The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Comprehensive research report: Human DCAF12L2 (UniProt Q5VW00; synonyms WDR40C)

Executive summary

Human DCAF12L2 (DDB1- and CUL4-associated factor 12-like protein 2; also called WDR40C) is a WD40-repeat protein proposed to act as a substrate receptor (DCAF) for CUL4–DDB1 (CRL4) cullin-RING E3 ubiquitin ligases, thereby providing substrate specificity for ubiquitin-dependent proteasomal degradation. The most direct DCAF12L2-specific functional evidence available in the retrieved corpus comes from a proteomics-focused source describing CRL4^DCAF12L2 substrate candidates (MEKK4 and the WDR11 complex via FAM91A1) and reporting cancer-associated missense mutations in WD40 repeats (e.g., P334L, R335C/H; ~337 region) that disrupt substrate binding. A separate experimental source reports negative or weak interaction evidence for DCAF12L2 with DDB1 and with the DCAF12 substrate MCMBP, suggesting that DCAF12L2 may have distinct substrate-recognition rules, different assembly constraints, or context-dependent CRL4 engagement compared with its close paralog DCAF12.

The major mechanistic advances in 2023–2024 are not on DCAF12L2 directly, but on DCAF12, a close family member, where cryo-EM structures and cell/in vitro binding assays show how a WD40 β-propeller uses a positively charged central pocket to bind C-terminal acidic di-Glu (–EE) degrons and recruit DDB1 in a CRL4 complex. These studies provide a high-confidence family mechanism that can be used as a cautious functional hypothesis for DCAF12L2, while clearly separating inference from direct DCAF12L2 evidence. (pla‐prats2023recognitionofthe pages 1-2, righetto2024probingthecrl4dcaf12 pages 2-2, righetto2024probingthecrl4dcaf12 pages 3-4, pla‐prats2023recognitionofthe media 671d1683, pla‐prats2023recognitionofthe media 05594edb)

1) Key concepts and definitions (current understanding)

1.1 CRL4 ubiquitin ligases and DCAFs

Cullin-RING ligases (CRLs) are multi-subunit E3 ubiquitin ligases. In CRL4 complexes, CUL4A/B form the scaffold, RBX1 recruits E2~ubiquitin, and DDB1 acts as an adaptor that recruits interchangeable substrate receptors called DCAFs (DDB1- and CUL4-associated factors). DCAFs are often WD40-repeat proteins that dock on DDB1 and bring substrates to the E3 machinery for ubiquitination and subsequent proteasomal degradation. (raisch2023pulsesilacandinteractomics pages 1-3, kolarova2025crl4dcaf12ubiquitinligasea pages 18-21)

1.2 WD40 repeats and WD40 β-propellers

WD40-repeat proteins commonly form β-propeller folds that provide versatile protein–protein interaction surfaces. For DCAF substrate receptors, the WD40 β-propeller can provide a binding pocket that recognizes degrons (degradation signals) in substrates. (pla‐prats2023recognitionofthe pages 1-2, righetto2024probingthecrl4dcaf12 pages 2-2, righetto2024probingthecrl4dcaf12 pages 3-4)

1.3 DCAF12 family mechanism (reference framework for DCAF12L2)

High-confidence structural/biochemical work on human DCAF12 shows it behaves as a canonical WD40 DCAF substrate receptor: it binds substrates carrying a C-terminal double glutamate (di-Glu; –EE) motif by using a positively charged central pocket at the center of its WD40 β-propeller. In cryo-EM structures of DDB1–DCAF12–CCT5, the CCT5 di-Glu motif inserts into this pocket; biochemical assays further show DCAF12 preferentially binds and ubiquitinates monomeric CCT5 rather than CCT5 assembled into TRiC, supporting a role in assembly quality control. (pla‐prats2023recognitionofthe pages 1-2, pla‐prats2023recognitionofthe media 671d1683, pla‐prats2023recognitionofthe media 05594edb)

2) Target identity verification (mandatory)

The literature examined here consistently refers to human DCAF12L2 (synonym WDR40C) as a WD40-repeat DCAF-family protein in a CRL4 context, matching the UniProt-specified identity (Q5VW00; DDB1- and CUL4-associated factor 12-like protein 2; WD40/DCAF12 family membership). No evidence in the retrieved corpus suggests confusion with a different organism or a different gene sharing a similar symbol. (onireti2022novelrolesof pages 1-6, kolarova2025crl4dcaf12ubiquitinligase pages 66-69)

