CC-122, a pleiotropic pathway modifier, mimics an interferon response and has antitumor activity in DLBCL

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

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

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 1,847

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

Long-Term Results of the R-CHOP Study in the Treatment of Elderly Patients With Diffuse Large B-Cell Lymphoma: A Study by the Groupe d'Etude des Lymphomes de l'Adulte

Feugier, 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 1,487

New approach to classifying non-Hodgkin's lymphomas: clinical features of the major histologic subtypes. Non-Hodgkin's Lymphoma Classification Project.

Armitage, J. O., & Weisenburger, D. D. (1998) · Journal of Clinical Oncology · doi:10.1200/jco.1998.16.8.2780 · Cited by 1,259

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

Determining cell-of-origin subtypes of diffuse large B-cell lymphoma using gene expression in formalin-fixed paraffin-embedded tissue

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 639

Immunomodulatory agents lenalidomide and pomalidomide co‐stimulate Tcells by inducing degradation of Tcell repressors Ikaros and Aiolos via modulation of the E 3 ubiquitin ligase complex CRL 4 CRBN

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

Rearrangement of MYC Is Associated With Poor Prognosis in Patients With Diffuse Large B-Cell Lymphoma Treated in the Era of Rituximab

Barrans, 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

Leveraging Gene Expression Subgroups to Classify DLBCL Patients and Enrich for Clinical Benefit to a Novel Agent

Risueño, A., Hagner, P. R., Towfic, F., Fontanillo, C., Djebbari, A., Parker, J. S., Drew, C. P., Nowakowski, G. S., Maurer, M. J., Cerhan, J. R., et al. (2020) · Blood · doi:10.1182/blood.2019002414 · Cited by 19

High-resolution structures of the bound effectors avadomide (CC-122) and iberdomide (CC-220) highlight advantages and limitations of the MsCI4 soaking system

Heim, C., & Hartmann, M. D. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322000092 · Cited by 20

Trends in Neosubstrate Degradation by Cereblon-Based Molecular Glues and the Development of Novel Multiparameter Optimization Scores

Szewczyk, S. M., Verma, I., Edwards, J. T., Weiss, D. R., & Chekler, E. L. P. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01872 · Cited by 20

Follicular lymphoma comprises germinal center–like and memory-like molecular subtypes with prognostic significance

Laurent, C., Trisal, P., Tesson, B. M., Seth, S., Beyou, A., Roulland, S., Lesne, B., Acker, N. V., Cerapio, J., Chartier, L., et al. (2024) · Blood · doi:10.1182/blood.2024024496 · Cited by 18

IRF4 modulates the response to BCR activation in chronic lymphocytic leukemia regulating IKAROS and SYK

Maffei, R., Fiorcari, S., Benatti, S., Atene, C. G., Martinelli, S., Zucchini, P., Potenza, L., Luppi, M., & Marasca, R. (2021) · Leukemia · doi:10.1038/s41375-021-01178-5 · Cited by 18

Recent advances in the pharmacological targeting of ubiquitin-regulating enzymes in cancer

Montagut, A. M., Armengol, M., Gorjón-de-Pablo, G., Estrada‐Tejedor, R., Borrell, J. I., & Roué, G. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.007 · Cited by 17

DESIGN, MOLECULAR MODELING AND SYNTHESIS OF NEW IMMUNOMODULATORY AGENTS FOR BIOLOGICAL STUDIES

El‐Zahabi, M. A. (2021) · Al-Azhar Journal of Pharmaceutical Sciences/Al-Azhar Journal of Pharmaceutical Sciences · doi:10.21608/ajps.2021.187700 · Cited by 16

Exploration of Tumor Biopsy Gene Signatures to Understand the Role of the Tumor Microenvironment in Outcomes to Lisocabtagene Maraleucel

