Ubiquitination and degradation of SUMO1 by small-molecule degraders extends survival of mice with patient-derived tumors
Open accessAbstract
Small-molecule degraders of SUMO1 induce its ubiquitination and degradation through binding of CAPRIN1 in tumor cells in vitro and in vivo.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Bellail et al. found FBXO42 and CAPRIN1 as drug interactors using genome-scale CRISPR screens and HB007-based pull-down proteomics.
“Bellail et al. found FBXO42 (a CRL1 substrate receptor) and CAPRIN1 as drug interactors, using genome-scale CRISPR screens and HB007-based pull-down proteomics.”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [163]
The authors screened the NCI drug-like library of 1596 compounds for SUMO1 degraders and identified CPD1, which was optimized to HB007.
“The authors screened the NCI drug-like library of 1596 compounds in search of SUMO1 degraders and identified the small-molecule hit CPD1, which was then optimized to the lead compound HB007 (Fig. 7 and 8).163”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [163]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Improved vectors and genome-wide libraries for CRISPR screening
Sanjana, N. E., Shalem, O., & Zhang, F. (2014) · Nature Methods · doi:10.1038/nmeth.3047 · Cited by 5,239 · see citing works
Hopkins, A. L., & Groom, C. R. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd892 · Cited by 3,305 · see citing works
Li, W., Xu, H., Xiao, T., Cong, L., Love, M. I., Zhang, F., Irizarry, R. A., Liu, J. S., Brown, M., & Liu, X. S. (2014) · Genome Biology · doi:10.1186/s13059-014-0554-4 · Cited by 2,684 · see citing works
Identification of a Primary Target of Thalidomide Teratogenicity
Ito, T., Ando, H., Suzuki, T., Ogura, T., Hotta, K., Imamura, Y., Yamaguchi, Y., & Handa, H. (2010) · Science · doi:10.1126/science.1177319 · Cited by 2,136 · see citing works
Lenalidomide Causes Selective Degradation of IKZF1 and IKZF3 in Multiple Myeloma Cells
Krönke, J., Udeshi, N. D., Narla, A., Grauman, P., Hurst, S. N., McConkey, M., Svinkina, T., Heckl, D., Comer, E., Li, X., et al. (2014) · Science · doi:10.1126/science.1244851 · Cited by 1,879 · see citing works
Hay, R. T. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.012 · Cited by 1,623 · see citing works
The Myeloma Drug Lenalidomide Promotes the Cereblon-Dependent Destruction of Ikaros Proteins
Lu, G., Middleton, R. E., Sun, H., Naniong, M., Ott, C. J., Mitsiades, C. S., Wong, K.-K., Bradner, J. E., & Kaelin, W. G. (2014) · Science · doi:10.1126/science.1244917 · Cited by 1,583 · see citing works
Mahajan, R. K., Delphin, C., Guan, T., Gerace, L., & Melchior, F. (1997) · Cell · doi:10.1016/s0092-8674(00)81862-0 · Cited by 1,258 · see citing works
Matunis, M. J., Coutavas, E. E., & Blobel, G. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.6.1457 · Cited by 1,199 · see citing works
Structure of the DDB1–CRBN E3 ubiquitin ligase in complex with thalidomide
Fischer, E. S., Böhm, K., Lydeard, J. R., Yang, H., Stadler, M. B., Cavadini, S., Nagel, J., Serluca, F., Acker, V., Lingaraju, G. M., et al. (2014) · Nature · doi:10.1038/nature13527 · Cited by 1,141 · see citing works
The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
Gareau, J. R., & Lima, C. D. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3011 · Cited by 1,106 · see citing works
Sumoylation: A Regulatory Protein Modification in Health and Disease
Flotho, A., & Melchior, F. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061909-093311 · Cited by 1,101 · see citing works
Targeted protein degradation: expanding the toolbox
Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960 · see citing works
The logic of the 26S proteasome.