3) Molecular function of DCAF12L2: what is directly supported vs inferred

3.1 Direct DCAF12L2-specific functional claims (available evidence)

CRL4 substrate receptor and candidate substrates (proteomics)
A proteomics-focused source reports DCAF12L2 as a CRL4 substrate receptor (CRL4^DCAF12L2) and describes affinity purification–mass spectrometry (AP-MS) evidence identifying MEKK4 and the WDR11 complex as two independent substrate contexts; it further reports that CRL4^DCAF12L2 mediates ubiquitylation of FAM91A1, a component of the WDR11 complex. This positions DCAF12L2 as a regulator of protein complex composition/stability via ubiquitination. (onireti2022novelrolesof pages 1-6)

Cancer-associated mutations that disrupt substrate binding
The same source reports that DCAF12L2 is hypermutated in cancer and highlights specific mutations in the WD40-repeat region—P334L, R335C, R335H, and a mutation near residue 337—that block DCAF12L2 binding to identified substrates, consistent with WD40-mediated substrate recognition. (onireti2022novelrolesof pages 1-6)

Degron recognition claim
This source also states that DCAF12L2 recognizes a C-terminal di-glutamic acid (EE) motif as a degron. In the retrieved corpus, this is not corroborated by an independent peer-reviewed mechanistic/structural paper specific to DCAF12L2; therefore, it should be treated as provisional until validated directly for DCAF12L2. (onireti2022novelrolesof pages 1-6)

3.2 Contrasting/negative DCAF12L2 functional evidence

A separate experimental source (2025) tested DCAF12L2 (and DCAF12L1) for interaction with MCMBP (a known DCAF12 substrate in that research program) and found no detectable binding, consistent with prior work that neither DCAF12L1 nor DCAF12L2 binds the same C-terminal acidic end degron as DCAF12. The authors also report no significant binding of DDB1 to DCAF12L1 or DCAF12L2 in their assays, concluding it remains unclear whether these paralogs can assemble a fully functional CRL4 complex under those conditions. (kolarova2025crl4dcaf12ubiquitinligase pages 66-69, kolarova2025crl4dcaf12ubiquitinligasea pages 66-69)

This discrepancy (proteomics evidence for CRL4^DCAF12L2 function vs weak/undetectable DDB1 binding in another assay system) can be reconciled by several non-exclusive explanations, including: context- and cell-type dependence; differing assay sensitivity; requirement for cofactors (e.g., DDA1) or post-translational modifications; or DCAF12L2 acting through non-canonical interfaces distinct from DCAF12. The available corpus does not resolve this definitively. (onireti2022novelrolesof pages 1-6, kolarova2025crl4dcaf12ubiquitinligase pages 66-69)

3.3 Family-based inference: likely biochemical activity

DCAF12 family proteins are not enzymes that catalyze small-molecule reactions; rather, they are expected to function as adaptor/substrate receptors that promote ubiquitin transfer to substrates by positioning them in proximity to the CRL4 catalytic core. Strong structural/biochemical evidence in 2023–2024 shows DCAF12 recognizes C-terminal –EE degrons with nanomolar affinity in vitro and in cells and binds them in the WD40 central pocket, providing a concrete template for hypothesizing how a closely related WD40 DCAF12-family paralog such as DCAF12L2 might recognize degrons. (pla‐prats2023recognitionofthe pages 1-2, righetto2024probingthecrl4dcaf12 pages 2-2, righetto2024probingthecrl4dcaf12 pages 3-4)

4) Subcellular localization and where the gene product carries out function

Direct DCAF12L2 localization evidence was not found in the retrieved corpus. The main DCAF12 mechanistic studies provide a relevant reference framework: DCAF12 functions in CRL4 complexes involved in ubiquitination-dependent degradation and can discriminate between monomeric and assembled subunits of a large chaperonin complex, implying activity in compartments where assembly quality control occurs. (pla‐prats2023recognitionofthe pages 1-2)

Given the conflicting evidence about DCAF12L2’s DDB1 binding/CRL4 assembly, any statement about DCAF12L2 localization should be treated as unresolved based on the currently retrieved texts. (kolarova2025crl4dcaf12ubiquitinligase pages 66-69)

