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Ubc9 acetylation modulates distinct SUMO target modification and hypoxia response

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The SUMO system: a master organizer of nuclear protein assemblies

Raman, N., Nayak, A., & Muller, S. (2013) · Chromosoma · doi:10.1007/s00412-013-0429-6 · Cited by 77 · see citing works

Post-translational Modification of Pregnane X Receptor

Staudinger, J., Xu, C.-S., Biswas, A., & Mani, S. (2011) · Pharmacological Research · doi:10.1016/j.phrs.2011.02.011 · Cited by 91 · see citing works

Control of SUMO and Ubiquitin by ROS: Signaling and disease implications

Stankovic‐Valentin, N., & Melchior, F. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.07.002 · Cited by 76 · see citing works

Sumoylation and Regulation of Cardiac Gene Expression

Wang, J., & Schwartz, R. J. (2010) · Circulation Research · doi:10.1161/circresaha.110.220491 · Cited by 76 · see citing works

SUMO and Transcriptional Regulation: The Lessons of Large-Scale Proteomic, Modifomic and Genomic Studies

Boulanger, M., Chakraborty, M., Tempé, D., Piechaczyk, M., & Bossis, G. (2021) · Molecules · doi:10.3390/molecules26040828 · Cited by 71 · see citing works

SUMO, a small, but powerful, regulator of double-strand break repair

Garvin, A. J., & Morris, J. R. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0281 · Cited by 73 · see citing works

Chromatin modification by SUMO-1 stimulates the promoters of translation machinery genes

Liu, H.-W., Zhang, J., Heine, G. F., Arora, M., Özer, H. G., Onti-Srinivasan, R., Huang, K., & Parvin, J. D. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks819 · Cited by 71 · see citing works

Regulation of the p53 pathway by ubiquitin and related proteins

Hock, A., & Vousden, K. H. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.06.011 · Cited by 69 · see citing works

Regulation of Epithelial–Mesenchymal Transition through SUMOylation of Transcription Factors

Bogachek, M. V., Andrade, J. P. D., & Weigel, R. J. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-2824 · Cited by 68 · see citing works

Deciphering the acetylation code of p53 in transcription regulation and tumor suppression

Xia, Z., Kon, N., Gu, A. P., Tavana, O., & Gu, W. (2022) · Oncogene · doi:10.1038/s41388-022-02331-9 · Cited by 60 · see citing works

MDM2 promotes SUMO-2/3 modification of p53 to modulate transcriptional activity

Stindt, M., Carter, S. A., Vigneron, A. M., Ryan, K. M., & Vousden, K. H. (2011) · Cell Cycle · doi:10.4161/cc.10.18.17436 · Cited by 60 · see citing works

Identification of TRIML2, a Novel p53 Target, that Enhances p53 SUMOylation and Regulates the Transactivation of Proapoptotic Genes

Kung, C.-P., Khaku, S., Jennis, M., Zhou, Y., & Murphy, M. E. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0385 · Cited by 57 · see citing works

PIASy-mediated Tip60 sumoylation regulates p53-induced autophagy

Naidu, S. R., Lakhter, A. J., & Androphy, E. J. (2012) · Cell Cycle · doi:10.4161/cc.21091 · Cited by 56 · see citing works

Sumoylation in gene regulation, human disease, and therapeutic action

Yang, X., & Chiang, C. (2013) · F1000Prime Reports · doi:10.12703/p5-45 · Cited by 54 · see citing works

Deciphering the PTM codes of the tumor suppressor p53

Wen, J., & Wang, D. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab047 · Cited by 52 · see citing works

Critical role of RanBP2-mediated SUMOylation of Small Heterodimer Partner in maintaining bile acid homeostasis

Kim, D.-H., Kwon, S., Byun, S., Xiao, Z., Park, S. S., Wu, S.-Y., Chiang, C., KEMPER, B. W., & Kemper, J. K. (2016) · Nature Communications · doi:10.1038/ncomms12179 · Cited by 51 · see citing works

Ubiquitin-like modifications in the DNA damage response

Wang, Z., Zhu, W., & Xu, X. (2017) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2017.07.001 · Cited by 50 · see citing works

Small ubiquitin-related modifier paralogs are indispensable but functionally redundant during early development of zebrafish

