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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 CTBP1 (UniProt Q13363) – Functional Annotation

0. Target verification (mandatory)

The research target is human C-terminal-binding protein 1 (CtBP1) encoded by CTBP1 (UniProt Q13363). The retrieved literature consistently describes CtBP1 as a D-isomer–specific 2‑hydroxyacid dehydrogenase (D2‑HDH)-like protein that contains an NAD(H)-binding Rossmann fold and a protein–protein interaction cleft that recognizes PXDLS/PLDLS short motifs in transcriptional regulators, matching the UniProt description and domain architecture provided (CtBP/CTBP_dehydrogenase/D‑isomer‑2‑hydroxyacid dehydrogenase family features). (huang2024cterminalbindingprotein pages 2-4, chen2021thetransrepressionand pages 1-2)

Table: Concise, evidence-mapped summary of CTBP1 (Q13363) covering mechanisms, partners, regulation, 2024 updates, and translational inhibitors with quantitative data. Citations point to primary and review sources supporting each entry.

1. Key concepts and definitions (current understanding)

1.1 What CtBP1 is

CtBP1 is best understood as a transcriptional coregulator (primarily a corepressor) that lacks intrinsic DNA-binding capacity and instead is recruited to chromatin by DNA-binding transcription factors and repressors that present PXDLS/PLDLS-like short linear motifs (SLiMs). (huang2024cterminalbindingprotein pages 2-4, chen2021thetransrepressionand pages 1-2)

1.2 How CtBP1 represses transcription

Mechanistically, CtBP1 functions as a scaffold that nucleates multi-protein corepressor assemblies. It binds PXDLS-bearing DNA-binding proteins and recruits chromatin-modifying enzymes including histone deacetylases (HDACs) and other epigenetic regulators (e.g., LSD1/KDM1A, RCOR1/CoREST, and methylation-related machinery), resulting in histone modification changes that favor transcriptional repression. (huang2024cterminalbindingprotein pages 2-4, chen2021thetransrepressionand pages 1-2, lee2025usingtheallen pages 6-8)

1.3 A “metabolic sensor” corepressor

A defining conceptual feature is that CtBP1 corepressor function is coupled to cellular redox/metabolic status through binding of NADH (and NAD+/related nucleotides) at its Rossmann fold. NADH binding promotes CtBP1 multimerization states (dimer/tetramer assemblies) that are linked to corepressor activity. This forms a molecular basis for CtBP1’s frequent description as a metabolic/redox sensor in transcriptional control. (chen2021thetransrepressionand pages 1-2, lee2025usingtheallen pages 1-2)

1.4 Enzyme-like domain: what is (and isn’t) established

CtBP1 is homologous to D2‑hydroxyacid dehydrogenases and contains a substrate-binding domain (SBD) plus a Rossmann fold. Small molecules such as MTOB (4‑methylthio‑2‑oxobutyric acid) bind in the active-site region; however, much of CtBP1 biology depends on its corepressor/scaffolding function rather than a well-defined, physiology-dominant metabolic catalytic reaction in vivo. (chen2021thetransrepressionand pages 1-2, chen2021thetransrepressionand pages 5-7)

2. Molecular functions, partners, pathways, and localization (evidence-based)

2.1 Interaction logic: PXDLS recruitment plus non-PXDLS partner binding

CtBP1 recognizes PXDLS-like motifs and can also associate with other partners through additional interfaces, enabling assembly of large transcriptional complexes. A 2024 review highlights both PXDLS recognition and interactions with non-PXDLS partners, including chromatin and DNA-damage-related factors. (huang2024cterminalbindingprotein pages 2-4)

2.2 Representative complex components and interactors

Evidence across the included sources supports CtBP1 association with:
- HDAC1/HDAC2 and LSD1/KDM1A with RCOR1/CoREST as a repressive chromatin module (lee2025usingtheallen pages 6-8)
- CtIP/RBBP8 as a component in CtBP-containing repression complexes relevant to DNA repair gene control in at least some settings (lee2025usingtheallen pages 6-8)
- DNA-binding transcriptional regulators such as ZEB1/2 and KLF family proteins that recruit CtBP via motif interactions (chen2021thetransrepressionand pages 1-2, lee2025usingtheallen pages 6-8)

