Ginkgolic Acid Inhibits Protein SUMOylation by Blocking Formation of the E1-SUMO Intermediate

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SUMO‐1 modification activates the transcriptional response of p53

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Activation of p53 by conjugation to the ubiquitin‐like protein SUMO‐1

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Inhibitors of Ubiquitin-Activating Enzyme (E1), a New Class of Potential Cancer Therapeutics

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Regulation of SUMOylation by Reversible Oxidation of SUMO Conjugating Enzymes

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The emerging field of dynamic lysine methylation of non-histone proteins

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The SUMO Pathway in Hematomalignancies and Their Response to Therapies

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A role for SUMOylation in the Formation and Cellular Localization of TDP-43 Aggregates in Amyotrophic Lateral Sclerosis

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Alpha synuclein post translational modifications: potential targets for Parkinson’s disease therapy?

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SUMOylation occurs in acute kidney injury and plays a cytoprotective role

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Current Status of SUMOylation Inhibitors

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Protein Kinase C-Mediated Phosphorylation of BCL11B at Serine 2 Negatively Regulates Its Interaction with NuRD Complexes during CD4+ T-Cell Activation

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Pharmacological inhibition of SUMO-1 with ginkgolic acid alleviates cardiac fibrosis induced by myocardial infarction in mice

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Post-translational modifications of the Fragile X Mental Retardation Protein in neuronal function and dysfunction

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Endogenous TRIM5α Function Is Regulated by SUMOylation and Nuclear Sequestration for Efficient Innate Sensing in Dendritic Cells

Portilho, D. M., Fernandez, J., Ringeard, M., Machado, A. K., Boulay, A., Mayer, M., Müller-Trutwin, M. C., Beignon, A., Kirchhoff, F., Nisole, S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.12.039 · Cited by 44

Identification of new SUMO activating enzyme 1 inhibitors using virtual screening and scaffold hopping

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SUMOylation of SAMHD1 at Lysine 595 is required for HIV-1 restriction in non-cycling cells

Martinat, C., Cormier, A., Tobaly-Tapiero, J., Palmic, N., Casartelli, N., Mahboubi, B., Coggins, S. A., Buchrieser, J., Persaud, M., Diaz‐Griffero, F., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24802-5 · Cited by 44

Non-specific SIRT inhibition as a mechanism for the cytotoxicity of ginkgolic acids and urushiols

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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

Broad Antiviral Activity of Ginkgolic Acid against Chikungunya, Mayaro, Una, and Zika Viruses

Campos, D., Navarro, S., Llamas-González, Y. Y., Sugasti-Salazar, M., & González, J. (2020) · Viruses · doi:10.3390/v12040449 · Cited by 38

An optimized ultrasound-assisted extraction and simultaneous quantification of 26 characteristic components with four structure types in functional foods from ginkgo seeds

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SUMOylation of the transcription factor ZFHX3 at Lys-2806 requires SAE1, UBC9, and PIAS2 and enhances its stability and function in cell proliferation

Wu, R., Fang, J., Liu, M., Jun, A., Liu, J., Chen, W., Li, J., Ma, G., Zhang, Z., Zhang, B., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012338 · Cited by 36

The SUMO pathway in pancreatic cancer: insights and inhibition

Schneeweis, C., Hassan, Z., Schick, M., Keller, U. B., & Schneider, G. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-01119-6 · Cited by 36

Deletion of SUMO1 attenuates behavioral and anatomical deficits by regulating autophagic activities in Huntington disease

Ramírez-Jarquín, U. N., Sharma, M., Zhou, W., Shahani, N., & Subramaniam, S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2107187119 · Cited by 36

Hepatocyte Growth Factor Improves the Therapeutic Efficacy of Human Bone Marrow Mesenchymal Stem Cells via RAD51

Lee, E. J., Hwang, I., Lee, J. Y., Park, J. N., Kim, K. C., Kim, G.-H., Kang, C.-M., Kim, I., Lee, S.-Y., & Kim, H.-S. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2017.12.015 · Cited by 34

Ginkgolic Acid is a Multi-Target Inhibitor of Key Enzymes in Pro-Inflammatory Lipid Mediator Biosynthesis

Gerstmeier, J., Seegers, J., Witt, F., Waltenberger, B., Temml, V., Rollinger, J. M., Stuppner, H., Koeberle, A., Schuster, D., & Werz, O. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00797 · Cited by 35

Targeting SUMO-1ylation Contrasts Synaptic Dysfunction in a Mouse Model of Alzheimer’s Disease

