Ras sumoylation in cell signaling and transformation

A Comprehensive Survey of Ras Mutations in Cancer

Prior, I. A., Lewis, P. D., & Mattos, C. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2612 · Cited by 2,063 · see citing works

Ras, PI(3)K and mTOR signalling controls tumour cell growth

Shaw, R. J., & Cantley, L. C. (2006) · Nature · doi:10.1038/nature04869 · Cited by 2,019 · see citing works

Drugging the undruggable RAS: Mission Possible?

Cox, A. D., Fesik, S. W., Kimmelman, A. C., Luo, J., & Der, C. J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4389 · Cited by 1,997 · see citing works

Proteins regulating Ras and its relatives

Boguski, M. S., & McCormick, F. P. (1993) · Nature · doi:10.1038/366643a0 · Cited by 1,905 · see citing works

The Cellular Functions of Small GTP-Binding Proteins

Hall, A. (1990) · Science · doi:10.1126/science.2116664 · Cited by 866 · see citing works

Ras and Rho GTPases

Bar‐Sagi, D., & Hall, A. (2000) · Cell · doi:10.1016/s0092-8674(00)00115-x · Cited by 778 · see citing works

Regulating the regulator: post-translational modification of RAS

Ahearn, I. M., Haigis, K. M., Bar‐Sagi, D., & Philips, M. R. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3255 · Cited by 557 · see citing works

A Molecular Redox Switch on p21

Lander, H. M., Hajjar, D. P., Hempstead, B. L., Mirza, U. A., Chait, B. T., Campbell, S. L., & Quilliam, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4323 · Cited by 488 · see citing works

PKC Regulates a Farnesyl-Electrostatic Switch on K-Ras that Promotes its Association with Bcl-Xl on Mitochondria and Induces Apoptosis

Bivona, T. G., Quatela, S. E., Bodemann, B. O., Ahearn, I. M., Soskis, M. J., Mor, A., Miura, J., Wiener, H. H., Wright, L. P., Saba, S. G., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.012 · Cited by 467 · see citing works

Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules

Resh, M. D. (2006) · Science s STKE · doi:10.1126/stke.3592006re14 · Cited by 415 · see citing works

COMPARTMENTALIZED RAS/MAPK SIGNALING

Mor, A., & Philips, M. R. (2006) · Annual Review of Immunology · doi:10.1146/annurev.immunol.24.021605.090723 · Cited by 400 · see citing works

Targeting RAS Membrane Association: Back to the Future for Anti-RAS Drug Discovery?

Cox, A. D., Der, C. J., & Philips, M. R. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3214 · Cited by 351 · see citing works

The EMT regulator slug and lung carcinogenesis

Shih, J.-Y., & Yang, P. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr110 · Cited by 315 · see citing works

Methionine oxidation and reduction in proteins

Kim, G., Weiss, S. J., & Levine, R. L. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.038 · Cited by 311 · see citing works

Resolution of Sister Centromeres Requires RanBP2-Mediated SUMOylation of Topoisomerase IIα

Dawlaty, M. M., Malureanu, L. A., Jeganathan, K. B., Kao, E., Sustmann, C., Tahk, S., Shuai, K., Grosschedl, R., & van Deursen, J. M. (2008) · Cell · doi:10.1016/j.cell.2008.01.045 · Cited by 309 · see citing works

PIAS proteins: pleiotropic interactors associated with SUMO

Rytinki, M. M., Kaikkonen, S., Pehkonen, P., Jääskeläinen, T. J., & Palvimo, J. J. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0061-z · Cited by 279 · see citing works

Impact of methionine oxidation on the binding of human IgG1 to FcRn and Fcγ receptors

Bertolotti‐Ciarlet, A., Wang, W., Lownes, R., Pristatsky, P., Fang, Y., McKelvey, T. W., Li, Y., Li, Y., Drummond, J., Prueksaritanont, T., et al. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.02.002 · Cited by 235 · see citing works

K-Ras4A splice variant is widely expressed in cancer and uses a hybrid membrane-targeting motif

Tsai, F. D., Lopes, M. S., Zhou, M., Court, H., Ponce, O., Fiordalisi, J. J., Gierut, J. J., Cox, A. D., Haigis, K. M., & Philips, M. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412811112 · Cited by 226 · see citing works

LZTR1 is a regulator of RAS ubiquitination and signaling

Bigenzahn, J. W., Collu, G. M., Kartnig, F., Pieraks, M., Vladimer, G. I., Heinz, L. X., Sedlyarov, V., Schischlik, F., Fauster, A., Rebsamen, M., et al. (2018) · Science · doi:10.1126/science.aap8210 · Cited by 224 · see citing works

Differential modification of Ras proteins by ubiquitination.

