Crbn I391V is sufficient to confer in vivo sensitivity to thalidomide and its derivatives in mice
Open accessAbstract
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.
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?
Mice harboring a homozygous CRBN I391V knock-in allele show increased miscarriage upon IMiD treatment compared with control mice, but do not exhibit IMiD-induced embryopathies resembling the human phenotype.
“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
The ‘Thalidomide-induced fetal loss in Crbn I391V mice’ section (page unavailable) reports high fetal loss after lenalidomide or thalidomide treatment in homozygous knock-in mice, with no effect in wild-type mice. It says surviving litters generally appeared normal, but notes a trend toward increased anophthalmia—a malformation seen in human thalidomide embryopathy. That qualification makes the claim that the mice do not exhibit human-like embryopathies too absolute. (LLM, conf=0.86)
Experimental — accuracy not yet measuredPosition V388 corresponds to position 391 in mouse Crbn, which features the critical isoleucine variant responsible for the lack of IMiD activity in mouse cells, masking thalidomide teratogenicity.
“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]
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
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 2,386 · 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
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · 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
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 925 · see citing works
Self-citationThalidomide-induced Teratogenesis: History and Mechanisms
Vargesson, N. (2015) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.21096 · Cited by 912 · see citing works
Efficacy of Lenalidomide in Myelodysplastic Syndromes
List, A., Kurtin, S., Roe, D. J., Buresh, A., Mahadevan, D., Fuchs, D., Rimsza, L., Heaton, R., Knight, R., & Zeldis, J. B. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa041668 · Cited by 880 · 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
Self-citationA short history of thalidomide embryopathy
Lenz, W. (1988) · Teratology · doi:10.1002/tera.1420380303 · Cited by 786 · see citing works
Continuous Lenalidomide Treatment for Newly Diagnosed Multiple Myeloma
Palumbo, A. P., Hájek, R., Delforge, M., Kropff, M. H., Petrucci, M. T., Catalano, J. V., Gisslinger, H., Wiktor-Jędrzejczak, W., Zodelava, M., Weisel, K. C., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1112704 · Cited by 739 · 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
Thalidomide: The Tragedy of Birth Defects and the Effective Treatment of Disease
Kim, J. H., & Scialli, A. R. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr088 · Cited by 667 · see citing works
Combination therapy with lenalidomide plus dexamethasone (Rev/Dex) for newly diagnosed myeloma
Rajkumar, S. V., Hayman, S. R., Lacy, M. Q., Dispenzieri, A., Geyer, S. M., Kabat, B., Zeldenrust, S. R., Kumar, S., Greipp, P. R., Fonseca, R., et al. (2005) · Blood · doi:10.1182/blood-2005-07-2817 · Cited by 648 · 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
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
Wang, J., Nichogiannopoulou, A., Wu, L. J., Sun, L., Sharpe, A. H., Bigby, M. E., & Georgopoulos, K. (1996) · Immunity · doi:10.1016/s1074-7613(00)80269-1 · Cited by 614 · see citing works
Haslett, P. A. J., Corral, L. G., Albert, M. L., & Kaplan, G. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.11.1885 · Cited by 572 · 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
Fenaux, P., Giagounidis, A. A. N., Selleslag, D., Beyne‐Rauzy, O., Mufti, G. J., Mittelman, M., Muus, P., Boekhorst, P. A. W. T., Sanz, G. F., del Cañizo, C., et al. (2011) · Blood · doi:10.1182/blood-2011-01-330126 · Cited by 488 · see citing works
Mechanism of action of lenalidomide in hematological malignancies
Kotla, V., Goel, S., Nischal, S., Heuck, C. J., Vivek, K., Das, B. C., & Verma, A. K. (2009) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-2-36 · Cited by 466 · see citing works
<i>TP53</i> Mutations in Low-Risk Myelodysplastic Syndromes With del(5q) Predict Disease Progression
Jädersten, M., Saft, L., Smith, A., Kulasekararaj, A., Pomplun, S., Göhring, G., Hedlund, A., Hast, R., Schlegelberger, B., Porwit, A., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2010.31.8576 · Cited by 463 · see citing works
Chanan-Khan, A. A., Miller, K. C., Musial, L., Lawrence, D. D., Padmanabhan, S., Takeshita, K., Porter, C. W., Goodrich, D. W., Bernstein, Z. P., Wallace, P. K., et al. (2006) · Journal of Clinical Oncology · doi:10.1200/jco.2005.05.0401 · Cited by 414 · see citing works
Quantitative production of macrophages or neutrophils ex vivo using conditional Hoxb8
Wang, G. G., Calvo, K. R., Pasillas, M. P., Sykes, D. B., Häcker, H., & Kamps, M. P. (2006) · Nature Methods · doi:10.1038/nmeth865 · Cited by 408 · see citing works
Ferrajoli, A., Lee, B.-N., Schlette, E. J., O'Brien, S. M., Gao, H., Wen, S., Wierda, W. G., Estrov, Z. E., Faderl, S., Cohen, E. N., et al. (2008) · Blood · doi:10.1182/blood-2007-12-130120 · Cited by 405 · see citing works
Dimopoulos, M. A., Chen, C. L., Spencer, A. G., Niesvizky, R., Attal, M., Stadtmauer, E. A., Petrucci, M. T., Yu, Z., Olesnyckyj, M., Zeldis, J. B., et al. (2009) · Leukemia · doi:10.1038/leu.2009.147 · Cited by 363 · see citing works
Aiolos Regulates B Cell Activation and Maturation to Effector State
Wang, J.-H., Avitahl, N., Cariappa, A., Friedrich, C., Ikeda, T., Renold, A., Andrikopoulos, K., Liang, L., Pillai, S., Morgan, B. A., et al. (1998) · Immunity · doi:10.1016/s1074-7613(00)80637-8 · Cited by 321 · see citing works
Recognition of thalidomide defects.