Collins, G. A., & Goldberg, A. L. (2017) · Cell · doi:10.1016/j.cell.2017.04.023 · Cited by 933 · see citing works
Lenalidomide induces ubiquitination and degradation of CK1α in del(5q) MDS
Krönke, J., Fink, E. C., Hollenbach, P. W., MacBeth, K. J., Hurst, S. N., Udeshi, N. D., Chamberlain, P. P., Mani, D. R., Man, H. W., Gandhi, A. K., et al. (2015) · Nature · doi:10.1038/nature14610 · Cited by 863 · see citing works
The Nucleoporin RanBP2 Has SUMO1 E3 Ligase Activity
Pichler, A., Gast, A., Seeler, J.-S., Dejean, A., & Melchior, F. (2002) · Cell · doi:10.1016/s0092-8674(01)00633-x · Cited by 817 · see citing works
Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15
Han, T., Goralski, M., Gaskill, N., Capota, E., Kim, J., Ting, T. C., Xie, Y., Williams, N. S., & Nijhawan, D. (2017) · Science · doi:10.1126/science.aal3755 · Cited by 762 · see citing works
A novel cereblon modulator recruits GSPT1 to the CRL4CRBN ubiquitin ligase
Matyskiela, M. E., Lu, G., Ito, T., Pagarigan, B., Lu, C.-C., Miller, K., Fang, W., Wang, N.-Y., Nguyen, D., Houston, J., et al. (2016) · Nature · doi:10.1038/nature18611 · Cited by 701 · see citing works
Mechanisms and function of substrate recruitment by F-box proteins
Skaar, J. R., Pagan, J. K., & Pagano, M. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3582 · Cited by 671 · see citing works
Structural basis of lenalidomide-induced CK1α degradation by the CRL4CRBN ubiquitin ligase
Petzold, G., Fischer, E. S., & Thomä, N. H. (2016) · Nature · doi:10.1038/nature16979 · Cited by 620 · see citing works
Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN
Sievers, Q. L., Petzold, G., Bunker, R. D., Renneville, A., Słabicki, M., Liddicoat, B. J., Abdulrahman, W., Mikkelsen, T., Ebert, B. L., & Thomä, N. H. (2018) · Science · doi:10.1126/science.aat0572 · Cited by 537 · cited 3× · see citing works
“Acknowledgments: We thank F. Melchior, R. T. Hay, and Z. J. Chen for providing the plasmid YFP-SUMO1∆C4 (1-97), YFP-SUMO3∆C11, pcDNA3 6xHis/SUMO1, pCMV-myc-UBC9, pEF-IRES-P-HA-Ub-K48, pEF-IRES-P-HA-Ub-K0, pEF-IRES-P-HA-Ub-WT, and pEF-IRES-P-HA-R48.”
The SUMO Pathway Is Essential for Nuclear Integrity and Chromosome Segregation in Mice
Nacerddine, K., Lehembre, F., Bhaumik, M., Artus, J., Cohen‐Tannoudji, M., Babinet, C., Pandolfi, P. P., & Dejean, A. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.10.007 · Cited by 535 · see citing works
The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress
Morris, J. R., Boutell, C., Epple, M., Densham, R. M., Weekes, D. B., Alamshah, A., Butler, L. R., Galanty, Y., Pangon, L., Kiuchi, T., et al. (2009) · Nature · doi:10.1038/nature08593 · Cited by 434 · see citing works
A SUMOylation-Dependent Transcriptional Subprogram Is Required for Myc-Driven Tumorigenesis
Kessler, J. D., Kahle, K. T., Sun, T., Meerbrey, K. L., Schlabach, M. R., Schmitt, E. M., Skinner, S. O., Xu, Q., Li, M. Z., Hartman, Z. C., et al. (2011) · Science · doi:10.1126/science.1212728 · Cited by 433 · see citing works
SUMO and the robustness of cancer
Seeler, J.-S., & Dejean, A. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2016.143 · Cited by 425 · see citing works
Zhang, Y., Wen, Z., Washburn, M. P., & Florens, L. A. (2010) · Analytical Chemistry · doi:10.1021/ac9023999 · Cited by 386 · see citing works
Dynamics of Cullin-RING Ubiquitin Ligase Network Revealed by Systematic Quantitative Proteomics
Bennett, E. J., Rush, A. J., Gygi, S. P., & Harper, J. W. (2010) · Cell · doi:10.1016/j.cell.2010.11.017 · Cited by 386 · see citing works
SCF ubiquitin ligase-targeted therapies
Skaar, J. R., Pagan, J. K., & Pagano, M. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4432 · Cited by 336 · see citing works
Building and remodelling Cullin–RING E3 ubiquitin ligases
Lydeard, J. R., Schulman, B. A., & Harper, J. W. (2013) · The EMBO Reports · doi:10.1038/embor.2013.173 · Cited by 327 · see citing works
SUMO: A Multifaceted Modifier of Chromatin Structure and Function
