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Pirh2 E3 Ubiquitin Ligase Targets DNA Polymerase Eta for 20S Proteasomal Degradation

Jung, Y.-S., Liu, G., & Chen, X. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01198-09 · Cited by 68 · see citing works

The RING Domain of cIAP1 Mediates the Degradation of RING-bearing Inhibitor of Apoptosis Proteins by Distinct Pathways

Cheung, H. H., Plenchette, S., Kern, C. J., Mahoney, D. J., & Korneluk, R. G. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-01-0107 · Cited by 67 · see citing works

Resistance mechanisms to inhibitors of p53-MDM2 interactions in cancer therapy: can we overcome them?

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Murine double minute 2: p53-independent roads lead to genome instability or death

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MDM2 as a Modifier Gene in Retinoblastoma

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Post-translational modifications on the retinoblastoma protein

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Targeting CDK4/6 in breast cancer

Shanabag, A., Armand, J., Son, E., & Yang, H. W. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01395-3 · Cited by 68 · see citing works

Mdm2 Is Required for Inhibition of Cdk2 Activity by p21, Thereby Contributing to p53-Dependent Cell Cycle Arrest

Giono, L. E., & Manfredi, J. J. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01967-06 · Cited by 62 · see citing works

The E2F1/Rb and p53/MDM2 Pathways in DNA Repair and Apoptosis: Understanding the Crosstalk to Develop Novel Strategies for Prostate Cancer Radiotherapy

Udayakumar, T. S., Shareef, M. M., Diaz, D. A., Ahmed, M. M., & Pollack, A. S. (2010) · Seminars in Radiation Oncology · doi:10.1016/j.semradonc.2010.05.007 · Cited by 62 · see citing works

Sequential activation of E2F via Rb degradation and c-Myc drives resistance to CDK4/6 inhibitors in breast cancer

Kim, S. S., Armand, J., Safonov, A. M., Zhang, M., Soni, R. K., Schwartz, G. K., McGuinness, J. E., Hibshoosh, H. H., Razavi, P., Kim, M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113198 · Cited by 60 · see citing works

HAUSP , a novel deubiquitinase for Rb – MDM 2 the critical regulator

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MdmX Promotes Bipolar Mitosis To Suppress Transformation and Tumorigenesis in p53-Deficient Cells and Mice

Matijasevic, Z., Steinman, H. A., Hoover, K., & Jones, S. N. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01108-07 · Cited by 58 · see citing works

Tied Up in Loops: Positive and Negative Autoregulation of p53Preprint

Lü, X. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000984 · Cited by 58 · see citing works

Pin1 modulates p63α protein stability in regulation of cell survival, proliferation and tumor formation

Li, C., Chang, D. L. F., Yang, Z., Qi, J., Liu, R., He, H., Li, D., & Xiao, Z. J. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.468 · Cited by 57 · see citing works

Mdm2 and MdmX as Regulators of Gene Expression

Biderman, L., Manley, J. L., & Prives, C. L. (2012) · Genes & Cancer · doi:10.1177/1947601912455331 · Cited by 55 · see citing works

Roles for negative cell regulator 14-3-3σ in control of MDM2 activities

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New frontiers in the treatment of liposarcoma, a therapeutically resistant malignant cohort

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MDM2 Regulates Dihydrofolate Reductase Activity through Monoubiquitination

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Osteosarcoma in Pediatric and Adult Populations: Are Adults Just Big Kids?

Kim, C., Davis, L. E., Albert, C. M., Samuels, B. L., Roberts, J. L., & Wagner, M. J. (2023) · Cancers · doi:10.3390/cancers15205044 · Cited by 54 · see citing works

Aurora-A kinase interacting protein 1 (AURKAIP1) promotes Aurora-A degradation through an alternative ubiquitin-independent pathway

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Targeting the ubiquitin–proteasome system to activate wild-type p53 for cancer therapy

Allende-Vega, N., & Saville, M. K. (2009) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2009.10.004 · Cited by 51 · see citing works

Tolerance of Chromosomal Instability in Cancer: Mechanisms and Therapeutic Opportunities

Gronroos, E. C., & López-García, C. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-1958 · Cited by 51 · see citing works

Ubiquitin-independent- versus ubiquitin-dependent proteasomal degradation of the c-Fos and Fra-1 transcription factors: Is there a unique answer?