Marcelli, S., Ficulle, E., Iannuzzi, F., Kövari, E., Nisticò, R., & Feligioni, M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0176-9 · Cited by 38

Activating transcription factor 3 SUMOylation is involved in angiotensin II-induced endothelial cell inflammation and dysfunction

Zhang, Z.-B., Ruan, C., Chen, D.-R., Zhang, K., Chen, Y., & Gao, P. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.02.001 · Cited by 34

Inhibition of HSF2 SUMOylation via MEL18 upregulates IGF-IIR and leads to hypertension-induced cardiac hypertrophy

Huang, C., Kuo, C., Pai, P., Ho, T.-J., Lin, Y., Chen, R., Tsai, F. C., Padma, V. V., Kuo, W., & Huang, C. (2017) · International Journal of Cardiology · doi:10.1016/j.ijcard.2017.10.102 · Cited by 34

SUMOylation determines turnover and localization of nephrin at the plasma membrane

Tossidou, I., Himmelseher, E., Teng, B., Haller, H. G., & Schiffer, M. (2014) · Kidney International · doi:10.1038/ki.2014.198 · Cited by 34

Ginkgolic Acid Protects against Aβ-Induced Synaptic Dysfunction in the Hippocampus

Mango, D., Weisz, F., & Nisticò, R. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00401 · Cited by 33

Temporal and SUMO-specific SUMOylation contribute to the dynamics of Polo-like kinase 1 (PLK1) and spindle integrity during mouse oocyte meiosis

Feitosa, W. B., Hwang, K., & Morris, P. L. (2017) · Developmental Biology · doi:10.1016/j.ydbio.2017.12.011 · Cited by 33

Progressing neurobiological strategies against proteostasis failure: Challenges in neurodegeneration

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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 36

SUMOylation, aging and autophagy in neurodegeneration

Vijayakumaran, S., & Pountney, D. L. (2018) · NeuroToxicology · doi:10.1016/j.neuro.2018.02.015 · Cited by 32

Exploring a New Frontier in Cancer Treatment: Targeting the Ubiquitin and Ubiquitin-like Activating Enzymes

da Silva, S. R., Paiva, S.-L., Lukkarila, J. L., & Gunning, P. T. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301420b · Cited by 33

The SUMO System and TGFβ Signaling Interplay in Regulation of Epithelial-Mesenchymal Transition: Implications for Cancer Progression

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Post-translational Mechanisms Regulating NK Cell Activating Receptors and Their Ligands in Cancer: Potential Targets for Therapeutic Intervention

Molfetta, R., Zingoni, A., Santoni, A., & Paolini, R. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02557 · Cited by 26

Evidence that Ginkgo Biloba could use in the influenza and coronavirus COVID-19 infections

Ibrahim, M. A., Ramadan, H. H., & Mohammed, R. N. (2021) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2020-0310 · Cited by 33

SUMOylation and DeSUMOylation: Prospective therapeutic targets in cancer

Wu, W., & Huang, C. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122085 · Cited by 30

The Key Regulator for Language and Speech Development, FOXP2, is a Novel Substrate for SUMOylation

Meredith, L. J., Wang, C., Nascimento, L. A., Liu, R., Wang, L., & Yang, W. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25288 · Cited by 30

Ginkgolic Acids Impair Mitochondrial Function by Decreasing Mitochondrial Biogenesis and Promoting FUNDC1-Dependent Mitophagy

Wang, W., Wang, M., Ruan, Y., Tan, J., Wang, H., Yang, T., Li, J., & Zhou, Q. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b04178 · Cited by 29

Using glycyrrhizic acid to target sumoylation processes during Epstein-Barr virus latency

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ARF Regulates the Stability of p16 Protein Via REGγ-Dependent Proteasome Degradation

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1 H NMR-based metabolomics study of liver damage induced by ginkgolic acid (15:1) in mice

Jiang, L., Si, Z.-H., Li, M., Zhao, H., Fu, Y.-H., Xing, Y.-X., Wei, H., Ruan, L., Li, P.-M., & Wang, J. (2016) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2016.12.033 · Cited by 28

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

Ginkgolic Acid Inhibits Herpes Simplex Virus Type 1 Skin Infection and Prevents Zosteriform Spread in Mice

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Ginkgoic acid impedes gastric cancer cell proliferation, migration and EMT through inhibiting the SUMOylation of IGF-1R

Liu, D., Li, Z., Yang, Z., Ma, J., & Mai, S. (2021) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2021.109394 · Cited by 28

