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Cereblon (CRBN, UniProt accession Q96SW2) is a highly conserved human protein that functions as the substrate receptor subunit of the Cullin-RING E3 ubiquitin ligase 4 (CRL4^CRBN) complex (kroupova2024designofa pages 1-3, cieslak2023cereblonrecruitingprotacswill pages 1-3, ito2021exploitingubiquitinligase pages 2-4). The gene encodes a 441-442 amino acid protein belonging to the CRBN family, with key domains including CULT, Lon protease N-terminal, and Yippee/Mis18/Cereblon domains, consistent with the UniProt annotation provided (ito2020molecularmechanismsof pages 2-4). CRBN came to prominence in 2010 when it was identified as the direct molecular target of thalidomide using affinity purification with ferrite glycidyl methacrylate (FG) beads, a discovery that revolutionized our understanding of both the teratogenic and therapeutic effects of thalidomide-class drugs (ito2020molecularmechanismsof pages 2-4).
The primary function of cereblon is to serve as a substrate receptor within the multi-subunit CRL4^CRBN E3 ubiquitin ligase complex (cieslak2023cereblonrecruitingprotacswill pages 1-3, merinocacho2025cullinringligasebioe3 pages 1-2, ito2021exploitingubiquitinligase pages 2-4). Unlike catalytic enzymes, CRBN does not possess enzymatic activity itself but rather acts as an adapter protein that confers substrate specificity to the ubiquitination machinery (watson2022moleculargluecelmoda pages 1-3). The complete CRL4^CRBN complex consists of four core components: RBX1/ROC1 (RING-box protein 1), CUL4A or CUL4B (Cullin-4), DDB1 (DNA damage-binding protein 1), and CRBN as the substrate receptor (cieslak2023cereblonrecruitingprotacswill pages 1-3, ito2020molecularmechanismsof pages 2-4).
In this complex, RBX1 recruits E2 ubiquitin-conjugating enzymes, CUL4 provides the scaffold, DDB1 serves as an adaptor linking CRBN to the catalytic core, and CRBN directly recognizes and binds substrate proteins, positioning them for ubiquitination and subsequent proteasomal degradation (ito2021exploitingubiquitinligase pages 2-4, ito2020molecularmechanismsof pages 2-4). Two E2 enzymes, UBE2D3 and UBE2G1, have been identified through CRISPR screening as cooperatively functioning upstream of CRL4^CRBN, with UBE2D3 involved in monoubiquitination and UBE2G1 extending polyubiquitin chains (ito2021exploitingubiquitinligase pages 2-4).
CRBN contains three folded domains that are critical for its function (kroupova2024designofa pages 1-3, watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3):
Lon protease-like domain (Lon domain): Located at the N-terminus, this domain participates in substrate recognition and contributes to the conformational rearrangement critical for drug-induced neosubstrate binding (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3).
Helical bundle (HB): This intermedial domain docks into a central hydrophobic cleft formed at the interface of DDB1's BPA and BPC β-propeller domains, mediating the interaction between CRBN and the adaptor protein DDB1 (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3).
Thalidomide-binding domain (TBD): The C-terminal domain contains the drug-binding pocket where immunomodulatory drugs (IMiDs) and cereblon E3 ligase modulators (CELMoDs) bind (kroupova2024designofa pages 1-3, watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3).
A critical recent discovery is that CRBN exists in dynamic equilibrium between "open" and "closed" conformational states (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3). In the open conformation, the Lon domain and TBD are separated at approximately a 45-degree angle relative to one another. Binding of CELMoD compounds to the TBD is necessary and sufficient to trigger allosteric rearrangement from the open to the closed conformation, where the Lon and TBD domains tightly interact (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3). This conformational change is essential for stable neosubstrate association, as neosubstrates like Ikaros only stably bind to the closed CRBN conformation (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3). An N-terminal belt (residues 48-63) becomes ordered during closure, extending from the Lon domain to truss the TBD and support the closed state (watson2022moleculargluecelmod pages 1-2).