Cubeñas-Potts, C., & Matunis, M. J. (2013) · Developmental Cell · doi:10.1016/j.devcel.2012.11.020 · Cited by 281 · see citing works
Waste disposal—An attractive strategy for cancer therapy
Salami, J., & Crews, C. M. (2017) · Science · doi:10.1126/science.aam7340 · Cited by 279 · see citing works
Solomon, S., Xu, Y., Wang, B., David, M. D., Schubert, P., Kennedy, D. D., & Schrader, J. W. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02300-06 · Cited by 260 · see citing works
Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 ligase complex
Bussiere, D. E., Xie, L., Srinivas, H., Shu, W., Burke, A., Be, C., Zhao, J., Godbole, A., King, D., Karki, R. G., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0411-6 · Cited by 257 · see citing works
Li, J., Xu, Y., Long, X., Wang, W., Jiao, H., Mei, Z., Yin, Q., Ma, L., Zhou, A., Wang, L., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2013.12.008 · Cited by 243 · see citing works
Self-citationProbing the roles of SUMOylation in cancer cell biology by using a selective SAE inhibitor
He, X., Riceberg, J., Soucy, T. A., Koenig, E. M., Minissale, J., Gallery, M. A., Bernard, H., Yang, X., Liao, H., Rabino, C., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2463 · Cited by 230 · see citing works
Ubc9 Sumoylation Regulates SUMO Target Discrimination
Knipscheer, P., Flotho, A., Klug, H., Olsen, J. V., van Dijk, W. J., Fish, A., Johnson, E. S., Mann, M., Sixma, T. K., & Pichler, A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.022 · Cited by 219 · see citing works
Detecting endogenous SUMO targets in mammalian cells and tissues
Becker, J., Barysch, S. V., Karaca, S., Dittner, C., Hsiao, H., Díaz, M. B., Herzig, S., Urlaub, H., & Melchior, F. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2526 · Cited by 209 · see citing works
SUMO2 is essential while SUMO3 is dispensable for mouse embryonic development
Wang, L., Wansleeben, C., Zhao, S., Miao, P., Paschen, W., & Yang, W. (2014) · EMBO Reports · doi:10.15252/embr.201438534 · Cited by 209 · see citing works
Du, X., Volkov, O. A., Czerwinski, R. M., Tan, H., Huerta, C., Morton, E. R., Rizzi, J. P., Wehn, P. M., Xu, R., Nijhawan, D., et al. (2019) · Structure · doi:10.1016/j.str.2019.10.005 · Cited by 181 · see citing works
Sumo-1 Function Is Dispensable in Normal Mouse Development
Zhang, F., Mikkonen, L., Toppari, J., Palvimo, J. J., Thesleff, I., & Jänne, O. A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00651-08 · Cited by 180 · see citing works
Evdokimov, E., Sharma, P., Lockett, S. J., Lualdi, M., & Kuehn, M. R. (2008) · Journal of Cell Science · doi:10.1242/jcs.038570 · Cited by 157 · see citing works
Roles of sumoylation of a reptin chromatin-remodelling complex in cancer metastasis
Kim, J. H., Choi, H. J., Kim, B., Kim, M. H., Lee, J. M., Kim, I. S., Lee, M. H., Choi, S. J., Kim, K. I., Kim, S., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1415 · Cited by 148 · see citing works
SUMO1 modification stabilizes CDK6 protein and drives the cell cycle and glioblastoma progression
Bellail, A. C., Olson, J. J., & Hao, C. (2014) · Nature Communications · doi:10.1038/ncomms5234 · Cited by 124 · see citing works
Self-citationDrąg, M., & Salvesen, G. S. (2008) · IUBMB Life · doi:10.1002/iub.113 · Cited by 114 · see citing works
Absence of Caprin-1 Results in Defects in Cellular Proliferation
Wang, B., David, M. D., & Schrader, J. W. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.7.4274 · Cited by 91 · see citing works
Grill, B. J., Wilson, G. M., Zhang, K., Wang, B., Doyonnas, R., Quadroni, M., & Schrader, J. W. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.4.2389 · Cited by 85 · see citing works
JFK, a Kelch domain-containing F-box protein, links the SCF complex to p53 regulation
Sun, L., Shi, L., Li, W., Yu, W., Liang, J., Zhang, H., Yang, X., Wang, Y., Li, R., Yao, X., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901864106 · Cited by 79 · see citing works