Ferritinophagy and α-Synuclein: Pharmacological Targeting of Autophagy to Restore Iron Regulation in Parkinson’s Disease

Boag, M. K., Roberts, A., Uversky, V. N., Ma, L., Richardson, D. R., & Pountney, D. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042378 · Cited by 31

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 28

SUMOylation in Glioblastoma: A Novel Therapeutic Target

Fox, B. M., Janssen, A., Estévez-Ordoñez, D., Gessler, F. A., Vicario, N., Chagoya, G., Elsayed, G., Sotoudeh, H., Stetler, W. R., Friedman, G. K., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081853 · Cited by 27

Metabolic profiling of the hepatotoxicity and nephrotoxicity of Ginkgolic acids in rats using ultra-performance liquid chromatography-high-definition mass spectrometry

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The SUMO Conjugation Complex Self-Assembles into Nuclear Bodies Independent of SIZ1 and COP1

Mazur, M. J., Kwaaitaal, M. A. C. J., Arroyo‐Mateos, M., Maio, F., Kini, K. R., Prins, M., & van den Burg, H. A. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.00910 · Cited by 26

SUMOylation mediates CtIP’s functions in DNA end resection and replication fork protection

Locke, A. J., Hossain, L., McCrostie, G., Ronato, D. A., Fitieh, A. M., Rafique, T. A., Mashayekhi, F., Motamedi, M., Masson, J., & Ismail, I. H. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1232 · Cited by 27

Targeting therapy-resistant lung cancer stem cells via disruption of the AKT/TSPYL5/PTEN positive-feedback loop

Kim, I., Lee, J.-H., Kim, S., Heo, C.-K., Kim, R.-K., & Cho, E. (2021) · Communications Biology · doi:10.1038/s42003-021-02303-x · Cited by 27

SUMO-defective c-Maf preferentially transactivates Il21 to exacerbate autoimmune diabetes

Hsu, C.-Y., Yeh, L., Fu, S., Chien, M., Liu, Y.-W., Miaw, S., Chang, D., & Sytwu, H. (2018) · Journal of Clinical Investigation · doi:10.1172/jci98786 · Cited by 26

Paradoxes of Cellular SUMOylation Regulation: A Role of Biomolecular Condensates?

Cheng, X., Yang, W., Lin, W., & Mei, F. C. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000784 · Cited by 25

Heterogeneous Nuclear Ribonucleoprotein A1 Loads Batched Tumor-Promoting MicroRNAs Into Small Extracellular Vesicles With the Assist of Caveolin-1 in A549 Cells

Li, Y., Zhang, J., Li, S., Guo, C., Li, Q., Zhang, X., Li, M., & Mi, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.687912 · Cited by 26

SUMOylation and NEDDylation in Primary and Metastatic Cancers to Bone

Gomarasca, M., Lombardi, G., & Maroni, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.889002 · Cited by 26

SUMO Modification of Hepatitis B Virus Core Mediates Nuclear Entry, Promyelocytic Leukemia Nuclear Body Association, and Efficient Formation of Covalently Closed Circular DNA

Hofmann, S., Plank, V., Groitl, P., Skvorc, N., Hofmann, K., Luther, J., Ko, C., Zimmerman, P., Bruss, V., Stadler, D., et al. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.00446-23 · Cited by 24

The Inhibitory Effects of Anacardic Acid on Hepatitis C Virus Life Cycle

Hundt, J., Li, Z., & Liu, Q. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117514 · Cited by 25

Ginkgolic acid, a sumoylation inhibitor, promotes adipocyte commitment but suppresses adipocyte terminal differentiation of mouse bone marrow stromal cells

Liu, H., Li, J., Lü, D., Li, J., Liu, M., He, Y., Williams, B. O., Li, J., & Yang, T. (2018) · Scientific Reports · doi:10.1038/s41598-018-20244-0 · Cited by 25

Age-related p53 SUMOylation accelerates senescence and tau pathology in Alzheimer’s disease

Wan, L., Yang, F., Yin, A., Luo, Y., Yi, L. I. U., Liu, F., Wang, J., Liu, R., & Wang, X. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01448-0 · Cited by 26

Identification of quinazolinyloxy biaryl urea as a new class of SUMO activating enzyme 1 inhibitors

Kumar, A., Ito, A., Hirohama, M., Yoshida, M., & Zhang, K. Y. J. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.07.022 · Cited by 23

Sumoylation of histone deacetylase 1 regulates MyoD signaling during myogenesis

Joung, H., Kwon, S., Kim, K. H., Lee, Y.-G., Shin, S., Kwon, D., Lee, Y.-U., Kook, T., Choe, N., Kim, J. C., et al. (2018) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.236 · Cited by 24

How Does SUMO Participate in Spindle Organization?