5) Pathways and biological processes implicated

5.1 Direct DCAF12L2-linked processes

The proteomics evidence implicating MEKK4 suggests a possible connection to MAPK signaling cascades, while the WDR11 complex/FAM91A1 ubiquitylation suggests a role in regulating multiprotein complex integrity. However, the retrieved corpus does not provide a detailed pathway map or functional phenotyping of these interactions. (onireti2022novelrolesof pages 1-6)

5.2 Family-level processes supported by strong 2023–2024 evidence

The best-supported mechanistic role for DCAF12 (family member) is in assembly quality control, where CRL4^DCAF12 targets proteins with exposed C-terminal di-Glu degrons and specifically ubiquitinates unassembled subunits (e.g., monomeric CCT5) while sparing fully assembled complexes (TRiC). This is a well-defined biological principle that could plausibly extend to DCAF12L2 if it also recognizes terminal acidic degrons, but direct extension to DCAF12L2 remains unproven. (pla‐prats2023recognitionofthe pages 1-2)

6) Recent developments and latest research (prioritizing 2023–2024)

6.1 2023: Cryo-EM mechanism for DCAF12 degron recognition and assembly QC

Pla-Prats et al. (EMBO Journal; publication date Jan 2023; https://doi.org/10.15252/embj.2022112253) report a 2.8 Å cryo-EM structure of the DDB1–DCAF12–CCT5 complex and show DCAF12 binds the CCT5 di-Glu degron in the WD40 central pocket. Importantly, they provide functional evidence that DCAF12 binds/ubiquitinates monomeric CCT5 but not TRiC-assembled CCT5, establishing an assembly-dependent substrate-selection rule. (pla‐prats2023recognitionofthe pages 1-2, pla‐prats2023recognitionofthe media 671d1683, pla‐prats2023recognitionofthe media 05594edb)

6.2 2024: Higher-resolution interrogation and assays enabling drug discovery (DCAF12)

Righetto et al. (PNAS Nexus; publication date Apr 2024; https://doi.org/10.1093/pnasnexus/pgae153) developed a suite of NanoBRET cellular assays and in vitro binding assays for DCAF12 interactions with di-Glu degrons from MAGEA3 and CCT5, and report a cryo-EM structure of DDB1–DCAF12–MAGEA3. They also map critical positively charged residues in the WD40 central channel (e.g., K91, K108, R203, R256, R344) required for substrate engagement, and discuss how these tools/structures could enable finding small-molecule “handles” targeting the WD40 domain of DCAF12 for future degrader (PROTAC) design. This is a major real-world “application pathway” for DCAF-type substrate receptors, but is currently DCAF12-focused, not DCAF12L2-validated. (righetto2024probingthecrl4dcaf12 pages 2-2, righetto2024probingthecrl4dcaf12 pages 3-4)

6.3 2023: Systematic DCAF interactomics and degradation measurement pipeline

Raisch et al. (Molecular & Cellular Proteomics; publication date Oct 2023; https://doi.org/10.1016/j.mcpro.2023.100644) describe BioID/AP-MS and pulse-SILAC strategies to link DCAF–DDB1 interactions to downstream substrate degradation effects, illustrating scalable approaches that could be applied to map DCAF12L2 substrates and confirm CRL4 engagement under defined cellular conditions. (raisch2023pulsesilacandinteractomics pages 1-3)

7) Current applications and real-world implementations

1. Cancer variant interpretation and functional genomics: DCAF12L2 mutations (P334L, R335C/H; ~337 region) reported to disrupt substrate binding provide candidate functional readouts for cancer genomics (i.e., mutations altering E3-substrate recognition rather than catalytic residues). Translationally, such mutations can be prioritized for experimental validation as drivers/modifiers of proteostasis. (onireti2022novelrolesof pages 1-6)

2. Targeted protein degradation (TPD) tool development (family-level, DCAF12): Recent 2024 work explicitly frames the DCAF12 WD40 pocket as potentially druggable and provides NanoBRET assays and structural constraints for ligand discovery, supporting the broader real-world push to expand the repertoire of E3 ligases used in PROTAC strategies. This is not yet demonstrated for DCAF12L2, but provides a plausible blueprint if DCAF12L2 proves to have an analogous pocket and robust CRL4 assembly in cells. (righetto2024probingthecrl4dcaf12 pages 2-2)