SMITHELLS, R. W., & Newman, C. G. H. (1992) · Journal of Medical Genetics · doi:10.1136/jmg.29.10.716 · Cited by 276 · see citing works
Narrowing and genomic annotation of the commonly deleted region of the 5q− syndrome
Boultwood, J., Fidler, C., Strickson, A., Watkins, F., Gama, S., Kearney, L., Tosi, S., Kasprzyk, A., Cheng, J., Jaju, R. J., et al. (2002) · Blood · doi:10.1182/blood.v99.12.4638 · Cited by 264 · 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
Habermann, T. M., Lossos, I. S., Justice, G. R., Vose, J. M., Wiernik, P. H., McBride, K., Wride, K., Ervin-Haynes, A. L., Takeshita, K., PIETRONIGRO, D. D., et al. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07626.x · Cited by 244 · see citing works
Rps14 haploinsufficiency causes a block in erythroid differentiation mediated by S100A8 and S100A9
Schneider, R. K., Schenone, M., Ferreira, M. S. V., Kramann, R., Joyce, C. E., Hartigan, C. R., Beier, F., Brümmendorf, T. H., Germing, U., Platzbecker, U., et al. (2016) · Nature Medicine · doi:10.1038/nm.4047 · Cited by 236 · see citing works
Self-citationDefects in Hemopoietic Stem Cell Activity in Ikaros Mutant Mice
Nichogiannopoulou, A., Trevisan, M., Neben, S., Friedrich, C., & Georgopoulos, K. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.9.1201 · Cited by 232 · see citing works
Equivalent ages in mouse and human embryos
Otis, E. M., & Brent, R. L. (1954) · The Anatomical Record · doi:10.1002/ar.1091200104 · Cited by 228 · see citing works
Chesi, M., Matthews, G. M., Garbitt, V. M., Palmer, S. E., Shortt, J., Lefebure, M., Stewart, A. K., Johnstone, R. W., & Bergsagel, P. L. (2012) · Blood · doi:10.1182/blood-2012-02-412783 · Cited by 215 · see citing works
CKIα ablation highlights a critical role for p53 in invasiveness control
Elyada, E., Pribluda, A., Goldstein, R. E., Morgenstern, Y., Brachya, G., Cojocaru, G., Snir-Alkalay, I., Burstain, I., Haffner‐Krausz, R., Jung, S., et al. (2011) · Nature · doi:10.1038/nature09673 · Cited by 199 · see citing works
Role of Casein Kinase 1A1 in the Biology and Targeted Therapy of del(5q) MDS
Schneider, R. K., Ademà, V., Heckl, D., Järås, M., Mallo, M., Lord, A. M., Chu, L. P., McConkey, M. E., Kramann, R., Mullally, A., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.08.001 · Cited by 188 · see citing works
Self-citationpSILAC mass spectrometry reveals ZFP91 as IMiD-dependent substrate of the CRL4CRBN ubiquitin ligase
An, J., Ponthier, C. M., Sack, R., Seebacher, J., Stadler, M. B., Donovan, K. A., & Fischer, E. S. (2017) · Nature Communications · doi:10.1038/ncomms15398 · Cited by 176 · see citing works
An Erythroid Differentiation Signature Predicts Response to Lenalidomide in Myelodysplastic Syndrome
Ebert, B. L., Galili, N., Tamayo, P., Bosco, J., Mak, R. H., Pretz, J. L., Tanguturi, S. K., Ladd‐Acosta, C., Stone, R. M., Golub, T. R., et al. (2008) · PLoS Medicine · doi:10.1371/journal.pmed.0050035 · Cited by 165 · see citing works
Self-citationTeratogenic effects of thalidomide in rabbits, rats, hamsters, and mice
Fratta, I., Sigg, E. B., & Maiorana, K. (1965) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(65)90095-5 · Cited by 155 · see citing works
Gene expression profiling of CD34+ cells in patients with the 5q− syndrome
Boultwood, J., Pellagatti, A., Cattan, H., Lawrie, C. H., Giagounidis, A. A. N., Malcovati, L., Porta, M. G. D., Jädersten, M., Killick, S. B., Fidler, C., et al. (2007) · British Journal of Haematology · doi:10.1111/j.1365-2141.2007.06833.x · Cited by 151 · see citing works
Early human development and the chief sources of information on staged human embryos
O’Rahilly, R. (1979) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/0028-2243(79)90068-6 · Cited by 138 · see citing works