Olson, N. E., Ragan, S. P., Reiss, D. J., Thorpe, J., Kim, Y., Abramson, J. S., McCoy, C., Newhall, K. J., & Fox, B. A. (2023) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0506 · Cited by 16

Development of Phenyl‐substituted Isoindolinone‐ and Benzimidazole‐type Cereblon Ligands for Targeted Protein Degradation

Nie, X., Zhao, Y. Q., Tang, H., Zhang, Z., Liao, J., Almodóvar‐Rivera, C. M., Sundaresan, R., Xie, H., Guo, L., Wang, B., et al. (2023) · ChemBioChem · doi:10.1002/cbic.202300685 · Cited by 17

Cancer vaccines and immunotherapeutic approaches in hepatobiliary and pancreatic cancers

Hochnadel, I., Kossatz-Boehlert, U., Jedicke, N., Lenzen, H., Manns, M. P., & Yevsa, T. (2017) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2017.1359362 · Cited by 16

Key regulators of sensitivity to immunomodulatory drugs in cancer treatment

Wang, S., Li, Z., & Gao, S. (2021) · Biomarker Research · doi:10.1186/s40364-021-00297-6 · Cited by 20

Ikaros Proteins in Tumor: Current Perspectives and New Developments

Xia, R., Cheng, Y., Han, X., Wei, Y., & Wei, X. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.788440 · Cited by 17

Methods to prevent and treat relapse after hematopoietic stem cell transplantation with tyrosine kinase inhibitors, immunomodulating drugs, deacetylase inhibitors, and hypomethylating agents

Chen, Y., McCarthy, P. L., Hahn, T., Holstein, S. A., Ueda, M., Kröger, N. M., Bishop, M. R., & Lima, M. J. G. D. (2018) · Bone Marrow Transplantation · doi:10.1038/s41409-018-0269-3 · Cited by 16

CD20-targeting in B-cell malignancies: novel prospects for antibodies and combination therapies

Safdari, Y., Ahmadzadeh, V., & Farajnia, S. (2016) · Investigational New Drugs · doi:10.1007/s10637-016-0349-4 · Cited by 15

Phase Ib study of avadomide (CC‐122) in combination with rituximab in patients with relapsed/refractory diffuse large B‐cell lymphoma and follicular lymphoma

Nastoupil, L. J., Kuruvilla, J. G., Chávez, J. C., Bijou, F. D., Witzig, T. E., Santoro, A., Flinn, I. W., Boccomini, C., Kenkre, V. P., Corradini, P., et al. (2022) · eJHaem · doi:10.1002/jha2.394 · Cited by 15

Cereblon: promise and challenges for combating human diseases

Kim, H. K., Seol, J. E., Ahn, S. W., Jeon, S., Park, C., & Han, J. (2021) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-021-02624-0 · Cited by 14

Repurposing of thalidomide and its derivatives for the treatment of SARS‐coV‐2 infections: Hints on molecular action

Sundaresan, L., Giri, S., Singh, H., & Chatterjee, S. (2021) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.14792 · Cited by 14

Emerging mechanisms of targeted protein degradation by molecular glues

Frere, G. A., de Araujo, E. D., & Gunning, P. T. (2022) · Methods in cell biology · doi:10.1016/bs.mcb.2022.01.001 · Cited by 13

Phenyl‐Glutarimides: Alternative Cereblon Binders for the Design of PROTACs

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 · doi:10.1002/ange.202108848 · Cited by 15

Development of a Buchwald–Hartwig Amination for an Accelerated Library Synthesis of Cereblon Binders

Lejava, A., Miseo, G. A., Phan, T., Zhu, J., Powers, H. L., Li, J., Mortensen, D. S., Zapf, C. W., Khambatta, G., Buenviaje, J., et al. (2024) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.4c00462 · Cited by 12

Overexpression of CD49d in trisomy 12 chronic lymphocytic leukemia patients is mediated by IRF4 through induction of IKAROS