Jura, N., Scotto–Lavino, E., Sobczyk, A., & Bar-Sagi, D. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.02.011 · Cited by 219 · see citing works

Deregulated Overexpression of hCdt1 and hCdc6 Promotes Malignant Behavior

Liontos, M., Koutsami, M., Sideridou, M., Evangelou, K., Kletsas, D., Levy, B., Kotsinas, A., Nahum, O., Zoumpourlis, V. C., Kouloukoussa, M., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2837 · Cited by 217 · see citing works

Ubiquitination of K-Ras Enhances Activation and Facilitates Binding to Select Downstream Effectors

Sasaki, A. T., Carracedo, A., Locasale, J. W., Anastasiou, D., Takeuchi, K., Kahoud, E. R., Haviv, S., Asara, J. M., Pandolfi, P. P., & Cantley, L. C. (2011) · Science Signaling · doi:10.1126/scisignal.2001518 · Cited by 182 · see citing works

Determination of synthetic lethal interactions in KRAS oncogene-dependent cancer cells reveals novel therapeutic targeting strategies

Steckel, M., Molina‐Arcas, M., Weigelt, B., Marani, M., Warne, P. H., Kuznetsov, H. S., Kelly, G. P., Saunders, B., Howell, M. T., Downward, J., et al. (2012) · Cell Research · doi:10.1038/cr.2012.82 · Cited by 171 · see citing works

PostprenylationCAAXProcessing Is Required for Proper Localization of Ras but Not Rho GTPases

Michaelson, D., Ali, W., Chiu, V. K., Bergö, M. O., Silletti, J., Wright, L. P., Young, S. G., & Philips, M. R. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-11-0960 · Cited by 166 · see citing works

Small Molecule Inhibition of ERK Dimerization Prevents Tumorigenesis by RAS-ERK Pathway Oncogenes

Herrero, A., Pinto, A., Colón‐Bolea, P., Casar, B., Jones, M., Agudo‐Ibáñez, L., Vidal, R., Tenbaum, S. P., Nuciforo, P. G., Valdizán, E. M., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.07.001 · Cited by 148 · see citing works

PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription

Palvimo, J. J. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351405 · Cited by 146 · see citing works

HDAC6 and SIRT2 Regulate the Acetylation State and Oncogenic Activity of Mutant K-RAS

Yang, M. H., Laurent, G., Bause, A. S., Spang, R., German, N. J., Haigis, M. C., & Haigis, K. M. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0040-t · Cited by 143 · see citing works

Oncogene-Induced Senescence Pathways Weave an Intricate Tapestry

Yaswen, P., & Campisi, J. (2007) · Cell · doi:10.1016/j.cell.2007.01.005 · Cited by 138 · see citing works

Redox Proteomics of Protein-bound Methionine Oxidation

Ghesquière, B., Jonckheere, V., Colaert, N., Durme, J. V., Timmerman, E., Goethals, M., Schymkowitz, J. W. H., Rousseau, F., Vandekerckhove, J. S., & Gevaert, K. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.006866 · Cited by 132 · see citing works

Ras acylation, compartmentalization and signaling nanoclusters (Review)

Henis, Y. I., Hancock, J. F., & Prior, I. A. (2009) · Molecular Membrane Biology · doi:10.1080/09687680802649582 · Cited by 124 · see citing works

LZTR1 facilitates polyubiquitination and degradation of RAS-GTPases

Abe, T., Umeki, I., Kanno, S., Inoue, S., Niihori, T., & Aoki, Y. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0395-5 · Cited by 120 · see citing works