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Regulation of p53 stability as a therapeutic strategy for cancer

Xu, Z., Wu, W., Yan, H., Hu, Y., He, Q., & Luo, P. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114407 · Cited by 50 · see citing works

PML, SUMOylation, and Senescence

Ivanschitz, L., de Thé, H., & Bras, M. L. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00171 · Cited by 45 · see citing works

The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G1arrest

Bennett, R. L., Pan, Y., Christian, J., Hui, T., & May, W. S. (2012) · Cell Cycle · doi:10.4161/cc.11.2.18999 · Cited by 45 · see citing works

Proteome-wide Identification of Ubiquitylation Sites by Conjugation of Engineered Lysine-less Ubiquitin

Oshikawa, K., Matsumoto, M., Oyamada, K., & Nakayama, K. I. (2011) · Journal of Proteome Research · doi:10.1021/pr200668y · Cited by 44 · see citing works

The regulation of radiosensitivity by p53 and its acetylation

Zhang, J., Shen, L., & Sun, L. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.04.015 · Cited by 45 · see citing works

p53 sumoylation: Mechanistic insights from reconstitution studies

Wu, S.-Y., & Cheng, C.-M. (2009) · Epigenetics · doi:10.4161/epi.4.7.10030 · Cited by 42 · see citing works

Binding Site Specificity and Factor Redundancy in Activator Protein-1-driven Human Papillomavirus Chromatin-dependent Transcription

Wang, W., Wu, S.-Y., Lee, A.-Y., & Chiang, C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.290874 · Cited by 41 · see citing works

In-vitro acetylation of SARS-CoV and SARS-CoV-2 nucleocapsid proteins by human PCAF and GCN5

Hatakeyama, D., Masuda, T., Miki, R., Ohtsuki, S., & Kuzuhara, T. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.03.173 · Cited by 38 · see citing works

Substrate and Functional Diversity of Protein Lysine Post-translational Modifications

Hao, B., Chen, K., Zhai, L., Liu, M., Liu, B., & Tan, M. (2024) · Genomics Proteomics & Bioinformatics · doi:10.1093/gpbjnl/qzae019 · Cited by 39 · see citing works

Sumoylation-deficient Prdx6 gains protective function by amplifying enzymatic activity and stability and escapes oxidative stress-induced aberrant Sumoylation

Chhunchha, B., Kubo, E., Fatma, N., & Singh, D. P. (2017) · Cell Death and Disease · doi:10.1038/cddis.2016.424 · Cited by 38 · see citing works

Olig2 SUMOylation protects against genotoxic damage response by antagonizing p53 gene targeting

Liu, H., Weng, W., Guo, R., Zhou, J., Xue, J., Zhong, S., Cheng, J., Zhu, M. X., Pan, S.-J., & Li, Y. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0569-1 · Cited by 37 · see citing works

The Nucleolar Protein Myb-binding Protein 1A (MYBBP1A) Enhances p53 Tetramerization and Acetylation in Response to Nucleolar Disruption

Ono, W., Hayashi, Y., Yokoyama, W., Kuroda, T., Kishimoto, H., Ito, I., Kimura, K., Akaogi, K., Waku, T., & Yanagisawa, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.474049 · Cited by 37 · see citing works

MEL-18 loss mediates estrogen receptor–α downregulation and hormone independence

Lee, J., Won, H., Park, J., Kim, H., Choi, H., Shin, D., Kang, J., Woo, J. K., Oh, S.-H., Son, T., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73743 · Cited by 36 · see citing works

SUMO1-activating enzyme subunit 1 is essential for the survival of hematopoietic stem/progenitor cells in zebrafish

Li, X., Lan, Y., Xu, J., Zhang, W., & Wen, Z. (2012) · Development · doi:10.1242/dev.081869 · Cited by 34 · see citing works

Crosstalk between SUMOylation and other post-translational modifications in breast cancer

Wei, B., Yang, F., Yu, L., & Qiu, C. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00624-3 · Cited by 32 · see citing works

Heterochromatin protects retinal pigment epithelium cells from oxidative damage by silencing p53 target genes

