Ask about this productRelated genes to: APEX1 antibody
- Gene:
- APEX1 NIH gene
- Name:
- apurinic/apyrimidinic endodeoxyribonuclease 1
- Previous symbol:
- APEX
- Synonyms:
- APE, REF1, HAP1, APX, APEN, REF-1, APE-1
- Chromosome:
- 14q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-05-22
- Date modifiied:
- 2016-03-08
Related products to: APEX1 antibody
Related articles to: APEX1 antibody
- To investigate the expression pattern, prognostic significance, and underlying molecular mechanisms of mutY homolog () in hepatocellular carcinoma (HCC), and to evaluate its clinical potential as a novel biomarker and therapeutic target. - Source: PubMed
Zhou YanjieZhang HeZhu YalanJiang PengjunFeng TianyuWu ZhenChen Jie - Accurate, real-time, noninvasive longitudinal diagnostic tools are essential for guiding personalized cancer therapy, and urine-based platforms represent a promising noninvasive avenue for continuous therapeutic monitoring. However, conventional approaches relying on passive detection of tumor-derived biomarkers shed into urine are often limited by physiological instability, low abundance, and poor specificity. Herein, we present a dual-enzyme-powered nanosensor for urine-based diagnostics that integrates apurinic/apyrimidinic endonuclease 1 (APE1)-triggered strand cleavage and telomerase (TE)-mediated extension to amplify the signal, enabling visual detection of tumor-associated enzymatic activity via a lateral flow assay (LFA). The nanosensor is constructed by assembling gold nanoclusters (AuNCs) with a synthetic DNA probe (A1T2) and encapsulating the complex with hyaluronic acid (HA). The AuNCs exhibit intrinsic fluorescence and enhanced DNA stability, thereby enabling structural integrity and real-time monitoring. The A1T2 strand is engineered with recognition motifs for APE1 and TE, which mediate sequential DNA cleavage and extension under pathological enzyme overexpression. Upon activation, the nanosensor is enzymatically processed, leaving a AuNC-tagged short single strand that is excreted into urine and detected by a competitive LFA strategy. This enables direct, visual, and instrument-free readout. The synergistic action of APE1 and TE confers a competitive advantage on the DNA substrate, leading to enhanced chromogenic shifts on test strips and improved visual resolution. This strategy translates intracellular enzyme activity into stable urinary signals and demonstrates the potential for low-cost, instrument-free companion diagnostics for personalized cancer treatment. - Source: PubMed
Publication date: 2026/04/13
Wang LuChen RuiyueLiu ZhiyongZhou DongtaoZhang YanyinTeng ChaoHe BangshunYin YiGao YanfengYang JingjingWang MengSong Yujun - Human apurinic/apyrimidinic endonuclease 1/redox effector factor 1 (APE1) is a multifunctional protein central to DNA repair and redox regulation, yet its dynamic post-translational modifications (PTMs) remain poorly understood. Here, we report a biotin-regulated avidin-based nano-catcher (bMIPAPE1) capable of capturing active APE1 in living cells. By leveraging biotin-saturated avidin assembled onto magnetic nanoparticles and surface-imprinted with polydopamine, we engineered highly specific binding cavities for APE1 that enable retention of labile PTMs. This platform revealed 25 previously unreported PTMs across 18 residues of APE1, encompassing acetylation, phosphorylation, ubiquitination, methylation, S-nitrosylation, palmitoylation, and succinylation, and highlighting several PTM hotspots. Representative modifications include phosphorylation at Y264 and Y269, and acetylation at K63, with several PTMs associated with APE1 nuclear export. In addition to high specificity and intracellular compatibility, bMIPAPE1 attenuated both the DNA repair and redox-related functions of APE1. Our findings demonstrate the utility of artificial nanocomposites as tools for live-cell PTM profiling and functional modulation of target proteins, offering a powerful approach to decode protein regulation in living systems and identify potential therapeutic targets in cancer. - Source: PubMed
Zhang RuilanXie HuaisyuanZhu ChenxuSun YingLi KexuanLi HongweiNiu XiaogangJin ChangwenZhao Meiping - - Source: PubMed
Publication date: 2026/04/03
Anisha J PShynu MRadhika GBeena VUma RLijo JAsaf V N MuhasinGleeja V L - G-quadruplexes (G4s) are non-canonical DNA secondary structures enriched at promoters, yet their regulatory role in transcription remains elusive. While G4-ligand-based studies suggest transcriptional repression, their prevalence at oncogene promoters and correlation with high expression suggest a positive regulatory role. Here, we provide direct genetic evidence that promoter G4s function as positive activators of gene expression through a novel mechanism. By selectively mutating endogenous promoter G4 motifs, we demonstrate that G4 loss significantly impairs oncogene expression. Using the endogenous CXCL1 promoter G4 as an example, we revealed that loss of a single promoter G4 motif led to a marked down-regulation of CXCL1 expression as well as inhibition of cellular functions such as cell migration and invasion. Mechanistically, we identified apurinic/apyrimidinic endonuclease (APE1), a multifunctional DNA repair and redox factor, as a G4-binding protein which was recruited to promoters via its unique N-terminus. Subsequently, the redox activity of APE1 enhances transcription factor binding at G4-containing promoters, driving a pro-metastatic gene expression program. Disruption of the G4-APE1 interaction, either genetically or pharmacologically, suppresses gene expression and impairs tumor cell malignant traits. Our findings establish a direct genetic link and mechanistic basis for promoter G4s as crucial drivers of oncogene expression and tumor progression. - Source: PubMed
Chen YinglingMohapatra BhopalPramanik SuraviTarpley MasonKalluchi AchyuthRay SutapaHewitt KyleRowley M JordanBand VimlaBhakat Kishor K