p53 regulation by ubiquitin

THE UBIQUITIN SYSTEM

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In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2

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Mdm2 promotes the rapid degradation of p53

Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506

Regulation of p53 stability by Mdm2

Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · cited 1×

Mechanisms Underlying Ubiquitination

Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184

Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas

Xue, W., Zender, L., Miething, C., Dickins, R. A., Hernando, E., Krizhanovsky, V., Cordon-Cardo, C., & Lowe, S. W. (2007) · Nature · doi:10.1038/nature05529 · Cited by 2,473

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,416

Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis

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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951

Simulating Molecular Mechanisms of the MDM2-Mediated Regulatory Interactions: A Conformational Selection Model of the MDM2 Lid Dynamics

Verkhivker, G. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040897 · Cited by 18

Promoter hypermethylation influences the suppressive role of long non‑coding RNA MEG3 in the development of multiple myeloma

Yu, W., Shi, Q., Wu, C., Shen, X., Chen, L., & Xu, J. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8723 · Cited by 18

Overexpression of RNF126 Promotes the Development of Colorectal Cancer via Enhancing p53 Ubiquitination and Degradation

Wang, S., Wang, T., Wang, L., Zhong, L., & Li, K. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s271855 · Cited by 18

The role of the 5' terminal region of p53 mRNA in the p53 gene expression

Świątkowska, A., Żydowicz-Machtel, P., Sroka, J., & Ciesiołka, J. (2016) · Acta Biochimica Polonica · doi:10.18388/abp.2016_1342 · Cited by 17

Hyperactivating p53 in Human Papillomavirus-Driven Cancers: A Potential Therapeutic Intervention

Idres, Y. M., McMillan, N. A. J., & Idris, A. (2022) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-022-00583-5 · Cited by 17

Cdk9 phosphorylates Pirh2 protein and prevents degradation of p53 protein

Bagashev, A., Fan, S., Mukerjee, R., Claudio, P. P., Chabrashvili, T., Leng, R. P., Benchimol, S., & Sawaya, B. E. (2013) · Cell Cycle · doi:10.4161/cc.24733 · Cited by 17

The Role of Structural Elements of the 5'-Terminal Region of p53 mRNA in Translation under Stress Conditions Assayed by the Antisense Oligonucleotide Approach

Świątkowska, A., Żydowicz-Machtel, P., Gorska, A. A., Suchacka, J., Dutkiewicz, M., & Ciesiołka, J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141676 · Cited by 16

S100A6 promotes proliferation and migration of HepG2 cells via increased ubiquitin-dependent degradation of p53

Song, D., Xu, B., Shi, D.-M., Li, S., & Cai, Y. (2020) · Open Medicine · doi:10.1515/med-2020-0101 · Cited by 16

Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR

Krois, A. S., Park, S., Martinez‐Yamout, M. A., Dyson, H. J., & Wright, P. E. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00528 · Cited by 14

TheDrosophilaubiquitin-specific protease Puffyeye regulates dMyc-mediated growth

Li, L., Anderson, S., Secombe, J., & Eisenman, R. N. (2013) · Development · doi:10.1242/dev.096941 · Cited by 14

Mechanisms of p53 Functional De-Regulation: Role of the IκB-α/p53 Complex

Carrà, G., Crivellaro, S., Taulli, R., Guerrasio, A., Saglio, G. N., & Morotti, A. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17121997 · Cited by 14

A novel mouse model of rhabdomyosarcoma underscores the dichotomy of MDM2-ALT1 function in vivo

Comiskey, D. F., Jacob, A. G., Sanford, B. L., Montes, M., Goodwin, A., Steiner, H. E., Matsa, E., Tapia-Santos, A. S., Bebee, T. W., Grieves, J. L., et al. (2017) · Oncogene · doi:10.1038/onc.2017.282 · Cited by 13

An oral second-generation proteasome inhibitor oprozomib significantly inhibits lung cancer in a p53 independent manner in vitro

Zhu, H., Wang, T., Xin, Z., Zhan, Y., Gu, G., Li, X., Wang, X., Shun-e, Y., & Liu, C. (2019) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmz093 · Cited by 13

STIP is a critical nuclear scaffolding protein linking USP7 to p53-Mdm2 pathway regulation

Ye, M., Tang, Y.-N., Tang, S.-J., Liu, J., Wu, K., Yao, S., Sun, Y., Zhou, L. J., Deng, T., Chen, Y., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5303 · Cited by 12