Abrieu, A., & Liakopoulos, D. (2019) · Cells · doi:10.3390/cells8080801 · Cited by 24

An efficient method for the preparative separation and isolation of ginkgolic acids from the sarcotesta of Ginkgo biloba L by pH-zone-refining counter-current chromatography coupled with inner-recycling mode

Wang, D., Zhu, H., Li, M., Song, X., Yan, H., Yu, J., & Wang, X. D. (2018) · Industrial Crops and Products · doi:10.1016/j.indcrop.2018.09.034 · Cited by 23

Targeting SUMOylation dependency in human cancer stem cells through a unique SAE2 motif revealed by chemical genomics

Benoit, Y. D., Mitchell, R. R., Wang, W., Orlando, L., Boyd, A. L., Tanasijevic, B., Aslostovar, L., Shapovalova, Z., Doyle, M., Bergin, C. J., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.014 · Cited by 24

The role of SUMOylation in biomolecular condensate dynamics and protein localization

Gutierrez-Morton, E., & Wang, Y. (2024) · Cell Insight · doi:10.1016/j.cellin.2024.100199 · Cited by 24

The Role of Protein SUMOylation in Human Hepatocellular Carcinoma: A Potential Target of New Drug Discovery and Development

Yuan, H., Lu, Y., Chan, Y.-T., Zhang, C., Wang, N., & Feng, Y. (2021) · Cancers · doi:10.3390/cancers13225700 · Cited by 22

Ubiquitin, SUMO, and Nedd8 as Therapeutic Targets in Cancer

Gâtel, P., Piechaczyk, M., & Bossis, G. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_2 · Cited by 23

Development of a High-Throughput Screen to Detect Inhibitors of TRPS1 Sumoylation

Brandt, M. A., Szewczuk, L. M., Zhang, H., Hong, X., McCormick, P. M., Lewis, T. S., Graham, T. I., Hung, S., Harper-Jones, A. D., Kerrigan, J. J., et al. (2013) · Assay and Drug Development Technologies · doi:10.1089/adt.2012.501 · Cited by 22

Inhibition of p53 deSUMOylation Exacerbates Puromycin Aminonucleoside-Induced Apoptosis in Podocytes

Wang, L., Zhu, J., Fang, M., Zhang, T., Xie, H., Wang, N., Shen, N., Guo, H., Fu, B., & Lin, H. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151121314 · Cited by 22

Macrophilone A: Structure Elucidation, Total Synthesis, and Functional Evaluation of a Biologically Active Iminoquinone from the Marine Hydroid Macrorhynchia philippina

Zlotkowski, K., Hewitt, W. M., Yan, P., Bokesch, H. R., Peach, M. L., Nicklaus, M. C., O’Keefe, B. R., McMahon, J. B., Gustafson, K. R., & Schneekloth, J. S. (2017) · Organic Letters · doi:10.1021/acs.orglett.7b00496 · Cited by 22

Targeting α-synuclein post-translational modifications in Parkinson’s disease

Canever, J. B., Soares, E. S., de Avelar, N. C. P., & Cimarosti, H. (2022) · Behavioural Brain Research · doi:10.1016/j.bbr.2022.114204 · Cited by 22

The SUMOylation and ubiquitination crosstalk in cancer

Li, K., Xia, Y., He, J., Wang, J., Li, J., Ye, M., & Jin, X. (2023) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-023-05310-z · Cited by 20

Protein modification in neurodegenerative diseases

Ramazi, S., Dadzadi, M., Darvazi, M., Seddigh, N., & Allahverdi, A. (2024) · MedComm · doi:10.1002/mco2.674 · Cited by 25

Differential Nanos 2 protein stability results in selective germ cell accumulation in the sea urchin

Oulhen, N., & Wessel, G. M. (2016) · Developmental Biology · doi:10.1016/j.ydbio.2016.07.007 · Cited by 21

An overview of the possible therapeutic role of SUMOylation in the treatment of Alzheimer’s disease

Marcelli, S., Ficulle, E., Piccolo, L., Corbo, M., & Feligioni, M. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.12.023 · Cited by 21