Regulation of RAS oncogenicity by acetylation

Yang, M. H., Nickerson, S., Kim, E. T., Liot, C., Laurent, G., Spang, R., Philips, M. R., Shan, Y., Shaw, D. E., Bar‐Sagi, D., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201487109 · Cited by 119 · see citing works

Post-translational modification by SUMO

Hannoun, Z., Greenhough, S., Jaffray, E., Hay, R. T., & Hay, D. C. (2010) · Toxicology · doi:10.1016/j.tox.2010.07.013 · Cited by 118 · see citing works

Feedback Regulation of Ras Signaling by Rabex-5-mediated Ubiquitination

Xu, L.-Z., Lubkov, V., Taylor, L. J., & Bar-Sagi, D. (2010) · Current Biology · doi:10.1016/j.cub.2010.06.051 · Cited by 110 · see citing works

Screening for E3-Ubiquitin ligase inhibitors: challenges and opportunities

Landré, V., Rotblat, B., Melino, S., Bernassola, F., & Melino, G. (2014) · Oncotarget · doi:10.18632/oncotarget.2431 · Cited by 105 · see citing works

H-Ras is degraded by Wnt/β-catenin signaling via β-TrCP-mediated polyubiquitylation

Kim, S., Yoon, J., Jeong, W.-J., Jeon, S.-H., Park, Y., Yoon, J., Park, Y. N., Kim, H., & Choi, K. (2009) · Journal of Cell Science · doi:10.1242/jcs.040493 · Cited by 101 · see citing works

Structural and biochemical studies of p21 Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange

Williams, J. G., Pappu, K., & Campbell, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1037299100 · Cited by 100 · see citing works

Cdc6 expression represses E-cadherin transcription and activates adjacent replication origins

Sideridou, M., Zakopoulou, R., Evangelou, K., Liontos, M., Kotsinas, A., Rampakakis, E., Gagos, S., Kahata, K., Grabušić, K., Gkouskou, K. K., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201108121 · Cited by 98 · see citing works

KRAS Protein Stability Is Regulated through SMURF2: UBCH5 Complex-Mediated β-TrCP1 Degradation

Shukla, S., Allam, U. S., Ahsan, A., Chen, G., Krishnamurthy, P. M., Marsh, K., Rumschlag, M., Shankar, S., Whitehead, C., Schipper, M., et al. (2014) · Neoplasia · doi:10.1593/neo.14184 · Cited by 96 · see citing works

Sumoylating and desumoylating enzymes at nuclear pores: underpinning their unexpected duties?

Palancade, B., & Doye, V. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.02.001 · Cited by 95 · see citing works

Impeded Nedd4-1-Mediated Ras Degradation Underlies Ras-Driven Tumorigenesis

Zeng, T., Wang, Q., Fu, J., Lin, Q., Bi, J., Ding, W., Qiao, Y., Zhang, S., Zhao, W., Lin, H., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.045 · Cited by 94 · see citing works

Posttranslational Modifications of RAS ProteinsPreprint

Ahearn, I. M., Zhou, M., & Philips, M. R. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031484 · Cited by 88 · see citing works

Phosphorylated K-Ras limits cell survival by blocking Bcl-xL sensitization of inositol trisphosphate receptors

Sung, P. J., Tsai, F. D., Vais, H., Court, H., Yang, J., Fehrenbacher, N., Foskett, J. K., & Philips, M. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306431110 · Cited by 84 · see citing works

Rho GTPases, oxidation, and cell redox control

Hobbs, G. A., Zhou, B., Cox, A. D., & Campbell, S. L. (2014) · Small GTPases · doi:10.4161/sgtp.28579 · Cited by 83 · see citing works

Differences in the Regulation of K-Ras and H-Ras Isoforms by Monoubiquitination

Baker, R., Wilkerson, E., Sumita, K., Isom, D. G., Sasaki, A. T., Dohlman, H. G., & Campbell, S. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.525691 · Cited by 77 · see citing works

Oncogenesis driven by the Ras/Raf pathway requires the SUMO E2 ligase Ubc9

Yu, B., Swatkoski, S., Holly, A. J., Lee, L. C., Giroux, V., Lee, C.-S., Hsu, D. J., Smith, J. L., Yuen, G., Yue, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415569112 · Cited by 76 · see citing works