3. Assembly quality-control biology (family-level, DCAF12): The rule that CRL4^DCAF12 targets unassembled subunits (monomeric CCT5) suggests a generalizable cellular mechanism for maintaining stoichiometry of large complexes; analogous mechanisms could be explored for DCAF12L2 in contexts such as WDR11 complex regulation. (pla‐prats2023recognitionofthe pages 1-2, onireti2022novelrolesof pages 1-6)

8) Expert opinions and analysis (authoritative sources)

• Mechanistic consensus for DCAF12 (closest paralog): Authoritative primary structural biology studies in 2023–2024 converge on the concept that DCAF12 is a canonical WD40 DCAF recognizing C-terminal acidic di-Glu degrons via a conserved positively charged pocket, recruiting DDB1 in a CRL4 complex to drive ubiquitination and degradation. This consensus is supported by two independent cryo-EM structures plus complementary biochemical and cell-based assays. (pla‐prats2023recognitionofthe pages 1-2, righetto2024probingthecrl4dcaf12 pages 2-2, righetto2024probingthecrl4dcaf12 pages 3-4)

• For DCAF12L2 specifically, the evidence base is fragmented: One line of evidence (proteomics and mutation-impact findings) argues for bona fide substrate receptor behavior with identifiable substrates and functional cancer mutations affecting binding. Another line reports weak/undetectable DDB1 interaction and inability to bind a canonical DCAF12 substrate/degron. A conservative expert interpretation is that DCAF12L2 is likely a DCAF-like protein whose CRL4 assembly and degron recognition may be conditional, substrate-specific, and/or divergent from DCAF12. (onireti2022novelrolesof pages 1-6, kolarova2025crl4dcaf12ubiquitinligase pages 66-69)

9) Relevant statistics and data from recent studies

9.1 Quantitative disease-association signals (Open Targets)

Open Targets lists modest disease–target associations for DCAF12L2 (ENSG00000198354), including:
- Glioblastoma multiforme: score ~0.2712
- Restless legs syndrome: ~0.2438
- Acquired thrombocytopenia: ~0.2247
- Lung adenocarcinoma: ~0.2232
- Prostate adenocarcinoma: ~0.2141

These scores summarize heterogeneous evidence types and should not be interpreted as proof of causality without examination of underlying studies. (OpenTargets Search: -DCAF12L2)

9.2 Mutation-level data (DCAF12L2)

Cancer-associated mutations highlighted for DCAF12L2 include P334L, R335C, R335H, and a mutation near 337 within WD40 repeat regions, with reported functional consequence of blocking substrate binding. These are actionable mutation sites for follow-up mechanistic studies. (onireti2022novelrolesof pages 1-6)

9.3 Binding-affinity statistics (family-level DCAF12)

In 2024, DCAF12 binding to C-terminal degron peptides (MAGEA3 and CCT5) is described as nanomolar affinity by assays developed in that work, strengthening the plausibility that WD40 central-pocket binding can yield tight and drug-targetable interactions. This is DCAF12 data, not DCAF12L2. (righetto2024probingthecrl4dcaf12 pages 2-2)

10) Visual evidence supporting mechanism (family-level)

The cryo-EM visual evidence showing the WD40 β-propeller pocket engaging a C-terminal di-Glu degron, and the overall architecture of the DDB1–DCAF12–CCT5 complex, is captured in the retrieved figure crops. (pla‐prats2023recognitionofthe media 671d1683, pla‐prats2023recognitionofthe media 05594edb)

11) Evidence summary table

The following table summarizes what is directly known for DCAF12L2 versus what is inferred from the better-studied paralog DCAF12.

Table: This table summarizes direct versus inferred functional annotation evidence for human DCAF12L2 (Q5VW00), separating sparse target-specific findings from stronger family-level DCAF12 mechanistic data. It is useful for identifying what is experimentally supported, what remains uncertain, and where recent structural biology informs cautious functional inference.

