Abstract Introduction: Dysregulated apoptotic machinery and signaling contribute to acquire resistance to regimens containing venetoclax (VEN), a BCL2 (B-cell lymphoma-2) inhibitor, in acute myeloid leukemia (AML) and pose a clinical challenge. Casein kinase 2 (CK2) is a serine/threonine kinase with 300+ substrates and regulate cell cycle, survival, differentiation, and apoptosis. Its aberrant activity promotes disease progression, poor prognosis, and drug resistance. CX-4945 (CX), a selective CK2 inhibitor, shows potent anticancer activity in leukemia and other solid tumors. Here, we tested combined CK2 and BCL2 targeting with CX and VEN in pre-clinical AML models. Methods: Cytotoxic and pro-apoptotic effects of the CX+VEN combo were tested in AML cell lines and primary samples by WST and annexin V assays. The ZIP synergy score was determined by SynergyFinder tool. Flow cytometry and immunoblotting assessed cell surface markers, various apoptosis regulators along with CK2 target levels after drug treatment. Dynamic BH3 profiling assessed priming of VEN-resistant (VR) cells to apoptosis after CX treatment. Transcriptome of VR-AML cells with and without drug treatment was analyzed by RNA sequencing. In vivo efficacy of CX+VEN combo was tested in cell line and patient-derived xenograft (PDX) mouse models. Results: CK2α (CSNK2A1) expression exhibited negative correlation similar to that of BCL2 levels with VEN activity in BeatAML cohort and VR-AML cells showed higher CK2 activity. CX+VEN combo showed synergistic cytotoxicity and augmented apoptosis in VEN-sensitive (MOLM13, HL60, THP1), VR-AML (U937, MOLM13/VR, HL60/VR) cell lines, and PDX cells in vitro. CX treatment enhanced VR-AML cells priming to BH3 peptides and increased cytochrome c release. Also, CX+VEN combo effectively induced apoptosis and decreased leukemia stem cells (CD34+CD38-) and chemo-resistant (CD47+CD123+) subpopulations in VR-AML cells. AML cells showed downregulation of CK2 activity and other pro-survival BCL2 member family proteins with increased PARP activity after CX+VEN combo treatment. Functional enrichment analysis of transcriptome after CX+VEN combo treatment showed upregulation of cell cycle arrest, TP53 and apoptotic signature genes that were repressed in VR-AML cells. Lastly, CX+VEN combo effectively decreased leukemia burden and prolonged overall median survival of xenograft (CDX/PDX) mice in vivo. Conclusions: CX+VEN combo showed a superior antileukemic activity in different pre-clinical AML models and CK2 inhibition overcome VEN resistance. CX-4945 (Silmitasertib) has favorable pharmacokinetics with good tolerability in human studies and is being evaluated in early phases of clinical trial. Our findings provide a rationale for CK2 and BCL2 co-targeting as an effective approach for AML treatment and to overcome VEN resistance. Citation Format: Upendarrao Golla, Muhammad Danial, Rajesh Rajaiah, Marudhu Pandiyan Shanmugam, Koby Duke, Katherine Mercer, Yi Qiu, Sinisa Dovat, Yasin Uzun, Hong Zheng, Suming Huang, Chandrika G. Behura. Clinical-grade CK2 inhibitor CX-4945 synergistically enhances venetoclax-mediated antileukemic activity in preclinical acute myeloid leukemia models [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2026; Part 1 (Regular Abstracts); 2026 Apr 17-22; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2026;86(7 Suppl):Abstract nr 4466.