RLIP76 Inhibition: A Promising Developmental Therapy for Neuroblastoma

Singhal, S. S., Nagaprashantha, L. D., Singhal, S. S., Singhal, J., Singhal, J., Awasthi, S., & Horne, D. A. (2017) · Pharmaceutical Research · doi:10.1007/s11095-017-2154-y · Cited by 12

High expression of RPL27A predicts poor prognosis in patients with hepatocellular carcinoma

Xing, H., Jiang, X., Yang, C., Tan, B., Hu, J., & Zhang, M. (2023) · World Journal of Surgical Oncology · doi:10.1186/s12957-023-03102-w · Cited by 11

OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy

Hu, C., Wang, A., Fan, D., Worth, M., Chen, Z., Huang, J., Xie, J., Macdonald, J., Li, L., & Jiang, J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2320867121 · Cited by 15

ZNF500 abolishes breast cancer proliferation and sensitizes chemotherapy by stabilizing P53 via competing with MDM2

Ma, X., Fan, M., Yang, K., Wang, Y., Hu, R., Guan, M., Hou, Y., Ying, J., Deng, N., Li, Q., et al. (2023) · Cancer Science · doi:10.1111/cas.15947 · Cited by 9

Structural-functional diversity of p53 proteoforms

Naryzhny, S., & Legina, O. K. (2019) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20196504263 · Cited by 10

XPC multifaceted roles beyond DNA damage repair: p53-dependent and p53-independent functions of XPC in cell fate decisions

Zebian, A., Dor, M. E., Shaito, A. A., Mazurier, F., Rezvani, H. R., & Zibara, K. (2021) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2021.108400 · Cited by 10

Integration of DNA damage and repair with murine double-minute 2 (Mdm2) in tumorigenesis

Lehman, J., & Mayo, L. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131216373 · Cited by 9

Ubiquitin-specific proteases as therapeutic targets in paediatric primary bone tumours?

Mullard, M., Lavaud, M., Regnier, L., Tesfaye, R. A., Ory, B., Rédiní, F., & Verrecchia, F. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114797 · Cited by 9

System‐based strategies for p53 recovery

Azam, M. R., Fazal, S., Ullah, M., & Bhatti, A. I. (2017) · IET Systems Biology · doi:10.1049/iet-syb.2017.0025 · Cited by 9

Targeting Post-Translational Regulation of p53 in Colorectal Cancer by Exploiting Vulnerabilities in the p53-MDM2 Axis

Lai, C. W., Xie, C., Raufman, J., & Xie, G. (2022) · Cancers · doi:10.3390/cancers14010219 · Cited by 9

New insights into cancer: MDM2 binds to the citrullinating enzyme PADI4

Araujo‐Abad, S., Rizzuti, B., Villamarin‐Ortiz, A., Pantoja‐Uceda, D., Moreno‐Gonzalez, C. M., Abián, O., Velázquez‐Campoy, A., Neira, J. L., & Romero, C. D. J. (2023) · Protein Science · doi:10.1002/pro.4723 · Cited by 9

Ubiquitin E3 ligases controlling p53 stability

Lee, S. W., Seong, M. W., Jeon, Y. J., & Chung, C. H. (2012) · Animal Cells and Systems · doi:10.1080/19768354.2012.688769 · Cited by 9

Laminar flow activation of ERK5 leads to cytoprotective effect via CHIP-mediated p53 ubiquitination in endothelial cells

Lim, J. H., & Woo, C.-H. (2011) · Anatomy & Cell Biology · doi:10.5115/acb.2011.44.4.265 · Cited by 9

Ubiquitination of transcription factors in cancer: unveiling therapeutic potential

Kim, D., Nam, H. J., & Baek, S. H. (2025) · Molecular Oncology · doi:10.1002/1878-0261.70033 · Cited by 9

Post-translational modifications in heat stress-related diseases

Cui, Q., Jia, K., Fang, L., Zheng, J., & Wang, F. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1666874 · Cited by 8

Engineering Optogenetic Control of Endogenous p53 Protein Levels

Wehler, P., & Ventura, B. D. (2019) · Applied Sciences · doi:10.3390/app9102095 · Cited by 8

A Hypoxia-Induced SCFFBXL1 E3 Ligase Ubiquitinates and Degrades the MEN1 Tumor Suppressor to Promote Colorectal Cancer Tumorigenesis

Zeng, J., Xiao, X., & Zhou, Z.-Y. (2021) · Cancer Research and Treatment · doi:10.4143/crt.2021.373 · Cited by 8

