CC-122, a pleiotropic pathway modifier, mimics an interferon response and has antitumor activity in DLBCL
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Key Points: CC-122 is a novel agent for DLBCL with antitumor and immunomodulatory activity. CC-122 binds CRBN and degrades Aiolos and Ikaros resulting in a mimicry of IFN signaling and apoptosis in DLBCL.
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Published proteome-wide mass spectrometry data confirmed degradation of endogenous full-length WIZ in WSU-DLCL2 and TMD8 cells in the presence of lenalidomide and CC-122.
“Examination of published proteome-wide mass spectrometry data confirmed degradation of endogenous, full-length WIZ in WSU-DLCL2 (human diffuse large B cell lymphoma) and TMD8 (human diffuse large B cell lymphoma) cells in the presence of lenalidomide and the thalidomide analog CC-122 (fig. S7C) (20).”
From Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN (2018) · cites this paper as [20]
Thalidomide, lenalidomide and pomalidomide are currently FDA approved in a variety of clinical settings, including MM, NHL, MDS and Kaposi sarcoma.
“Thalidomide, lenalidomide and pomalidomide are currently FDA approved in a variety of clinical settings, including MM, NHL and MDS as well as Kaposi sarcoma (KS)19–22.”
From Cancer therapies based on targeted protein degradation — lessons learned with lenalidomide (2021) · cites this paper as [20]
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Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling
Alizadeh, A. A., Eisen, M. B., Davis, R. E., Ma, C., Lossos, I. S., Rosenwald, A., Boldrick, J. C., Sabet, H., Tran, T., Yu, X., et al. (2000) · Nature · doi:10.1038/35000501 · Cited by 9,925 · 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
Stromal Gene Signatures in Large-B-Cell Lymphomas
Lenz, G., Wright, G. W., Davé, S. S., Xiao, W., Powell, J. I., Zhao, H., Xu, W., Tan, B. T., Goldschmidt, N., Iqbal, J., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0802885 · Cited by 1,818 · 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
Self-citationFeugier, P., Hoof, A. V., Sebban, C., Solal-Céligny, P., Bouabdallah, R., Fermé, C., Christian, B., Lepage, É., Tilly, H., Morschhauser, F., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.09.131 · Cited by 1,483 · see citing works
Armitage, J. O., & Weisenburger, D. D. (1998) · Journal of Clinical Oncology · doi:10.1200/jco.1998.16.8.2780 · Cited by 1,263 · 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
Scott, D. W., Wright, G. W., Williams, P. M., Lih, C., Walsh, W. D., Jaffe, E. S., Rosenwald, A., Campo, E., Chan, W. C., Connors, J. M., et al. (2014) · Blood · doi:10.1182/blood-2013-11-536433 · Cited by 627 · see citing works
Gandhi, A. K., Kang, J., Havens, C. G., Conklin, T., Ning, Y., Wu, L., Ito, T., Ando, H., Waldman, M. F., Thakurta, A., et al. (2014) · British Journal of Haematology · doi:10.1111/bjh.12708 · Cited by 619 · see citing works
Self-citationBarrans, S., Crouch, S., Smith, A. G., Turner, K., Owen, R. G., Patmore, R. D., Roman, E., & Jack, A. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.26.3947 · Cited by 552 · see citing works