Acute myeloid leukemia (AML), the most common hematologic malignancy, generally has a poor prognosis. Despite initial favorable responses to the BCL2 inhibitor venetoclax (VEN), remission is transient, and AML is eventually fatal. Resistance to VEN is primarily due to the overexpression of anti-apoptotic proteins, including MCL-1, BCL2L1 (BCL-XL), and BCL2A1. Casein kinase II (CK2) is a serine-threonine kinase and a known suppressor of apoptosis. We and others have reported that protein kinase CK2 activity is high in leukemic stem cells (LSCs) and associated with resistance to chemotherapy. We have shown that the selective CK2 inhibitor, CX-4945, suppresses BCL-XL and has a significant anti-tumor effect in AML preclinical models. CK2 expression and activity are high in venetoclax-resistant AML (VR-AML) cell lines. Genetic and pharmacological inhibition of CK2 significantly altered VR-AML gene signature, decreased MCL-1 protein level, increased BH3 priming and sensitized VR-AML cells to apoptosis. More importantly, CX-4945 selectively targeted LSCs (CD34+CD38-) and chemoresistant (CD123+CD47+) subpopulation in VR-AML. CX-4945 combined with VEN decreased leukemia burden and prolonged the survival of VR-AML cell line-derived and patient-derived xenografts compared to either drug alone. The combinatorial treatment was well tolerated in mice without additional myelosuppression or organ toxicity. CX-4945 (silmitasertib) is being tested in several early-phase clinical trials against adult and pediatric cancers. These preclinical results support the use of CX-4945 in combination with VEN to overcome resistance to apoptosis and re-sensitize VR-AML to chemotherapy.

Hematopoietic transcription is a combinatorial control of transcription factors, chromatin modifiers, and non-coding RNAs. TAL1 is a critical regulator of normal and malignant hematopoiesis. However, mechanism underlying regulation of TAL1 activity during erythropoiesis versus leukemogenesis remains elusive. Here, we showed that an enhancer RNA, ncRNA-a3 transcribed from TAL1 + 51Kb-enhancer, is positively correlated with TAL1 locus chromatin accessibility and transcription, and required for TAL1 activation during EPO-induced erythropoiesis. Loss of ncRNA-a3 in CD34+ hematopoietic stem and progenitor cells leads to reduction of TAL1 transcription, followed by impaired terminal erythroid differentiation. The effect of ncRNA-a3 loss on erythroid differentiation is partially rescued by overexpression of Tal1 cDNA, suggesting an important role of ncRNA-a3/TAL1 regulatory axis in erythropoiesis. Mechanistically, ncRNA-a3 regulates long-range chromatin interactions between +51Kb erythroid-specific enhancer, promoter and other regulatory elements in the TAL1 locus to maintain the erythroid interaction hub. By facilitating the binding and recruitment of p300/BRG1 to the TAL1 locus, ncRNA-a3 promotes chromatin accessibility in the TAL1 locus and activates TAL1 transcription program, including subsequent epigenetic and transcriptional activation of erythroid-specific TAL1 target genes. Our study reveals a novel role for ncRNA-a3 in TAL1 dependent erythropoiesis and establishes a new mode of ncRNA-a3 action in TAL1 transcriptional activation.

Although nucleoporin 98 (NUP98) fusion oncogenes often drive aggressive pediatric leukemia by altering chromatin structure and expression of homeobox (HOX) genes, underlying mechanisms remain elusive. Here, we report that the Hoxb-associated lncRNA HoxBlinc was aberrantly activated in NUP98-PHF23 fusion-driven leukemias. HoxBlinc chromatin occupancies led to elevated mixed-lineage leukemia 1 (MLL1) recruitment and aberrant homeotic topologically associated domains (TADs) that enhanced chromatin accessibilities and activated homeotic/hematopoietic oncogenes. HoxBlinc depletion in NUP98 fusion- driven leukemia impaired HoxBlinc binding, TAD integrity, MLL1 recruitment, and the MLL1-driven chromatin signature within HoxBlinc-defined TADs in a CCCTC-binding factor-independent (CTCF-independent) manner, leading to inhibited homeotic/ leukemic oncogenes that mitigated NUP98 fusion-driven leukemogenesis in xenografted mouse models. Mechanistically, HoxBlinc overexpression in the mouse hematopoietic compartment induced leukemias resembling those in NUP98-PHF23- knockin (KI) mice via enhancement of HoxBlinc chromatin binding, TAD formation, and Hox gene aberration, leading to expansion of hematopoietic stem and progenitor cell and myeloid/lymphoid cell subpopulations. Thus, our studies reveal a CTCF-independent role of HoxBlinc in leukemic TAD organization and oncogene-regulatory networks.