Human cell-expressed tag-free rhMFG-E8 as an effective radiation mitigator

Chaung, W. W., Zhang, F., Ma, G., Yen, H., Jacob, A., Brenner, M., & Wang, P. (2023) · Scientific Reports · doi:10.1038/s41598-023-49499-y · Cited by 8

Antiproliferative activity exerted by tricyclohexylphosphanegold(I) n-mercaptobenzoate against MCF-7 and A2780 cell lines: the role of p53 signaling pathways

Ang, K. P., Chan, P. F., & Hamid, R. A. (2020) · BioMetals · doi:10.1007/s10534-020-00269-7 · Cited by 8

IKAROS is required for the measured response of NOTCH target genes upon external NOTCH signaling

Lemarié, M., Bottardi, S., Mavoungou, L. O., Pak, H., & Milot, É. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009478 · Cited by 6

Ubiquitin, Ubiquitin-Like Proteins, and Proteasome-Mediated Degradation

Dohmen, R. J., Huibregtse, J. M., & Scheffner, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10069-0 · Cited by 8

ARTS and small-molecule ARTS mimetics upregulate p53 levels by promoting the degradation of XIAP

Abbas, R., Hartmann, O., Asiss, D. T., Abbas, R., Kagan, J., Kim, H.-T., Oren, M., Diefenbacher, M. E., Orian, A., & Larisch, S. (2024) · APOPTOSIS · doi:10.1007/s10495-024-01957-2 · Cited by 6

Interferon‐stimulated gene 15 enters posttranslational modifications of p53

Wang, Y., Ding, Q., Lu, Y., Cao, S., Liu, Q., & Zhang, L. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27347 · Cited by 6

Impact of the Adenoviral E4 Orf3 Protein on the Activity and Posttranslational Modification of p53

DeHart, C. J., Perlman, D. H., & Flint, S. J. (2015) · Journal of Virology · doi:10.1128/jvi.03072-14 · Cited by 7

Effect of pharmacodynamical interaction between nutlin-3a and aspirin in the activation of p53

Awan, M. S., Aslam, M., Liaquat, M., Bhatti, A. I., & Liaquat, A. (2021) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2021.110696 · Cited by 5

Modeling and Simulation of p53-Mdm2 Protein Pathway in Normal Cells

Patra, T., Chatterjee, S., Pandit, S., & Barman, S. (2021) · Lecture notes in networks and systems · doi:10.1007/978-981-15-8366-7_10 · Cited by 5

A heterozygous mutation in UBE2H in a patient with developmental delay leads to an aberrant brain development in zebrafish

Shin, U., Choi, Y., Ko, H. S., Myung, K., Lee, S., Cheon, C. K., & Lee, Y. (2023) · Human Genomics · doi:10.1186/s40246-023-00491-7 · Cited by 5

Binding kinetics of mutant p53R175H with wild type p53 and p63: A Surface Plasmon Resonance and Atomic Force Spectroscopy study

Moscetti, I., Bizzarri, A. R., & Cannistraro, S. (2017) · Biophysical Chemistry · doi:10.1016/j.bpc.2017.07.002 · Cited by 5

Cryptochromes and UBP12/13 deubiquitinases antagonistically regulate DNA damage response in ArabidopsisPreprint

Hu, Y., Rosado, D., Norén, L., Micko, J., & Pedmale, U. V. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.15.524001 · Cited by 5

Citrullination negatively regulates the functions of the p53 protein and opposes its ubiquitination and degradation

Yang, Y., Lee, C., Liu, G., Hsieh, J., Lin, Y.-C., Wang, L., Chan, K.-H., Yen, W.-S., Chen, Y.-C., Lin, C., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2423526122 · Cited by 4

Inhibition of the ubiquitin-proteasome system by an NQO1-activatable compound

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Peptide and protein chemistry approaches to study the tumor suppressor protein p53

Chatterjee, C., & Singh, S. K. (2022) · Organic & Biomolecular Chemistry · doi:10.1039/d2ob00902a · Cited by 4

Cancer-derived mutation in the OGA stalk domain promotes cell malignancy through dysregulating PDLIM7 and p53Preprint

Hu, C., Wang, A., Fan, D., Worth, M., Chen, Z., Huang, J., Xie, J., Macdonald, J., Li, L., & Jiang, J. (2023) · Research Square · doi:10.21203/rs.3.rs-2709128/v1 · Cited by 4

A short SUMOylation tag modulates transcription factor activity

Bouchard, A. Y., Vivet, A. J. I., Cabana, V. C., Li, C., Thibault, P., Lussier, M. P., Mader, S., & Cappadocia, L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110807 · Cited by 3

Role of ubiquitin-specific proteases in programmed cell death of breast cancer cells

Yan, W., Xiang, S., Feng, J., & Zu, X. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101341 · Cited by 4

Current Perspectives in Human Papilloma Virus: Where We are and What We Need?