Saft, L., Karimi, M., Ghaderi, M., Matolcsy, A., Mufti, G. J., Kulasekararaj, A. G., Göhring, G., Giagounidis, A. A. N., Selleslag, D., Muus, P., et al. (2014) · Haematologica · doi:10.3324/haematol.2013.098103 · Cited by 137 · see citing works
Fehniger, T. A., Uy, G. L., Trinkaus, K., Nelson, A. D., Demland, J., Abboud, C. N., Cashen, A. F., Stockerl-Goldstein, K. E., Westervelt, P., DiPersio, J. F., et al. (2011) · Blood · doi:10.1182/blood-2010-07-297143 · Cited by 107 · see citing works
Sekeres, M. A., Maciejewski, J. P., Giagounidis, A. A. N., Wride, K., Knight, R., Raza, A., & List, A. F. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.15.5770 · Cited by 107 · see citing works
Dexamethasone and lenalidomide have distinct functional effects on erythropoiesis
Narla, A., Dutt, S., McAuley, J. R., Al‐Shahrour, F., Hurst, S. N., McConkey, M. E., Neuberg, D. S., & Ebert, B. L. (2011) · Blood · doi:10.1182/blood-2010-11-318543 · Cited by 85 · see citing works
Self-citationMallo, M., Rey, M. D., Ibáñez, M., Calasanz, M. J., Arenillas, L., Larráyoz, M. J., Pedro, C., Jerez, A., Maciejewski, J. P., Costa, D., et al. (2013) · British Journal of Haematology · doi:10.1111/bjh.12354 · Cited by 85 · see citing works
Thalidomide Syndrome in Monkeys
Delahunt, C. S., & Lassen, L. J. (1964) · Science · doi:10.1126/science.146.3649.1300 · Cited by 79 · see citing works
Chung, F., Lu, J., Palmer, B. D., Kestell, P., Browett, P., Baguley, B. C., Tingle, M. D., & Ching, L. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-0421 · Cited by 62 · see citing works
The effect of thalidomide intake during 113 human pregnancies
Kajii, T., Kida, M., & Takahashi, K. (1973) · Teratology · doi:10.1002/tera.1420080208 · Cited by 55 · see citing works
Metabolism of Thalidomide in Liver Microsomes of Mice, Rabbits, and Humans
Lu, J., Helsby, N. A., Palmer, B. D., Tingle, M. D., Baguley, B. C., Kestell, P., & Ching, L. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.067793 · Cited by 51 · see citing works
EFFECTS OF THALIDOMIDE ON PREGNANCY IN THE RABBIT
HAY, M. F. (1964) · Reproduction · doi:10.1530/jrf.0.0080059 · Cited by 40 · see citing works
‘Thalidomide’ Syndrome in Baboons
Hendrickx, A. G., Axelrod, L. R., & CLAYBORN, L. D. (1966) · Nature · doi:10.1038/210958a0 · Cited by 37 · see citing works
Pharmacokinetics and Tissue Disposition of Lenalidomide in Mice
Rozewski, D. M., Herman, S. E. M., Towns, W. H., Mahoney, E., Stefanovski, M. R., Shin, J. D., Yang, X., Gao, Y., Li, X., Jarjoura, D. G., et al. (2012) · The AAPS Journal · doi:10.1208/s12248-012-9401-2 · Cited by 35 · see citing works
Thalidomide: Effect upon Pregnancy in the Rhesus Monkey
Lucey, J. F., & Behrman, R. E. (1963) · Science · doi:10.1126/science.139.3561.1295 · Cited by 33 · see citing works
Thalidomide malformations and genetic background in the rabbit
SAWIN, P. B., Crary, D. D., Fox, R. R., & Wuest, H. M. (1965) · Cellular and Molecular Life Sciences · doi:10.1007/bf02144076 · Cited by 33 · see citing works
Canadian Thalidomide Experience
WEBB, J. F. (1963) · JAMA · doi:10.1001/jama.1963.03710100122084 · Cited by 23 · see citing works
The effect of thalidomide on a prosimian: the greater galago (Galago crassicaudatus)
Butler, H. (1977) · Journal of Medical Primatology · doi:10.1159/000459764 · Cited by 17 · see citing works
Flagged first, then by citations
Research works printed but not linked: 3
- Gandhi AK, Kang J, Havens CG, et al. Immunomodulatory agents lenalidomide and pomalidomide co-stimulate T cells by in- ducing 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.
- Petzold G, Fischer ES, Thom ä NH. Structural basis of lenalidomide-induced CK1a degra- dation by the CRL4(CRBN) ubiquitin ligase. Nature. 2016;532(7597):127-130.
- Delahunt CS, Lassen LJ. Thalidomide syn- drome in monkeys. Science. 1964;146(3649): 1300-1305.