Early activation and phenotypic transformation of monocytes and macrophages are essential for inflammatory activities and tissue repair following myocardial infarction (MI). However, the involvement of histone succinylation in monocyte phenotypic regulation during MI remains poorly understood. Here we show that succinylation, particularly histone H3K23succ, is significantly upregulated in monocytes from both MI patients and male mouse models, correlating with enhanced inflammatory responses. We further reveal that histone acetyltransferase 1 (Hat1) acts as a succinyltransferase essential for catalytic activity, and is upregulated together with histone succinylation in proinflammatory monocytes. Deficiency in Hat1 expression improves cardiac function, reduces infarct size, and suppresses inflammatory responses in infarcted hearts after MI. Mechanistically, Hat1 modulates chromatin accessibility and recruits H3K23 succinylation to regulate proinflammatory gene expression in monocytes and macrophages post-MI. Our study reveals a critical role for histone succinylation in early MI progression and establishes that Hat1 acts as an epigenetic regulator promoting proinflammatory monocyte transformation, highlighting its therapeutic potential for MI treatment.

Supplementary Figure S10. A proposed mechanism for the CS055/chiglitazar-induced ferroptosis-like cell death in LSC-like cells by blocking the HDAC3-SLC7A11-GSH-GPX4 pathway.

Supplementary Figure S5. The chiglitazar activates PPARα and transcriptionally represses HDAC3 expression. (A-B) Western blotting analysis of PPARα, HDAC1,2,3, and 10 expressions in KG-1α and Kasumi-1 cells treated with CS055 and/or chiglitazar for 24 h and removed dead cells by Dead Cell Removal kit. (C-E) Western blotting (C-D) and quantitative real-time PCR (E) analysis of PPARα and/or HDAC3 expressions in KG-1α and Kasumi-1 cells treated with chiglitazar (4 μM, 8 μM, 16 μM) for 24 h. (F) The chiglitazar significantly inhibit the transcriptional activity of the HDAC3 gene promoter in KG-1α and Kasumi-1 cells treated with chiglitazar (4 μM, 8 μM, 16 μM) for 24 h. (G) ChIP assay analyzed the recruitment of PPARα on the HADC3 gene promoter in KG-1α and Kasumi-1 cells treated with chiglitazar (16 μM) for 24 h. Western blotting data was quantified and analyzed by Image J Soft. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.

Supplementary Figure S9. (A-B) Representative data for flow cytometric analysis of mCD45/hCD34 staining in the spleen (A) and bone marrow (B). (C) Flow cytometry analysis of human CD34+ AML cells sorted from bone marrow of PDX#1 and PDX#2 mice by human CD34 Nanobeads.

Supplementary Figure S7. (A) Knockdown of HDAC3 enhanced the endogenous lipid peroxidation levels in KG-1α and Kasumi-1cells, and the lipid peroxidation was detected by flow cytometry using C11-BODIPY staining. (B-C) The glutamate release (B) and intracellular GSH (C) were detected in HDAC3 knockdown KG-1α and Kasumi-1 cells. (D) Cell viability was counted in HDAC3 knockdown KG-1α and Kasumi-1 cells after treatments Ferr-1 (2 μM) for 72 h. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.

Supplementary Figure S1. (A-B) The CD34+CD38−cell population was sorted from LSC-like cell lines KG-1α (A) and Kasumi-1 (B) and was further identified by flow cytometry using CD123, CD96, CD47, CD44, CD32, and CD25 antibodies. (C) Flow cytometric plots show the gating strategy to determine the percentages of cell death.

Supplementary Table S1. Clinical characteristics of AML patients

Supplementary Figure S2. The combination of CS055 and chiglitazar synergistic inhibited AML progression in vivo. (A) Schematic outline of the CDX models. (B) CS055 and Chiglitazar were synergistic inhibited the AML progression in CDX mice models (n = 5/group). The AML progression was measured by the living imaging system. (C) Image and weight of representative spleens from CDX mice models (n = 3/group). (D-E) The human CD45 positive cell insulation rate was measured by flow cytometry in bone marrow (D) and spleen (E) (n = 3/group). (F) The combination of CS055 and chiglitazar improved the survival of CDX mice models (n = 5/group), and animal survival was analyzed using the Kaplan-Meier survival curve. (G) Statistical results of body weight from CDX mice models (n = 5/group). *P < 0.05, **P < 0.01.