Fiorcari, S., Benatti, S., Zucchetto, A., Zucchini, P., Gattei, V., Luppi, M., Marasca, R., & Maffei, R. (2019) · Leukemia · doi:10.1038/s41375-018-0296-5 · Cited by 12

Phase I, multicenter, dose‐escalation study of avadomide in adult Japanese patients with advanced malignancies

Hatake, K., Chou, T., Doi, T., Terui, Y., Kato, H., Hirose, T., Seo, S., Pourdehnad, M., Ogaki, Y., Fujimoto, H., et al. (2020) · Cancer Science · doi:10.1111/cas.14704 · Cited by 11

Discovery of Rigid Linker-Based IRAK4 PROTACs with Improved Metabolic Stability for the Treatment of Inflammatory Diseases

Fan, Y., Ma, R., Njobvu, K. M., Wang, Y., Ren, Y., Fu, R., Zhang, C., Liu, F., Jiang, Z., Rao, Y., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01620 · Cited by 11

Targeted Protein Degradation

Mainolfi, N., & Rasmusson, T. (2017) · Annual reports in medicinal chemistry · doi:10.1016/bs.armc.2017.08.005 · Cited by 11

Targeting the ubiquitin pathway in lymphoid malignancies

Li, B., Eichhorn, P. J. A., & Chng, W. J. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216978 · Cited by 10

New immunomodulatory anticancer quinazolinone-based thalidomide analogs: design, synthesis and biological evaluation

Ward, M. M. S. A., Abdallah, A. E., Zayed, M. F., Ayyad, R. R. A., Abdelghany, T. M., Bakhotmah, D. A., & El‐Zahabi, M. A. (2024) · Future Medicinal Chemistry · doi:10.1080/17568919.2024.2419361 · Cited by 9

Open resources for chemical probes and their implications for future drug discovery

Balıkçı, E., Marques, A.-S. M. C., Hansen, J. S., & Huber, K. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2199979 · Cited by 11

Immunomodulation by durvalumab and pomalidomide in patients with relapsed/refractory multiple myeloma

Young, M. H., Pietz, G. E., Whalen, E., Copeland, W. B., Thompson, E. G., Fox, B. A., & Newhall, K. J. (2021) · Scientific Reports · doi:10.1038/s41598-021-95902-x · Cited by 9

New drugs in early development for treating multiple myeloma: all that glitters is not gold

Bertamini, L., Bonello, F., Boccadoro, M., & Bringhen, S. (2020) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2020.1772753 · Cited by 9

Discovery of Novel Potent Triple IKZF1/2/3 Degraders for the Treatment of Hematological Cancers

Wei, T., Sun, S., Hu, X., Wei, P., Fan, Z., Yan, J. W., Wang, Y., Qi, Z., Jia, C., Mao, Y., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01086 · Cited by 9

Modular PROTAC/IMiD Bifunctional Molecule Design for the Degradation of Synergistic Targets in the Treatment of Lymphoma

Jin, Y., Liao, X., Zhang, J., Duan, H., Xu, R., Luo, X., Yu, X., Li, B., Wang, J., Li, X., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01159 · Cited by 9

Application and progress of CRISPR/Cas9 gene editing in B-cell lymphoma: a narrative review

Jin, Y., Wu, H., Liu, J., Cho, W. C. S., & Song, G. (2024) · Translational Cancer Research · doi:10.21037/tcr-23-1146 · Cited by 7

Discovery of novel benzosultam CRBN ligands

Park, H., Raikar, S. S., Kim, Y., Chae, C. H., Cho, Y., & Kim, P. (2025) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.12921 · Cited by 7

Discovery of New Immunomodulatory Anticancer Thalidomide Analogs: Design, Synthesis, Biological Evaluation and In Silico Studies