Cited by
Sorted by citations
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 · see citing works
Self-citationTargeted protein degradation: from mechanisms to clinic
Tsai, J. M., Nowak, R. P., Ebert, B. L., & Fischer, E. S. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00729-9 · Cited by 438 · see citing works
Self-citationPROTAC: An Effective Targeted Protein Degradation Strategy for Cancer Therapy
Qi, S., Dong, J., Xu, Z., Cheng, X., Zhang, W., & Qin, J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.692574 · Cited by 299 · see citing works
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 220 · see citing works
Immunotherapy of multiple myeloma
Minnie, S. A., & Hill, G. R. (2020) · Journal of Clinical Investigation · doi:10.1172/jci129205 · Cited by 216 · see citing works
Targeted protein degradation as a powerful research tool in basic biology and drug target discovery
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 182 · see citing works
Harnessing the Power of Proteolysis for Targeted Protein Inactivation
Verma, R., Mohl, D., & Deshaies, R. J. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.010 · Cited by 185 · see citing works
EP300 Selectively Controls the Enhancer Landscape of MYCN -Amplified Neuroblastoma
Durbin, A. D., Wang, T., Wimalasena, V. K., Zimmerman, M. W., Li, D., Dharia, N. V., Mariani, L., Shendy, N. A. M., Nance, S., Patel, A. G., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-0385 · Cited by 174 · see citing works
Cell of Origin and Genetic Alterations in the Pathogenesis of Multiple Myeloma
Barwick, B. G., Gupta, V. A., Vertino, P. M., & Boise, L. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01121 · Cited by 165 · see citing works
Yamamoto, J., Ito, T., Yamaguchi, Y., & Handa, H. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00116k · Cited by 164 · see citing works
Lenalidomide promotes the development of TP53 -mutated therapy-related myeloid neoplasms
Sperling, A. S., Guerra, V. A., Kennedy, J. A., Yan, Y., Hsu, J. I., Wang, F., Nguyen, A. T., Miller, P. G., McConkey, M. E., Barrios, V. A. Q., et al. (2022) · Blood · doi:10.1182/blood.2021014956 · Cited by 153 · see citing works
Self-citationDissecting the biology of allogeneic HSCT to enhance the GvT effect whilst minimizing GvHD
Blazar, B. R., Hill, G. R., & Murphy, W. J. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0356-4 · Cited by 144 · see citing works
Functional E3 ligase hotspots and resistance mechanisms to small-molecule degraders
Hanzl, A., Casement, R., Imrichova, H., Hughes, S. J., Barone, E., Testa, A., Bauer, S., Wright, J., Brand, M., Ciulli, A., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-022-01177-2 · Cited by 133 · see citing works
Acute pharmacological degradation of Helios destabilizes regulatory T cells
Wang, E. S., Verano, A. L., Nowak, R. P., Yuan, J. C., Donovan, K. A., Eleuteri, N. A., Yue, H., Ngo, K. H., Lizotte, P. H., Gokhale, P. C., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00802-w · Cited by 124 · see citing works
Molecular mechanisms of thalidomide and its derivatives
Ito, T., & Handa, H. (2020) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.96.016 · Cited by 121 · see citing works
Rapid and deep-scale ubiquitylation profiling for biology and translational research
Udeshi, N. D., Mani, D. R., Satpathy, S., Fereshetian, S., Gasser, J. A., Svinkina, T., Olive, M. E., Ebert, B. L., Mertins, P., & Carr, S. A. (2020) · Nature Communications · doi:10.1038/s41467-019-14175-1 · Cited by 112 · see citing works
Self-citationMeermeier, E. W., Welsh, S. J., Sharik, M. E., Du, M. T., Garbitt, V. M., Riggs, D. L., Shi, C., Stein, C. K., Bergsagel, M., Chau, B. H., et al. (2021) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-21-0038 · Cited by 112 · see citing works
Cereblon modulators: Low molecular weight inducers of protein degradation
Chamberlain, P. P., & Cathers, B. E. (2019) · Drug Discovery Today: Technologies · doi:10.1016/j.ddtec.2019.02.004 · Cited by 106 · see citing works
Molecular bottlebrush prodrugs as mono- and triplex combination therapies for multiple myeloma
Detappe, A., Nguyen, H. V. ‐., Jiang, Y., Agius, M. P., Wang, W., Mathieu, C., Su, N. K., Kristufek, S. L., Lundberg, D. J., Bhagchandani, S. H., et al. (2023) · Nature Nanotechnology · doi:10.1038/s41565-022-01310-1 · Cited by 104 · see citing works