Supplementary Figure S3. (A) The statistical results of fluorescence intensity in CDX mice models (n = 5/group). (B-C) Flow cytometry analysis of the percentage of hCD45+ cells in bone marrow (B) and spleen (C) (n=3/group). *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001.

AbstractPurpose: Leukemic stem cells (LSC) are responsible for leukemia initiation, relapse, and therapeutic resistance. Therefore, the development of novel therapeutic approaches targeting LSCs is urgently needed for patients with acute myeloid leukemia (AML). Experimental Design: The LSC-like cell lines (KG-1α and Kasumi-1) and CD34+ primary AML cells purified from patients with AML (n = 23) treated with CS055 and/or chiglitazar and were analyzed for viability, death, and colony formation assay. We performed RNA sequencing, glutamate release, intracellular glutathione, lipid reactive oxygen species, transmission electron microscopy, and Western blotting assay and confirmed ferroptosis in LSC-like cells. The luciferase reporter, co-immunoprecipitation, histone deacetylase 3 (HDAC3)-shRNA/HDAC3/deacetylase-deficient LSC-like cell lines, histidine pull-down, and chromatin immunoprecipitation assays performed to clarify the molecular mechanism of CS055/chiglitazar in LSC-like cells. We also established cell-derived xenograft and patient-derived xenograft mouse models to evaluate the therapeutic efficacy of CS055/chiglitazar against AML in vivo. Results: We report that the HDAC inhibitor CS055, in combination with peroxisome proliferator–activated receptor pan-agonist (chiglitazar), synergistically targets leukemic stem-like cells from leukemia cell lines and patient samples while sparing normal hematopoietic progenitor cells. Mechanistically, chiglitazar enhances the inhibitory effect of CS055 on HDAC3 and induces ferroptosis in LSC-like cells by downregulating the expression of ferroptosis suppressor SLC7A11. In fact, the inhibition of HDAC3 increases H3K27AC levels in the promoter region of activating transcription factor 3 (ATF3), a transcriptional repressor of the SLC7A11 gene, and upregulates the expression of ATF3. In contrast, ATF4, a SLC7A11 activator, is suppressed by HDAC3 inhibition. Conclusions: Our findings suggest that treatment with CS055 combined with chiglitazar will target LSCs by inducing ferroptosis and may confer an effective approach for the treatment of AML.

Supplementary Figure S8. (A) The CD34+ and CD34- primary AML cells identified by flow cytometry using CD34, CD38, CD123, CD96, CD47, CD44, CD32, and CD25 antibodies. (B) The quantitative analysis for Western blotting analysis of HDAC3, SLC7A11, and GPX4 expression in primary CD34+ AML cells (n = 20) and CD34+ hematopoietic blood stem cells (HBSCs; n = 15). (C-D) HDAC3 protein levels were positively correlated with SLC7A11 protein levels (C) in primary CD34+ AML cells (n = 20), but not for GPX4 protein levels (D). The quantitative analysis of western blotting data was measured by image J software and the GAPDH serves as a loading control. (E) Representative image of colony formation in CD34+ HBSCs treated with CS055 and/or chiglitazar, with 3000 cells seeded per well. Scale bars, 500 μm. (F-H) Transmission electron microscopy revealed the morphology of primary CD34+ AML #1. Scale bars, 2 μm. The primary CD34+ AML cells treated with CS055 and/or chiglitazar for 24 h. The mitochondrial area was measured by the Image J Soft. (I) Cell viability was counted in primary CD34+ AML #1 cells after treatments with erastin (1.875 μM, 3.75 μM, 7.5 μM, 15 μM, 30 μM) for 24h. (J) primary CD34+ AML #1 cells treated with erastin (7.5 μM, 15 μM, 30 μM) for 24h and stained with C11-BODIPY and endogenous lipid peroxidation analysis by flow cytometry. (K-L) The glutamate release (K) and intracellular GSH (L) were detected in primary CD34+ AML #1 cells treated with erastin (15 μM, 30 μM) for 24h. (M) Cell viability was counted in primary CD34+ AML #1 cells after treatments with erastin (30 μM), Ferr-1 (2 μM), DFO (10 μM), Z-VAD (10 μM) and Nec-1 (10 μM) for 24 h. Clinical information of patients with AML is summarized in Supplementary Table S1. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.