Abdallah, A. E., Eissa, I. H., Mehany, A. B. M., Celik, I., Sakr, H. M., Metwaly, K. H., El‐Adl, K., & El‐Zahabi, M. A. (2024) · Chemistry & Biodiversity · doi:10.1002/cbdv.202401768 · Cited by 7

Phase Ib study of combinations of avadomide (CC‐122), CC‐223, CC‐292, and rituximab in patients with relapsed/refractory diffuse large B‐cell lymphoma

Ribrag, V., Chávez, J. C., Boccomini, C., Kaplan, J. B., Chandler, J. C., Santoro, A., Corradini, P., Flinn, I. W., Advani, R. H., Cassier, P. A., et al. (2022) · eJHaem · doi:10.1002/jha2.375 · Cited by 7

Meta-Analysis of MS-Based Proteomics Studies Indicates Interferon Regulatory Factor 4 and Nucleobindin1 as Potential Prognostic and Drug Resistance Biomarkers in Diffuse Large B Cell Lymphoma

Ejtehadifar, M., Zahedi, S., Gameiro, P., Cabeçadas, J., da Silva, M. G., Beck, H. C., Carvalho, A. S., & Matthiesen, R. (2023) · Cells · doi:10.3390/cells12010196 · Cited by 7

Combination therapy with the type II anti-CD20 antibody obinutuzumab

Klein, C., Bacac, M., Umaña, P., & Fingerle‐Rowson, G. (2017) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2017.1373087 · Cited by 7

Drug‐Drug Interaction Study to Assess the Effect of Cytochrome P450 Inhibition and Induction on the Pharmacokinetics of the Novel Cereblon Modulator Avadomide (CC‐122) in Healthy Adult Subjects

Ogasawara, K., MacGorman, K., Liu, L., Chen, J., Carayannopoulos, L. N., Zhou, S. Y., Palmisano, M., & Li, Y. (2019) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.1453 · Cited by 7

Design and Applications of Bifunctional Small Molecules in Biology

Boyd, S. R., Chang, L., de Rezende, W. C., Raji, I. O., Kandel, P., Holmes, S. L., & Young, D. W. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140534 · Cited by 7

Recent Advances in Targeted Protein Degradation Molecular Glues as Anticancer Drugs

Shen, Y., Wen, W., Chen, L., Zhang, N., Wei, C., & Hu, H. (2025) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.70064 · Cited by 7

Golcadomide: An Oral CELMoD Agent Targeting IKZF1/3 for Diffuse Large B-cell Lymphoma

Mo, Z., Groocock, L., Wood, S., Jankeel, D., Mendy, D., Watson, E. R., Yan, K., Deb, G., Côte, M., Janardhanan, P., et al. (2025) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-25-0059 · Cited by 6

Design, synthesis and biological evaluation of novel quinazolinone derivatives as CRBN E3 ligase modulators

Liu, L., Sun, R., Liu, H., Ren, C., Zhou, Y., Qiu, X., Kong, Y., Jiang, B., & Yang, X. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.115016 · Cited by 6

Evolution: IMiDs to PPMs, revolution in DLBCL?

Nowakowski, G. S. (2015) · Blood · doi:10.1182/blood-2015-06-649483 · Cited by 6

Interactome of Aiolos/Ikaros Reveals Combination Rationale of Cereblon Modulators with HDAC Inhibitors in DLBCL

Hagner, P. R., Chiu, H., Chopra, V. S., Colombo, M., Patel, N., Estévez, M. O., Waldman, M. F., Loos, R., Towfic, F., & Gandhi, A. K. (2022) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-3347 · Cited by 6

Discovery of the target for immunomodulatory drugs (IMiDs).