A Unique SUMO-Interacting Motif of Trx2 Is Critical for Its Mitochondrial Presequence Processing and Anti-oxidant Activity

Chen, C.-F., Wang, K., Zhang, H.-F., Zhou, H., Chen, Y.-X., & Min, W. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01089 · Cited by 19

Synthesis and Evaluation of Ginkgolic Acid Derivatives as SUMOylation Inhibitors

Brackett, C. M., García‐Casas, A., Castillo‐Lluva, S., & Blagg, B. S. J. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00353 · Cited by 20

Distinctive tumorigenic significance and innovative oncology targets of SUMOylation

Zhou, H., Deng, N., Li, Y., Hu, X., Xue, Y., Jia, S., Zheng, C., Gao, S., Wu, H., & Li, K. (2024) · Theranostics · doi:10.7150/thno.97162 · Cited by 25

Protective Effect of Ginkgolic Acid in Attenuating LDL Induced Inflammation Human Peripheral Blood Mononuclear Cells via Altering the NF-κB Signaling Pathway

Zhang, J., & Yan, J. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01241 · Cited by 19

SUMO modulation of protein aggregation and degradation

Feligioni, M., Marcelli, S., Knock, E., Nadeem, U., Arancio, O., & Fraser, P. E. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.4.382 · Cited by 19

SUMOylation in atherosclerosis

Liu, Y.-Z., Xiao, X., Hu, C.-T., Dai, Y., Qu, S.-L., Huang, L., & Zhang, C. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.05.033 · Cited by 19

SUMOylation in fungi: A potential target for intervention

Gupta, D., Garapati, H. S., Kakumanu, A. V. S., Shukla, R., & Mishra, K. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.10.037 · Cited by 19

Dynamic regulation of HIF1Α stability by SUMO2/3 and SENP3 in the human placenta

Bhattacharjee, J., Alahari, S., Sallais, J., Tagliaferro, A., Post, M., & Caniggia, I. (2016) · Placenta · doi:10.1016/j.placenta.2016.02.002 · Cited by 18

Inhibition of CDK1 activity by sumoylation

Xiao, Y., Lucas, B., Molcho, E., Schiff, T., & Vigodner, M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.051 · Cited by 18

Differential effects of SUMO1 and SUMO3 on PKR activation and stability

Maarifi, G., Asmi, F. E., Maroui, M. A., Dianoux, L., & Chelbi‐Alix, M. K. (2018) · Scientific Reports · doi:10.1038/s41598-018-19683-6 · Cited by 18

Talin is a substrate for SUMOylation in migrating cancer cells

Huang, Z., Barker, D., Gibbins, J. M., & Dash, P. R. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.07.005 · Cited by 18

Guanosine modulates SUMO2/3-ylation in neurons and astrocytes via adenosine receptors

Zanella, C. A., Tasca, C. I., Henley, J. M., Wilkinson, K. A., & Cimarosti, H. (2020) · Purinergic Signalling · doi:10.1007/s11302-020-09723-0 · Cited by 18

Targeting the SUMO pathway as a novel treatment for anaplastic thyroid cancer

Andrade, J. P. D., Lorenzen, A. W., Wu, V. T., Bogachek, M. V., Park, J. M., Gu, V. W., Sevenich, C. M., Cassady, V. C., Beck, A. C., Kulak, M. V., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.21954 · Cited by 18

Tricyclic antidepressants target FKBP51 SUMOylation to restore glucocorticoid receptor activity

Budziñski, M. L., Sokn, C., Gobbini, R., Ugo, B., Antunica-Noguerol, M., Senin, S., Bajaj, T., Gassen, N. C., Rein, T., Schmidt, M. V., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01491-0 · Cited by 17

Rethinking Parkinson's: The role of proteostasis networks and autophagy in disease progression

Sharma, A., Mannan, A., & Singh, T. G. (2025) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2025.104023 · Cited by 19

Plant-Derived Epi-Nutraceuticals as Potential Broad-Spectrum Anti-Viral Agents

Gabbianelli, R., Shahar, E., de Simone, G., Rucci, C., Bordoni, L., Feliziani, G., Zhao, F., Ferrati, M., Maggi, F., Spinozzi, E., et al. (2023) · Nutrients · doi:10.3390/nu15224719 · Cited by 20

Selective potentiation of alpha 1 glycine receptors by ginkgolic acid

Maleeva, G., Buldakova, S., & Bregestovski, P. D. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00064 · Cited by 17