Gong, L., Liu, F., Xiong, Z., Qi, R., Luo, Z., Gong, X., Nie, Q., Sun, Q., Liu, Y.-F., Qing, W., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715237115 · Cited by 32 · see citing works

Modifications of p53 and the DNA Damage Response in Cells Expressing Mutant Form of the Protein Huntingtin

Illuzzi, J. L., Vickers, C. A., & Kmiec, E. B. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9516-4 · Cited by 32 · see citing works

Dynamic modification of the ETS transcription factor PEA3 by sumoylation and p300-mediated acetylation

Guo, B., Panagiotaki, N., Warwood, S., & Sharrocks, A. D. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr267 · Cited by 29 · see citing works

Sumoylation-deficient Prdx6 repairs aberrant Sumoylation-mediated Sp1 dysregulation-dependent Prdx6 repression and cell injury in aging and oxidative stress

Chhunchha, B., Kubo, E., Singh, P., & Singh, D. P. (2018) · Aging · doi:10.18632/aging.101547 · Cited by 28 · see citing works

Heat shock transcription factor 1 is SUMOylated in the activated trimeric state

Kmiecik, S. W., Drzewicka, K., Melchior, F., & Mayer, M. P. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100324 · Cited by 28 · see citing works

The Function of SUMOylation and Its Role in the Development of Cancer Cells under Stress Conditions: A Systematic Review

Zhao, Q., Ma, Y., Li, Z., Zhang, K., Zheng, M., & Zhang, S. (2020) · Stem Cells International · doi:10.1155/2020/8835714 · Cited by 27 · see citing works

Regulating the p53 Tumor Suppressor Network at PML Biomolecular Condensates

Liebl, M. C., & Hofmann, T. G. (2022) · Cancers · doi:10.3390/cancers14194549 · Cited by 26 · see citing works

Class I HDAC inhibition stimulates cardiac protein SUMOylation through a post-translational mechanism

Blakeslee, W. W., Wysoczynski, C. L., Fritz, K. S., Nyborg, J. K., Churchill, M. E. A., & McKinsey, T. A. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.09.005 · Cited by 25 · see citing works

PML Degradation: Multiple Ways to Eliminate PML

Rabellino, A., & Scaglioni, P. P. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00060 · Cited by 25 · see citing works

TATA-binding Protein (TBP)-like Protein Is Required for p53-dependent Transcriptional Activation of Upstream Promoter of p21 Gene

Suzuki, H., Ito, R., Ikeda, K., & Tamura, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.369629 · Cited by 24 · see citing works

SUMO modification regulates the transcriptional activity of MAML1

Lindberg, M. J., Popko-Ścibor, A. E., Hansson, M. L., & Wallberg, A. E. (2010) · The FASEB Journal · doi:10.1096/fj.09-149401 · Cited by 24 · see citing works

The SUMO‐specific protease SENP1 deSUMOylates p53 and regulates its activity

Chauhan, K. M., Chen, Y., Chen, Y., Liu, A. T., Sun, X., & Dai, M. (2020) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29838 · Cited by 23 · see citing works

SUMO-Modification of the La Protein Facilitates Binding to mRNA In Vitro and in Cells

Kota, V., Sommer, G., Durette, C., Thibault, P., van Niekerk, E. A., Twiss, J. L., & Heise, T. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156365 · Cited by 21 · see citing works

Functional mimicry of the acetylated C‐terminal tail of p53 by a SUMO‐1 acetylated domain, SAD

Cheema, A. K., Knights, C. D., Rao, M., Catania, J., Perez, R. E., Simons, B. L., Dakshanamurthy, S., Kolukula, V. K., Tilli, M. T., Furth, P. A., et al. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22224 · Cited by 20 · see citing works

Sumoylation in Cellular Senescence and Aging

Gong, L., Sun, Q., & Li, D. (2017) · Current Molecular Medicine · doi:10.2174/1566524016666161223104915 · Cited by 20 · see citing works

Expression and Prognosis Analysis of SUMOylation Regulators in Oral Squamous Cell Carcinoma Based on High-Throughput Sequencing

Meng, Y., & Li, X. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.671392 · Cited by 20 · see citing works

From regulation to deregulation of p53 in hematologic malignancies: implications for diagnosis, prognosis and therapy