Ito, T., Ando, H., & Handa, H. (2016) · PubMed · doi:10.11406/rinketsu.57.556 · Cited by 7

Design, synthesis, and biological evaluation of a novel series of 2-(2,6-dioxopiperidin-3-yl)isoquinoline-1,3(2 H ,4 H )-dione derivatives as cereblon modulators

Liu, Y., Song, Y., Xu, Y., Jiang, M., & Lu, H. (2022) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2022.2087219 · Cited by 5

Exposure-response analysis to assess concentration–QTc relationship of CC-122

Li, Y., Carayannopoulos, L. N., Thomas, M. A., Palmisano, M., & Zhou, S. Y. (2016) · Clinical Pharmacology Advances and Applications · doi:10.2147/cpaa.s111867 · Cited by 5

Immunomodulatory drugs and their therapeutic effect in hematological malignancies through cereblon

Fuchs, O. (2017) · Hematology & Medical Oncology · doi:10.15761/hmo.1000129 · Cited by 5

Inducing or enhancing protein-protein interaction to develop drugs: Molecular glues with various biological activity

Zhang, R., Zheng, Y., Xiang, F., & Zhou, J. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116756 · Cited by 5

Identification of small molecule agonists of fetal hemoglobin expression for the treatment of sickle cell disease

Yang, J.-P., Toughiri, R., Gounder, A. P., Scheibe, D., Petrus, M. J., Fink, S. J., Vallée, S., Kenniston, J. A., Papaioannou, N., Langston, S., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0307049 · Cited by 5

Significance of Selective Protein Degradation in the Development of Novel Targeted Drugs and Its Implications in Cancer Therapy

Yang, J., Wang, Q.-L., Feng, G., & Zeng, M. (2020) · Advanced Therapeutics · doi:10.1002/adtp.201900210 · Cited by 4

High-content imaging of primary chronic lymphocytic leukemia cells predicts patient cohorts with distinct cellular drug responses

Li, X., Brito, G. C., Ylanko, J., Buzina, A., Leber, B. F., Usta, S., Tsui, H., Spaner, D., & Andrews, D. W. (2025) · iScience · doi:10.1016/j.isci.2025.114216 · Cited by 3

Bruton Tyrosine Kinase Degraders in B-Cell Malignancies

Huynh, T., Rodrı́guez, S., & Danilov, A. V. (2024) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-23-0520 · Cited by 4

Prognostication of Primary Tumor Location in Early-Stage Nodal Diffuse Large B-Cell Lymphoma: An Analysis of the SEER Database

Xia, Y., Huang, S., Wang, Y., Lei, D., Wang, Y., Yang, H., Gao, Y., & Liu, P. (2021) · Cancers · doi:10.3390/cancers13163954 · Cited by 3

Anti-tumor effect of avadomide in gemcitabine-resistant pancreatic ductal adenocarcinoma

Nishi, H., Gotoh, K., Tomimaru, Y., Kobayashi, S., Sasaki, K., Iwagami, Y., Yamada, D., Akita, H., Asaoka, T., Noda, T., et al. (2023) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-023-04531-w · Cited by 3

Recent Developments in Ocular Oncology

Damato, B. E. (2019) · Springer eBooks · doi:10.1007/978-3-030-25389-9_10 · Cited by 3

Tumor Vasculature Targeted TNFα Therapy: Reversion of Microenvironment Anergy and Enhancement of the Anti-tumor Efficiency

Balza, E., Carnemolla, B., Orecchia, P., Rubartelli, A., Poggi, A. D., & Mortara, L. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180904121118 · Cited by 3

Evaluating the Role of CAR-T Cell Therapy in the Context of Current Therapy Options for Patients With Relapsed or Refractory Follicular Lymphoma

Chávez, J. C., Hoffmann, M. S., & Popplewell, L. L. (2025) · Transplantation and Cellular Therapy · doi:10.1016/j.jtct.2025.06.013 · Cited by 2

Optimization and Evaluation of Complementary Degrader Discovery Assays for Application in Screening

Huchting, J., Weller, A., Schweizer, M., Brandt, M., Heering, J., Kuzikov, M., Wolf, M., Reinshagen, J., Queisser, M. A., Gribbon, P. M., et al. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00195 · Cited by 2

Evolving CRBN ligands enhance the drug-like properties of protein degraders

Ji, X.-Q., Wang, L., & Dai, X. (2026) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2026.2700038 · Cited by 2

[Research Progress on the Mechanism and Clinical Data of Cereblon in Reversing the Resistance of Lung Cancer to PD-1 Antibody by T cells].