12) Key limitations and recommended next experiments (to close annotation gaps)

Limitations of the current evidence base:
- The strongest DCAF12L2-specific functional claims in this retrieved corpus derive from a source with incomplete bibliographic metadata (thesis/unknown venue), and thus should be corroborated in peer-reviewed primary literature. (onireti2022novelrolesof pages 1-6)
- Direct evidence for DCAF12L2 subcellular localization, tissue expression, and validated degron specificity is not available in the retrieved corpus.
- Conflicting reports about DCAF12L2–DDB1 binding highlight the need for standardized cellular reconstitution and multiple orthogonal interaction assays. (kolarova2025crl4dcaf12ubiquitinligase pages 66-69)

High-value experiments to functionally annotate DCAF12L2:
- Reconstitute DCAF12L2 with DDB1 (±DDA1) and test binding to candidate substrates MEKK4 and FAM91A1 using AP-MS, NanoBRET, and purified-protein assays analogous to the validated DCAF12 workflows. (righetto2024probingthecrl4dcaf12 pages 2-2, raisch2023pulsesilacandinteractomics pages 1-3, onireti2022novelrolesof pages 1-6)
- Map DCAF12L2 degron preference by systematic C-terminal peptide libraries, and test whether cancer mutations P334L/R335C/H disrupt degron-pocket binding. (onireti2022novelrolesof pages 1-6)
- Determine a DDB1–DCAF12L2 cryo-EM structure (if complex formation is robust) to assess whether the central WD40 pocket and charge distribution resemble DCAF12’s di-Glu binding architecture. (pla‐prats2023recognitionofthe pages 1-2, pla‐prats2023recognitionofthe media 671d1683, pla‐prats2023recognitionofthe media 05594edb)

References (URLs and publication dates from retrieved sources)

• Pla-Prats C. et al. The EMBO Journal (Jan 2023). “Recognition of the CCT5 di-Glu degron by CRL4DCAF12 is dependent on TRiC assembly.” https://doi.org/10.15252/embj.2022112253 (pla‐prats2023recognitionofthe pages 1-2, pla‐prats2023recognitionofthe media 671d1683, pla‐prats2023recognitionofthe media 05594edb)
• Raisch J. et al. Molecular & Cellular Proteomics (Oct 2023). “Pulse-SILAC and Interactomics Reveal Distinct DDB1-CUL4–Associated Factors, Cellular Functions, and Protein Substrates.” https://doi.org/10.1016/j.mcpro.2023.100644 (raisch2023pulsesilacandinteractomics pages 1-3)
• Righetto G.L. et al. PNAS Nexus (Apr 2024). “Probing the CRL4DCAF12 interactions with MAGEA3 and CCT5 di-Glu C-terminal degrons.” https://doi.org/10.1093/pnasnexus/pgae153 (righetto2024probingthecrl4dcaf12 pages 2-2, righetto2024probingthecrl4dcaf12 pages 3-4)
• Open Targets Platform (accessed in current session): DCAF12L2 disease association scores. (OpenTargets Search: -DCAF12L2)
• Onireti J.O. (2022; thesis/unknown venue in retrieved corpus): DCAF12L2 substrates, cancer mutations, and EE degron claim. (onireti2022novelrolesof pages 1-6)
• Kolářová K. (2025; unknown venue in retrieved corpus): negative/weak DCAF12L2 binding to MCMBP and DDB1 in their assay; higher expression than DCAF12. (kolarova2025crl4dcaf12ubiquitinligase pages 66-69, kolarova2025crl4dcaf12ubiquitinligasea pages 66-69)

References

1. (pla‐prats2023recognitionofthe pages 1-2): Carlos Pla‐Prats, Simone Cavadini, Georg Kempf, and Nicolas H Thomä. Recognition of the cct5 di‐glu degron by crl4dcaf12 is dependent on tric assembly. The EMBO Journal, Jan 2023. URL: https://doi.org/10.15252/embj.2022112253, doi:10.15252/embj.2022112253. This article has 26 citations.

2. (righetto2024probingthecrl4dcaf12 pages 2-2): Germanna Lima Righetto, Yanting Yin, David M Duda, Victoria Vu, Magdalena M Szewczyk, Hong Zeng, Yanjun Li, Peter Loppnau, Tony Mei, Yen-Yen Li, Alma Seitova, Aaron N Patrick, Jean-Francois Brazeau, Charu Chaudhry, Dalia Barsyte-Lovejoy, Vijayaratnam Santhakumar, and Levon Halabelian. Probing the crl4dcaf12 interactions with magea3 and cct5 di-glu c-terminal degrons. PNAS Nexus, Apr 2024. URL: https://doi.org/10.1093/pnasnexus/pgae153, doi:10.1093/pnasnexus/pgae153. This article has 6 citations and is from a peer-reviewed journal.