2.3 Subcellular localization: nucleus ↔ cytoplasm/Golgi and specialized roles

CtBP1 is functionally nuclear as a corepressor, but also has well-described non-nuclear roles. CtBP1/BARS is described as having both transcriptional corepressor activity and a membrane fission function relevant to membrane trafficking and Golgi dynamics, linking localization to cell-cycle and secretory phenotypes. (huang2024cterminalbindingprotein pages 2-4, filograna2024identificationandcharacterization pages 1-2)

In neuronal contexts, CtBP1 can shuttle between nucleus and cytoplasm and has reported interactions with presynaptic scaffold proteins (e.g., Bassoon/Piccolo), supporting specialized synaptic roles alongside transcriptional regulation. (lee2025usingtheallen pages 9-11)

2.4 Pathways and biological processes most directly supported by this evidence set

Across the cited works, CtBP1 is most directly implicated in:
- Epithelial–mesenchymal transition (EMT) and malignant transcriptional programs via repression of epithelial genes and/or modulation of EMT-related networks (chen2021thetransrepressionand pages 1-2, filograna2024identificationandcharacterization pages 22-25)
- Apoptosis/cell survival programs, via repression of pro-apoptotic genes and tumor-suppressor pathways in cancer contexts (lim2024transcriptionalcorepressoractivity pages 3-7, filograna2024identificationandcharacterization pages 25-27)
- DNA damage response (DDR) gene regulation through transcriptional control (distinct from direct enzymatic repair), including repression of DDR-related genes in cancer cell models (lee2025usingtheallen pages 6-8)

3. Recent developments (prioritizing 2023–2024)

3.1 2024 structural/mechanistic breakthrough: RAI2-driven CtBP polymerization inactivates corepressor function

A 2024 Nature Communications study reports a mechanism whereby RAI2, a largely intrinsically disordered protein, contains two tandem ALDLS (PxDLS-like) SLiMs that bind CtBP and drive multivalent interaction–induced polymerization of CtBP into filamentous assemblies (stacked tetrameric layers). The study connects polymerization to nuclear CtBP foci and functional inactivation of CtBP corepressor activity, including relief of repression at CDKN1A (p21) with increased promoter activity (~2.5-fold) and decreased H3K27me3 at the promoter in RAI2-present settings. Methods include cryo-EM (3.0 Å structure for filaments), X-ray crystallography, SAXS, NMR, and SEC. (goradia2024mastercorepressorinactivation pages 1-4, goradia2024mastercorepressorinactivation pages 8-11, goradia2024mastercorepressorinactivation pages 4-8)

Clinical association within the same work indicates that RAI2 decreases in advanced treatment-resistant prostate cancer subtypes and reports circulating tumor cell (CTC) positivity rates consistent with progression: RAI2 detected in 89% of CRPC CTCs vs 35% in AVPC vs 19% in NEPC, supporting RAI2 loss as linked to aggressive disease phenotypes and suggesting a disease-relevant shift away from RAI2-mediated CtBP inactivation. (goradia2024mastercorepressorinactivation pages 11-14)

3.2 2024 post-translational regulation: CtBP1 ISGylation increases partner affinity and repression potency

A 2024 study reports that CtBP1 is modified by ISG15 (ISGylation) following interferon-α stimulation and that this modification is regulated by an ISGylation E3 ligase (EFP) and reversed by the deISGylase (USP18). Functionally, ISGylation increases CtBP1 binding to HDAC1 and LSD1, while not changing CtBP1 association with HDAC4, and enhances CtBP1 transcriptional repression of genes linked to EMT and apoptosis (including E-cadherin, Bax, Noxa in their tested system). The authors note that the CtBP1 ISGylation site(s) remain to be identified. (lim2024transcriptionalcorepressoractivity pages 1-2, lim2024transcriptionalcorepressoractivity pages 3-7, lim2024transcriptionalcorepressoractivity pages 7-8)