Guo, J., Mu, D., & Han, Y. (2021) · PubMed Central · doi:10.3779/j.issn.1009-3419.2020.102.49 · Cited by 2

Targeted Protein Degradation: "The Gold Rush is On!"

Kotlarek, D., Pawlik, A., Sagan, M., Sowała, M., Zawiślak-Architek, A., & Walczak, M. (2020) · Technology Transfer and Entrepreneurship · doi:10.2174/2213809907666200130111436 · Cited by 2

A Cryptic Interfacial Pocket Uncovered in Full CRL4 CRBN –IKZF3 Ubiquitylation Complex Enhances IMiD EfficacyPreprint

Deng, Z., Ai, H., Shi, Q., Liang, J., He, Z., Zheng, J., Li, H., Zhang, L., He, W., Tao, S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.08.658527 · Cited by 2

NATURALLY OCCURRING AND SYNTHETIC IMMUNOMODULATORS WITH DIFFERENT BIOLOGICAL ACTIVITIES: LITERATURE SURVEY AND HISTORICAL INSIGHT

El‐Zahabi, M. A. (2021) · Al-Azhar Journal of Pharmaceutical Sciences/Al-Azhar Journal of Pharmaceutical Sciences · doi:10.21608/ajps.2021.187750 · Cited by 1

E3 ubiquitin ligase components in GtoPdb v.2022.1

Faccenda, E., & Layfield, R. (2022) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f1023/2022.1 · Cited by 1

E3 ubiquitin ligase components in GtoPdb v.2022.3

Faccenda, E., & Layfield, R. (2022) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f1023/2022.3 · Cited by 1

E3 ubiquitin ligase components in GtoPdb v.2023.2

Faccenda, E., & Layfield, R. (2023) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f1023/2023.2 · Cited by 1

Computational approaches enhance the design of molecular glue degraders for undruggable proteins

Deshani, S. G. M. A., Madushani, G. R. D. S., Karunaratne, V., Vinit, K., & Hao, G. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104577 · Cited by 2

The synthetic landscape of cereblon (CRBN) binders: from thalidomide to emerging chemotypes

Rafael, S., Sánchez, C., Whelan, R., Harris, C., Verdaguer, X., Mayor‐Ruiz, C., & Riéra, A. (2026) · Chemical Society Reviews · doi:10.1039/d6cs00247a · Cited by 1

The dual role of Natural Killer cells during tumor progression and angiogenesis: Implications for tumor microenvironment-targeted immunotherapies

Mortara, L., Baci, D., Coco, G., Poggi, A. D., & Bruno, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-824375-6.00014-x · Cited by 1

Discovery of a selective and reversible LSD1 inhibitor with potent anticancer effects in vitro and in vivo

Zhang, X., Liu, J.-Z., Mei, Y.-Y., Zhang, M., & Sun, L. (2025) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2025.2466093 · Cited by 1

History of IMiDs and Protein Degradation as a Pharmacological Modality

Yamamoto, J., Asatsuma‐Okumura, T., Ito, T., Yamaguchi, Y., & Handa, H. (2022) · Wiley eBooks · doi:10.1002/9781119774198.ch8 · Cited by 1

New immunomodulatory anticancer quinazolinone based thalidomide analogs: Design, synthesis and biological evaluationPreprint

Ward, M. M. S. A., Abdallah, A. E., Zayed, M. F., Ayyad, R. R. A., & El‐Zahabi, M. A. (2023) · Research Square · doi:10.21203/rs.3.rs-2916749/v1 · Cited by 1