CRBN recognizes substrates through specific structural motifs, most notably the G-loop degron (oleinikovas2024fromthalidomideto pages 2-4). The G-loop is an eight-amino-acid stretch characterized by an invariant glycine at the sixth position (designated as position G), with flanking residues designated G-5 through G+2 (oleinikovas2024fromthalidomideto pages 2-4). This motif typically forms an alpha-turn or beta-hairpin structure that enables key molecular interactions:
Deep mutational scanning studies have confirmed that CRBN residues involved in these hydrogen bonds (particularly N351, H357, W400) are critical hot spots for mutation-acquired resistance to molecular glue degraders (oleinikovas2024fromthalidomideto pages 2-4). However, recent research has identified non-canonical degron motifs beyond the G-loop, such as the RT-loop (RDxS motif) in VAV1, expanding our understanding of CRBN substrate recognition diversity (oleinikovas2024fromthalidomideto pages 2-4).
Under physiological conditions, CRBN recognizes several endogenous substrates, although the complete native substrate repertoire remains an active area of investigation (ito2021exploitingubiquitinligase pages 2-4):
MEIS2 (Meis homeobox 2): Identified as an endogenous substrate of CRL4^CRBN (costacurta2021molecularmechanismsof pages 2-4, ito2021exploitingubiquitinligase pages 2-4).
SLO1 (KCNMA1): A calcium-activated potassium channel that represents another native CRBN substrate (ito2021exploitingubiquitinligase pages 2-4).
ILF2 (Interleukin enhancer-binding factor 2): A DNA and RNA-binding protein identified through quantitative proteomics using stable isotope labeling by amino acids in cell culture (SILAC). CRBN promotes the ubiquitination and proteasomal degradation of ILF2, with lysine 45 (K45) identified as a key ubiquitination site (lian2020cereblonpromotesthe pages 1-2).
Endogenous substrates may contain cyclic imide structures arising from intramolecular cyclization of glutamine or asparagine residues, which are chemically reminiscent of IMiDs and could drive physiological protein degradation (oleinikovas2024fromthalidomideto pages 2-4).
A defining feature of CRBN is its capacity to recognize "neosubstrates" - proteins that are recruited for degradation only in the presence of specific small-molecule ligands (costacurta2021molecularmechanismsof pages 2-4, ito2021exploitingubiquitinligase pages 2-4, ito2020molecularmechanismsof pages 2-4). This drug-induced change in substrate specificity forms the molecular basis for the therapeutic and adverse effects of thalidomide and its derivatives:
Classical IMiD-induced neosubstrates:
IKZF1 (Ikaros) and IKZF3 (Aiolos): Transcription factors of the Ikaros family that are degraded in the presence of lenalidomide and pomalidomide. These were identified in 2014 through quantitative proteomics and genetic screening approaches (costacurta2021molecularmechanismsof pages 2-4, ito2021exploitingubiquitinligase pages 2-4). IKZF1/3 degradation is central to the anti-myeloma activity of IMiDs, as these proteins sustain expression of IRF4 and MYC, which are critical for myeloma cell survival (costacurta2021molecularmechanismsof pages 2-4).
CK1α (Casein kinase 1 alpha): Targeted for degradation by lenalidomide specifically in myelodysplastic syndrome with del(5q), where haploinsufficiency of CK1α sensitizes cells to apoptosis via p53 stabilization (costacurta2021molecularmechanismsof pages 2-4).
GSPT1 (G1-to-S phase transition 1): A translation termination factor degraded by compounds such as CC-885 and CC-90009, with implications for viral infection treatment (oleinikovas2024fromthalidomideto pages 2-4).
SALL4 (Spalt-like transcription factor 4): A key mediator of thalidomide teratogenicity. SALL4 degradation disrupts limb development, explaining the birth defects historically associated with thalidomide exposure (costacurta2021molecularmechanismsof pages 2-4, oleinikovas2024fromthalidomideto pages 2-4).