Ahmadi, S. E., Rahimian, E., Rahimi, S., Zarandi, B., Bahraini, M., Soleymani, M., Safdari, S. M., Shabannezhad, A., Jaafari, N., & Safa, M. (2024) · Biomarker Research · doi:10.1186/s40364-024-00676-9 · Cited by 22 · see citing works

Functions of nuclear receptors SUMOylation

Liu, W., Min De, Z. E. N. G., & Fu, N. (2021) · Clinica Chimica Acta · doi:10.1016/j.cca.2021.01.007 · Cited by 19 · see citing works

Arabidopsis thaliana proliferating cell nuclear antigen has several potential sumoylation sites

Strzałka, W., Labecki, P., Bartnicki, F., Aggarwal, C., Rąpała‐Kozik, M., Tani, C., Tanaka, K., & Gabryś, H. (2012) · Journal of Experimental Botany · doi:10.1093/jxb/ers002 · Cited by 18 · see citing works

SUMOylation regulates tumorigenesis and progression: Molecular mechanisms and therapeutic applications

Wu, Y., Chen, Z., Hu, Y., Zengin, G., Zhang, Q., Li, M., & Sun, W. (2026) · Interdisciplinary medicine · doi:10.1002/inmd.70120 · Cited by 17 · see citing works

p53 SUMOylation Mediates AOPP-Induced Endothelial Senescence and Apoptosis Evasion

Chen, Y., Liu, Z., Chen, H., Huang, X., Huang, X., Yang, L., Liang, Q. D., Wei, J., Zhang, Q., Guo, X., et al. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.795747 · Cited by 16 · see citing works

Utilizing Optimized Tools to Investigate PTM Crosstalk: Identifying Potential PTM Crosstalk of Acetylated Mitochondrial Proteins

Horita, H. N., Law, A., & Middleton, K. M. (2018) · Proteomes · doi:10.3390/proteomes6020024 · Cited by 17 · see citing works

Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans

Surana, P., Gowda, C. M., Tripathi, V., Broday, L., & Das, R. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186622 · Cited by 16 · see citing works

Construction of a SUMOylation regulator‐based prognostic model in low‐grade glioma

Li, X., & Meng, Y. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16553 · Cited by 15 · see citing works

The SUMO E3 Ligase Siz2 Exerts a Locus-Dependent Effect on Gene Silencing in Saccharomyces cerevisiae

Pasupala, N., Easwaran, S., Hannan, A., Shore, D., & Mishra, K. (2012) · Eukaryotic Cell · doi:10.1128/ec.05243-11 · Cited by 15 · see citing works

Sumoylation of the P Protein at K254 Plays an Important Role in Growth of Parainfluenza Virus 5

Sun, D., Xu, P., & He, B. (2011) · Journal of Virology · doi:10.1128/jvi.00389-11 · Cited by 15 · see citing works

Lens epithelium‐derived growth factor deSumoylation by Sumo‐specific protease‐1 regulates its transcriptional activation of small heat shock protein and the cellular response

Ishihara, K., Fatma, N., Bhargavan, B., Chhunchha, B., Kubo, E., Dey, S., Takamura, Y., Kumar, A., & Singh, D. P. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08686.x · Cited by 14 · see citing works

MDM2 is a Potential Target Gene of Glycyrrhizic Acid for Circumventing Breast Cancer Resistance to Tamoxifen: Integrative Bioinformatics Analysis

Azzahra, S., Hanif, N., & Hermawan, A. (2022) · Asian Pacific Journal of Cancer Prevention · doi:10.31557/apjcp.2022.23.7.2341 · Cited by 13 · see citing works

TRIM28 regulates transcriptional activity of methyl-DNA binding protein Kaiso by SUMOylation

Lobanova, Y., Filonova, G. E., Kaplun, D., Zhigalova, N., Prokhortchouk, E., & Zhenilo, S. V. (2022) · Biochimie · doi:10.1016/j.biochi.2022.10.006 · Cited by 13 · see citing works

A Flp-SUMO hybrid recombinase reveals multi-layered copy number control of a selfish DNA element through post-translational modification

Ma, C.-H., Su, B.-Y., Maciaszek, A. D., Fan, H., Guga, P., & Jayaram, M. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008193 · Cited by 13 · see citing works