Chamberlain, P. P., Lopez-Girona, A., Miller, K., Carmel, G., Pagarigan, B., Chie-Leon, B., Rychak, E., Corral, L. G., Ren, Y. J., Wang, M., et al. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2874 · Cited by 531 · see citing works
Self-citationExploiting Synthetic Lethality for the Therapy of ABC Diffuse Large B Cell Lymphoma
Yang, Y., Shaffer, A. L., Emre, N. C. T., Ceribelli, M., Zhang, M., Wright, G. W., Xiao, W., Powell, J. I., Platig, J., Kohlhammer, H., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.05.024 · Cited by 524 · see citing works
Witzig, T. E., Vose, J. M., Zinzani, P. L., Reeder, C. B., Buckstein, R. J., Polikoff, J. A., Bouabdallah, R., Haïoun, C., Tilly, H., Guo, P., et al. (2011) · Annals of Oncology · doi:10.1093/annonc/mdq626 · Cited by 392 · see citing works
Lenalidomide Monotherapy in Relapsed or Refractory Aggressive Non-Hodgkin's Lymphoma
Wiernik, P. H., Lossos, I. S., Tuscano, J. M., Justice, G. R., Vose, J. M., Cole, C. E., Lam, W., McBride, K., Wride, K., PIETRONIGRO, D. D., et al. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.15.3429 · Cited by 371 · see citing works
Rimsza, L. M. (2004) · Blood · doi:10.1182/blood-2003-07-2365 · Cited by 343 · see citing works
Early hematopoietic lineage restrictions directed by Ikaros
Yoshida, T., Ng, S. Y., Zúñiga‐Pflücker, J. C., & Georgopoulos, K. (2006) · Nature Immunology · doi:10.1038/ni1314 · Cited by 324 · see citing works
Shin, S., Dimitri, C. A., Yoon, S.-O., Dowdle, W. E., & Blenis, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.020 · Cited by 291 · see citing works
Thiéblemont, C., Brière, J., Mounier, N., Voelker, H.-U., Cuccuini, W., Hirchaud, E., Rosenwald, A., Jack, A., Sundström, C., Cogliatti, S., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2011.35.4423 · Cited by 277 · see citing works
Treatment of Advanced Non-Hodgkin's Lymphoma with Recombinant Leukocyte a Interferon
Foon, K. A., Sherwin, S. A., Abrams, P. G., Longo, D. L., Fer, M. F., Stevenson, H. C., Ochs, J. J., Bottino, G. C., SCHOENBERGER, C., Zeffren, J., et al. (1984) · New England Journal of Medicine · doi:10.1056/nejm198411013111803 · Cited by 274 · see citing works
Aiolos promotes TH17 differentiation by directly silencing Il2 expression
Quintana, F. J., Jin, H., Burns, E. J., Nadeau, M., Yeste, A., Kumar, D., Rangachari, M., Zhu, C. Y., Xiao, S., Seavitt, J., et al. (2012) · Nature Immunology · doi:10.1038/ni.2363 · Cited by 250 · see citing works
Ng, S. Y., Yoshida, T., Zhang, J., & Georgopoulos, K. (2009) · Immunity · doi:10.1016/j.immuni.2009.01.014 · Cited by 245 · see citing works
Prognostic factors for diffuse large B-cell lymphoma in the R(X)CHOP era
Vaidya, R., & Witzig, T. E. (2014) · Annals of Oncology · doi:10.1093/annonc/mdu109 · Cited by 187 · see citing works
Zhang, J., Jackson, A. F., Naito, T., Dose, M., Seavitt, J. R., Liu, F., Heller, E. J., Kashiwagi, M., Yoshida, T., Gounari, F., et al. (2011) · Nature Immunology · doi:10.1038/ni.2150 · Cited by 178 · see citing works
Zhang, L., Kosek, J., Wang, M., Heise, C. C., Schafer, P. H., & Chopra, R. (2012) · British Journal of Haematology · doi:10.1111/bjh.12172 · Cited by 167 · see citing works