Recently identified neosubstrates (2024-2025):
G3BP2 (Ras-GTPase-activating protein SH3 domain-binding protein 2): Identified through high-throughput proteomics as a cereblon neosubstrate using molecular surface mimicry, without containing a classical G-loop degron (oleinikovas2024fromthalidomideto pages 2-4).
KDM4B, VCL (Vinculin): Additional novel neosubstrates identified through comprehensive screening platforms (oleinikovas2024fromthalidomideto pages 2-4).
VAV1: A hematopoietic-specific signaling protein degraded via an RT-loop degron (RDxS motif at residues 796-799), representing a non-canonical recognition mechanism distinct from the G-loop (oleinikovas2024fromthalidomideto pages 2-4).
Over 2,500 proteins in the human proteome contain potential G-loop motifs and could theoretically be targeted by rationally designed CRBN-based molecular glues (oleinikovas2024fromthalidomideto pages 2-4).
Cereblon is localized in both the nucleus and cytoplasm, enabling it to ubiquitinate and degrade substrates in multiple cellular compartments (kaji2020characterizationofcereblondependent pages 1-2, lian2020cereblonpromotesthe pages 1-2). Studies using TurboID proximity labeling with nuclear-localized CRBN (CRBN-Flag-NLS-TurboID) and cytoplasmic-localized constructs have demonstrated that CRBN functions in both compartments (lian2020cereblonpromotesthe pages 1-2).
Visualization studies using the Fluoppi system to detect ternary complex formation have shown that CRBN-recruiting degraders form complexes in subcellular locations corresponding to their target protein localization. For example, BRD4-targeting degraders form ternary complexes mainly in the nucleus, while FKBP12-targeting degraders form complexes in the cytoplasm, demonstrating that CRBN utilizes the proteasome to degrade target proteins in their corresponding localized regions (kaji2020characterizationofcereblondependent pages 1-2).
CRBN plays a critical role in regulating hematopoietic transcriptional programs through degradation of IKZF1 and IKZF3 (costacurta2021molecularmechanismsof pages 2-4). These transcription factors form part of a core regulatory network in B cells and plasma cells, where they:
IMiD-induced CRBN activity affects cell cycle progression through multiple mechanisms. Treatment with IMiDs causes G0-G1 cell cycle arrest by inducing tumor suppressors p21 and p27, increasing expression of Early Growth Response (EGR) protein family members, and inhibiting cyclin-dependent kinases 2, 4, and 6 (costacurta2021molecularmechanismsof pages 2-4).
CRBN's role in development is most dramatically illustrated by thalidomide teratogenicity. Drug binding to CRBN leads to degradation of SALL4, a transcription factor essential for limb development, as well as p63 (tumor protein p63), disrupting normal developmental programs in embryos (costacurta2021molecularmechanismsof pages 2-4, ito2020molecularmechanismsof pages 2-4). Expression of thalidomide-binding-deficient CRBN mutants (such as Y384A/W386A) in zebrafish and chicken embryos confers resistance to thalidomide-induced developmental defects, confirming CRBN as the primary target for teratogenicity (ito2020molecularmechanismsof pages 2-4).
As part of the ubiquitin-proteasome system, CRBN contributes to cellular protein quality control by marking specific substrates for degradation. For instance, CRBN promotes the ubiquitination and degradation of ILF2, a protein involved in gene expression regulation and highly expressed in multiple tumor tissues (lian2020cereblonpromotesthe pages 1-2).
Cereblon is the direct molecular target of immunomodulatory imide drugs (IMiDs), including thalidomide, lenalidomide (Revlimid), and pomalidomide (Pomalyst) (cieslak2023cereblonrecruitingprotacswill pages 1-3, costacurta2021molecularmechanismsof pages 2-4, ito2021exploitingubiquitinligase pages 2-4, ito2020molecularmechanismsof pages 2-4). These drugs have FDA approval for:
As of 2023, twelve out of fifteen PROTACs in clinical trials recruit CRBN as the E3 ligase, highlighting its dominant position in targeted protein degradation therapeutics (cieslak2023cereblonrecruitingprotacswill pages 1-3).