Supplementary Figure S6. (A-D) Histone deacetylase activity analysis of HDAC1 (A), HDAC2 (B), HDAC3 (C), and HDAC10 (D) in KG-1α and Kasumi-1 cells after treatments with CS055 (4 μM) and chiglitazar (16 μM) by HDAC Activity Assay kit. (E) Quantitative real-time PCR analysis of SLC7A11 mRNA levels in KG-1α and Kasumi-1 cells treated with CS055 and/or chiglitazar for 24 h. (F) Western blotting analysis of HDAC3 expression in KG-1α and Kasumi-1 cells treated with CS055 and/or chiglitazar for 24 h. (G) Western blotting analysis of HDAC3 expression in HDAC3 knockdown KG-1α and Kasumi-1 cells. (H) Western blotting analysis of HDAC3 expression in HDAC3, and HDAC3 mutant (H134A and H135A) overexpressed KG-1α and Kasumi-1 cells. Western blotting data was quantified and analyzed by Image J Soft. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.

Supplementary Figure S4. (A) Heatmap of differentially expressed genes involved in ferroptosis in KG-1α cells after treatments with CS055 (4 μM) and chiglitazar (16 μM). (B) GSEA analysis for lipid metabolism pathway in KG-1α cells after treatments with CS055 (4 μM) and chiglitazar (16 μM). (C) Cell viability was counted in KG-1α and Kasumi-1 cells after treatments with erastin (1.875 μM, 3.75 μM, 7.5 μM, 15 μM, 30 μM) for 24h. (D) Erastin induced the death level of KG-1α and Kasumi-1 cells, and cell death was measured by PI staining and analyzed by flow cytometry. (E) KG-1α and Kasumi-1 cells treated with erastin (3.75 μM, 7.5 μM, 15 μM, 30 μM) for 24h and stained with C11-BODIPY and endogenous lipid peroxidation analysis by flow cytometry. (F-G) The glutamate release (F) and intracellular GSH (G) were detected in KG-1α and Kasumi-1 cells treated with erastin (3.75 μM, 7.5 μM, 15 μM, 30 μM) for 24h. (H) Cell viability was counted in KG-1α and Kasumi-1 cells after treatments with erastin (15 μM), Ferr-1 (2 μM), DFO (10 μM), Z-VAD (10 μM) and Nec-1 (10 μM) for 24 h. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.

Nucleophosmin1 mutation (NPM1c) is the most common mutation in adult acute myeloid leukemia (AML) and known as a driver mutation causing leukemogenesis through upregulating homeotic gene transcription. Mutated NPM1 is reported to mis-localize in the cytoplasm. However, how cytoplasmic NPM1c regulates leukemic transcription remains poorly understood. We previously reported that NPM1c reprograms homeotic and leukemogenic transcription through reshaping CTCF-defined three-dimensional topology associated domain (TAD). Also, re-localization of cytoplasmic NPM1c to the nucleus switches MIZ1/MYC repressive transcription regulatory axis to MIZ1/NPM1 active transcription regulatory axis at CDKN locus and CEBPA locus leading to cell cycle arrest and myeloid differentiation in NPM1 mutated AML. In this study, we are focused on regulation of myeloid differentiation and hypothesized upregulation of myeloid master regulators, PU.1 and CEBPA may suppress the leukemogenic transcription and induce myeloid differentiation in NPM1 mutated AML cells. To confirm NPM1c regulates TAD formation at CEBPA locus, we performed HiC-seq in OCI-AML3 with nuclear re-localized NPM1c using XPO1 inhibitor treatment and NPM1-wildtype overexpression. Nuclear re-localized NPM1 upregulates CTCF-defined TAD interaction at CEBPA locus and upregulates CEBPA and CEBPD transcription which indicates NPM1c regulates CEBPA transcription via altering CEBPA TAD formation. We then test whether activation of CEBPA or SPI1 in NPM1 C+ AML cells induced myeloid differentiation and blocked NPM1 C+ driven leukemogenesis. We transcriptionally activated SPI1 or CEBPA gene in OCI-AML3 using CRISPR-dCas9-VP160 system to determine how these myeloid regulators changed the leukemic transcription and leukemic cell phenotype. PU.1- or CEBPA- activated OCI-AML3 reduces cell proliferation, especially affecting the G2/M phase in cell cycle. They have monocyte-like nuclei with large cytoplasm and induce myeloid differentiation with upregulating both of CD11b and CD14 myeloid cell surface markers. Moreover, compared to parental OCI-AML3 cells, Pu.1- or CEBPA-activated cells showed lower colony formation ability and in xenograft mouse models produced diminished leukemic symptoms and prolonged survival. We further conducted RNA-seq to explore how PU.1 or CEBPA changed the gene transcription leading to the blockage of leukemogenesis. Between PU.1- and CEBPA-activated cells, 58% of differentially expressed genes overlap and GO or GSEA analysis revealed that both of them downregulates G2M checkpoint/mitotic-spindle cell cycle related gene sets, indicating that PU.1 or CEBPA activation controls cell cycle control rather than myeloid cell differentiation in NPM1 C+ AML. In summary, our data revealed that re-localization of NPM1 C+ into nucleus activates master myeloid transcription factors, PU.1 and CEBPA, which, in turn, suppress leukemogenesis via inducing cell cycle arrest and myeloid cell differentiation in NPM1 C+ AML.