Self-citationPerry, A. M., Alvarado-Bernal, Y. L., Laurini, J. A., Smith, L. M., Slack, G. W., Tan, K. L., Sehn, L. H., Fu, K., Aoun, P. A., Greiner, T. C., et al. (2014) · British Journal of Haematology · doi:10.1111/bjh.12763 · Cited by 166 · see citing works
Ikaros and Aiolos Inhibit Pre-B-Cell Proliferation by Directly Suppressing c-Myc Expression
Ma, S., Pathak, S., Mandal, M., Trinh, L., Clark, M. R., & Lu, R. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00224-10 · Cited by 138 · see citing works
Mitochondrial localization and pro-apoptotic effects of the interferon-inducible protein ISG12a
Rosebeck, S., & Leaman, D. W. (2008) · APOPTOSIS · doi:10.1007/s10495-008-0190-0 · Cited by 131 · see citing works
Koipally, J., & Georgopoulos, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202079200 · Cited by 72 · see citing works
Farrugia, M. M., Duan, L., Reis, M., Ngan, B., & Berinstein, N. L. (1994) · Blood · doi:10.1182/blood.v83.1.191.191 · Cited by 54 · see citing works
Wang, J., Gu, Q., Li, M., Zhang, W., Yang, M., Zou, B., Chan, S., Qiao, L., Jiang, B., Tu, S., et al. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp155 · Cited by 43 · see citing works
Czuczman, M. S., Davies, A. J., Linton, K., Wagner‐Johnston, N. D., Gascoyne, R. D., Eberhard, D. A., Salles, G., Witzig, T. E., Zinzani, P. L., Wright, G. W., et al. (2014) · Blood · doi:10.1182/blood.v124.21.628.628 · Cited by 20 · see citing works
Silencing of the I l2 gene transcription is regulated by epigenetic changes in anergic T cells
Bandyopadhyay, S., Montagna, C., & Macián, F. (2012) · European Journal of Immunology · doi:10.1002/eji.201142307 · Cited by 19 · see citing works
Relapsed and refractory aggressive NHL: Time for a change
Gangatharan, S. A., & Kuruvilla, J. G. (2013) · Transfusion and Apheresis Science · doi:10.1016/j.transci.2013.05.029 · Cited by 17 · see citing works
Ribrag, V., Damien, S., Gharibo, M. M., Gironella, M., Santoro, A., Rasco, D. W., Edenfield, W. J., Wei, X., James, A. J., Hagner, P. R., et al. (2014) · Blood · doi:10.1182/blood.v124.21.3500.3500 · Cited by 12 · see citing works
Self-citationRasco, D. W., Gandhi, A. K., James, A. J., Li, S., O'Mara, E. M., Chopra, R., DiMartino, J. F., & Shih, K. C. (2013) · Blood · doi:10.1182/blood.v122.21.2905.2905 · Cited by 9 · see citing works
Self-citationHavens, C. G., Bjorklund, C. C., Kang, J., Ortiz, M., Fontanillo, C., Amatangelo, M. D., Lu, L., Neri, P. E., Lopez‐Girona, A., Bahlis, N. J., et al. (2014) · Blood · doi:10.1182/blood.v124.21.3432.3432 · Cited by 4 · see citing works
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- [13]13. Gandhi AK, Kang J, Havens CG, et al. Immunomodulatory agents lenalidomide and pomalidomide co-stimulate T cells by inducing degradation of T cell repressors Ikaros and Aiolos via modulation of the E3 ubiquitin ligase complex CRL4(CRBN.). Br J Haematol. 2014;164(6): 811-821.
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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 · see citing works
“Consistent with our earlier finding that CC-122 and CC-220 were capable of degrading ZFs not affected by pomalidomide, all three thalidomide analogs exhibited distinct ZF degradation patterns across the ZF library (Fig.”