Synthesis of 2′,3′,4′-trihydroxyflavone (2-D08), an inhibitor of protein sumoylation

Kim, Y. S., Keyser, S. G. L., & Schneekloth, J. S. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.01.010 · Cited by 76 · see citing works

Conspiracy Theory

Sternberg, P. W., & Alberola‐Ila, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81612-8 · Cited by 74 · see citing works

Modification of Ras in Eukaryotic Cells by Pseudomonas aeruginosa Exoenzyme S

McGuffie, E. M., Frank, D. W., Vincent, T. S., & Olson, J. C. (1998) · Infection and Immunity · doi:10.1128/iai.66.6.2607-2613.1998 · Cited by 74 · see citing works

The Mdm-2 Amino Terminus Is Required for Mdm2 Binding and SUMO-1 Conjugation by the E2 SUMO-1 Conjugating Enzyme Ubc9

Buschmann, T., Lerner, D., Lee, C.-G., & Ronai, Z. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103786200 · Cited by 73 · see citing works

Dnmt3b, de Novo DNA Methyltransferase, Interacts with SUMO-1 and Ubc9 through Its N-Terminal Region and Is Subject to Modification by SUMO-1

Kang, E. S., Park, C. W., & Chung, J. H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.6057 · Cited by 69 · see citing works

Rabex-5 Ubiquitin Ligase Activity Restricts Ras Signaling to Establish Pathway Homeostasis in Drosophila

Yan, H., Jahanshahi, M., Horvath, E., Liu, H.-Y., & Pfleger, C. M. (2010) · Current Biology · doi:10.1016/j.cub.2010.06.058 · Cited by 68 · see citing works

Competition between Sumoylation and Ubiquitination of Serine Hydroxymethyltransferase 1 Determines Its Nuclear Localization and Its Accumulation in the Nucleus

Anderson, D. D., Eom, J. Y., & Stover, P. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.302174 · Cited by 67 · see citing works

AMPK and Endothelial Nitric Oxide Synthase Signaling Regulates K-Ras Plasma Membrane Interactions via Cyclic GMP-Dependent Protein Kinase 2

Cho, K., Casteel, D. E., Prakash, P., Tan, L., van der Hoeven, D., Salim, A. A., Kim, C., Capon, R. J., Lacey, E., Cunha, S. R., et al. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00365-16 · Cited by 67 · see citing works

Geranylgeranyltransferase I as a target for anti-cancer drugs

Philips, M. R., & Cox, A. D. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32108 · Cited by 65 · see citing works

Tax ubiquitylation and SUMOylation control the dynamic shuttling of Tax and NEMO between Ubc9 nuclear bodies and the centrosome

Kfoury, Y. S., Setterblad, N., El-Sabban, M. E., Zamborlini, A., Dassouki, Z., Hajj, H. E., Hermine, O., Pique, C., de Thé, H., Saı̈b, A., et al. (2010) · Blood · doi:10.1182/blood-2010-05-285742 · Cited by 57 · see citing works

The Differential Palmitoylation States of N-Ras and H-Ras Determine Their Distinct Golgi Sub-compartment Localizations

Lynch, S. J., Snitkin, H., Gumper, I., Philips, M. R., Sabatini, D., & Pellicer, A. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.24779 · Cited by 53 · see citing works

Cysteine-based regulation of redox-sensitive Ras small GTPases

Messina, S., Simone, G. D., & Ascenzi, P. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101282 · Cited by 52 · see citing works

Tax ubiquitylation and SUMOylation control the dynamic shuttling of Tax and NEMO between Ubc9 nuclear bodies and the centrosome

Kfoury, Y. S., Setterblad, N., El-Sabban, M. E., Zamborlini, A., Dassouki, Z., Hajj, H. E., Hermine, O., Pique, C., de Thé, H., Saı̈b, A., et al. (2011) · Retrovirology · doi:10.1186/1742-4690-8-s1-a146 · Cited by 49 · see citing works