Larráyoz, M., Garcia-Barchino, M. J., Celay, J., Etxebeste, A., Jiménez, M., Pérez, C., Ordóñez, R., Cobaleda, C., Botta, C., Fresquet, V. J., et al. (2023) · Nature Medicine · doi:10.1038/s41591-022-02178-3 · Cited by 90 · see citing works
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 · see citing works
Molecular Mechanisms of the Teratogenic Effects of Thalidomide
Asatsuma‐Okumura, T., Ito, T., & Handa, H. (2020) · Pharmaceuticals · doi:10.3390/ph13050095 · Cited by 88 · see citing works
Continuous evolution of compact protein degradation tags regulated by selective molecular glues
Mercer, J. A. M., DeCarlo, S. J., Burman, S. S. R., Sreekanth, V., Nelson, A. T., Hunkeler, M., Chen, P. J., Donovan, K. A., Kokkonda, P., Tiwari, P. K., et al. (2024) · Science · doi:10.1126/science.adk4422 · Cited by 82 · see citing works
Humanized cereblon mice revealed two distinct therapeutic pathways of immunomodulatory drugs
Gemechu, Y., Millrine, D., Hashimoto, S., Prakash, J., Sanchenkova, K., Metwally, H., Parajuli, G., Kang, S., & Kishimoto, T. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814446115 · Cited by 81 · see citing works
Recent advances in the molecular mechanism of thalidomide teratogenicity
Gao, S., Wang, S., Fan, R., & Hu, J. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110114 · Cited by 78 · see citing works
Sellar, R. S., Sperling, A. S., Slabicki, M. M., Gasser, J. A., McConkey, M. E., Donovan, K. A., Mageed, N., Adams, D. N., Zou, C., Miller, P. G., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci153514 · Cited by 75 · see citing works
Self-citationEvolution of Cereblon-Mediated Protein Degradation as a Therapeutic Modality
Chamberlain, P. P., D’Agostino, L. A., Ellis, J. M., Hansen, J. D., Matyskiela, M. E., McDonald, J. J., Riggs, J. R., & Hamann, L. G. (2019) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00425 · Cited by 69 · see citing works
Induced protein degradation for therapeutics: past, present, and future
Yoon, H., Rutter, J. C., Li, Y.-D., & Ebert, B. L. (2024) · Journal of Clinical Investigation · doi:10.1172/jci175265 · Cited by 70 · see citing works
Self-citationPeptidic degron for IMiD-induced degradation of heterologous proteins
Koduri, V., McBrayer, S. K., Liberzon, E., Wang, A. C., Briggs, K. J., Cho, H., & Kaelin, W. G. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818109116 · 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
Hahn, F., Hamilton, S. T., Wangen, C., Wild, M. R., Kicuntod, J., Brückner, N., Follett, J. E. L., Herrmann, L., Kheimar, A., Kaufer, B. B., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312858 · Cited by 60 · see citing works
Carratt, S. A., Zuch de Zafra, C. L., Oziolor, E., Rana, P., Vansell, N. R., Mangipudy, R., & Vaidya, V. S. (2025) · Toxicological Sciences · doi:10.1093/toxsci/kfae122 · Cited by 59 · see citing works
Aubrey, B., Cutler, J., Bourgeois, W., Donovan, K., Gu, S., Hatton, C., Perlee, S., Perner, F., Rahnamoun, H., Theall, A., et al. (2022) · Nature Cancer · doi:10.1038/s43018-022-00366-1 · Cited by 50 · see citing works
Dual IKZF2 and CK1α degrader targets acute myeloid leukemia cells
Park, S.-M., Miyamoto, D. K., Han, G. Y. Q., Chan, M., Curnutt, N. M., Tran, N. L., Velleca, A., Kim, J. H., Schurer, A., Chang, K., et al. (2023) · Cancer Cell · doi:10.1016/j.ccell.2023.02.010 · Cited by 56 · see citing works
SLC44A2 regulates vascular smooth muscle cell phenotypic switching and aortic aneurysm
Song, T.-Y., Zhao, S., Luo, S.-S., Chen, C., Liu, X., Wu, X., Sun, Z., Cao, J., Wang, Z., Wang, Y., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci173690 · Cited by 43 · 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
Catalytic Degraders Effectively Address Kinase Site Mutations in EML4-ALK Oncogenic Fusions
Gao, Y., Jiang, B., Kim, H., Berberich, M. J., Che, J., Donovan, K. A., Hatcher, J. M., Huerta, F., Kwiatkowski, N. P., Liu, Y., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01864 · Cited by 50 · see citing works
Avadomide 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
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
Martinez-Høyer, S., Deng, Y., Parker, J., Jiang, J., Mo, A., Docking, T. R., Gharaee, N., Li, J., Umlandt, P., Fuller, M., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0497-9 · Cited by 42 · see citing works
Chang, Y., Keramatnia, F., Ghate, P. S., Nishiguchi, G., Gao, Q., Iacobucci, I., Yang, L., Chepyala, D., Mishra, A., High, A. A., et al. (2023) · Blood · doi:10.1182/blood.2022017813 · Cited by 41 · see citing works