Introduction: Resistance to frontline cytotoxic therapy is rampant in AML. Molecular mechanisms promoting drug resistance are being identified to develop an effective strategy to overcome resistance. Protein kinase CK2 (casein kinase II) is a constitutively active, serine-threonine kinase that promotes cell survival and resistance to apoptosis in AML. A selective inhibitor of CK2, CX-4945 shows in vivo therapeutic efficacy in AML patient-derived xenografts. Here we report that CK2 kinase activity is high in AML cells resistant to cytarabine. Cytarabine-resistant cells are enriched for leukemia stem cells (CD34+/38-) and expansion of TP53 mutant clones. Specific inhibitors of CK2, CX4945 show selective cytotoxicity against the cytarabine-resistant cells. Methods: We developed cytarabine-resistant AML cell lines (MOLM-13, MV4-11, U937, Kasumi-1). We used TP53 mutant clone isolated and expanded from cytarabine resistant MV4-11 cell line. Gene expression of cytarabine-resistant AML cells and that of cell lines with and without CX-4945 treatment was analyzed using RNA sequencing. mRNA expression of genes was measured using qPCR and protein level was measured using western blot. Drug response and drug synergy were assessed using MTT assay. AML patient-derived xenograft was used to evaluate in vivo therapeutic efficacy of the combination of cytarabine and CX-4945. Results: Cytarabine-resistant cells have high expression of CK2. Gene expression analysis shows that the cytarabine metabolism gene is significantly altered in cytarabine-resistant cells and CX4945-treated AML cells. NT5C2 is a cytosolic nucleotidase that dephosphorylates monophosphates, preventing cytarabine from being phosphorylated to active form. hENT1 is a nucleoside transporter that brings cytarabine into the cells for metabolism. In cytarabine resistant cells, NT5C2 has been found to be high while hENT1 is low, preventing ideal cytarabine metabolism. CX4945 treatment decreased the expression of NT5C2 and increases expression of hENT1. Cytarabine sensitivity is restored following genetic inhibition (shRNA) or treatment with a CK2 inhibitor. AML xenograft mice treated with a combination of CX-4945 and cytarabine have decreased leukemia burden and prolonged survival compared to either drug alone. Conclusion: These results suggest that: 1) Overactive CK2 promotes AML drug resistance in leukemia stem cells; 2) CK2 inhibitor CX-4945 selectively targets cytarabine-resistant cells; 3) The potential role of CK2 in leukemia stem cell survival and drug resistance in vivo needs further evaluation. Citation Format: Katherine Mercer, Koby Duke, Rajesh Rajaiah, Muhammad Daniyal, Yi Qiu, Sinisa Dovat, Yasin Uzun, Lijun Zhang, Suming Huang, Morgann Klink, Chandrika Gowda. Targeting drug-resistant acute myeloid leukemia (AML) clone using casein kinase II inhibitor [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2023; Part 1 (Regular and Invited Abstracts); 2023 Apr 14-19; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2023;83(7_Suppl):Abstract nr 392.