3.3 2024 translational inhibitor development: targeting CtBP1/BARS Rossmann fold with “Comp.11”

A 2024 Journal of Experimental & Clinical Cancer Research paper reports a structure-guided discovery of Comp.11 (N-(3,4-dichlorophenyl)-4-{[(4-nitrophenyl)carbamoyl]amino}benzenesulfonamide) as a potent and selective inhibitor of CtBP1/BARS (not CtBP2) that binds the Rossmann fold near the NADH-binding region and forms a ternary complex with NADH, altering oligomerization and preventing productive partner interactions. (filograna2024identificationandcharacterization pages 1-2, filograna2024identificationandcharacterization pages 9-11, filograna2024identificationandcharacterization pages 25-27)

Quantitative binding: ITC reports Kd = 0.66 ± 0.20 μM for Comp.11 binding (with one ligand per protein in their model). (filograna2024identificationandcharacterization pages 9-11, filograna2024identificationandcharacterization media a3db0a0a)

Mechanistic cellular effects: Comp.11 promotes redistribution of CtBP1/BARS from nucleus to cytoplasm/Golgi, disrupts partner interactions (including transcriptional and membrane fission partners), induces Golgi tubulation consistent with impaired fission, blocks mitotic entry and secretion-related functions, and shifts transcriptional programs toward a more epithelial phenotype with reduced invasion. (filograna2024identificationandcharacterization pages 9-11, filograna2024identificationandcharacterization pages 11-14, filograna2024identificationandcharacterization pages 22-25)

In vivo efficacy (mouse xenograft): In an A375MM melanoma xenograft model, Comp.11 at 20 mg/kg produced significant tumor growth inhibition with reported reductions in tumor-burden metrics and significant tumor weight reduction (p-values reported around 0.02–0.03), with percent change in tumor burden reported as ~39.39% (day 14, 20 mg/kg) versus a smaller effect at 10 mg/kg; treatment was described as well tolerated with maintained body weight. (filograna2024identificationandcharacterization pages 22-25, filograna2024identificationandcharacterization media a3db0a0a, filograna2024identificationandcharacterization media 4353de2d, filograna2024identificationandcharacterization media 440b0878)

4. Current applications and real-world implementations

4.1 Preclinical oncology targeting

The most concrete real-world implementation in this evidence set is preclinical pharmacologic targeting of CtBP1/BARS with Comp.11 in melanoma models (cell lines and mouse xenografts), providing a translational path toward CtBP1-directed therapies. (filograna2024identificationandcharacterization pages 22-25, filograna2024identificationandcharacterization pages 9-11)

4.2 Biomarker/clinical stratification concepts

The RAI2–CtBP polymerization work provides a clinically oriented application: RAI2 expression in CTCs and tumor progression states may serve as a biomarker axis reflecting CtBP repression states in prostate cancer subtypes (CRPC vs AVPC vs NEPC). (goradia2024mastercorepressorinactivation pages 11-14)

4.3 Virus–cancer interface (emerging application area)

A 2024 review frames CtBP proteins as regulators at the intersection of viral infection and tumorigenesis, synthesizing evidence that CtBP proteins contribute to oncogenic transcriptional programs and may be exploitable for antiviral/anticancer strategies; it also emphasizes that antiviral applications remain comparatively less developed. (huang2024cterminalbindingprotein pages 2-4)

5. Expert opinions/authoritative analysis (as expressed in reviews and mechanistic papers)

5.1 CtBP1 as an actionable hub: why experts consider it druggable

Authoritative synthesis emphasizes CtBP1’s D2‑HDH-like Rossmann fold and ligand-binding pocket as an attractive intervention site, and frames inhibitor development as feasible via structure-guided design targeting the Rossmann fold or substrate-binding region, with the expectation that blocking CtBP1 oligomerization/partner binding can reprogram transcriptional outputs in disease. (huang2024cterminalbindingprotein pages 2-4, filograna2024identificationandcharacterization pages 1-2)