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Dong, G., Ding, Y., He, S., & Sheng, C. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00895 · Cited by 369 · see citing works
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Zhong, G., Chang, X., Xie, W., & Zhou, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02004-x · Cited by 326 · see citing works
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Burslem, G. M., & Crews, C. M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00077 · Cited by 294 · see citing works
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Coiffier, B., & Sarkozy, C. (2016) · Hematology · doi:10.1182/asheducation-2016.1.366 · Cited by 294 · see citing works
Nowakowski, G. S., Chiappella, A., Gascoyne, R. D., Scott, D. W., Zhang, Q., Jurczak, W. J., Özcan, M., Hong, X., Zhu, J., Jin, J., et al. (2021) · Journal of Clinical Oncology · doi:10.1200/jco.20.01366 · Cited by 280 · see citing works
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Sasso, J. M., Tenchov, R., Wang, D.-S., Johnson, L. S., Wang, X., & Zhou, Q. A. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00245 · Cited by 259 · see citing works
Surka, C., Jin, L., Mbong, N., Lu, C.-C., Jang, I. S., Rychak, E., Mendy, D., Clayton, T., Tindall, E., Hsu, C., et al. (2021) · Blood · doi:10.1182/blood.2020008676 · Cited by 229 · see citing works
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Bondeson, D. P., & Crews, C. M. (2017) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010715-103507 · Cited by 207 · see citing works
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Wu, T., Yoon, H., Xiong, Y., Dixon-Clarke, S. E., Nowak, R. P., & Fischer, E. S. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0438-0 · Cited by 188 · see citing works
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Min, J., Mayasundari, A., Keramatnia, F., Jonchère, B., Yang, S. W., Jarusiewicz, J., Actis, M., Das, S., Young, B. M., Slavish, J., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202108848 · Cited by 182 · see citing works
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Camicia, R., Winkler, H. C., & Hassa, P. O. (2015) · Molecular Cancer · doi:10.1186/s12943-015-0474-2 · Cited by 169 · see citing works
Czuczman, M. S., Trněný, M., Davies, A. J., Rule, S. A., Linton, K., Wagner‐Johnston, N. D., Gascoyne, R. D., Slack, G. W., Brousset, P., Eberhard, D. A., et al. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-2818 · Cited by 163 · see citing works
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Collins, I., Wang, H., Caldwell, J., & Chopra, R. (2017) · Biochemical Journal · doi:10.1042/bcj20160762 · Cited by 135 · see citing works
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Asatsuma-Okumura, T., Ando, H., De Simone, M., Yamamoto, J., Sato, T., Shimizu, N., Asakawa, K., Yamaguchi, Y., Ito, T., Guerrini, L., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0366-7 · Cited by 134 · see citing works
Sievers, Q. L., Gasser, J. A., Cowley, G. S., Fischer, E. S., & Ebert, B. L. (2018) · Blood · doi:10.1182/blood-2018-01-821769 · Cited by 124 · see citing works
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Ito, T., & Handa, H. (2020) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.96.016 · Cited by 121 · see citing works
Poggi, A. D., Varesano, S., & Zocchi, M. R. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00262 · Cited by 111 · see citing works
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Gao, S., Wang, S., & Song, Y. (2020) · Biomarker Research · doi:10.1186/s40364-020-0182-y · Cited by 95 · see citing works
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Yang, K., Zhao, Y., Nie, X., Wu, H., Wang, B., Almodóvar‐Rivera, C. M., Xie, H., & Tang, W. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.04.008 · Cited by 82 · see citing works