Dietary flavonoid fisetin binds human SUMO1 and blocks sumoylation of p53

Velazhahan, V., Glaza, P., Herrera, A. I., Prakash, O., Žółkiewski, M., Geisbrecht, B. V., & Schrick, K. (2020) · PLoS ONE · doi:10.1371/journal.pone.0234468 · Cited by 12 · see citing works

Novel insights into the impact of the SUMOylation pathway in hematological malignancies (Review)

Wang, L., Qian, J., Yang, Y., & Gu, C. (2021) · International Journal of Oncology · doi:10.3892/ijo.2021.5253 · Cited by 11 · see citing works

HOPS and p53: thick as thieves in life and death

Fazia, M. A. D., Castelli, M., Piobbico, D., Pieroni, S., & Servillo, G. (2020) · Cell Cycle · doi:10.1080/15384101.2020.1838772 · Cited by 9 · see citing works

DNMT3b SUMOylation Mediated MMP-2 Upregulation Contribute to Paclitaxel Induced Neuropathic Pain

Wang, H., Shen, Y., Li, X., Xia, J., Sun, L. J., Xu, Y., Ma, Y., Li, D., & Xiong, Y.-C. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03260-x · Cited by 9 · see citing works

Protein sumoylation in normal and cancer stem cells

Zhu, Q., Liang, P., Chu, C., Zhang, A., & Zhou, W. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1095142 · Cited by 9 · see citing works

Comparative analysis of protein expression systems and PTM landscape in the study of transcription factor ELK-1

Ducker, C. E., Ratnam, M., Shaw, P. E., & Layfield, R. (2022) · Protein Expression and Purification · doi:10.1016/j.pep.2022.106216 · Cited by 7 · see citing works

Targeting Moonlighting Enzymes in Cancer

Lin, C., Yu, M., Wu, X., Wang, H., Wei, M., & Zhang, L. (2024) · Molecules · doi:10.3390/molecules29071573 · Cited by 7 · see citing works

p53-Aurora A mitotic feedback loop regulates cell cycle progression and genomic stability

Chiang, C. (2012) · Cell Cycle · doi:10.4161/cc.22113 · Cited by 6 · see citing works

The Four Homeostasis Knights: In Balance upon Post-Translational Modifications

Pieroni, S., Castelli, M., Piobbico, D., Ferracchiato, S., Scopetti, D., Di-Iacovo, N., Fazia, M. A. D., & Servillo, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214480 · Cited by 6 · see citing works

In Silico Identification of SOX1 Post-Translational Modifications Highlights a Shared Protein Motif

Ahmad, A., Strohbuecker, S., Scotti, C., Tufarelli, C., & Sottile, V. (2020) · Cells · doi:10.3390/cells9112471 · Cited by 5 · see citing works

The role of SUMOylation in epithelial-mesenchymal transition

Li, S., Yu, X.-M., Liang, L., & Zheng, Y. (2025) · Journal of Molecular Medicine · doi:10.1007/s00109-025-02568-3 · Cited by 4 · see citing works

The effects of SUMO modification of the tumour suppressor p53

Marouco, D. M. (2016) · Figshare

p53 sumoylation: Mechanistic insights from reconstitution studies

Wu, S.-Y., & Cheng, C.-M. (2009) · Epigenetics · doi:10.4161/epi.4.7.10030 · Cited by 42 · see citing works

Functional mimicry of the acetylated C‐terminal tail of p53 by a SUMO‐1 acetylated domain, SAD

Cheema, A. K., Knights, C. D., Rao, M., Catania, J., Perez, R. E., Simons, B. L., Dakshanamurthy, S., Kolukula, V. K., Tilli, M. T., Furth, P. A., et al. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22224 · Cited by 20 · see citing works

Functional analysis and intracellular localization of p53 modified by SUMO-1

Kwek, S. S., Derry, J. J., Tyner, A. L., Shen, Z., & Gudkov, A. V. (2001) · Oncogene · doi:10.1038/sj.onc.1204362 · Cited by 130 · see citing works

SUMO-1 and p53

Melchior, F., & Hengst, L. (2002) · Cell Cycle · doi:10.4161/cc.1.4.131 · Cited by 109 · see citing works