Basbous, J., Jariel‐Encontre, I., Gomard, T., Bossis, G., & Piechaczyk, M. (2007) · Biochimie · doi:10.1016/j.biochi.2007.07.016 · Cited by 50 · see citing works

MDM2 Overexpression Deregulates the Transcriptional Control of RB/E2F Leading to DNA Methyltransferase 3A Overexpression in Lung Cancer

Tang, Y.-A., Lin, R.-K., Tsai, Y.-T., Hsu, H., Yang, Y., Chen, C., & Wang, Y. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-2617 · Cited by 49 · see citing works

NRF3-POMP-20S Proteasome Assembly Axis Promotes Cancer Development via Ubiquitin-Independent Proteolysis of p53 and Retinoblastoma Protein

Waku, T., Nakamura, N., Koji, M., Watanabe, H., Katoh, H., Tatsumi, C., Tamura, N., Hatanaka, A., Hirose, S., Katayama, H., et al. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00597-19 · Cited by 47 · see citing works

The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a

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Proteomic analysis of the 20S proteasome (PSMA3)-interacting proteins reveals a functional link between the proteasome and mRNA metabolism

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p38 phosphorylates Rb on Ser567 by a novel, cell cycle-independent mechanism that triggers Rb–Hdm2 interaction and apoptosis

Delston, R. B., Matatall, K. A., Sun, Y., Onken, M. D., & Harbour, J. W. (2010) · Oncogene · doi:10.1038/onc.2010.442 · Cited by 46 · see citing works

Targeting RING domains of Mdm2–MdmX E3 complex activates apoptotic arm of the p53 pathway in leukemia/lymphoma cells

Wu, W., Xu, C., Ling, X., Fan, C., Buckley, B., Chernov, M. V., Ellis, L., Li, F., Muñoz, I. G., & Wang, X. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.358 · Cited by 46 · see citing works

Mdm2 and Tumorigenesis: Evolving Theories and Unsolved Mysteries

Senturk, E., & Manfredi, J. J. (2012) · Genes & Cancer · doi:10.1177/1947601912457368 · Cited by 46 · see citing works

MDM2 interacts with and downregulates a sarcomeric protein, TCAP

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Regulation of the retinoblastoma–E2F pathway by the ubiquitin–proteasome system

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Ubiquitin-independent proteasomal degradation during oncogenic viral infections

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Targeted Protein Degradation: Principles and Applications of the Proteasome

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Cardiac-specific ablation of the E3 ubiquitin ligase Mdm2 leads to oxidative stress, broad mitochondrial deficiency and early death

Hauck, L., Stanley-Hasnain, S., Fung, A., Grothe, D., Rao, V., Mak, T. W., & Billia, F. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189861 · Cited by 44 · see citing works

Roles of pRB in the Regulation of Nucleosome and Chromatin Structures

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Pin1 inhibits PP2A-mediated Rb dephosphorylation in regulation of cell cycle and S-phase DNA damage

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MDM2 Promotes Proteasomal Degradation of p21Waf1 via a Conformation Change

Xu, H., Zhang, Z., Li, M., & Zhang, R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.059568 · Cited by 41 · see citing works

The E3 ubiquitin protein ligase MDM2 dictates all-trans retinoic acid-induced osteoblastic differentiation of osteosarcoma cells by modulating the degradation of RARα

Ying, M., Zhang, L., Zhou, Q., Shao, X., Cao, J., Zhang, N., Li, W., Zhu, H., Yang, B., & He, Q. (2016) · Oncogene · doi:10.1038/onc.2015.503 · Cited by 41 · see citing works

Dual function of MDM2 and MDMX toward the tumor suppressors p53 and RB

Hernández‐Monge, J., Rousset-Roman, A. B., Medina‐Medina, I., & Olivares‐Illana, V. (2016) · Genes & Cancer · doi:10.18632/genesandcancer.120 · Cited by 41 · see citing works

Role of proteasomes in transcription and their regulation by covalent modifications

Mittenberg, A. G. (2008) · Frontiers in bioscience · doi:10.2741/3220 · Cited by 40 · see citing works

Proteasome: a Nanomachinery of Creative Destruction

Kudriaeva, A. A., & Belogurov, A. A. (2019) · Biochemistry (Moscow) · doi:10.1134/s0006297919140104 · Cited by 41 · see citing works

The overexpression of multidrug resistance-associated proteins and gankyrin contribute to arsenic trioxide resistance in liver and gastric cancer cells

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Human T-cell Leukemia Virus Type 1 HBZ Protein Bypasses the Targeting Function of Ubiquitination

Isono, O., Ohshima, T., Saeki, Y., Matsumoto, J., Hijikata, M., Tanaka, K., & Shimotohno, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802527200 · Cited by 37 · see citing works

