanov, A. A., & Bulatov, E. (2020) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2020.00023 · Cited by 70 · see citing works
Strategies of Targeting CK2 in Drug Discovery: Challenges, Opportunities, and Emerging Prospects
Chen, Y., Wang, Y., Wang, J., Zhou, Z., Cao, S., & Zhang, J. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01523 · Cited by 70 · see citing works
Small molecule PROTACs in targeted therapy: An emerging strategy to induce protein degradation
Xi, M., Chen, Y., Yang, H., Xu, H., Du, K., Wu, C., Xu, Y., Deng, L., Luo, X., Yu, L., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.04.036 · Cited by 56 · see citing works
Triazol: A Privileged Scaffold for Proteolysis Targeting Chimeras
Xia, L., Ba, M.-Y., Liu, W., Cheng, W., Hu, C.-P., Zhao, Q., Yao, Y., Sun, M., & Duan, Y. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0159 · Cited by 50 · see citing works
Proteases and Their Modulators in Cancer Therapy: Challenges and Opportunities
Song, R., Qiao, W., He, J., Huang, J., Luo, Y., & Yang, T. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01640 · Cited by 45 · see citing works
Chen, H., Chen, F., Pei, S., & Gou, S. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.03.035 · Cited by 44 · see citing works
Self-citationManeiro, M., Vita, E. D., Conole, D., Kounde, C. S., Zhang, Q., & Tate, E. W. (2021) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2021.01.002 · Cited by 38 · see citing works
Protein kinase CK2 inhibition as a pharmacological strategy
Borgo, C., & Ruzzene, M. (2021) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2020.09.003 · Cited by 36 · see citing works
Small-molecule PROTACs: Novel Agents for Cancer Therapy
Wan, Y., Yan, C., Gao, H. J., & Liu, T. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0340 · Cited by 32 · see citing works
Progress of small molecules for targeted protein degradation: PROTACs and other technologies
Zhao, H., Xin, M., & Zhang, S. (2023) · Drug Development Research · doi:10.1002/ddr.22026 · Cited by 31 · see citing works
PROTAC unleashed: Unveiling the synthetic approaches and potential therapeutic applications
Pravin, N., & Jóźwiak, K. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116837 · Cited by 28 · see citing works
Advances of bioorthogonal coupling reactions in drug development
Zhan, F., Zhu, J., Xie, S., Xu, J., & Xu, S. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115338 · Cited by 24 · see citing works
Synthesis, biological evaluation and clinical trials of Cereblon-based PROTACs
Vicente, A. T. S., Moura, S. P. S. P., & Salvador, J. A. R. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01598-9 · Cited by 23 · see citing works
Recent advances of PROTACs technology in neurodegenerative diseases
Wang, C., Zhang, Y., Yang, S., & Xing, D. (2023) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2023.105015 · Cited by 17 · see citing works
Degraders: The Ultimate Weapon Against Amplified Driver Kinases in Cancer
Torres‐Ayuso, P., & Brognard, J. (2022) · Molecular Pharmacology · doi:10.1124/molpharm.121.000306 · Cited by 15 · see citing works
Pan, Y., Wang, Y., & Gou, S. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108491 · Cited by 15 · see citing works
Self-citationPROTAC Beyond Cancer- Exploring the New Therapeutic Potential of Proteolysis Targeting Chimeras
Bhole, R. P., Patil, S., Kapare, H. S., Chikhale, R. V., & Gurav, S. S. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266309968240621072550 · Cited by 14 · see citing works
Wang, Y., Deng, S., & Xu, J. (2020) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2020.0066 · Cited by 10 · see citing works
Xu, T., Ma, B., Li, Y., Guo, Z., Zhang, M., & Ng, W. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00223 · Cited by 10 · see citing works
Discovery of a potent BRD4 PROTAC and evaluation of its bioactivity in breast cancer cell lines
Hu, J., Yang, J., Zhou, R., Chen, K., Zhao, H., & Zhou, Y. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117159 · Cited by 10 · see citing works
CK2 Inhibitors Targeting Inside and Outside the Catalytic Box