5.2 Regulatory layers beyond NADH: polymerization and ISGylation

The 2024 Nature Communications study proposes polymerization as an additional structural/regulatory layer that can switch CtBP from an active tetrameric corepressor assembly to an inactivated filament/foci state, suggesting new ways to modulate CtBP activity beyond classic competitive inhibition. (goradia2024mastercorepressorinactivation pages 1-4, goradia2024mastercorepressorinactivation pages 8-11)

The 2024 ISGylation work provides a distinct perspective: immune signaling (IFN-α) can potentiate CtBP1 repression by increasing its affinity for specific epigenetic enzymes, implying that CtBP1 activity is integrated with inflammatory signaling states. (lim2024transcriptionalcorepressoractivity pages 1-2, lim2024transcriptionalcorepressoractivity pages 3-7)

6. Statistics and data highlights from recent studies

• Comp.11 binding affinity: CtBP1/BARS Kd = 0.66 ± 0.20 μM by ITC. (filograna2024identificationandcharacterization pages 9-11, filograna2024identificationandcharacterization media a3db0a0a)
• Melanoma xenograft response: Comp.11 shows significant growth inhibition at 20 mg/kg, with reported tumor-burden percent change metrics including ~39.39% (day 14, 20 mg/kg) and significant tumor weight reduction. (filograna2024identificationandcharacterization pages 22-25, filograna2024identificationandcharacterization media 4353de2d)
• Prostate cancer CTC RAI2 positivity across progression: 89% CRPC, 35% AVPC, 19% NEPC. (goradia2024mastercorepressorinactivation pages 11-14)

7. Evidence gaps and interpretation boundaries

• While CtBP1 is enzyme-homologous and ligandable, the present evidence set supports a well-established binding pocket and dehydrogenase-like fold and substrate/inhibitor binding (e.g., MTOB), but does not fully establish a single dominant physiological catalytic reaction as the primary biological role; instead, the strongest experimental narrative centers on transcriptional corepressor scaffolding regulated by NADH and oligomeric state. (chen2021thetransrepressionand pages 1-2, chen2021thetransrepressionand pages 5-7)
• Many pathway-level claims about broad disease roles exist in the literature; this report prioritizes mechanistic and experimentally anchored functions supported by the retrieved primary studies and reviews.

Key 2024 sources (URLs and publication dates)

• Filograna et al. May 2024, Journal of Experimental & Clinical Cancer Research: “Identification and characterization of a new potent inhibitor targeting CtBP1/BARS in melanoma cells.” https://doi.org/10.1186/s13046-024-03044-5 (filograna2024identificationandcharacterization pages 1-2)
• Goradia et al. May 2024, Nature Communications: “Master corepressor inactivation through multivalent SLiM-induced polymerization mediated by the oncogene suppressor RAI2.” https://doi.org/10.1101/2023.06.16.545227 (goradia2024mastercorepressorinactivation pages 1-4)
• Lim et al. Feb 2024, Animal Cells and Systems: “Transcriptional corepressor activity of CtBP1 is regulated by ISG15 modification.” https://doi.org/10.1080/19768354.2024.2321354 (lim2024transcriptionalcorepressoractivity pages 1-2)
• Huang et al. Jun 2024, Viruses: “C-Terminal Binding Protein: Regulator between Viral Infection and Tumorigenesis.” https://doi.org/10.3390/v16060988 (huang2024cterminalbindingprotein pages 2-4)

References

1. (huang2024cterminalbindingprotein pages 2-4): Meihui Huang, Yucong Li, Yuxiao Li, and Shuiping Liu. C-terminal binding protein: regulator between viral infection and tumorigenesis. Viruses, 16:988, Jun 2024. URL: https://doi.org/10.3390/v16060988, doi:10.3390/v16060988. This article has 3 citations.