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The crosstalk between ubiquitin-conjugating enzyme E2Q1 and p53 in colorectal cancer: An in vitro analysis

Rasouli, M., Khakshournia, S., Vakili, O., Dastghaib, S., Seghatoleslam, A., & Shafiee, S. M. (2023) · Medical Oncology · doi:10.1007/s12032-023-02039-0 · Cited by 3

CMTM3 Suppresses Proliferation and Osteogenic Transdifferentiation of C2C12 Myoblasts through p53 Upregulation

Shen, E., Piao, M., Li, Y., Wu, Y., Li, S., Lee, S. H., Jin, L., & Lee, K. Y. (2024) · Cells · doi:10.3390/cells13161352 · Cited by 3

Cytotoxic activity of the leaf extract of Gardenia sokotensis (Hutch) against human colon cancer cells.

Fornari, E., Nadembega, P., Quassinti, L., Bramucci, M., Khalife, K. H., Poli, F., Muhtasib, H.-G., & Lupidi, G. (2014) · Unicam Scientific Publications (University of Camerino) · Cited by 2

Ubiquitin Signaling in Ovarian Cancer: From Potential to Challenges

Mitra, S. (2018) · InTech eBooks · doi:10.5772/intechopen.75485 · Cited by 2

AML-Related NPM Mutations Drive p53 Delocalization into the Cytoplasm with Possible Impact on p53-Dependent Stress Response

Holoubek, A., Strachotová, D., Otevřelová, P., Röselová, P., Heřman, P., & Brodská, B. (2021) · Cancers · doi:10.3390/cancers13133266 · Cited by 2

Vanished MDM2 amplification in multiple recurrences of an irradiated poorly differentiated sarcoma with amplified TRIO::TERT fusion gene

Goffinet, S., Mauro, I. D., Doyen, J., Boyer, J., Birtwisle‐Peyrottes, I., Keslair, F., Pédeutour, F., & Dadone‐Montaudié, B. (2023) · Genes Chromosomes and Cancer · doi:10.1002/gcc.23137 · Cited by 2

Quantitative Proteomics Combined with Two Genetic Strategies for Screening Substrates of Ubiquitin Ligase Hrt3

Lan, Q., Wang, Y., Sun, Z., Li, Y., Zhang, C., Chang, L., Gao, Y., Wu, J., Wang, F., & Xu, P. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00673 · Cited by 2

High-Throughput siRNA Screening Applied to the Ubiquitin–Proteasome System

Poulsen, E. G., Nielsen, S. V., Pietras, E. J., Johansen, J. V., Steinhauer, C., & Hartmann‐Petersen, R. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_28 · Cited by 2

Space Radiation

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Nanomaterials exert biological effects by influencing the ubiquitin-proteasome system

Ai, Z., Li, D., Lan, S., & Zhang, C. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116974 · Cited by 1

Analysis of the Interaction of UBE2Q1 with B4GALT1 and P53: Experimental and Molecular Modeling Study

Ghasemi, H., Seghatoleslam, A., Kar, M. A. F., Mahbudi, L., Gharesi‐Fard, B., & Jamshidi, M. (2023) · Protein and Peptide Letters · doi:10.2174/0929866530666230517121827 · Cited by 1

The Role of Pirh2 E3 Ligases in Ubiquitination and p73 Regulation

Abou Zeinab, R. M. (2015) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3610vx4f · Cited by 1

Post-translational Modifications of the p53 Protein and the Impact in Alzheimer’s Disease: A Review of the LiteraturePreprint

Clark, J., Piccirella, S., Kayed, R., Abate, G., Uberti, D. L., & Kinnon, P. (2021) · Preprints.org · doi:10.20944/preprints202109.0359.v1 · Cited by 1

The role of TRIM39 in cell cycle and apoptosis

Huang, N.-J. (2013) · DukeSpace (Duke University)

The role of PATZ1 transcription factor in the DNA damage response

Deniz, E. (2014) · Sabanci University

Redox regulation of the tumor suppressor p53

Shi, T. (2021) · Utrecht University Repository (Utrecht University) · doi:10.33540/966