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Carpio, C., Bouabdallah, R., Ysebaert, L., Sancho, J.-M., Salles, G., Cordoba, R., Pinto, A., Gharibo, M., Rasco, D., Panizo, C., et al. (2020) · Blood · doi:10.1182/blood.2019002395 · Cited by 72 · see citing works
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Yamanaka, S., Furihata, H., Yanagihara, Y., Taya, A., Nagasaka, T., Usui, M., Nagaoka, K., Shoya, Y., Nishino, K., Yoshida, S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40385-9 · Cited by 73 · see citing works
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Sun, Q., Wang, H., Xie, J., Wang, L., Mu, J., Li, J., Ren, Y., & Lai, L. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00969 · Cited by 69 · see citing works
Sperling, A. S., Burgess, M. W., Keshishian, H., Gasser, J. A., Bhatt, S., Jan, M., Slabicki, M. M., Sellar, R. S., Fink, E. C., Miller, P. G., et al. (2019) · Blood · doi:10.1182/blood.2019000789 · Cited by 65 · see citing works
Ito, T., Yamaguchi, Y., & Handa, H. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.012 · Cited by 60 · see citing works
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Norris, S. H., Ba, X., Rhodes, J., Huang, D., Khambatta, G., Buenviaje, J., Nayak, S. K., Meiring, J., Reiss, S. M., Xu, S., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01848 · Cited by 61 · see citing works
Self-citationGeiger, T. M., Schäfer, S. C., Dreizler, J. K., Walz, M., & Hausch, F. (2021) · Current Research in Chemical Biology · doi:10.1016/j.crchbi.2021.100018 · Cited by 55 · see citing works
Akuffo, A. A., Alontaga, A. Y., Metcalf, R. S., Beatty, M. S., Becker, A., McDaniel, J. M., Hesterberg, R. S., Goodheart, W. E., Gunawan, S., Ayaz, M., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.816868 · Cited by 55 · see citing works
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Davis, D. A., Mishra, S., Anagho, H. A., Aisabor, A. I., Shrestha, P., Wang, V., Takamatsu, Y., Maeda, K., Mitsuya, H., Zeldis, J. B., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.17960 · Cited by 54 · see citing works
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Lindner, S., & Krönke, J. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1450-z · Cited by 50 · see citing works
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Carnevale, J. C., & Rubenstein, J. L. (2016) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2016.07.013 · Cited by 51 · see citing works
The IKZF1–IRF4/IRF5 Axis Controls Polarization of Myeloma-Associated Macrophages
Mougiakakos, D., Bach, C., Böttcher, M., Beier, F., Röhner, L., Stoll, A., Rehli, M., Gebhard, C., Lischer, C., Eberhardt, M., et al. (2021) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-20-0555 · Cited by 50 · see citing works
Ioannou, N., Hagner, P. R., Stokes, M., Gandhi, A. K., Apollonio, B., Fanous, M., Papazoglou, D., Sutton, L., Rosenquist, R., Amini, R., et al. (2020) · Blood · doi:10.1182/blood.2020006073 · Cited by 49 · see citing works
Self-citationInvestigational drugs for the treatment of diffuse large B-cell lymphoma
Patriarca, A., & Gaïdano, G. (2020) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2021.1855140 · Cited by 47 · see citing works
Molecular glues to stabilise protein–protein interactions
Soini, L., Leysen, S., Davis, J., & Ottmann, C. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102169 · Cited by 49 · see citing works
Čermáková, K., & Hodges, H. C. (2018) · Molecules · doi:10.3390/molecules23081958 · Cited by 49 · see citing works
Chiu, H., Trisal, P., Bjorklund, C. C., Carrancio, S., Toraño, E. G., Guarinós, C., Papazoglou, D., Hagner, P. R., Beldi‐Ferchiou, A., Tarte, K., et al. (2019) · British Journal of Haematology · doi:10.1111/bjh.15797 · Cited by 48 · see citing works
Self-citationAvadomide Induces Degradation of ZMYM2 Fusion Oncoproteins in Hematologic Malignancies
Renneville, A., Gasser, J. A., Grinshpun, D. E., Beltran, P. M. J., Udeshi, N. D., Matyskiela, M. E., Clayton, T., McConkey, M. E., Viswanathan, K., Tepper, A., et al. (2021) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-20-0105 · Cited by 48 · see citing works