Next-generation cereblon E3 ligase modulators (CELMoDs) such as mezigdomide (CC-92480) and iberdomide (CC-220) have been developed with enhanced potency for CRBN binding and neosubstrate degradation (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3). These compounds show:
The improved efficacy of CELMoDs has been linked to their superior ability to induce the closed CRBN conformation, thereby more efficiently activating the E3 ligase complex for neosubstrate recruitment (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3).
Resistance to IMiD therapy in multiple myeloma and other cancers can arise through several CRBN-related mechanisms (cieslak2023cereblonrecruitingprotacswill pages 1-3, costacurta2021molecularmechanismsof pages 2-4):
Deep sequencing has revealed that CRBN aberrations significantly reduce survival in multiple myeloma patients treated with IMiDs (costacurta2021molecularmechanismsof pages 2-4). Recent structural biology analyses suggest that certain CRBN mutations may be overcome by more potent CELMoDs that can still induce conformational closure and neosubstrate recruitment despite the mutations (watson2022moleculargluecelmoda pages 1-3).
Major advances in 2022-2024 using cryo-electron microscopy have revealed that CRBN exists in dynamic equilibrium between open and closed states (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3). Watson et al. demonstrated that CELMoD compound binding to the TBD is both necessary and sufficient to trigger the allosteric rearrangement from open to closed conformation, and that neosubstrates only stably associate with the closed form (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3). This mechanistic insight has profound implications for drug design, as compounds that more efficiently promote closure tend to be more efficacious degraders.
In 2024, Kroupova et al. developed CRBNmidi, a novel construct that expresses from E. coli with high yields as soluble, stable protein without requiring co-expression with DDB1 (kroupova2024designofa pages 1-3). This construct has been benchmarked for wild-type functionality and enables high-resolution crystallographic and biophysical studies of CRBN-degrader complexes, accelerating structure-based drug discovery.
High-throughput proteomics platforms deployed in 2024-2025 have dramatically expanded the known CRBN neosubstrate landscape (oleinikovas2024fromthalidomideto pages 2-4):
The ProxiCapture method developed by Kazi et al. (2026) combines purified CRBN with native cell or tissue lysates to map context-dependent neosubstrate profiles across different cell types, maturation states, and tissues. This work revealed that degrader-dependent interactors of CRBN are highly context-dependent, requiring broad sampling to uncover the full "glueable" proteome (oleinikovas2024fromthalidomideto pages 2-4).
O'Connor et al. (2025) demonstrated that tuning the open-close equilibrium of CRBN with different small molecules directly influences protein degradation efficacy, identifying key residues in the ligand-binding pocket and N-terminal belt essential for closure. Compounds that cannot induce CRBN closure have greatly reduced probability of yielding active degrader molecules (kroupova2024designofa pages 1-3).