Immune checkpoint inhibitors for multiple myeloma immunotherapy
Liu, Z., Xu, X., Liu, H., Zhao, X., Yang, C., & Fu, R. (2023) · Experimental Hematology & Oncology · doi:10.1186/s40164-023-00456-5 · Cited by 40 · see citing works
Identification and characterization of cancer vulnerabilities via targeted protein degradation
Mayor-Ruiz, C., & Winter, G. E. (2019) · Drug Discovery Today: Technologies · doi:10.1016/j.ddtec.2018.12.003 · Cited by 33 · see citing works
Bourgeois, W., Cutler, J. A., Aubrey, B. J., Wenge, D. V., Perner, F., Martucci, C., Henrich, J. A., Klega, K. S., Nowak, R. P., Donovan, K. A., et al. (2023) · Blood · doi:10.1182/blood.2023021105 · Cited by 32 · see citing works
Self-citationHe, T., Cheng, C., Qiao, Y., Cho, H., YOUNG, E. A., Mannan, R., Mahapatra, S., Miner, S. J., Zheng, Y., Kim, N. H., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2322563121 · Cited by 32 · 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
Beedie, S., Huang, P. A., Harris, E. M., Strope, J. D., Mahony, C. B., Chau, C. H., Vargesson, N., & Figg, W. D. (2020) · The FASEB Journal · doi:10.1096/fj.201903060rr · Cited by 28 · see citing works
Chen, Z., Dhruv, H., Zhang, X., Rej, R. K., Bai, L., McEachern, D., Kirchhoff, P. D., Nagilla, R., Jolivette, L. J., Rice, C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58431-z · Cited by 26 · see citing works
Discovering new biology with drug-resistance alleles
Freedy, A. M., & Liau, B. B. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00865-9 · Cited by 25 · see citing works
Li, P., Hu, X., Fan, Z., Sun, S., Ran, Q., Wei, T., Wei, P., Jiang, Q., Yan, J. W., Yang, N., et al. (2024) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01592-z · Cited by 24 · see citing works
Minnie, S. A., Waltner, O. G., Ensbey, K. S., Olver, S. D., Collinge, A. D., Sester, D. P., Schmidt, C. R., Legg, S. R. W., Takahashi, S., Nemychenkov, N. S., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci157907 · Cited by 22 · see citing works
Immunomodulatory drugs: a promising clinical ally for cancer immunotherapy
Colley, A., Brauns, T. A., Sluder, A. E., Poznansky, M. C., & Gemechu, Y. (2024) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2024.05.001 · Cited by 21 · see citing works
Development of an AchillesTAG degradation system and its application to control CAR-T activity
Veits, G. K., Henderson, C. S., Vogelaar, A. L., Eron, S. J., Lee, L., Hart, A. A., Deibler, R. W., Baddour, J., Elam, W. A., Agafonov, R. V., et al. (2021) · Current Research in Chemical Biology · doi:10.1016/j.crchbi.2021.100010 · Cited by 21 · 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
Song, Z.-M., Cui, Y.-L., Xin, L., Xiao, R.-J., Feng, J., Li, C., Yin, Z.-N., Wang, H.-H., Li, Q., Wang, M.-X., et al. (2025) · Cell Stem Cell · doi:10.1016/j.stem.2025.01.013 · Cited by 20 · see citing works
Nutt, M. J., & Stewart, S. G. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104010 · Cited by 18 · see citing works
Lecca, D., Hsueh, S., Luo, W., Tweedie, D., Kim, D. S., Baig, A. M., Vargesson, N., Kim, Y. K., Hwang, I., Kim, S., et al. (2023) · Journal of Biomedical Science · doi:10.1186/s12929-023-00907-5 · Cited by 17 · see citing works
Zhou, L., & Xu, G. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167457 · Cited by 17 · see citing works
The emerging role of targeted protein degradation to treat and study cancer
Brodermann, M. H., Henderson, E. K., & Sellar, R. S. (2024) · The Journal of Pathology · doi:10.1002/path.6301 · Cited by 15 · see citing works
Zou, J., Jones, R. J., Wang, H., Kuiatse, I., Shirazi, F., Manasanch, E. E., Lee, H. C., Sullivan, R., Fung, L. M., Richard, N., et al. (2020) · Journal of Molecular Medicine · doi:10.1007/s00109-020-01943-6 · Cited by 14 · see citing works
Ponatinib sensitizes myeloma cells to MEK inhibition in the high-risk VQ model
Flietner, E., Wen, Z. H., Rajagopalan, A., Jung, O., Watkins, L. R., Wiesner, J., You, X., Zhou, Y., Sun, Y., Kingstad-Bakke, B. A., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-14114-z · Cited by 14 · see citing works
Precision preclinical modeling to advance cancer treatment
Gutmann, D. H., Boehm, J. S., Karlsson, E. K., Padron, E., Seshadri, M., WALLIS, D. E., & Snyder, J. C. (2024) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djae249 · Cited by 14 · see citing works
iTAG an optimized IMiD-induced degron for targeted protein degradation in human and murine cells