Potential of E3 Ubiquitin Ligases in Cancer Immunity: Opportunities and Challenges
Ye, P., Chi, X., Cha, J., Luo, S., Yang, G., Yan, X., & Yang, W. (2021) · Cells · doi:10.3390/cells10123309 · Cited by 49 · see citing works
Activity of lenalidomide in mantle cell lymphoma can be explained by NK cell‐mediated cytotoxicity
Hagner, P. R., Chiu, H., Ortiz, M., Apollonio, B., Wang, M., Couto, S. S., Waldman, M. F., Flynt, E., Ramsay, A. G., Trotter, M. W. B., et al. (2017) · British Journal of Haematology · doi:10.1111/bjh.14866 · Cited by 47 · see citing works
Self-citationMechanisms of lenalidomide sensitivity and resistance
Martínez-Høyer, S., & Karsan, A. (2020) · Experimental Hematology · doi:10.1016/j.exphem.2020.09.196 · Cited by 45 · see citing works
Routes to molecular glue degrader discovery
Liu, Y., Bai, J., Li, D., & Cang, Y. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.12.006 · Cited by 45 · see citing works
Davis, D. A., Shrestha, P., Aisabor, A. I., Stream, A., Galli, V., Pise-Masison, C. A., Tagawa, T., Ziegelbauer, J. M., Franchini, G., & Yarchoan, R. (2018) · OncoImmunology · doi:10.1080/2162402x.2018.1546544 · Cited by 43 · see citing works
Repurposing DNA repair factors to eradicate tumor cells upon radiotherapy
Bhattacharya, S., & Asaithamby, A. (2017) · Translational Cancer Research · doi:10.21037/tcr.2017.05.22 · Cited by 42 · see citing works
Identification and selectivity profiling of small-molecule degraders via multi-omics approaches
Scholes, N. S., Mayor‐Ruiz, C., & Winter, G. E. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.03.007 · Cited by 41 · see citing works
Kotb, A. R., Bakhotmah, D. A., Abdallah, A. E., Elkady, H., Taghour, M. S., Eissa, I. H., & El‐Zahabi, M. A. (2022) · RSC Advances · doi:10.1039/d2ra06188k · Cited by 40 · see citing works
Immunomodulatory Drugs for the Treatment of B Cell Malignancies
Ioannou, N., Jain, K., & Ramsay, A. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168572 · Cited by 40 · see citing works
Discovery of novel BTK PROTACs with improved metabolic stability via linker rigidification strategy
Chen, S., Chen, Z., Lu, L., Zhao, Y., Zhou, R., Xie, Q., Shu, Y., Lin, J., Yu, X., & Wang, Y. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115403 · Cited by 39 · see citing works
Abdallah, A. E., Eissa, I. H., Mehany, A. B. M., Sakr, H. M., Atwa, A., El‐Adl, K., & El‐Zahabi, M. A. (2023) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2023.135164 · Cited by 39 · see citing works
Applications of protein ubiquitylation and deubiquitylation in drug discovery
Chen, Y., Xue, H., & Jin, J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107264 · Cited by 37 · see citing works
Molecular glue degraders: exciting opportunities for novel drug discovery
Lemaitre, T., Cornu, M., Schwalen, F., Since, M., Kieffer, C., & Voisin-Chiret, A. S. (2024) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2024.2306845 · Cited by 36 · see citing works
Krasavin, M., Adamchik, M., Bubyrev, A. I., Heim, C., Maiwald, S. A., Zhukovsky, D., Zhmurov, P. A., Bunev, A. S., & Hartmann, M. D. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114990 · Cited by 36 · see citing works
Phillips, T. J., Michot, J., & Ribrag, V. (2020) · Clinical Lymphoma Myeloma & Leukemia · doi:10.1016/j.clml.2020.08.022 · Cited by 34 · see citing works
Michot, J., Bouabdallah, R., Vitolo, U., Doorduijn, J. K., Salles, G., Chiappella, A., Zinzani, P. L., Bijou, F. D., Kersten, M. J., Sarmiento, R., et al. (2020) · The Lancet Haematology · doi:10.1016/s2352-3026(20)30208-8 · Cited by 32 · see citing works
Self-citationTargeted Protein Degradation: Clinical Advances in the Field of Oncology
Salama, A. K. A. A., Trkulja, M. V., Casanova, E., & Uras, I. Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315440 · Cited by 32 · see citing works