Comprehensive analysis of regulation of DNA methyltransferase isoforms in human breast tumors

Hegde, M., & Joshi, M. B. (2021) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-021-03519-4 · Cited by 36 · see citing works

Retinoblastoma protein modulates gankyrin–MDM2 in regulation of p53 stability and chemosensitivity in cancer cells

Qiu, W., Wu, J., Walsh, E. M., Zhang, Y., Chen, C. Y., Fujita, J., & Xiao, Z.-X. J. (2008) · Oncogene · doi:10.1038/onc.2008.43 · Cited by 35 · see citing works

Proteasomal degradation of the KLF5 transcription factor through a ubiquitin‐independent pathway

Chen, C., Zhou, Z., Guo, P., & Dong, J. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.02.018 · Cited by 35 · see citing works

MdmX regulates transformation and chromosomal stability in p53-deficient cells

Matijasevic, Z., Krzywicka-Racka, A., Sluder, G., & Jones, S. N. (2008) · Cell Cycle · doi:10.4161/cc.7.19.6797 · Cited by 34 · see citing works

Non-canonical pathway for Rb inactivation and external signaling coordinate cell-cycle entry without CDK4/6 activity

Zhang, M., Kim, S., & Yang, H. W. (2023) · Nature Communications · doi:10.1038/s41467-023-43716-y · Cited by 34 · see citing works

Herpes simplex virus type 1 ICP0 induces CD83 degradation in mature dendritic cells independent of its E3 ubiquitin ligase function

Heilingloh, C. S., Mühl-Zürbes, P., Steinkasserer, A., & Kummer, M. (2014) · Journal of General Virology · doi:10.1099/vir.0.062810-0 · Cited by 34 · see citing works

A Novel Retinoblastoma Protein (RB) E3 Ubiquitin Ligase (NRBE3) Promotes RB Degradation and Is Transcriptionally Regulated by E2F1 Transcription Factor

Wang, Y., Zheng, Z., Zhang, J., Wang, Y., Kong, R., Liu, J., Zhang, Y., Deng, H., Du, X., & Ke, Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.655597 · Cited by 33 · see citing works

The Role and Clinical Implications of the Retinoblastoma (RB)-E2F Pathway in Gastric Cancer

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Proteasome-dependent degradation of α-catenin is regulated by interaction with ARMc8α

Suzuki, T., Ueda, A., Kobayashi, N., Yang, J. H., Tomaru, K., Yamamoto, M., Takeno, M., & Ishigatsubo, Y. (2008) · Biochemical Journal · doi:10.1042/bj20071312 · Cited by 34 · see citing works

The roles of MDM2 and MDMX phosphorylation in stress signaling to p53

Chen, J. (2012) · Genes & Cancer · doi:10.1177/1947601912454733 · Cited by 33 · see citing works

Nutlin-3 Affects Expression and Function of Retinoblastoma Protein

Du, W., Wu, J., Walsh, E. M., Zhang, Y., Chen, C. Y., & Xiao, Z.-X. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.046904 · Cited by 33 · see citing works

SETDB1 Modulates Degradation of Phosphorylated RB and Anticancer Efficacy of CDK4/6 Inhibitors

Huang, Z., Li, X., Tang, B., Li, H., Zhang, J., Sun, R., Ma, J., Pan, Y., Yan, B., Zhou, Y., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-0264 · Cited by 33 · see citing works

Targeting Retinoblastoma Protein for Degradation by Proteasomes

Ying, H., & Xiao, Z.-X. J. (2006) · Cell Cycle · doi:10.4161/cc.5.5.2515 · Cited by 69 · see citing works

Enhanced Mdm2 activity inhibits pRB function via ubiquitin‐dependent degradation

Uchida, C., Miwa, S., Kitagawa, K., Hattori, T., Isobe, T., Otani, S., Oda, T., Sugimura, H., Kamijo, T., Ookawa, K., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600486 · Cited by 184 · see citing works

Abstract 2459: The oncogenic activity of MDMx is associated with physical interaction and suppression of retinoblastoma protein

Xiao, Z. J., Zhang, H., & Zhang, Y. (2014) · Cancer Research · doi:10.1158/1538-7445.am2014-2459

MDMX exerts its oncogenic activity via suppression of retinoblastoma protein

Zhang, H., Hu, L., Qiu, W., Deng, T., Zhang, Y., Bergholz, J. S., & Xiao, Z.-X. (2015) · Oncogene · doi:10.1038/onc.2015.11 · Cited by 26 · see citing works

Effects of MdmX on Mdm2‐mediated downregulation of pRB

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