SUMO‐Mimicking Peptides Inhibiting Protein SUMOylation

Zhao, B., Villhauer, E. B., Bhuripanyo, K., Kiyokawa, H., Schindelin, H., & Yin, J. (2014) · ChemBioChem · doi:10.1002/cbic.201402472 · Cited by 17

SUMOylation regulates germinal vesicle breakdown and the Akt/PKB pathway during mouse oocyte maturation

Feitosa, W. B., & Morris, P. L. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00038.2018 · Cited by 17

Constitutively active androgen receptor supports the metastatic phenotype of endocrine-resistant hormone receptor-positive breast cancer

Bahnassy, S., Thangavel, H., Quttina, M., Khan, A. F., Dhanyalayam, D., Ritho, J., Karami, S., Ren, J. F., & Bawa‐Khalfe, T. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00649-z · Cited by 17

Poly-SUMO-2/3 chain modification of Nuf2 facilitates CENP-E kinetochore localization and chromosome congression during mitosis

Subramonian, D., Chen, T.-A., Paolini, N., & Zhang, X. D. (2021) · Cell Cycle · doi:10.1080/15384101.2021.1907509 · Cited by 17

SUMOylating Two Distinct Sites on the A-type Potassium Channel, Kv4.2, Increases Surface Expression and Decreases Current Amplitude

Welch, M. A., Forster, L. A., Atlas, S. I., & Baro, D. J. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00144 · Cited by 17

Formation of SUMO3-conjugated chains of MAVS induced by poly(dA:dT), a ligand of RIG-I, enhances the aggregation of MAVS that drives the secretion of interferon-β in human keratinocytes

Choi, G. W., Lee, Y. J., Yun, M., Kang, J., & Lee, S. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.11.189 · Cited by 17

Sumoylation as an Emerging Target in Therapeutics against Cancer

Liu, S., Wang, L., Jiang, D., Wei, W., Nasir, M. F., Khan, M. S., Yousafi, Q., Liu, X., Fu, X., Li, X., et al. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200622124134 · Cited by 16

Effects of targeting sumoylation processes during latent and induced Epstein-Barr virus infections using the small molecule inhibitor ML-792

Garcia, P., Harrod, A. E., Jha, S., Jenkins, J., Barnhill, A., Lee, H., Thompson, M., Williams, J. P., Barefield, J., McKinnon, A., et al. (2021) · Antiviral Research · doi:10.1016/j.antiviral.2021.105038 · Cited by 15

The Pharmacology and Toxicology of Ginkgolic Acids: Secondary Metabolites from Ginkgo biloba

Shao, Y., Chen, Y., Zhu, Q., Yi, L., Ma, Y., Zang, X., & Yao, W. (2025) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x25500077 · Cited by 15

Small ubiquitin‐related modifier‐1 modification regulates all‐trans‐retinoic acid‐induced differentiation via stabilization of retinoic acid receptor α

Zhou, Q., Zhang, L., Chen, Z., Zhao, P.-G., Ma, Y., Yang, B., He, Q., & Ying, M. (2014) · FEBS Journal · doi:10.1111/febs.12840 · Cited by 15

Synthesis and Evaluation of Ginkgolic Acid Derivatives as SUMOylation Inhibitors

Brackett, C. M., García‐Casas, A., Castillo‐Lluva, S., & Blagg, B. S. J. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00353 · Cited by 20

Inhibition of protein SUMOylation by natural quinones

Fukuda, I., Hirohama, M., Ito, A., Tariq, M., Igarashi, Y., Saitoh, H., & Yoshida, M. (2016) · The Journal of Antibiotics · doi:10.1038/ja.2016.23 · Cited by 5

Inhibition of protein SUMOylation by davidiin, an ellagitannin from Davidia involucrata

Takemoto, M., Kawamura, Y., Hirohama, M., Yamaguchi, Y., Handa, H., Saitoh, H., Nakao, Y., Kawada, M., Khalid, K., Koshino, H., et al. (2014) · The Journal of Antibiotics · doi:10.1038/ja.2013.142 · Cited by 62

Targeting SUMOylation with Anacardic Acid Derivatives: Novel Insights into EGF Pathway Dysregulation in Cancer Using an In Silico Approach

Padmakumar, S., Gopichand, B., Melge, A. R., Madhavan, A., Babu, P., Nair, B. G., Perry, J. J. P., & Kumar, G. B. (2025) · ACS Omega · doi:10.1021/acsomega.5c06377 · Cited by 1

Controlling protein SUMOylation

Schneekloth, J. S. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2496 · Cited by 7