SUMO-Specific Proteases and the Cell Cycle

Bacco, A. D., & Gill, G. (2006) · Cell Cycle · doi:10.4161/cc.5.20.3367 · Cited by 47 · see citing works

K-Ras Lys-42 is crucial for its signaling, cell migration, and invasion

Choi, B. H., Philips, M. R., Chen, Y., Lu, L., & Dai, W. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003723 · Cited by 42 · see citing works

PIAS4 is an activator of hypoxia signalling via VHL suppression during growth of pancreatic cancer cells

Chien, W., Lee, K. L., Ding, L., Wuensche, P., Kato, H., Doan, N., Poellinger, L., Said, J. W., & Koeffler, H. P. (2013) · British Journal of Cancer · doi:10.1038/bjc.2013.531 · Cited by 41 · see citing works

Proteasome inhibitors in acute leukemia

Niewerth, D., Dingjan, I., Cloos, J. J., Jansen, G., & Kaspers, G. J. L. (2013) · Expert Review of Anticancer Therapy · doi:10.1586/era.13.4 · Cited by 41 · see citing works

Neuronal nitric oxide synthase-induced S-nitrosylation of H-Ras inhibits calcium ionophore-mediated extracellular-signal-regulated kinase activity

Raines, K. W., Cao, G.-L., Lee, E. K., Rosen, G. M., & Shapiro, P. S. (2006) · Biochemical Journal · doi:10.1042/bj20052002 · Cited by 39 · see citing works

BubR1 Is Modified by Sumoylation during Mitotic Progression

Yang, F., Hu, L., Chen, C., Yu, J., O’Connell, C. B., Khodjakov, A. L., Pagano, M., & Dai, W. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.318261 · Cited by 37 · see citing works

Sumoylation Is Important for Stability, Subcellular Localization, and Transcriptional Activity of SALL4, an Essential Stem Cell Transcription Factor

Yang, F., Yao, Y., Jiang, Y., Lu, L., Ma, Y., & Dai, W. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.391441 · Cited by 33 · see citing works

RAS GTPases are modified by SUMOylation

Choi, B. H., Chen, C., Philips, M., & Dai, W. (2018) · Oncotarget · doi:10.18632/oncotarget.23269 · Cited by 32 · see citing works

Across the Universe of K-Ras Mutations in Non-Small-Cell-Lung Cancer

Piva, S., Ganzinelli, M., Garassino, M. C., Caiola, E., Farina, G., Broggini, M., & Marabese, M. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113196660761 · Cited by 28 · see citing works

KRAS Ubiquitination at Lysine 104 Retains Exchange Factor Regulation by Dynamically Modulating the Conformation of the Interface

Yin, G., Zhang, J., Nair, V. V., Truong, V. H., Chaia, A. I., Petela, J., Harrison, J. S., Gorfe, A. A., & Campbell, S. L. (2020) · iScience · doi:10.1016/j.isci.2020.101448 · Cited by 21 · see citing works

Sumoylated BubR1 plays an important role in chromosome segregation and mitotic timing

Yang, F., Huang, Y., & Dai, W. H. (2012) · Cell Cycle · doi:10.4161/cc.11.4.19307 · Cited by 19 · see citing works

ADP-Ribosylated Proteins as Old and New Drug Targets for Anticancer Therapy: The Example of ARF6

Dani, N., Barbosa, A. J. M., Río, A. D., & Girolamo, M. D. (2012) · Current Pharmaceutical Design · doi:10.2174/138161213804581882 · Cited by 19 · see citing works

A Methionine Residue Promotes Hyperoxidation of the Catalytic Cysteine of Mouse Methionine Sulfoxide Reductase A

Kim, G., & Levine, R. L. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00180 · Cited by 15 · see citing works

Sensitization of Human Pancreatic Cancer Cells Harboring Mutated K-ras to Apoptosis

Shen, L., Kim, S., & Chen, C. Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040435 · Cited by 14 · see citing works

PIASγ expression in relation to clinicopathological, tumour factors and survival in indigenous black breast cancer women

Agboola, A., Musa, A. A., Banjo, A. A. F., Ayoade, B., Deji-Agboola, A. M., Nolan, C. C., Rakha, E. A., Ellis, I. O., & Green, A. R. (2013) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2013-201658 · Cited by 11 · see citing works