Highly Reproducible Label Free Quantitative Proteomic Analysis of RNA Polymerase Complexes
Mosley, A. L., Sardiu, M. E., Pattenden, S. G., Workman, J. L., Florens, L. A., & Washburn, M. P. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.000687 · Cited by 77 · see citing works
Self-citationOncogenic 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
Martin, S., Zekri, L., Metz, A., Maurice, T., Chébli, K., Vignes, M., & Tazi, J. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12189 · Cited by 69 · see citing works
Shiina, N., Yamaguchi, K., & Tokunaga, M. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.6386-09.2010 · Cited by 68 · see citing works
Demarque, M., Nacerddine, K., Neyret‐Kahn, H., Andrieux, A., Danenberg, E., Jouvion, G., Bomme, P., Hamard, G., Romagnolo, B., Terris, B., et al. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.10.002 · Cited by 68 · see citing works
Molecular glue concept solidifies
Baek, K., & Schulman, B. A. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0414-3 · Cited by 61 · see citing works
le Sage, C., Lawo, S., Panicker, P., Scales, T. M. E., Rahman, S. A., Little, A. S., McCarthy, N., Moore, J. D., & Cross, B. C. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-18172-6 · Cited by 54 · see citing works
Self-citationGuo, W.-H., Yuan, L.-H., Xiao, Z.-H., Liu, D., & Zhang, J. (2010) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-010-0920-x · Cited by 41 · see citing works
Yan, R., He, L., Li, Z., Han, X., Liang, J., Si, W., Chen, Z., Li, L., Xie, G., Li, W., et al. (2015) · Genes & Development · doi:10.1101/gad.254292.114 · Cited by 38 · see citing works
Increasing the performance of pooled CRISPR–Cas9 drop-out screening
Cross, B. C. S., Lawo, S., Archer, C. R., Hunt, J. R., Yarker, J. L., Riccombeni, A., Little, A. S., McCarthy, N., & Moore, J. D. (2016) · Scientific Reports · doi:10.1038/srep31782 · Cited by 37 · see citing works
Self-citationWu, Y., Zhu, J., Huang, X., & Du, Z. (2016) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798316004903 · Cited by 31 · see citing works
Over-Expression of Small Ubiquitin-Related Modifier-1 and Sumoylated p53 in Colon Cancer
Zhang, H., Kuai, X., Ji, Z., Li, Z., & Shi, R. (2013) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-013-9612-x · Cited by 30 · see citing works
Study of MDM2 and SUMO-1 expression in actinic cheilitis and lip cancer
Alves, M. G. O., Delgado, A. D. M., Balducci, I., Carvalho, Y. R., Cavalcante, A. S. R., & Almeida, J. D. (2014) · Archives of Dermatological Research · doi:10.1007/s00403-014-1500-8 · Cited by 12 · see citing works
Modification of Cul1 regulates its association with proteasomal subunits
Bloom, J., Peschiaroli, A., Demartino, G., & Pagano, M. (2006) · Cell Division · doi:10.1186/1747-1028-1-5 · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works
Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works
Zhang, X.-W., Feng, N., Liu, Y.-C., Guo, Q., Wang, J., Bai, Y.-Z., Ye, X., Yang, Z., Yang, H., Liu, Y., et al. (2022) · Science Advances · doi:10.1126/sciadv.abo0789 · Cited by 120 · see citing works
Targeting the undruggables—the power of protein degraders
Zhang, C., Liu, Y., Li, G., Yang, Z., Han, C., Sun, X., Sheng, C., Ding, K., & Rao, Y. (2024) · 中国科学通报：英文版 · doi:10.1016/j.scib.2024.03.056 · Cited by 108 · see citing works
Huang, X., Liu, X., Li, X., Zhang, Y., Gao, J., Yang, Y., Jiang, Y., Gao, H., Sun, C., Xuan, L., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40327-5 · Cited by 35 · see citing works
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 · see citing works
The emerging roles of SUMOylation in pulmonary diseases
Zheng, X., Wang, L., Zhang, Z., & Tang, H. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00719-1 · Cited by 21 · see citing works
Facilitating the development of molecular glues: Opportunities from serendipity and rational design