Structural-Functional Diversity of p53 Proteoforms

Naryzhny, S., & Legina, O. (2019) · Biochemistry (Moscow), Supplement Series B: Biomedical Chemistry · doi:10.1134/s199075081904005x · Cited by 2

Malfunction of Signaling Pathways and Tumorigenesis: Oncogenes and Tumor Suppressor Genes

Krauss, G. (2014) · doi:10.1002/9783527667475.ch16

Application of nuclear magnetic resonance spectroscopy for the detection of metabolic changes in blood cells with defective DNA repair

Vanderstichelen, G. (2022) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.68013

Non-canonical functions of the MDM2 oncoprotein

Manzini, V. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9537

Temporal Coordination of the Transcription Factor Response to H 2 O 2 stressPreprint

Jose, E., March-Steinman, W., Wilson, B. A., Shanks, L., & Paek, A. L. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.07.531593

ZNF500 suppresses the proliferation of breast cancer cells and sensitizes them to chemotherapy by stabilizing p53 in a manner that is competitive to MDM2Preprint

Ma, X., Fan, M., Yang, K., Wang, Y., Hu, R., Guan, M., Hou, Y., Ying, J., Deng, N., Li, Q., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2694228/v1

Differential genomic effects of four nano-sized and one micro-sized CeO2 particles on HepG2 cells

Thai, S., Jones, C. P., Robinette, B. L., Ren, H., Vallanat, B., Fisher, A., & Kitchin, K. T. (2023) · Materials Express · doi:10.1166/mex.2023.2527

The Effect of siRNA Transfection on the ARID3A and ERIC3A Gene Expression in Various Cell Lines Invitro

Yassin, A. R. (2024) · Kufa Medical Journal · doi:10.36330/kmj.v20i2.17142

TF-chRDP: a method for simultaneously capturing transcription factor binding chromatin-associated RNA, DNA and protein

Ning, D., Deng, Y., Gao, T., Yang, Y., Chen, G., Tian, S. Z., & Zheng, M. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1561540

The Coordination of Pathways in Metazoans: An Integrated Framework

Tang, S. (2025) · Biological Theory · doi:10.1007/s13752-025-00498-4

Additional file 1 of A heterozygous mutation in UBE2H in a patient with developmental delay leads to an aberrant brain development in zebrafish

Shin, U., Choi, Y., Ko, H. S., Myung, K., Lee, S., Cheon, C. K., & Lee, Y. (2023) · Figshare · doi:10.6084/m9.figshare.22978150

A crucial role for PIH1D1 in modulating p53 stability via the R2TP complexPreprint

Singh, D. K., Mir, Q. A., & Mir, R. A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.07.704515

The role of adenoviral capsid protein VI in cell cycle modulation

Vaillant, R. (2014) · theses.fr (ABES) · doi:10.70675/9c98c98dz044bz49ccz8fbbzd1aaa3b8327a

Implication de la voie p53 dans les syndromes d'insuffisance médullaire

Toufektchan, E. (2018) · theses.fr (ABES) · doi:10.70675/58dfec7cz94b0z449fz96a6z9051bf80c551

Determinants of C16-Ceramide Binding to p53

Childress, M. S., Jeffries, K. A., Krupenko, S. A., & Krupenko, N. I. (2026) · Biomolecules · doi:10.3390/biom16091343

BindingDB Entry 50010808: Medicinal Chemistry of Inhibiting RING-Type E3 Ubiquitin Ligases.

BindingDB (2021) · UC San Diego · doi:10.7270/q2qn6bbk

Ubiquitylation - Dependent Signaling in Heart Disease

Willis, M. S., Portbury, A. L., Ronnebaum, S. M., Zungu, M., Townley-Tilson, W. H. D., & Patterson, C. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-891-7_8

Dissecting Roles of Ubiquitination in the p53 Pathway

Shan, J., Brooks, C. L., Kon, N., Li, M., & Gu, W. J. (2008) · Ernst Schering Research Foundation workshop/Ernst Schering Foundation Symposium proceedings · doi:10.1007/2789_2008_105 · Cited by 15

Ubiquitin Family Members in the Regulation of the Tumor Suppressor p53

Xirodimas, D. P., & Scheffner, M. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4419-6676-6_10 · Cited by 5

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

Dynamics in the p53-Mdm2 Ubiquitination Pathway

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Limiting the power of p53 through the ubiquitin proteasome pathwayPreprint

Pant, V., & Lozano, G. (2014) · Genes & Development · doi:10.1101/gad.247452.114 · Cited by 170