2. (chen2021thetransrepressionand pages 1-2): Zhi Chen. The transrepression and transactivation roles of ctbps in the pathogenesis of different diseases. Journal of Molecular Medicine, 99:1335-1347, Jul 2021. URL: https://doi.org/10.1007/s00109-021-02107-w, doi:10.1007/s00109-021-02107-w. This article has 30 citations.

3. (chen2021thetransrepressionand pages 5-7): Zhi Chen. The transrepression and transactivation roles of ctbps in the pathogenesis of different diseases. Journal of Molecular Medicine, 99:1335-1347, Jul 2021. URL: https://doi.org/10.1007/s00109-021-02107-w, doi:10.1007/s00109-021-02107-w. This article has 30 citations.

4. (lee2025usingtheallen pages 6-8): Suhjin Lee and Uthayashanker R. Ezekiel. Using the allen brain cell atlas of the human brain to gain insights into c-terminal-binding protein 1 (ctbp1)’s potential function. Biologics, 5:14, May 2025. URL: https://doi.org/10.3390/biologics5020014, doi:10.3390/biologics5020014. This article has 1 citations and is from a peer-reviewed journal.

5. (lee2025usingtheallen pages 9-11): Suhjin Lee and Uthayashanker R. Ezekiel. Using the allen brain cell atlas of the human brain to gain insights into c-terminal-binding protein 1 (ctbp1)’s potential function. Biologics, 5:14, May 2025. URL: https://doi.org/10.3390/biologics5020014, doi:10.3390/biologics5020014. This article has 1 citations and is from a peer-reviewed journal.

6. (goradia2024mastercorepressorinactivation pages 4-8): Nishit Goradia, Stefan Werner, Edukondalu Mullapudi, Sarah Greimeier, Lina Merkens, Andras Lang, Haydyn Mertens, Aleksandra Węglarz, Simon Sander, Grzegorz Chojnowski, Harriet Wikman, Oliver Ohlenschläger, Gunhild von Amsberg, Klaus Pantel, and Matthias Wilmanns. Master corepressor inactivation through multivalent slim-induced polymerization mediated by the oncogene suppressor rai2. Nature Communications, May 2024. URL: https://doi.org/10.1101/2023.06.16.545227, doi:10.1101/2023.06.16.545227. This article has 1 citations and is from a highest quality peer-reviewed journal.

7. (goradia2024mastercorepressorinactivation pages 1-4): Nishit Goradia, Stefan Werner, Edukondalu Mullapudi, Sarah Greimeier, Lina Merkens, Andras Lang, Haydyn Mertens, Aleksandra Węglarz, Simon Sander, Grzegorz Chojnowski, Harriet Wikman, Oliver Ohlenschläger, Gunhild von Amsberg, Klaus Pantel, and Matthias Wilmanns. Master corepressor inactivation through multivalent slim-induced polymerization mediated by the oncogene suppressor rai2. Nature Communications, May 2024. URL: https://doi.org/10.1101/2023.06.16.545227, doi:10.1101/2023.06.16.545227. This article has 1 citations and is from a highest quality peer-reviewed journal.

8. (goradia2024mastercorepressorinactivation pages 8-11): Nishit Goradia, Stefan Werner, Edukondalu Mullapudi, Sarah Greimeier, Lina Merkens, Andras Lang, Haydyn Mertens, Aleksandra Węglarz, Simon Sander, Grzegorz Chojnowski, Harriet Wikman, Oliver Ohlenschläger, Gunhild von Amsberg, Klaus Pantel, and Matthias Wilmanns. Master corepressor inactivation through multivalent slim-induced polymerization mediated by the oncogene suppressor rai2. Nature Communications, May 2024. URL: https://doi.org/10.1101/2023.06.16.545227, doi:10.1101/2023.06.16.545227. This article has 1 citations and is from a highest quality peer-reviewed journal.