Day-Riley, S., West, R. M., Brear, P., Hyvönen, M., & Spring, D. R. (2024) · Kinases and Phosphatases · doi:10.3390/kinasesphosphatases2020007 · Cited by 9 · see citing works
Yang, X., He, Y., Kim, R. D., Fleming, J. B., & Xie, H. (2020) · Targeted Oncology · doi:10.1007/s11523-020-00782-2 · Cited by 9 · see citing works
Márquez-Cantudo, L., Ramos, A., Coderch, C., & de Pascual‐Teresa, B. (2021) · Molecules · doi:10.3390/molecules26185606 · Cited by 7 · see citing works
Khan, M. Z. I., Nazli, A., Pan, Y., & Chen, J. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220803112409 · Cited by 7 · see citing works
Computational Modeling of PROTAC Ternary Complexes and Linker Design
Miller, S. A., Andrianov, G. V., Mischley, V., Wharton, K. A., Chen, J. J., & Karanicolas, J. (2022) · doi:10.1002/9783527836208.ch5 · Cited by 4 · see citing works
Preclinical Studies of PROTACs in Hematological Malignancies
Fuchs, O., & Bokorová, R. (2021) · Cardiovascular & Haematological Disorders - Drug Targets · doi:10.2174/1871529x21666210308111546 · Cited by 3 · see citing works
Towards the targeted protein degradation of CK2: design and synthesis of CAM4066-based PROTACs
Day-Riley, S., Krajčovičová, S., Sokhal, A. R., Venne, J. L., Brear, P., Hyvönen, M., Whitehurst, B. C., Carroll, J. S., & Spring, D. R. (2026) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.22.47 · Cited by 1 · see citing works
Zhai, X. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-96121-9.00004-8 · Cited by 1 · see citing works
Proteolysis-targeting chimeras (PROTACs) as novel biotechnology for cancer therapy
Fuchs, O. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90042-3.15001-7 · Cited by 1 · see citing works
WITHDRAWN: Targeted protein degradation: A promising approach for cancer treatment
Khan, M. Z. I., Nazli, A., Naz, I., Khan, D., Haq, I., & Chen, J. (2023) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2023.09.004 · Cited by 1 · see citing works
RetractedPROTACS- targeted protein degradation as a path to precision cancer therapeutics
Gatley, H. R., Fisher, P. B., & Das, S. K. (2025) · Advances in cancer research · doi:10.1016/bs.acr.2025.08.001
McCarthy, F. O., Hélesbeux, J., Bazin, M., Bernoussi, T., Bonnet, J., Logé, C., Ourliac‐Garnier, I., Robert, J.-M., Scaviner, M., Thiéfaine, J., et al. (2026) · Drugs and Drug Candidates · doi:10.3390/ddc5030045
Discovery of a Potent and Selective KRAS G12D Degrader based on PROTAC Degradation
Jiang, L., Yang, W., Liu, Y., Li, G., Luo, X., Zhou, Y., Qin, J., Pan, Y., & Huang, W. (2026) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2026.107633
BindingDB Entry 50020161: Advances of bioorthogonal coupling reactions in drug development.
BindingDB (2024) · UC San Diego · doi:10.7270/q2th8s34
BindingDB Entry 50018659: Developments of CRBN-based PROTACs as potential therapeutic agents.
BindingDB (2024) · UC San Diego · doi:10.7270/q27948wc
BindingDB (2024) · UC San Diego · doi:10.7270/q26977r0
- Authors
- Chen, H., Chen, F., Liu, N., Wang, X., & Gou, S.
- Affiliations
- Southeast University (CN)
- Corresponding author
- Gou, Shaohua
- Venue
- Bioorganic Chemistry
- Publisher
- Elsevier BV
- Published
- 2018-12
- Volume
- 81
- Pages
- 536-544
- ISSN
- 0045-2068 (ISSN-L)
- OpenAlex
- W2891648995
- Cited by
- 51
- References
- 33
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 6 · 2023: 5 · 2022: 6 · 2021: 9 · 2020: 7 · 2019: 9
- FWCI
- 2.31
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Bioorganic Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (21571033, 81503099)
- Jiangsu Province Natural Science Foundation (BK20150643)
- Fundamental Research Funds for the Central Universities (2242016K30020, 2242017K41024)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- casein kinase 2, PROTACs, ubiquitin-proteasome system, protein degradation, CX-4945, pomalidomide, click chemistry, Akt phosphorylation, p53 upregulation, cancer therapy, protein kinase inhibitors
- MeSH terms
- Antineoplastic Agents, Cell Survival, Humans, Neoplasms, Apoptosis, Ubiquitin, Cell Line, Tumor, Proteasome Endopeptidase Complex, Casein Kinase II, Protein Kinase Inhibitors, Proteolysis
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