Bouguenina, H., Nicolaou, S., Bihan, Y. L., Bowling, E. A., Calderon, C., Caldwell, J., Harrington, B., Hayes, A., McAndrew, C., Mitsopoulos, C., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107059 · Cited by 12 · see citing works
Molecular glue degraders of HuR suppress BRAF-mutant colorectal cancer
Lu, X., Wang, X., Yang, Z., Wang, X., Wang, L., Xu, C., Lo, I., Geng, C., Wang, L., Pu, Y., et al. (2026) · Nature · doi:10.1038/s41586-026-10613-5 · Cited by 10 · see citing works
A Molecular Glue Approach to Control the Half-Life of CRISPR-Based Technologies
Sreekanth, V., Jan, M., Zhao, K. T., Lim, D., Siriwongsup, S., Davis, J. R., McConkey, M. E., Kovalcik, V., Barkal, S., Law, B. K., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c06230 · Cited by 12 · see citing works
Self-citationThalidomide-induced limb malformations: an update and reevaluation
Collins, M. D., & Scott, W. J. (2025) · Archives of Toxicology · doi:10.1007/s00204-024-03930-z · Cited by 10 · see citing works
Kotagiri, S., Wang, Y., Han, Y., Liang, X., Blazanin, N., Mazhar, H., Sebastian, M. M., Nguyen, P. K., Jiang, Y., & Lissanu, Y. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02577 · Cited by 9 · see citing works
ZBTB11 depletion targets metabolic vulnerabilities in KRAS inhibitor-resistant PDAC
Tran, N. L., Jiang, J., Ma, M., Gadbois, G. E., Gulay, K. C. M., Verano, A. L., Schiavon, C. R., Rebollo, E., Zhou, H., Huang, C., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01978-1 · Cited by 12 · see citing works
Drug Repurposing in Oncology, an Attractive Opportunity for Novel Combinatorial Regimens
Falvo, P., Orecchioni, S., Roma, S., Raveane, A., & Bertolini, F. (2020) · Current Medicinal Chemistry · doi:10.2174/0929867327999200817104912 · Cited by 9 · see citing works
Zhang, X., Dhruv, H., Deng, Q., Tudor, M., Bechtel, N., Nagilla, R., Jolivette, L. J., Rice, C., Orth, P., Behshad, E., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00668 · Cited by 8 · see citing works
Drugging the undruggable: Chemical and biological insights into molecular glues in the pipeline
Metwally, K. A., Yahya, G., & Abo-Dya, N. E. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118132 · Cited by 9 · see citing works
Cancer Biology of GSPT1: Mechanisms and Targeted Therapy Opportunities of Molecular Glue Degraders
Lin, Q., Liu, W., Lu, W., Zhao, M., Cao, L., Li, Z., Wang, J., Xu, X. J., & Wu, H. (2025) · Advanced Science · doi:10.1002/advs.202511789 · Cited by 8 · see citing works
Hsueh, S., Scerba, M. T., Tweedie, D., Lecca, D., Kim, D. S., Baig, A. M., Kim, Y. K., Hwang, I., Kim, S., Selman, W. R., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10102449 · Cited by 8 · see citing works
Cereblon gene variants and clinical outcome in multiple myeloma patients treated with lenalidomide
Huang, P. A., Beedie, S., Chau, C. H., Venzon, D. J., Gere, S., Kazandjian, D. G., Korde, N., Mailankody, S., Landgren, O., & Figg, W. D. (2019) · Scientific Reports · doi:10.1038/s41598-019-51446-9 · Cited by 7 · see citing works
Loberg, L. I., Proctor, W. R., Burdick, A. D., Cauvin, A. J., DeLise, A. M., Hemkens, M. D., Hohlbaum, A. M., Hukkanen, R. R., Sedgwick, A., Shuey, D. L., et al. (2025) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2025.105793 · Cited by 7 · see citing works
Kollotzek, F., Mott, K., Fischer, M., Fındık, B., Göb, V., Manke, M.-C., Borst, C. E., Polzin, A., Burkhalter, M. D., Eckly, A. E., et al. (2025) · Blood · doi:10.1182/blood.2025028460 · Cited by 7 · see citing works
PROTACs in Ovarian Cancer: Current Advancements and Future Perspectives
Vorderbruggen, M., Velázquez‐Martínez, C. A., Natarajan, A., & Karpf, A. R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105067 · Cited by 7 · see citing works
Cenzano, I., Cócera, M., Larráyoz, M., Campos‐Dopazo, L., Sanz, S., Bantan, A., Vilas‐Zornoza, A., Martín‐Úriz, P. S., Aguirre‐Ruiz, P., Alignani, D., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74389-y · Cited by 7 · see citing works
Self-citationChen, L., Aleman, A., Larráyoz, M., Chiu, H., Zhao, J., Oekelen, O. V., Kelly, G., Kim‐Schulze, S., Laganà, A., Jagannath, S., et al. (2026) · Blood · doi:10.1182/blood.2025030891 · Cited by 6 · see citing works
Self-citationFinding the Optimal Partner to Pair with Bispecific Antibody Therapy for Multiple Myeloma
Louvet, C., Nadeem, O., & Smith, E. L. (2021) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-21-0073 · Cited by 6 · see citing works
Drug Repurposing in Veterinary Oncology: Myth or Reality?