| Aspect | Summary | Key details / examples | Evidence |
|---|---|---|---|
| Gene/protein identity | CRBN (cereblon), UniProt Q96SW2, human is the substrate receptor of the CRL4^CRBN E3 ubiquitin ligase complex | CRBN associates with DDB1, CUL4A/4B, and RBX1/ROC1 to confer substrate specificity for ubiquitination and subsequent proteasomal degradation | (cieslak2023cereblonrecruitingprotacswill pages 1-3, merinocacho2025cullinringligasebioe3 pages 1-2, ito2021exploitingubiquitinligase pages 2-4, watson2022moleculargluecelmoda pages 1-3) |
| Primary molecular function | Substrate recognition adaptor/receptor in a Cullin-RING ligase, rather than a catalytic enzyme itself | CRBN recruits substrates to the CRL4 core, enabling E2-dependent ubiquitin transfer; drug binding can reprogram substrate specificity toward neosubstrates | (cieslak2023cereblonrecruitingprotacswill pages 1-3, ito2021exploitingubiquitinligase pages 2-4, watson2022moleculargluecelmoda pages 1-3, ito2020molecularmechanismsof pages 2-4) |
| Structural organization | CRBN contains three folded domains plus an N-terminal region important for conformational control | Lon protease-like domain (Lon), helical bundle (HB) that docks to DDB1, and C-terminal thalidomide-binding domain (TBD) harboring the ligand pocket; ligand binding promotes open-to-closed rearrangement | (kroupova2024designofa pages 1-3, watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3) |
| Conformational mechanism | Small-molecule binding regulates CRBN conformation and thereby substrate recruitment | CELMoD/IMiD binding to the TBD is sufficient to trigger transition from an open to closed CRBN state; stable neosubstrate engagement requires the closed state | (watson2022moleculargluecelmod pages 1-2, watson2022moleculargluecelmoda pages 1-3) |
| Endogenous substrate recognition | CRBN recognizes native cellular substrates in the absence of exogenous drugs, although the endogenous substrate landscape is still being defined | Reviews summarize MEIS2 and SLO1 as endogenous CRL4^CRBN substrates; experimental work identified ILF2 as a CRBN-interacting substrate whose ubiquitination and proteasomal degradation are promoted by CRBN | (ito2021exploitingubiquitinligase pages 2-4, lian2020cereblonpromotesthe pages 1-2) |
| Endogenous substrates highlighted in this report | Representative native targets linked to physiological CRBN activity | MEIS2; SLO1; ILF2 (with ILF2 K45 implicated as a key ubiquitination site in one study) | (ito2021exploitingubiquitinligase pages 2-4, lian2020cereblonpromotesthe pages 1-2) |
| Drug-induced neosubstrates | IMiDs/CELMoDs convert CRBN into a recruiter of neosubstrates that are not normally targeted in the same way | Canonical examples include IKZF1 (Ikaros) and IKZF3 (Aiolos); additional therapeutically or biologically important neosubstrates include CK1α, GSPT1, and teratogenicity-linked SALL4 | (costacurta2021molecularmechanismsof pages 2-4, ito2021exploitingubiquitinligase pages 2-4, oleinikovas2024fromthalidomideto pages 2-4, ito2020molecularmechanismsof pages 2-4) |
| Degron / binding principles | Many CRBN molecular-glue neosubstrates use a recognizable structural motif | Structural analyses describe a G-loop motif whose backbone and side chains contact CRBN residues such as N351, H357, and W400 in drug-stabilized ternary complexes; this explains selectivity rules for many neosubstrates | (oleinikovas2024fromthalidomideto pages 2-4) |
| Subcellular localization | CRBN functions in both nucleus and cytoplasm | Prior work summarized in later studies notes CRBN localization in both compartments; ternary complex imaging showed CRBN-based degraders can operate mainly in the nucleus for BRD4-directed degradation and in the cytoplasm for FKBP12-directed degradation | (kaji2020characterizationofcereblondependent pages 1-2, lian2020cereblonpromotesthe pages 1-2) |
| Role in IMiD mechanism | CRBN is the direct target of thalidomide-class drugs and the central mediator of their downstream effects | Thalidomide/lenalidomide/pomalidomide bind the TBD; this rewires CRBN substrate specificity, causing ubiquitination and degradation of selected neosubstrates and explaining major therapeutic as well as teratogenic effects | (kroupova2024designofa pages 1-3, costacurta2021molecularmechanismsof pages 2-4, ito2021exploitingubiquitinligase pages 2-4, ito2020molecularmechanismsof pages 2-4) |
| Therapeutic relevance | CRBN is a major E3 ligase co-opted in modern targeted protein degradation | A large fraction of clinical PROTACs/degraders recruit CRBN; next-generation CELMoDs such as mezigdomide exploit improved CRBN engagement and neosubstrate degradation potency | (cieslak2023cereblonrecruitingprotacswill pages 1-3, watson2022moleculargluecelmoda pages 1-3) |
Table: This table summarizes the core functional annotation of human cereblon (CRBN), including its structural domains, molecular role in CRL4 ubiquitin ligase complexes, key endogenous and drug-induced substrates, localization, and importance in IMiD pharmacology. It is useful as a compact evidence-backed reference for the main biological and translational features of CRBN.