Application of affinity purification of drug target proteins with practical magnetic nanoparticles to drug development

Ito, T., Sakamoto, S., & Handa, H. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813629-4.00012-7

Investigating the Molecular Mechanisms of Action of Lenalidomide and Other Immunomodulatory Derivatives

Haldar, S. D. (2018) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)

E3 ubiquitin ligase components (version 2019.5) in the IUPHAR/BPS Guide to Pharmacology Database

Faccenda, E., & Layfield, R. (2019) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f1023/2019.5

New Activities of CELMoDs, Cereblon E3 Ligase-modulating Drugs

Matyskiela, M. E., Clayton, T., Thompson, J. W., Carroll, C. W., Bateman, L. A., LeBrun, L. A., & Chamberlain, P. P. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160691-00094

E3 ubiquitin ligase components in GtoPdb v.2021.3

Faccenda, E., & Layfield, R. (2021) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f1023/2021.3

Advances in the Treatment of Non-Hodgkin’s Lymphoma: Exploring New Frontiers

Ibbotson, T. (2016) · EMJ Hematology · doi:10.33590/emjhematol/10312986

Data from Combined EZH2 Inhibition and IKAROS Degradation Leads to Enhanced Antitumor Activity in Diffuse Large B-cell Lymphoma

Tong, K. I., Yoon, S. J., Isaev, K., Bakhtiari, M., Lackraj, T., He, M. Y., Joynt, J., Silva, A., Xu, M. C., Privé, G. G., et al. (2023) · doi:10.1158/1078-0432.c.6530741

Data from Combined EZH2 Inhibition and IKAROS Degradation Leads to Enhanced Antitumor Activity in Diffuse Large B-cell Lymphoma

Tong, K. I., Yoon, S. J., Isaev, K., Bakhtiari, M., Lackraj, T., He, M. Y., Joynt, J., Silva, A., Xu, M. C., Privé, G. G., et al. (2023) · doi:10.1158/1078-0432.c.6530741.v1

Data from 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. (2023) · doi:10.1158/2326-6066.c.6550200

Application and progress of CRISPR Cas9 gene editing in B-cell lymphomaPreprint

Jin, Y., Wu, H., Liu, J., & Song, G. (2023) · doi:10.22541/au.168076273.32417889/v1

E3 ubiquitin ligase components in GtoPdb v.2023.1

Faccenda, E., & Layfield, R. (2023) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f1023/2023.1

Emerging synthetic drugs for the treatment of diffuse large B-cell lymphoma

Dong, N. C., Pérez‐Lamas, L., & Chávez, J. C. (2023) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2023.2250722

Mechanistic Basis and Role of Immunomodulatory Drugs

Gribben, J. G. (2024) · Wiley eBooks · doi:10.1002/9781119824572.ch25

E3 ubiquitin ligase components in GtoPdb v.2023.3

Faccenda, E., & Layfield, R. (2023) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f1023/2023.3

Research Progress of IMiDs as PPI Stabilizer in Protein Degradation

宋, 冰. (2025) · Hans Journal of Medicinal Chemistry · doi:10.12677/hjmce.2025.131006

Dynamic ubiquitination networks in liver cancer: decoding E3 ligases and deubiquitinases as gatekeepers of therapeutic resistance

Xu, N., Tong, Y., Ma, K., Jiang, L., & Zheng, W. (2025) · Medical Oncology · doi:10.1007/s12032-025-02912-0 · Cited by 1

Targeting transcription factors in cancers

Hu, L., Zhang, J., & Wu, X. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00043-1

Progress on molecular glue degraders

Chen, J., Deng, Z., Li, H., & Liu, L. (2025) · Scientia Sinica Chimica · doi:10.1360/ssc-2025-0228

Targeting PRKCN, an Essential Driver Orchestrating mTOR‐IRF4 Axis Independently of Kinase Activity, in Multiple Myeloma

