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Crbn I391V is sufficient to confer in vivo sensitivity to thalidomide and its derivatives in mice
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Key Points: Crbn I391V mice degrade known thalidomide derivative targets and recapitulate thalidomide-induced cytopenias and teratogenicity. Degradation of Ck1α is sufficient to explain the in vivo therapeutic window of lenalidomide in del(5q) myelodysplastic syndrome.
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“In line with these findings, mice harboring a homozygous CRBN I391V knock-in allele, despite exhibiting degradation of mmIKZF1/3, mmZFP91, and mmCSNK1A1 Fink et al., 2018, show increased miscarriage upon IMiD treatment compared with control mice; however, they do not exhibit IMiD-induced embryopathies resembling the human phenotype Fink et al., 2018 .”
From Thalidomide promotes degradation of SALL4, a transcription factor implicated in Duane Radial Ray syndrome (2018) · cites this paper as Fink et al., 2018
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“Intriguingly, this site corresponds to position 391 in mouse Crbn, which features the critical isoleucine variant that is responsible for the lack of IMiD activity in mouse cells, hence masking the teratogenicity of thalidomide39.”
From Functional E3 ligase hotspots and resistance mechanisms to small-molecule degraders (2023) · cites this paper as [39]
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Cites
Thompson, A., Schäfer, J., Kuhn, K., Kienle, S., Schwarz, J., Schmidt, G., Neumann, T., & Hamon, C. (2003) · Analytical Chemistry · doi:10.1021/ac0262560 · Cited by 2,425
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
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
Self-citationThe 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
Lenalidomide in the Myelodysplastic Syndrome with Chromosome 5q Deletion
List, A., Dewald, G., Bennett, J., Giagounidis, A., Raza, A., Feldman, E., Powell, B., Greenberg, P., Thomas, D., Stone, R., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa061292 · Cited by 1,319
Lenalidomide plus Dexamethasone for Relapsed Multiple Myeloma in North America
Weber, D. M., Chen, C., Niesvizky, R., Wang, M., Belch, A., Stadtmauer, E. A., Siegel, D., Borrello, I., Rajkumar, S. V., Chanan-Khan, A. A., et al. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa070596 · Cited by 1,233
Lenalidomide Maintenance after Stem-Cell Transplantation for Multiple Myeloma
Attal, M., Lauwers-Cances, V., Marit, G., Caillot, D., Moreau, P., Facon, T., Stoppa, A. M., Hulin, C., Benboubker, L., Garderet, L., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1114138 · Cited by 1,155
Lenalidomide after Stem-Cell Transplantation for Multiple Myeloma
McCarthy, P. L., Owzar, K., Hofmeister, C. C., Hurd, D. D., Hassoun, H., Richardson, P. G., Giralt, S., Stadtmauer, E. A., Weisdorf, D. J., Vij, R., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1114083 · Cited by 1,147
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
Identification of RPS14 as a 5q- syndrome gene by RNA interference screen
Ebert, B. L., Pretz, J. L., Bosco, J., Chang, C. Y., Tamayo, P., Galili, N., Raza, A., Root, D. E., Attar, E. C., Ellis, S. R., et al. (2008) · Nature · doi:10.1038/nature06494 · Cited by 953
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Donovan, K. A., An, J., Nowak, R. P., Yuan, J. C., Fink, E. C., Berry, B. C., Ebert, B. L., & Fischer, E. S. (2018) · eLife · doi:10.7554/elife.38430 · Cited by 509
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Guo, W., Qi, X., Yu, X., Liu, Y., Chung, C.-I., Bai, F., Lin, X., Lu, D., Wang, L., Chen, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17997-6 · Cited by 228
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Larráyoz, M., Garcia-Barchino, M. J., Celay, J., Etxebeste, A., Jiménez, M., Pérez, C., Ordóñez, R., Cobaleda, C., Botta, C., Fresquet, V., et al. (2023) · Nature Medicine · doi:10.1038/s41591-022-02178-3 · Cited by 93
Yamanaka, S., Murai, H., Saito, D., Abe, G., Tokunaga, E., Iwasaki, T., Takahashi, H., Takeda, H., Suzuki, T., Shibata, N., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020105375 · Cited by 89
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Ito, T., Yamaguchi, Y., & Handa, H. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.012 · Cited by 60
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Metadata
- Authors
- Fink, E. C., McConkey, M., Adams, D. N., Haldar, S. D., Kennedy, J. A., Guirguis, A. A., Udeshi, N. D., Mani, D. R., Chen, M., Liddicoat, B., Svinkina, T., Nguyen, A. T., Carr, S. A., & Ebert, B. L.
- Affiliations
- Broad Institute (US)
- ORCID
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2018-10-04
- Volume
- 132
- Issue
- 14
- Pages
- 1535-1544
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC6172563
- OpenAlex
- W2886628870
- Cited by
- 131
- References
- 62
- Citations by year
- 2026: 19 · 2025: 22 · 2024: 20 · 2023: 13 · 2022: 14 · 2021: 16 · 2020: 16 · 2019: 7 · 2018: 3
- FWCI
- 3.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- Edward P. Evans Foundation
- Henry and Marilyn Taub Foundation
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL082945)
- National Cancer Institute (F30CA199988, P01CA108631, P50CA206963, P01CA066996)
- National Institute of General Medical Sciences (T32GM007753)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Health Sciences › Medicine › Hematology › Multiple Myeloma Research and Treatments
- Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
- Keywords
- thalidomide, lenalidomide, thalidomide derivatives, del(5q) myelodysplastic syndrome, teratogenicity, therapeutic window, E3 ubiquitin ligase
- MeSH terms
- Lenalidomide, Animals, Antineoplastic Agents, Disease Models, Animal, Female, Hematopoiesis, Male, Mice, Inbred C57BL, Myelodysplastic Syndromes, Nerve Tissue Proteins, Thalidomide, Point Mutation, Casein Kinase I, Adaptor Proteins, Signal Transducing, Mice
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