Li, J., Li, C., Zhang, Z., Zhang, Z., Wu, Z., Liao, J., Wang, Z., McReynolds, M. G., Xie, H., Guo, L., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115567 · Cited by 30 · see citing works
Yamshon, S., & Ruan, J. (2019) · Current Hematologic Malignancy Reports · doi:10.1007/s11899-019-00536-6 · Cited by 30 · see citing works
Fu, L., Zhang, J., Shen, B., Kong, L., Liu, Y., Tu, W., Wang, W., Cai, X., Wang, X., Cheng, N., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00103 · Cited by 29 · see citing works
Progress of small molecules for targeted protein degradation: PROTACs and other technologies
Zhao, H., Xin, M., & Zhang, S. (2023) · Drug Development Research · doi:10.1002/ddr.22026 · Cited by 31 · see citing works
Patil, A., Manzano, M., & Gottwein, E. (2019) · Blood Advances · doi:10.1182/bloodadvances.2019031732 · Cited by 29 · see citing works
Ege, N., Bouguenina, H., Tatari, M. N., & Chopra, R. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.02.011 · Cited by 30 · see citing works
Self-citationA FRET-Based Assay for the Identification and Characterization of Cereblon Ligands
Boichenko, I., Deiss, S., Bär, K., Hartmann, M. D., & Alvarez, B. H. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01735 · Cited by 29 · see citing works
The application of ubiquitin ligases in the PROTAC drug design
Chen, Y., & Jin, J. (2020) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmaa053 · Cited by 28 · see citing works
Feng, Y., Hu, X., & Wang, X. (2024) · Biomarker Research · doi:10.1186/s40364-024-00638-1 · Cited by 27 · see citing works
Understanding the Immune-Stroma Microenvironment in B Cell Malignancies for Effective Immunotherapy
Apollonio, B., Ioannou, N., Papazoglou, D., & Ramsay, A. G. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.626818 · Cited by 26 · see citing works
Takwale, A. D., Kim, E. Y., Jang, Y., Lee, D.-H., Kim, S., Choi, Y., Kim, J. H., Lee, D. Y., Kim, Y., Lee, S. M., et al. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.105923 · Cited by 25 · see citing works
Treatment of Lymphoid and Myeloid Malignancies by Immunomodulatory Drugs
Fuchs, O. (2018) · Cardiovascular & Haematological Disorders - Drug Targets · doi:10.2174/1871529x18666180522073855 · Cited by 26 · see citing works
Mabrouk, R. R., Abdallah, A. E., Mahdy, H. A., El-Kalyoubi, S. A., Kamal, O., Abdelghany, T. M., Zayed, M. F., Alshaeri, H. K., Alasmari, M. M., & El‐Zahabi, M. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512416 · Cited by 24 · see citing works
CC-122 immunomodulatory effects in refractory patients with diffuse large B-cell lymphoma
Cubillos‐Zapata, C., Córdoba, R., Ortiz, J. A., Arribas-Jiménez, C., Hernández-Jiménez, E., Toledano, V., Villaescusa, T., Moreno, V., & López‐Collazo, E. (2016) · OncoImmunology · doi:10.1080/2162402x.2016.1231290 · Cited by 23 · see citing works
Tong, K. I., Yoon, S., Isaev, K., Bakhtiari, M., Lackraj, T., He, M. Y., Joynt, J., Silva, A., Xu, M. C., Privé, G. G., et al. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-20-4027 · Cited by 23 · see citing works
Crbn-based molecular Glues: Breakthroughs and perspectives
An, J., & Zhang, X. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117683 · Cited by 22 · see citing works
Novel Targets for the Treatment of Melanoma
Ambrosi, L., Khan, S., Carvajal, R., & Yang, J. (2019) · Current Oncology Reports · doi:10.1007/s11912-019-0849-4 · Cited by 19 · see citing works
Cereblon harnesses Myc-dependent bioenergetics and activity of CD8+ T lymphocytes
Hesterberg, R. S., Beatty, M. S., Han, Y., Fernandez, M. R., Akuffo, A. A., Goodheart, W. E., Yang, C., Chang, S., Colin, C., Alontaga, A. Y., et al. (2020) · Blood · doi:10.1182/blood.2019003257 · Cited by 22 · see citing works
Geng, C., Chen, J., Song, T., Jung, J. H., Long, M., Song, M., Ji, T., Min, B. S., Lee, J. G., Peng, B., et al. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.05.012 · Cited by 21 · see citing works
SimPLIT: Simplified Sample Preparation for Large-Scale Isobaric Tagging Proteomics
