NEDD8 Antibody
- Known as:
- NEDD8 Antibody
- Catalog number:
- 32194
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- NEDD8 Antibody
Related genes to: NEDD8 Antibody
- Gene:
- NEDD8 NIH gene
- Name:
- NEDD8 ubiquitin like modifier
- Previous symbol:
- -
- Synonyms:
- Nedd-8
- Chromosome:
- 14q12
- Locus Type:
- gene with protein product
- Date approved:
- 1994-01-21
- Date modifiied:
- 2019-04-04
Related products to: NEDD8 Antibody
Related articles to: NEDD8 Antibody
- Type I interferon (IFN-I) signaling is crucial for antiviral innate immunity. F-box protein-mediated ubiquitination regulates this pathway. FBXO11 positively regulates IFN-I signaling via TRAF3 K63-linked ubiquitination, but whether other F-box proteins act synergistically during HBV infection remains unknown. This study investigates FBXO32 expression and function in HBV infection, and whether FBXO11 and FBXO32 synergistically activate innate immunity through a NEDD8-dependent mechanism. - Source: PubMed
Publication date: 2026/09/03
Li LiqiangTao ShunZhang YunfeiZeng ZihanLi LiangZhang Jun - Ovarian cancer (OV) is a highly lethal gynecological tumor, often developing platinum chemotherapy resistance and treatment failure. With their diverse and complex structures, natural products offer potential solutions to drug resistance. This study systematically examines chaetocin's effects on cisplatin-resistant OV cells and its underlying molecular mechanisms. We utilized a cell counting Kit-8, transwell assays, flow cytometry, immunohistochemistry, and western blotting to evaluate chaetocin's effects on cisplatin-resistant OV cells. Proteomic analysis and bioinformatics were utilized to identify the molecular targets of chaetocin, which were validated via cell transfection and co-immunoprecipitation. Additionally, a cisplatin-resistant OV xenograft model was developed for in vivo studies. Chaetocin suppressed the malignancy of cisplatin-resistant OV cells in a dose-dependent manner to suppress cell proliferation, impede cell migration and invasion, and induce both cell apoptosis and cell cycle arrest. Furthermore, in vivo studies showed that chaetocin inhibited tumor growth in a cisplatin-resistant OV xenograft model. In terms of mechanism, chaetocin induced ferroptosis in these cells, inhibiting TFRC ubiquitination and upregulating its expression by reducing the levels of cullin1 and its neddylation binding (cullin1-NEDD8). Our study uncovers a previously unrecognized mechanism: Chaetocin induces ferroptosis by inhibiting TFRC neddylation to upregulate its expression in OV. Unlike its known role as an SUV39H1 inhibitor, chaetocin functions through the neddylation-TFRC-ferroptosis axis, a pathway not previously linked to this compound. Moreover, while neddylation has recently been reported to regulate ferroptosis via SLC7A11, our study reveals an entirely distinct mechanism involving TFRC-mediated iron transport. This epigenetic regulation stabilizes TFRC, sensitizing resistant cells to ferroptosis, providing a dual-mechanistic insight not found in existing literature. By linking chaetocin's gene regulation to iron-dependent cell death, we offer new insights and potential therapies for cisplatin-resistant OV. - Source: PubMed
Publication date: 2026/09/14
Xie HanfeiDai WuminSun LuGong WangangZhu TaoZhang Yingli - Non‑small cell lung cancer (NSCLC) is a major cause of cancer‑associated death globally. Elucidating novel molecular drivers is essential for targeted therapy development. This study sought to investigate the function and regulatory mechanism of proteasome 20S subunit alpha 6 (PSMA6) in NSCLC. - Source: PubMed
Publication date: 2026/08/27
Deng ShiyangLi ZixuanLiu NanWang YueSun JialuGuan BinDu Jiang - A. flavus, as a pathogen, poses a grave threat to both human and livestock health, significantly influencing agricultural production as well. This study aimed to investigate the inactivation effect and mechanism of dielectric barrier discharge cold plasma (DBD-CP) on A. flavus spores. The results exhibited that DBD-CP effectively inactivated A. flavus spores by the Weibull + Tail model. Furthermore, the physiological and proteomic analysis revealed that DBD-CP destructed cell wall and membrane integrity, causing cellular protein leakage and increasing membrane penetration of ROS generated from DBD-CP. Although intracellular ROS was excessively accumulated, the protein levels and activities of SOD and CAT were decreased, indicating that intracellular redox homeostasis was disrupted by DBD-CP. Subsequently, DBD-CP treatment induced cellular protein oxidation and changed protein structures, resulting in unstable protein structures. Meanwhile, protein synthesis and degradation in A. flavus spores were disturbed by inhibiting ribosome biogenesis, initiation process and NEDD8-mediated UPS, which did not compensate for the loss of protein caused by oxidative damage and leakage, leading to A. flavus spore inactivation. Besides, DBD-CP could attenuate A. flavus virulence by downregulating hydrolytic enzymes and CFEM-related proteins. This study provides novel insight into the inactivation mechanism of DBD-CP against A. flavus spores, which establishes a basis for the application of DBD-CP in controlling pathogenic fungi contamination in grains and crops, promoting the development of DBD-CP in food and agricultural decontamination. - Source: PubMed
Publication date: 2026/08/03
Zhao LulingSheng XiaoweiYan WenjingZhang HaoZhang JianhaoQian JingWang Jin - A high-glucose microenvironment is a key feature of tumor metabolic reprogramming that promotes lung cancer cell progression. Previous studies have revealed that protein arginine methyltransferase 5 (PRMT5) is overactivated in various cancers and regulates neddylation of the tumor suppressor phosphatase and tensin homolog (PTEN). This study established a high-glucose (25 mM) model using human non-small cell lung cancer A549 cells. Cell proliferation, invasion and cell cycle progression were assessed using the cell counting kit-8, Transwell, 5-ethynyl-2'-deoxyuridine and flow cytometry assays. The expression levels of neural precursor cells expressed developmentally downregulated protein 8 (NEDD8) and PTEN in total and nuclear protein fractions were analyzed using Western blotting and PTEN localization was determined using immunofluorescence. Cellular NEDD8 levels were manipulated by overexpressing Flag-NEDD8 and using MLN4924, an inhibitor of NEDD8-activating enzyme. The association between PTEN and NEDD8 was further assessed through co-immunoprecipitation. Finally, the mechanism underlying the action of flavokawain A (FKA) was explored by comparing its effects on high-glucose-induced PTEN neddylation with those of GSK3326595, a selective inhibitor of PRMT5. A high-glucose environment promoted A549 cell proliferation and viability while inhibiting cell apoptosis, accompanied by enhanced neddylation of PTEN and its nuclear translocation. NEDD8 overexpression promoted the nuclear import of PTEN; however, MLN4924 treatment effectively blocked this effect. FKA treatment markedly reduced PRMT5 activity, thereby reducing the neddylation modification of PTEN, limiting the nuclear localization of PTEN, ultimately inhibiting the proliferation and invasion ability of A549 cells and promoting cell apoptosis. Notably, GSK3326595 exhibited an inhibitory effect similar to that of FKA. The results indicated that FKA suppressed high glucose-induced carcinogenic effects by inhibiting PRMT5-mediated PTEN neddylation and subsequent nuclear translocation. - Source: PubMed
Publication date: 2026/08/14
Zheng LeiLi JuanSong ChaoShi LepingZhou QianGuan Yuyao