Cdc6 licenses tumor growth

Leslie, M. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.1957iti3 · Cited by 1 · see citing works

Autism Spectrum Disorder: Neurodevelopmental Risk Factors, Biological Mechanism, and Precision Therapy

Wang, X., Wang, B., Wu, C., Wang, J., & Sun, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031819 · Cited by 274 · see citing works

Targeting KRAS mutant cancers: from druggable therapy to drug resistance

Zhu, C., Guan, X., Zhang, X., Luan, X., Song, Z., Cheng, X., Zhang, W., & Qin, J.-J. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01629-2 · Cited by 231 · see citing works

Pioneer in Molecular Biology: Conformational Ensembles in Molecular Recognition, Allostery, and Cell Function

Nussinov, R. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169044 · Cited by 33 · see citing works

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 · see citing works

SENP2-mediated deSUMOylation of NCOA4 protects against ferritinophagy-dependent ferroptosis in myocardial ischemia-reperfusion injury

Xue, S., Zeng, J., Hao, J., Cai, W., Ding, Y., Chao, Y., Miao, Z., Xu, G., Xu, L., & Jiang, Z. (2025) · Autophagy · doi:10.1080/15548627.2025.2504792 · Cited by 30 · see citing works

Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01613-x · Cited by 24 · see citing works

Dynamic Multilevel Regulation of EGFR, KRAS, and MYC Oncogenes: Driving Cancer Cell Proliferation Through (Epi)Genetic and Post-Transcriptional/Translational Pathways

Šereš, M., Spacayova, K., Sulová, Z., Špaldová, J., Breier, A., & Pavlíková, L. (2025) · Cancers · doi:10.3390/cancers17020248 · Cited by 26 · see citing works

FSTL1 promotes alveolar epithelial cell aging and worsens pulmonary fibrosis by affecting SENP1‐mediated DeSUMOylation

Sun, W., Yang, X., Chen, L., Guo, L., Huang, H. F., Liu, X., Yang, Y., Xu, Z., & Xu, Z. (2023) · Cell Biology International · doi:10.1002/cbin.12062 · Cited by 18 · see citing works

Stress Granule Homeostasis, Aberrant Phase Transition, and Amyotrophic Lateral Sclerosis

Li, Z., Liu, X., & Liu, M. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00262 · Cited by 17 · see citing works

Regulation of transforming growth factor-β signalling by SUMOylation and its role in fibrosis

Wang, X., Liu, T., Huang, Y., Dai, Y., & Lin, H. (2021) · Open Biology · doi:10.1098/rsob.210043 · Cited by 14 · see citing works

Inhibition of TRIM32 by ibr‐7 treatment sensitizes pancreatic cancer cells to gemcitabine via mTOR/p70S6K pathway

Zhang, B., Yan, Y., Gu, Y., Teng, F., Xu, L., Zhou, X., Che, J., Dong, X., Zhou, L., & Lin, N. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17109 · Cited by 11 · see citing works

MicroRNA-145-5p inhibits the tumorigenesis of breast cancer through SENP2-regulated ubiquitination of ERK2

Chen, X., Li, D., Su, Q., Ling, X., Ding, S., Xu, R., Liu, Z., Qin, Y., Zhang, J., Yang, Z., et al. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05505-8 · Cited by 10 · see citing works

PLX8394, a RAF inhibitor, inhibits enterovirus 71 replication by blocking RAF/MEK/ERK signaling

Wu, C., Zhu, G., Qiu, F., Ren, F., Lin, B., Zhang, D., Yang, Q., & Huang, C. (2023) · Virologica Sinica · doi:10.1016/j.virs.2023.01.006 · Cited by 10 · see citing works

SUMO : A new perspective to decipher fibrosis

Li, L., Gao, P., Chen, T., Li, N., Zhang, H., Li, M., Chen, Y., Wei, W., Wang, H., & Sun, W. (2024) · Acta Physiologica · doi:10.1111/apha.14240 · Cited by 9 · see citing works