Ciccarelli, S., Perrone, C., Cavalera, M. A., & Giuliano, A. (2025) · Veterinary Sciences · doi:10.3390/vetsci12111067 · Cited by 5 · see citing works
Röhner, L., Ng, Y. L. D., Scheffold, A., Lindner, S., Köpff, S., Brandl, A., Beilhack, A., & Krönke, J. (2020) · Experimental Hematology · doi:10.1016/j.exphem.2020.11.004 · Cited by 5 · see citing works
Kowalski, T. W., Caldas-Garcia, G. B., Gomes, J. D. A., Fraga, L. R., Schüler‐Faccini, L., Recamonde‐Mendoza, M., Paixão‐Côrtes, V. R., & Vianna, F. S. L. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.680217 · Cited by 5 · see citing works
Nutt, M. J., Yee, Y. S., Buyan, A., Andrewartha, N., Corry, B., Yeoh, G. C., & Stewart, S. G. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113353 · Cited by 4 · see citing works
Safety considerations for cereblon-recruiting targeted protein degraders
Garside, H., Aslamkhan, A. G., Daniels, D. L., Datta, K., Pedersen, M. E., Hukkanen, R. R., Jones, L. H., Ketter, N., Lahoti, T. S., Loberg, L. I., et al. (2026) · Nature Reviews Drug Discovery · doi:10.1038/s41573-026-01426-2 · Cited by 3 · see citing works
Lin, Z., Zhang, Y., Liu, X., Luo, H., Li, Q., Gao, Q., Wang, X., Wen, J., Li, L., Yu, F., et al. (2024) · British Journal of Haematology · doi:10.1111/bjh.19468 · Cited by 3 · see citing works
Repurposing the repurposed: thalidomide analogs as immune stimulants to overcome T cell exhaustion
Slabicki, M. M., & Sperling, A. S. (2022) · Cell chemical biology · doi:10.1016/j.chembiol.2022.07.004 · Cited by 3 · see citing works
ZBTB11 Depletion Targets Metabolic Vulnerabilities in K-Ras Inhibitor Resistant PDACPreprint
Tran, N. L., Jiang, J., Ma, M., Gadbois, G. E., Gulay, K. C. M., Verano, A. L., Zhou, H., Huang, C., Scott, D. A., Bang, A. G., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.19.594824 · Cited by 3 · see citing works
Kotagiri, S., Wang, Y., Han, Y., Liang, X., Blazanin, N., Nguyen, P. K., Jiang, Y., & Lissanu, Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.23.608456 · Cited by 3 · see citing works
Optimised genome editing for precise DNA insertion and substitution using prime editors in zebrafishPreprint
Ono, Y., Peterka, M., Love, M. I., Khan, A., Bowers, F., Bhandari, A., Gordon, E., Ball, J. S., Hammond, C., Tyler, C. R., et al. (2025) · eLife · doi:10.7554/elife.107475 · Cited by 3 · see citing works
Palyada, K., Hukkanen, R. R., Leuenroth-Quinn, S., Vitsky, A., Peterson, R. E., Stamp, K., Hoover, C., & Volak, L. P. (2024) · Toxicologic Pathology · doi:10.1177/01926233241300452 · Cited by 2 · see citing works
Bjorklund, C. C., Larráyoz, M., Kang, J., Chiu, H., Shtraizent, N., Wu, L., Li, S., Hsu, C.-C., Zhao, J., Amatangelo, M. D., et al. (2025) · Blood Neoplasia · doi:10.1016/j.bneo.2025.100179 · Cited by 2 · see citing works
Discovery of Highly Potent and Selective IKZF2 Degraders for Cancer Immunotherapy
Wang, Y., Qi, Z., Sun, S., Wei, T., Wei, P., Jia, C., Cai, X., Zhao, Z., Qiao, M., Zou, Y., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c00500 · Cited by 2 · see citing works
Zhou, L., Sun, Q. P., & Cao, D. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117606 · Cited by 2 · see citing works
Gharaee, N., Wegrzyn-Woltosz, J., Jiang, J., Akhade, V. S., Bridgers, J., Stubbins, R. J., Hiwase, D., Kutyna, M., Chan, O., Komrokji, R. S., et al. (2025) · Leukemia · doi:10.1038/s41375-025-02537-2 · Cited by 2 · see citing works
Thalidomide – From a Banned Drug to Molecular Glues, PROTACs, and New Concepts in Drug Discovery
Yamamoto, J., Handa, H., & Yamaguchi, Y. (2024) · Wiley eBooks · doi:10.1002/9781394182862.ch24 · Cited by 2 · see citing works
Optimised genome editing for precise DNA insertion and substitution using Prime Editors in zebrafishPreprint
Ono, Y., Peterka, M., Love, M. I., Bhandari, A., Gordon, E., Ball, J. S., Tyler, C. R., Rees, S., Bohlooly‐Y, M., Maresca, M., et al. (2025) · eLife · doi:10.7554/elife.107475.1 · Cited by 2 · see citing works
Ehinger, E., Perez, K. C., Sanchez, E., Reveles, B. V., Dash, B., Arteaga-Vazquez, L. J., Johnson, E., Rao, A., & Hogan, P. G. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.02.701413 · Cited by 2 · see citing works
Optimised genome editing for precise DNA insertion and substitution using prime editors in zebrafish
Ono, Y., Peterka, M., Love, M. I., Khan, A., Bowers, F., Bhandari, A., Gordon, E., Ball, J. S., Hammond, C. L., Tyler, C. R., et al. (2026) · eLife · doi:10.7554/elife.107475.3 · Cited by 1 · see citing works
Drug discovery technologies–Current and future trends
Noe, M. C., Steppan, C. M., & Weston, A. D. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00019-4 · Cited by 1 · see citing works
- 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
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