The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
CC-122, a pleiotropic pathway modifier, mimics an interferon response and has antitumor activity in DLBCL
Open accessAbstract
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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“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]
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“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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Cites
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
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 1,487
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
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
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
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
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Items 201–207 of 207
BindingDB (2024) · UC San Diego · doi:10.7270/q2dz0drt
BindingDB Entry 50002775: Inducing protein-protein interactions with molecular glues.
BindingDB (2020) · UC San Diego · doi:10.7270/q21g0px4
BindingDB (2017) · UC San Diego · doi:10.7270/q2pr7xvf
Metadata
- 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 › Hematology › 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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