Sialana, F. J., Roumeliotis, T. I., Bouguenina, H., Hak, L. C. W., Wang, H., Caldwell, J., Collins, I., Chopra, R., & Choudhary, J. S. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00092 · Cited by 21 · see citing works
Self-citationFacilitating 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
Stokes, M. E., Wenzl, K., Huang, C. C., Ortiz, M., Hsu, C.-C., Maurer, M. J., Stong, N., Nakayama, Y., Wu, L., Chiu, H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50830-y · Cited by 23 · see citing works
Self-citationLin, W., Li, Y., Min, J., Liu, J., Yang, L., Lee, R. E., Jr., & Chen, T. (2020) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.0c00507 · Cited by 21 · see citing works
Deciphering the mechanisms of CC-122 resistance in DLBCL via a genome-wide CRISPR screen
Mo, Z., Wood, S., Namiranian, S., Mizukoshi, R., Weng, S., Jang, I. S., Fontanillo, C., Baughman, J. M., Silva-Torres, A., Slade, M., et al. (2021) · Blood Advances · doi:10.1182/bloodadvances.2020003431 · Cited by 21 · see citing works
Self-citationKim, S. Y., Lee, J. Y., Jhin, C., Shin, J. M., Kim, M., Ahn, H. R., Yoo, G., Son, Y., Jung, S. H., & Nho, C. W. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b01488 · Cited by 20 · see citing works
Reshaping the tumor microenvironment: The versatility of immunomodulatory drugs in B-cell neoplasms
Guo, H., Yang, J., Wang, H., Liu, X., Liu, Y., & Zhou, K. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1017990 · Cited by 21 · see citing works
Recent Advances in the Applications of Small Molecules in the Treatment of Multiple Myeloma
Abramson, H. N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032645 · Cited by 20 · see citing works
Guo, L., Lin, P., Xiong, H., Tu, S., & Chen, G. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.01.001 · Cited by 19 · see citing works
- Authors
- Hagner, P. R., Man, H.-W., Fontanillo, C., Wang, M., Couto, S., Breider, M., Bjorklund, C., Havens, C. G., Lu, G., Rychak, E., Raymon, H., Narla, R. K., Barnes, L., Khambatta, G., Chiu, H., Kosek, J., Kang, J., Amantangelo, M. D., Waldman, M., Lopez-Girona, A., Cai, T., Pourdehnad, M., Trotter, M., Daniel, T. O., Schafer, P. H., Klippel, A., Thakurta, A., Chopra, R., & Gandhi, A. K.
- Affiliations
- Celgene (United States) (US)
- Celgene Corporation, Sevilla, Spain;
- Celgene Corporation, San Diego, CA; and
- Celgene Corporation, San Francisco, CA
- ORCID
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2015-08-06
- Volume
- 126
- Issue
- 6
- Pages
- 779-789
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC4528065
- OpenAlex
- W1628369270
- Cited by
- 203
- References
- 36
- Citations by year
- 2026: 9 · 2025: 20 · 2024: 20 · 2023: 24 · 2022: 21 · 2021: 30 · 2020: 24 · 2019: 12 · 2018: 18 · 2017: 12 · 2016: 11 · 2015: 2
- FWCI
- 6.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Cancer Research UK (11566)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Health Sciences › Medicine › Pathology and Forensic Medicine › Lymphoma Diagnosis and Treatment
- Health Sciences › Medicine › Genetics › Chronic Lymphocytic Leukemia Research
- Keywords
- cereblon, lenalidomide, pomalidomide, Aiolos, Ikaros, diffuse large B-cell lymphoma, interferon-stimulated genes, interferon response, ubiquitination, protein degradation, apoptosis, germinal center B-cell DLBCL, T cells, immunomodulators
- MeSH terms
- Lenalidomide, Animals, Antineoplastic Agents, B-Lymphocytes, Humans, Interferons, Peptide Hydrolases, Piperidones, T-Lymphocytes, Thalidomide, Signal Transduction, Gene Expression Regulation, Neoplastic, Lentivirus, Lymphoma, Large B-Cell, Diffuse, Mice, SCID, Molecular Mimicry, Xenograft Model Antitumor Assays, RNA, Small Interfering, Ubiquitin-Protein Ligases, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, Interferon Regulatory Factor-7, Mice, Ikaros Transcription Factor, Quinazolinones, Proteolysis
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