Cereblon (CRBN, UniProt Q96SW2) functions as the substrate receptor of the CRL4^CRBN E3 ubiquitin ligase complex, where it confers substrate specificity for targeted protein degradation. The protein contains three key domains—Lon, helical bundle, and thalidomide-binding domain—that undergo dynamic conformational rearrangement between open and closed states upon ligand binding. This conformational change is critical for stable neosubstrate recruitment and subsequent ubiquitination.
CRBN recognizes both endogenous substrates (MEIS2, SLO1, ILF2) and, when bound to small-molecule ligands, drug-induced neosubstrates (IKZF1/3, CK1α, GSPT1, SALL4). The G-loop degron motif is a primary recognition element, though non-canonical degrons have recently been identified. The protein localizes to both nucleus and cytoplasm, enabling substrate degradation in multiple cellular compartments.
As the direct target of thalidomide and related IMiDs, CRBN mediates both the therapeutic effects (via IKZF1/3 degradation in hematological malignancies) and adverse effects (via SALL4 degradation causing teratogenicity) of these drugs. CRBN is currently the most widely recruited E3 ligase in clinical-stage targeted protein degradation therapeutics, with next-generation CELMoDs and numerous PROTACs in development or clinical trials.
Recent advances (2023-2026) have revealed the importance of conformational dynamics in degrader function, expanded the neosubstrate landscape to include non-canonical degron-containing proteins, and developed new tools (CRBNmidi construct, ProxiCapture) for studying CRBN biology. These discoveries provide a foundation for rational design of more effective and selective CRBN-based therapeutics for cancer and other diseases.
References
(kroupova2024designofa pages 1-3): Alena Kroupova, Valentina A. Spiteri, Hirotake Furihata, Darren Darren, Sarath Ramachandran, Zoe J. Rutter, Sohini Chakraborti, Kevin Haubrich, Julie Pethe, Denzel Gonzales, Andre Wijaya, Maria Rodriguez-Rios, Dylan M. Lynch, William Farnaby, Mark A. Nakasone, David Zollman, and Alessio Ciulli. Design of a cereblon construct for crystallographic and biophysical studies of protein degraders. BioRxiv, Jan 2024. URL: https://doi.org/10.1101/2024.01.17.575503, doi:10.1101/2024.01.17.575503. This article has 48 citations.
(cieslak2023cereblonrecruitingprotacswill pages 1-3): Marcin Cieślak and Marta Słowianek. Cereblon-recruiting protacs: will new drugs have to face old challenges? Pharmaceutics, 15:812, Mar 2023. URL: https://doi.org/10.3390/pharmaceutics15030812, doi:10.3390/pharmaceutics15030812. This article has 45 citations.
(ito2021exploitingubiquitinligase pages 2-4): Takumi Ito, Yuki Yamaguchi, and Hiroshi Handa. Exploiting ubiquitin ligase cereblon as a target for small-molecule compounds in medicine and chemical biology. Cell Chemical Biology, 28:987-999, Jul 2021. URL: https://doi.org/10.1016/j.chembiol.2021.04.012, doi:10.1016/j.chembiol.2021.04.012. This article has 66 citations and is from a domain leading peer-reviewed journal.
(ito2020molecularmechanismsof pages 2-4): Takumi ITO and Hiroshi HANDA. Molecular mechanisms of thalidomide and its derivatives. Proceedings of the Japan Academy. Series B, Physical and Biological Sciences, 96:189-203, Jun 2020. URL: https://doi.org/10.2183/pjab.96.016, doi:10.2183/pjab.96.016. This article has 152 citations.
