Ask about this productRelated genes to: USP7 antibody
- Gene:
- USP7 NIH gene
- Name:
- ubiquitin specific peptidase 7
- Previous symbol:
- HAUSP
- Synonyms:
- -
- Chromosome:
- 16p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-12
- Date modifiied:
- 2017-01-04
Related products to: USP7 antibody
Related articles to: USP7 antibody
- CCAAT/enhancer-binding protein B (CEBPB) has been reported as a transcription factor implicated in the occurrence and development of various human tumors. However, its role and mechanism in hypopharyngeal squamous cell carcinoma (HpSCC) remain unclear. - Source: PubMed
Publication date: 2026/04/28
Li HonghuiFan RongQu YipingShao YuanBai YanxiaXu ChongwenHu JinsongZhang Xiaozhi - - Source: PubMed
Publication date: 2026/04/24
Pang WenguangFang MingxingWu Weidong - Radioresistance remains the primary cause of radiotherapy failure in non-small cell lung cancer (NSCLC). This study investigated the regulatory role of HMOX1-mediated ferroptosis in NSCLC radiosensitivity. Radioresistant cell models (H1650R/H1975R) were established through fractionated irradiation of parental H1650/H1975 cells. Transcriptomic analysis by RNA sequencing revealed significant HMOX1 suppression in resistant cells. Functional validation demonstrated that HMOX1 overexpression enhanced radiation sensitivity via ferroptosis induction, whereas HMOX1 knockdown aggravated radioresistance. Mechanistic investigations identified USP7 as a key deubiquitinating enzyme that stabilizes KEAP1 through K48-linked polyubiquitin chain cleavage, thereby promoting NRF2 ubiquitination and suppressing HMOX1 transcription. Pharmacological inhibition using KI696 blocked KEAP1-NRF2 interaction, restoring HMOX1 expression. Notably, the USP7 inhibitor GNE-6640 destabilized KEAP1, upregulated NRF2/HMOX1 axis activity, and triggered ferroptosis in resistant cells. In vivo studies confirmed that GNE-6640 synergized with radiotherapy to suppress tumor growth and pulmonary metastasis in xenograft and NSG mouse models, as monitored by bioluminescence imaging. These findings establish the USP7-KEAP1-NRF2-HMOX1 axis as a critical determinant of radioresistance, demonstrating that targeted USP7 inhibition with GNE-6640 reactivates ferroptosis and restores radiosensitivity. This dual-mechanistic approach provides a novel therapeutic strategy to overcome treatment resistance in NSCLC. - Source: PubMed
Publication date: 2026/04/23
Tang JianweiXu LeiGong ZetianChen Liang - - Source: PubMed
Publication date: 2026/04/22
Tian PinggeDu QianZeng FangChen JinWang PengzhenZhang LishuangLi Yangyu - The E3 ubiquitin ligase tripartite motif 27 (TRIM27) is a negative regulator of NF-κB activation and the innate immune response, and TRIM27 deficiency significantly impairs dextran sulfate sodium (DSS)-induced colitis. The function of TRIM27 in intestinal epithelial cells (IECs), the mechanism by which TRIM27 inhibits the NF-κB pathway and its dysregulation in ulcerative colitis (UC) remain unclear. Here, it is report that epithelial TRIM27 functions as an anti-inflammatory factor that inhibited intestinal inflammation in IECs in vitro and in epithelial Trim27 knockout mice in vivo. Mechanistically, TRIM27 destabilized IKKα and TRAF6 via polyubiquitination of IKKα at the K569 site and TRAF6 at the K489 site. In response to TNF-α, IKKβ phosphorylated TRIM27 at S173 to decrease TRIM27 expression by impairing its binding to ubiquitin-specific protease 7 (USP7) and USP7-mediated TRIM27 deubiquitination. Notably, overexpression of TRIM27 enhanced the anti-inflammatory effect of infliximab (IFX) in IECs. TRIM27 is downregulated in inflamed colons from UC patients and is associated with the therapeutic effect of IFX. Overall, this study identifies epithelial TRIM27 as a bona fide negative modulator of intestinal inflammation and USP7/TRIM27-IKK as a new double negative feedback mechanism of the NF-κB pathway, which supports the use of TRIM27 replenishment as a potential therapeutic strategy for UC. - Source: PubMed
Publication date: 2026/04/22
Xu WeiminHua ZhebinDai ZhujiangZhang ShashaJiang YihanGe WensongChen YingWeiWang ZhongchuanZhang BingLiu Chen-YingDu Peng