The ubiquitin code of RAS proteins: Decoding its role in cancer progression

Shi, Y., Shen, Y., Zhang, X., Zhu, N. W., Ding, Y., Yuan, Y., & Wang, J. (2025) · iScience · doi:10.1016/j.isci.2025.113029 · Cited by 7 · see citing works

Role of non-canonical post-translational modifications in gastrointestinal tumors

Liu, Y., Liu, J., Peng, N., Hai, S., Zhang, S., Zhao, H., & Liu, W. (2023) · Cancer Cell International · doi:10.1186/s12935-023-03062-x · Cited by 7 · see citing works

FSTL1 Promotes Alveolar epithelial cells Aging and Worsens Pulmonary Fibrosis by Affecting SENP1-Mediated DeSUMOylationPreprint

Sun, W., Yang, X., Duan, C., Jing, X., Gao, L., Huang, H., Guo, L., Yang, Y., & Xu, Z. (2022) · Research Square · doi:10.21203/rs.3.rs-1723160/v1

FTase inhibitors and cancer: prospects for use in targeted therapies

Xia, M.-T., Yu, L. D., Yan, Z., Wang, Y., Zhang, L., Miao, G., & Li, S. (2023) · Medicinal Chemistry Research · doi:10.1007/s00044-023-03171-2

Additional file 14 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812467

Additional file 8 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812449

Additional file 9 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812452

Additional file 18 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812479

Additional file 20 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812485

Additional file 7 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812446

Additional file 15 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812470

Additional file 16 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812473

Additional file 12 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812461

Additional file 6 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812443

Additional file 13 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812464

Additional file 19 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812482

Additional file 11 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812458

Additional file 17 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812476

Additional file 10 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812455

Effects of silencing farnesyltransferase on the migration, invasion, and epithelial-mesenchymal transition of salivary adenoid cystic carcinoma cells.

Li, W., Tong, L., Wang, Q., Han, H., & Chen, Z. (2022) · PubMed Central · doi:10.7518/hxkq.2022.04.004

Investigating post-translational modifications of B-Raf in cancer

Williams, J. A. (2024) · Queensland University of Technology · doi:10.5204/thesis.eprints.250811

Particulate matter-shaped Th17 cell plasticity impairs the colonic mucus layer

Li, B., Huang, N., Wang, J., Zhang, X., Meng, Q., Wu, S., & Chen, R. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.118219

Additional file 1 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812425

Additional file 3 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812431

Additional file 4 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812434

Additional file 2 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812428

Additional file 5 of Decoding key cell sub-populations and molecular alterations in glioblastoma at recurrence by single-cell analysis

Wang, X., Sun, Q., Wang, W., Liu, B., Gu, Y., & Chen, L. (2023) · Figshare · doi:10.6084/m9.figshare.23812437

Vibrio anguillarum hijacks fish host CypA to activate Ras-MAPK signaling and promote Edwardsiella piscicida entry during co-infection

Wang, Y., Wu, J., Wang, Y., Chen, N., Wang, Q., & Ma, Y. (2026) · Microbiological Research · doi:10.1016/j.micres.2026.128578

RAS GTPases are modified by SUMOylation

Choi, B. H., Chen, C., Philips, M., & Dai, W. (2018) · Oncotarget · doi:10.18632/oncotarget.23269 · Cited by 32 · see citing works

Abstract 3544: Ras GTPases are modified by SUMOylation

Choi, B. H., Chen, C., Philips, M. R., & Dai, W. H. (2018) · Cancer Research · doi:10.1158/1538-7445.am2018-3544 · Cited by 2 · see citing works

K-Ras Lys-42 is crucial for its signaling, cell migration, and invasion

Choi, B. H., Philips, M. R., Chen, Y., Lu, L., & Dai, W. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003723 · Cited by 42 · see citing works

SUMO wrestling with Ras

Zhang, H., & Luo, J. (2016) · Small GTPases · doi:10.1080/21541248.2016.1161698 · Cited by 8 · see citing works

Oncogenic Ras abrogates MEK SUMOylation that suppresses the ERK pathway and cell transformation

Kubota, Y., O'Grady, P., Saito, H., & Takekawa, M. (2011) · Nature Cell Biology · doi:10.1038/ncb2169 · Cited by 71 · see citing works