(merinocacho2025cullinringligasebioe3 pages 1-2): Laura Merino-Cacho, Orhi Barroso-Gomila, Mónica Pozo-Rodríguez, Veronica Muratore, Claudia Guinea-Pérez, Álvaro Serrano, Coralia Pérez, Sandra Cano-López, Ainhoa Urcullu, Mikel Azkargorta, Ibon Iloro, Carles Galdeano, Jordi Juárez-Jiménez, Ugo Mayor, Felix Elortza, Rosa Barrio, and James D. Sutherland. Cullin-ring ligase bioe3 reveals molecular-glue-induced neosubstrates and rewiring of the endogenous cereblon ubiquitome. Cell Communication and Signaling, Feb 2025. URL: https://doi.org/10.1186/s12964-025-02091-5, doi:10.1186/s12964-025-02091-5. This article has 12 citations and is from a peer-reviewed journal.
(watson2022moleculargluecelmoda pages 1-3): Edmond R. Watson, Scott Novick, Mary E. Matyskiela, Philip P. Chamberlain, Andres H. de la Peña, Jinyi Zhu, Eileen Tran, Patrick R. Griffin, Ingrid E. Wertz, and Gabriel C. Lander. Molecular glue celmod compounds are regulators of cereblon conformation. Science, 378:549-553, Nov 2022. URL: https://doi.org/10.1126/science.add7574, doi:10.1126/science.add7574. This article has 203 citations and is from a highest quality peer-reviewed journal.
(watson2022moleculargluecelmod pages 1-2): Edmond R. Watson, Scott J. Novick, Mary E. Matyskiela, Philip P. Chamberlain, Andres Hernandez de la Peña, Jin-Yi Zhu, Eileen Tran, Patrick R. Griffin, Ingrid E. Wertz, and Gabriel C. Lander. Molecular glue celmod compounds are allosteric regulators of cereblon conformation. bioRxiv, Jul 2022. URL: https://doi.org/10.1101/2022.07.02.498551, doi:10.1101/2022.07.02.498551. This article has 2 citations.
(oleinikovas2024fromthalidomideto pages 2-4): Vladas Oleinikovas, Pablo Gainza, Thomas Ryckmans, Bernhard Fasching, and Nicolas H. Thomä. From thalidomide to rational molecular glue design for targeted protein degradation. Jan 2024. URL: https://doi.org/10.1146/annurev-pharmtox-022123-104147, doi:10.1146/annurev-pharmtox-022123-104147. This article has 175 citations and is from a highest quality peer-reviewed journal.
(costacurta2021molecularmechanismsof pages 2-4): Matteo Costacurta, Jackson He, Philip E. Thompson, and Jake Shortt. Molecular mechanisms of cereblon-interacting small molecules in multiple myeloma therapy. Nov 2021. URL: https://doi.org/10.3390/jpm11111185, doi:10.3390/jpm11111185. This article has 31 citations.
(lian2020cereblonpromotesthe pages 1-2): Qihui Lian, Yuan Gao, Qian Li, Xian He, Xiaogang Jiang, Zhongjian Pu, and Guoqiang Xu. Cereblon promotes the ubiquitination and proteasomal degradation of interleukin enhancer-binding factor 2. The Protein Journal, 39:411-421, Oct 2020. URL: https://doi.org/10.1007/s10930-020-09918-9, doi:10.1007/s10930-020-09918-9. This article has 7 citations.
(kaji2020characterizationofcereblondependent pages 1-2): Tomohiro Kaji, Hiroshi Koga, Mutsumi Kuroha, Toshihiko Akimoto, and Kenji Hayata. Characterization of cereblon-dependent targeted protein degrader by visualizing the spatiotemporal ternary complex formation in cells. Scientific Reports, Feb 2020. URL: https://doi.org/10.1038/s41598-020-59966-5, doi:10.1038/s41598-020-59966-5. This article has 14 citations and is from a peer-reviewed journal.