Jiang, W., Jiang, Y., Luo, Y., Qiao, W., & Yang, T. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115950 · Cited by 21 · see citing works
Self-citationZhong, C., Zhu, R., Jiang, T., Tian, S., Zhao, X., Wan, X., Jiang, S., Chen, Z., Gong, R., He, L., et al. (2023) · Advanced Science · doi:10.1002/advs.202305035 · Cited by 21 · see citing works
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 · see citing works
Self-citationXia, L., Lin, J., Peng, M., Jiang, X., Peng, Q., Cui, S., Zhang, W., Li, S., Wang, J., Oyang, L., et al. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.91206 · Cited by 17 · see citing works
The association and clinical relevance of phase-separating protein CAPRIN1 with noncoding RNA
Zhang, M., & Peng, S. (2023) · Cell Stress and Chaperones · doi:10.1007/s12192-023-01320-5 · Cited by 15 · see citing works
Zhao, Y. Q., Jin, H. R., Kim, D.-H., Jung, S. H., Liu, S., Wan, J., Lo, H., Fu, X. Q., Wang, Q., Hao, C., et al. (2023) · Molecular Carcinogenesis · doi:10.1002/mc.23560 · Cited by 15 · see citing works
Self-citationCaprin-1 influences autophagy-induced tumor growth and immune modulation in pancreatic cancer
Yang, W., Chen, H., Li, G., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04693-4 · Cited by 12 · see citing works
The impact of dysregulation SUMOylation on prostate cancer
Li, K., Wang, H., Jiang, B., & Jin, X. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06271-2 · Cited by 8 · see citing works
Yuan, Y., Fu, L., Liu, W., Dong, R., Shi, F., Liu, J., Li, H., & Zhang, G. (2025) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2025.106772 · Cited by 6 · see citing works
Positioning SUMO as an immunological facilitator of oncolytic viruses for high-grade glioma
Karandikar, P. V., Suh, L., Gerstl, J. V. E., Blitz, S. E., Qu, Q. R., Won, S., Gessler, F. A., Arnaout, O. M., Smith, T. R., Peruzzi, P., et al. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1271575 · Cited by 6 · see citing works
PROTACs in targeted protein degradation: Advances in development and AI-enhanced drug discovery
Du, M., Liu, T., Wang, W., Fan, S., Tian, M., Du, Q., Wang, Z., Li, X., Liu, X., Xia, Q., et al. (2026) · European Journal of Medicinal Chemistry Reports · doi:10.1016/j.ejmcr.2026.100332 · Cited by 4 · see citing works
Advances of E3 ligases in lung cancer
Yu, J., Zhao, Y., & Xie, Y. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101740 · Cited by 4 · see citing works
Self-citationCUL1 exacerbates glucocorticoid-induced osteoporosis by enhancing ASAP1 ubiquitination
Wu, J., Ren, W., Liu, J., & Bai, X. (2024) · HORMONES · doi:10.1007/s42000-024-00599-y · Cited by 3 · see citing works
Cao, S., Zhong, C., Jiang, S., Li, Y., Xi, Y., Xiao, M., Jiang, T., Wan, X., Chen, Z., Yu, X., et al. (2026) · Advanced Science · doi:10.1002/advs.202520863 · Cited by 2 · see citing works
Liu, X., Yang, F., Duan, Y., Xiao, H., Cao, Z., Wang, Z., Zhang, H., & Kang, X. (2026) · Cell Proliferation · doi:10.1111/cpr.70256 · Cited by 2 · see citing works
Zhou, B., Wu, S., Hong, S., Li, H., Jiang, Z., Sun, Y., Qiu, J., & Qin, L. (2025) · European journal of medical research · doi:10.1186/s40001-025-03050-z · Cited by 1 · see citing works
Jung, S. H., Wang, X., Liu, B., Roy, R. N., Jaiswal, N., Rai, R. K., Takagi, Y., Gao, C., Zeng, L., Lo, H., et al. (2026) · Advanced Science · doi:10.1002/advs.77575 · Cited by 1 · see citing works
Self-citationSUMO1 degrader extends mouse survival
Crunkhorn, S. (2021) · Nature Reviews Drug Discovery · doi:10.1038/d41573-021-00182-9
Jung, S. H., Roy, R., Zhao, Y. Q., O’Connell, T. M., Wohlford, R. K., Kim, D.-H., Hao, C., & Bellail, A. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.08.647644
Self-citationTumor suppressor OSR1 is modified by SUMO1 and regulates the Wnt/β-catenin signaling pathway in HCC
Lin, X., Liu, Y., Lai, Z., Wang, X., Cui, Y., & Weng, S. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114693
He, Y., Zhang, H., Gu, J., Ju, M., & Zhang, C. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl45811