Tang, K., Jiang, D., Ke, P., Bian, X., Zhang, L., Zhang, Y., Zhu, T., Qu, W., Qi, W., Xu, Y., et al. (2026) · Advanced Science · doi:10.1002/advs.202518975

Optimization of novel quinazolinone derivatives as CRBN E3 ligase modulators for enhanced degradative activity and metabolic stability

Chen, P., Peng, H., Liu, C., Li, Y., Yang, T., Li, M., Hu, C., Li, S., Deng, Z., Wang, Z., et al. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.109816

From immunomodulators (IMiDs) to cereblon E3 ligase modulator (CELMoDs): the evolution of cereblon modulators in lymphoma therapy

Saha, A., Jhaveri, K. S., Perini, G. F., & Chávez, J. C. (2026) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2026.2662494

Molecular Glue-Mediated Targeted Protein Degradation: Mechanisms and Therapeutic Potential in Prostate Cancer

郑, 一. (2026) · Journal of Organic Chemistry Research · doi:10.12677/jocr.2026.143033

First demonstration of benzosultam CRBN ligand-mediated PROTACs for BTK and BRD4 degradation

Park, H., Jeun, M., Choi, J. U., Bang, Y., Park, C. H., & Kim, P. (2026) · RSC Medicinal Chemistry · doi:10.1039/d6md00815a

Emerging drug profile: bexobrutideg

Huynh, T. N., Rodriguez‐Rodriguez, S., & Danilov, A. V. (2026) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2026.2743355

BindingDB Entry 50011291: Monomeric Targeted Protein Degraders.

BindingDB (2022) · UC San Diego · doi:10.7270/q2mc93n5

BindingDB Entry 50014745: Discovery of Highly Potent and Selective IRAK1 Degraders to Probe Scaffolding Functions of IRAK1 in ABC DLBCL.

BindingDB (2023) · UC San Diego · doi:10.7270/q2ms3xmh

CC-122 Has Potent Anti-Lymphoma Activity through Destruction of the Aiolos and Ikaros Transcription Factors and Induction of Interferon Response Pathways

Hagner, P. R., Wang, M., Couto, S. S., Breider, M. A., Fontanillo, C., Trotter, M. W. B., Bjorklund, C. C., Havens, C. G., Raymon, H. K., Narla, R. K., et al. (2014) · Blood · doi:10.1182/blood.v124.21.3035.3035 · Cited by 15

CC-122 Has Robust Anti-Proliferative Activity in a Primary Chronic Lymphocytic Leukemia (CLL) Co-Culture Model and Is Superior to Lenalidomide

Blocksidge, J., Glenn, M. A., Gandhi, A. K., Klippel, A., Pourdehnad, M., Chopra, R., & Kalakonda, N. (2014) · Blood · doi:10.1182/blood.v124.21.4682.4682 · Cited by 10

CC-122 Degrades the Lymphoid Transcription Factor Aiolos (IKZF3) By Modulating Cereblon and Shows Clinical Activity in a Phase Ib Study of Subjects with Relapsed or Refractory Non-Hodgkin’s Lymphoma and Multiple Myeloma

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

CC-122 Is a Novel Pleiotropic Pathway Modifier with Potent in Vitro Immunomodulatory and Anti-Angiogenic Properties and in Vivo Anti-Tumor Activity in Hematological Cancers.

Gandhi, A. K., Mendy, D., Parton, A., Wu, L., Kosek, J., Zhang, L., Capone, L., Lopez‐Girona, A., Schafer, P. H., & Chopra, R. (2012) · Blood · doi:10.1182/blood.v120.21.2963.2963 · Cited by 8

Immunomodulatory agents lenalidomide and pomalidomide co‐stimulate Tcells by inducing degradation of Tcell repressors Ikaros and Aiolos via modulation of the E 3 ubiquitin ligase complex CRL 4 CRBN

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