9. (lim2024transcriptionalcorepressoractivity pages 3-7): Yun Hwan Lim, Yoon Jin Park, Jieun Lee, and Jung Hwa Kim. Transcriptional corepressor activity of ctbp1 is regulated by isg15 modification. Animal Cells and Systems, 28:66-74, Feb 2024. URL: https://doi.org/10.1080/19768354.2024.2321354, doi:10.1080/19768354.2024.2321354. This article has 5 citations and is from a peer-reviewed journal.

10. (lee2025usingtheallen pages 1-2): Suhjin Lee and Uthayashanker R. Ezekiel. Using the allen brain cell atlas of the human brain to gain insights into c-terminal-binding protein 1 (ctbp1)’s potential function. Biologics, 5:14, May 2025. URL: https://doi.org/10.3390/biologics5020014, doi:10.3390/biologics5020014. This article has 1 citations and is from a peer-reviewed journal.

11. (filograna2024identificationandcharacterization pages 22-25): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

12. (filograna2024identificationandcharacterization pages 9-11): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

13. (filograna2024identificationandcharacterization pages 25-27): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

14. (filograna2024identificationandcharacterization pages 27-28): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

15. (filograna2024identificationandcharacterization pages 2-4): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

16. (filograna2024identificationandcharacterization pages 11-14): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

17. (filograna2024identificationandcharacterization pages 8-9): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

18. (filograna2024identificationandcharacterization media a3db0a0a): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

19. (filograna2024identificationandcharacterization media 4353de2d): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

20. (filograna2024identificationandcharacterization media 440b0878): Angela Filograna, Stefano De Tito, Matteo Lo Monte, Rosario Oliva, Francesca Bruzzese, Maria Serena Roca, Antonella Zannetti, Adelaide Greco, Daniela Spano, Inmaculada Ayala, Assunta Liberti, Luigi Petraccone, Nina Dathan, Giuliana Catara, Laura Schembri, Antonino Colanzi, Alfredo Budillon, Andrea Rosario Beccari, Pompea Del Vecchio, Alberto Luini, Daniela Corda, and Carmen Valente. Identification and characterization of a new potent inhibitor targeting ctbp1/bars in melanoma cells. Journal of Experimental & Clinical Cancer Research, May 2024. URL: https://doi.org/10.1186/s13046-024-03044-5, doi:10.1186/s13046-024-03044-5. This article has 6 citations and is from a domain leading peer-reviewed journal.

21. (goradia2024mastercorepressorinactivation pages 11-14): Nishit Goradia, Stefan Werner, Edukondalu Mullapudi, Sarah Greimeier, Lina Merkens, Andras Lang, Haydyn Mertens, Aleksandra Węglarz, Simon Sander, Grzegorz Chojnowski, Harriet Wikman, Oliver Ohlenschläger, Gunhild von Amsberg, Klaus Pantel, and Matthias Wilmanns. Master corepressor inactivation through multivalent slim-induced polymerization mediated by the oncogene suppressor rai2. Nature Communications, May 2024. URL: https://doi.org/10.1101/2023.06.16.545227, doi:10.1101/2023.06.16.545227. This article has 1 citations and is from a highest quality peer-reviewed journal.

22. (lim2024transcriptionalcorepressoractivity pages 7-8): Yun Hwan Lim, Yoon Jin Park, Jieun Lee, and Jung Hwa Kim. Transcriptional corepressor activity of ctbp1 is regulated by isg15 modification. Animal Cells and Systems, 28:66-74, Feb 2024. URL: https://doi.org/10.1080/19768354.2024.2321354, doi:10.1080/19768354.2024.2321354. This article has 5 citations and is from a peer-reviewed journal.

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24. (lim2024transcriptionalcorepressoractivity pages 1-2): Yun Hwan Lim, Yoon Jin Park, Jieun Lee, and Jung Hwa Kim. Transcriptional corepressor activity of ctbp1 is regulated by isg15 modification. Animal Cells and Systems, 28:66-74, Feb 2024. URL: https://doi.org/10.1080/19768354.2024.2321354, doi:10.1080/19768354.2024.2321354. This article has 5 citations and is from a peer-reviewed journal.

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22. (4-nitrophenyl)carbamoyl
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