Yang, W., Chen, H., Guanqun, L., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26652255
Yang, W., Chen, H., Guanqun, L., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26652252
Yang, W., Chen, H., Guanqun, L., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26652243
Yang, W., Chen, H., Guanqun, L., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26652240
Yang, W., Chen, H., Guanqun, L., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26652258
Yang, W., Chen, H., Guanqun, L., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26652249
Yang, W., Chen, H., Guanqun, L., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26652246
Yang, W., Chen, H., Guanqun, L., Zhang, T., Sui, Y., Liu, L., Hu, J., Wang, G., Chen, H., Wang, Y., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26652237
ARHGEF26 Maintains SOX2 Stability by Inhibiting Ubiquitination to Enhance Glioblastoma Stemness
Chen, X.-Q., Qin, Z., Li, Z.-B., Huang, J.-F., Hou, N.-N., Fu, W.-J., Niu, Q., Wang, S., Luo, M., Tang, C., et al. (2026) · Laboratory Investigation · doi:10.1016/j.labinv.2026.106123
Chrysosplenetin-induced TMED3 aggregation triggers unfolded protein response in pancreatic cancer
Zhang, Z., Weng, N., Gu, X., Zang, Y., Chen, Q., Zheng, R., Yang, X., Amu, G., Zhao, D., Ma, Z., et al. (2026) · EMBO Molecular Medicine · doi:10.1038/s44321-026-00506-5
Liu, L., Voulgaris, O., Wang, C., Gannon, D., Ritchie, M. E., Feltham, R., & Vervoort, S. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.14.744749
The role of cell cycle-associated protein 1 (CAPRIN1) in diseases
Li, C., Tang, P., Fu, Y., & Ji, R. (2026) · PeerJ · doi:10.7717/peerj.21772
ASIC1a promotes liver fibrosis by inhibiting METTL3 SUMOylation
Li, Z.-H., Li, M., Song, Y.-H., Ren, R.-H., Zhang, T.-T., Huang, W.-J., Harry, A. M., Shah, K. A., Wang, Y.-Y., Liu, Z., et al. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-026-01951-1
- Authors
- Bellail, A. C., Jin, H. R., Lo, H.-Y., Jung, S. H., Hamdouchi, C., Kim, D., Higgins, R. K., Blanck, M., le Sage, C., Cross, B. C. S., Li, J., Mosley, A. L., Wijeratne, A. B., Jiang, W., Ghosh, M., Zhao, Y. Q., Hauck, P. M., Shekhar, A., & Hao, C.
- Affiliations
- Indiana University Melvin and Bren Simon Comprehensive Cancer Center (US)
- Indiana University School of Medicine (US)
- Institut des Systèmes Complexes Paris Île-de-France (FR)
- Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
- Horizon Discovery (United Kingdom) (GB)
- Horizon Discovery, Cambridge, CB25 9TL, UK.
- Wayne State University (US)
- Purdue University West Lafayette (US)
- Indiana Clinical and Translational Sciences Institute (US)
- Corresponding author
- Bellail, Anita C.
- Jin, Hong Ri
- Hao, Chunhai
- ORCID
- Venue
- Science Translational Medicine
- Published
- 2021-10-13
- Volume
- 13
- Issue
- 615
- Pages
- eabh1486-eabh1486
- ISSN
- 1946-6234 (ISSN-L)
- 1946-6242
- PMC
- PMC9450956
- OpenAlex
- W3206807389
- Cited by
- 42
- References
- 61
- Citations by year
- 2026: 9 · 2025: 7 · 2024: 11 · 2023: 12 · 2022: 2 · 2021: 1
- FWCI
- 2.12
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Translational Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- IUScholarWorks (Indiana University) (submittedVersion, public-domain)
- Purdue University Indianapolis (Indiana University) (submittedVersion, public-domain)
- Funders
- Eli Lilly and Company
- Purdue University
- Lilly Endowment
- National Institutes of Health
- School of Medicine, Indiana University
- National Cancer Institute (R01CA203893, R43CA224461)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- SUMO1, small-molecule degraders, protein degradation, ubiquitination, CAPRIN1, structure-activity relationship, patient-derived xenografts, CRISPR-Cas9 knockout screen, brain cancer, breast cancer, colon cancer, lung cancer
- MeSH terms
- Animals, Humans, Neoplasms, SUMO-1 Protein, Mice, Ubiquitination
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