3. (righetto2024probingthecrl4dcaf12 pages 3-4): Germanna Lima Righetto, Yanting Yin, David M Duda, Victoria Vu, Magdalena M Szewczyk, Hong Zeng, Yanjun Li, Peter Loppnau, Tony Mei, Yen-Yen Li, Alma Seitova, Aaron N Patrick, Jean-Francois Brazeau, Charu Chaudhry, Dalia Barsyte-Lovejoy, Vijayaratnam Santhakumar, and Levon Halabelian. Probing the crl4dcaf12 interactions with magea3 and cct5 di-glu c-terminal degrons. PNAS Nexus, Apr 2024. URL: https://doi.org/10.1093/pnasnexus/pgae153, doi:10.1093/pnasnexus/pgae153. This article has 6 citations and is from a peer-reviewed journal.

4. (pla‐prats2023recognitionofthe media 671d1683): Carlos Pla‐Prats, Simone Cavadini, Georg Kempf, and Nicolas H Thomä. Recognition of the cct5 di‐glu degron by crl4dcaf12 is dependent on tric assembly. The EMBO Journal, Jan 2023. URL: https://doi.org/10.15252/embj.2022112253, doi:10.15252/embj.2022112253. This article has 26 citations.

5. (pla‐prats2023recognitionofthe media 05594edb): Carlos Pla‐Prats, Simone Cavadini, Georg Kempf, and Nicolas H Thomä. Recognition of the cct5 di‐glu degron by crl4dcaf12 is dependent on tric assembly. The EMBO Journal, Jan 2023. URL: https://doi.org/10.15252/embj.2022112253, doi:10.15252/embj.2022112253. This article has 26 citations.

6. (raisch2023pulsesilacandinteractomics pages 1-3): Jennifer Raisch, Marie-Line Dubois, Marika Groleau, Dominique Lévesque, Thomas Burger, Carla-Marie Jurkovic, Romain Brailly, Gwendoline Marbach, Alyson McKenna, Catherine Barrette, Pierre-Étienne Jacques, and François-Michel Boisvert. Pulse-silac and interactomics reveal distinct ddb1-cul4–associated factors, cellular functions, and protein substrates. Molecular & Cellular Proteomics, 22:100644, Oct 2023. URL: https://doi.org/10.1016/j.mcpro.2023.100644, doi:10.1016/j.mcpro.2023.100644. This article has 13 citations and is from a domain leading peer-reviewed journal.

7. (kolarova2025crl4dcaf12ubiquitinligasea pages 18-21): K Kolářová. Crl4dcaf12 ubiquitin ligase: a novel factor in dna replication control. Unknown journal, 2025.

8. (onireti2022novelrolesof pages 1-6): JO Onireti. Novel roles of cullin-ring ligases in cell signalling and implications in health and disease. Unknown journal, 2022.

9. (kolarova2025crl4dcaf12ubiquitinligase pages 66-69): K Kolářová. Crl4dcaf12 ubiquitin ligase: a novel factor in dna replication control. Unknown journal, 2025.

10. (kolarova2025crl4dcaf12ubiquitinligasea pages 66-69): K Kolářová. Crl4dcaf12 ubiquitin ligase: a novel factor in dna replication control. Unknown journal, 2025.

11. (OpenTargets Search: -DCAF12L2): Open Targets Query (-DCAF12L2, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

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Citations

1. onireti2022novelrolesof pages 1-6
2. raisch2023pulsesilacandinteractomics pages 1-3
3. https://doi.org/10.15252/embj.2022112253
4. https://doi.org/10.1093/pnasnexus/pgae153
5. https://doi.org/10.1016/j.mcpro.2023.100644
6. https://doi.org/10.15252/embj.2022112253;
7. https://doi.org/10.1093/pnasnexus/pgae153;
8. https://doi.org/10.15252/embj.2022112253,
9. https://doi.org/10.1093/pnasnexus/pgae153,
10. https://doi.org/10.1016/j.mcpro.2023.100644,