Ask about this productRelated genes to: ELK3 antibody
- Gene:
- ELK3 NIH gene
- Name:
- ETS transcription factor ELK3
- Previous symbol:
- -
- Synonyms:
- ERP, NET, SAP2
- Chromosome:
- 12q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-12-23
- Date modifiied:
- 2019-01-21
Related products to: ELK3 antibody
Related articles to: ELK3 antibody
- Left-sided colorectal cancer (LCRC) and right-sided colorectal cancer (RCRC) show marked differences in prognosis and therapeutic response, yet the underlying molecular mechanisms remain poorly understood. We hypothesize that these clinical differences reflect distinct cell-type-specific transcriptional programs and microenvironmental interactions that can be resolved at single-cell resolution. To test this hypothesis, this study analyzed single-cell transcriptomic data from 16 colorectal cancer (CRC) patients (8 LCRC and 8 RCRC), revealing molecular differences between LCRC and RCRC in tumor cells, T cells, B cells, myeloid cells, fibroblasts, and endothelial cells, and constructing a differential atlas of LCRC versus RCRC. Significant molecular and cellular differences were observed between LCRC and RCRC. was markedly upregulated in RCRC tumor cells and associated with poorer patient survival, potentially regulated by transcription factors , , and . RCRC showed an increased proportion of the CD8-EFFECTOR 3 subpopulation, which co-expresses effector and exhaustion markers, suggesting favorable immunotherapy response. In contrast, the CD4-heat shock proteins (CD4-HSP) subpopulation was almost exclusively present in LCRC, suggesting a potential correlation with a weaker response to immune checkpoint inhibitors. Additionally, ligand-receptor interactions were significantly enhanced in RCRC, potentially contributing to worse prognosis by inhibiting APP protein cleavage and promoting its accumulation. Validation was performed using an independent single-cell transcriptomic dataset, bulk RNA-seq data from TCGA CRC samples, and qPCR on locally collected CRC tissue specimens. In addition, a spatial transcriptomic dataset of CRC and immunohistochemistry data from the Human Protein Atlas (HPA) database were also used to validate part of the findings. This study provides a comprehensive single-cell transcriptomic atlas highlighting the molecular and cellular disparities between LCRC and RCRC, offering novel insights into tumor biology and informing the development of personalized therapeutic strategies. - Source: PubMed
Publication date: 2026/03/17
Zhao ChengzhiZhou WeiyeZeng GuangjianHuang YeenShi ChuanMa HaibeiLi YangLv JiachunLiang XiaohuaFang Shenying - Fat mass and obesity-associated protein (FTO) is a Fe(II)/2-oxoglutarate-dependent RNA demethylase that removes the N6-methyladenosine (m6A) mark and rewires post-transcriptional gene control. In leukemia, FTO is often overexpressed and promotes leukemogenesis by increasing the stability and translation of mRNAs that govern differentiation, metabolism, and survival. In acute myeloid leukemia (AML), FTO-dependent m6A erasure is associated with impaired differentiation (e.g., ASB2/RARA), reinforcement of MYC/CEBPA programs, and glycolytic and stress-adaptation pathways that support therapy resistance and relapse. In acute lymphoblastic leukemia (ALL), FTO contributes to disease maintenance through metabolic rewiring (e.g., ELK3-driven glycolysis), repression of tumor-suppressive transcripts (e.g., IRF8), and stabilization of ribosome-biogenesis mRNAs that sustain proliferative fitness, with additional influence from microenvironmental cues such as exosome-mediated transfer. Preclinical studies show that genetic depletion, small-molecule inhibition, or targeted degradation of FTO increases m6A on key targets, suppresses leukemic growth, and can sensitize cells to standard therapies, supporting FTO as a druggable epitranscriptomic vulnerability. This review summarizes FTO structure and function, highlights subtype-specific mechanisms in AML and ALL, and discusses emerging therapeutic strategies and translational challenges. - Source: PubMed
Publication date: 2026/02/04
Zhang YinliQian Shenxian - Femoroacetabular impingement (FAI) and synovitis have been recognized as essential factors for developing osteoarthritis (OA) in the hip joints. However, little is known about altered synovial cellular compositions, their associated transcriptomic profiles, and cell-cell interactions in FAI and hip OA. - Source: PubMed
Publication date: 2026/01/12
Kulzhanova GulzadaKlee AlexisBotros MinaHansen Victoria LReuter JohnTashbib Eliya TazreenaFadial EloiseRicciardi Benjamin FGiordano BrianWu Chia-Lung - Noncoding single-nucleotide variants (SNVs) that alter transcription factor (TF) binding can affect gene expression and contribute to disease. Sequence-based methods can excel at predicting TF binding, but rely on training data and can exhibit TF-specific biases. Here, we propose a structure-guided approach for noncoding SNVs, using AlphaFold 3 (AF3) to model TF-DNA complexes and FoldX for downstream physics-based assessment. Benchmarked against single nucleotide polymorphism-systematic evolution of ligands by exponential enrichment (SNP-SELEX) data for six TFs (SPIB, ELK3, ETV4, SF-1, PAX5, and MEIS2), the FoldX-based strategy showed good agreement with experimental allele preferences. Interestingly, differences in AF3's interface-predicted template modelling (ipTM) score aligned even more closely with SNP-SELEX results, generally surpassing energy-based metrics. Application to known disease-associated variants recapitulated most reported effects for TFs including NKX2-5, GATA3, and USF2A-USF1. In these examples, considering both ΔipTM and FoldX energies proved more reliable than either metric alone. While less accurate than state-of-the-art sequence-based methods, this work demonstrates that structural modelling can yield interpretable insights into how noncoding variants influence TF binding. By highlighting both the promise and limitations of AF3 in this context, our study provides a framework for complementary structural evaluation of regulatory variants. - Source: PubMed
Gerasimavicius LukasBiddie Simon CMarsh Joseph A - To investigate the role and mechanism of SERPINE1 in gefitinib (GEF) resistance in lung cancer and to identify a novel therapeutic target for overcoming chemoresistance. - Source: PubMed
Publication date: 2025/12/11
Zhu XunxiaWei JionglinChen XiaoyuZhang XuelinLi ZhengYang FuzhiJiang ShuaiYang ZhengyaoGe HaiyanShen Xiaoyong