Ask about this productRelated genes to: ETF1 antibody
- Gene:
- ETF1 NIH gene
- Name:
- eukaryotic translation termination factor 1
- Previous symbol:
- SUP45L1, ERF1, ERF
- Synonyms:
- eRF1, TB3-1, RF1
- Chromosome:
- 5q31.2
- Locus Type:
- gene with protein product
- Date approved:
- 1991-06-13
- Date modifiied:
- 2014-11-19
Related products to: ETF1 antibody
Related articles to: ETF1 antibody
- Emerging and reemerging viruses pose a significant threat to global health. Although direct-acting antivirals have shown success, their efficacy is limited by the rapid emergence of drug-resistant viral variants. Hence, there is an urgent need for additional broad spectrum antiviral therapeutic strategies. Here, we identify by phenotypic screening a set of stereochemically defined photoreactive small molecules (photo-stereoprobes) that stereoselectively suppress SARS-CoV-2 replication in human lung epithelial cells. Structure-activity relationship-guided chemical proteomics identified the eukaryotic translation termination factor 1 (ETF1) as a target of the photo-stereoprobes, and this interaction was recapitulated with recombinant purified ETF1. We found that the photo-stereoprobes modulate programmed ribosomal frameshifting mechanisms essential for SARS-CoV-2 infection without causing ETF1 degradation, thus distinguishing the photo-stereoprobes from other known ETF1-directed small molecules. We finally show that the photo-stereoprobes also inhibit the replication of additional viruses with noncanonical ribosomal frameshifting mechanisms. Our findings identify a mechanistically distinct class of ETF1 ligands that implicate host translation termination processes as a potential drug target for antiviral development. - Source: PubMed
Publication date: 2026/01/28
Kim Arthur SMa KevinReinhardt Christopher JLazar Daniel COgasawara DaisukeShaw Teressa Mde la Torre Juan CarlosBailey Adam LMelillo BrunoTeijaro John RCravatt Benjamin F - Eukaryotic translation initiation factor eIF3 plays a pivotal role in 48S preinitiation complex assembly and ribosomal scanning. It binds simultaneously to the 40S ribosomal subunit and the eIF4F cap-binding complex, which, through its interaction with poly(A)-binding protein (PABP), facilitates closed-loop mRNA structure formation. PABP also interacts with the eukaryotic release factor eRF3, thereby co-localizing initiation and release factors, and suggesting potential functional crosstalk. Using a reconstituted mammalian translation system, we demonstrate that eIF3 significantly enhances translation termination. Specifically, eIF3 promotes the loading of eRF1 into the ribosomal A site, accelerating the GTPase activity of eRF3 and the rate of peptide release. We also show that eIF3 facilitates the binding of suppressor or near-cognate tRNAs to stop codons to enable readthrough and continued elongation. These findings establish a conserved, direct role of eIF3 in regulation both translation termination and stop codon readthrough, a mechanism particularly relevant within closed-loop mRNA structures and during upstream open reading frame translation. - Source: PubMed
Shuvalova EkaterinaShuvalov AlexeyAl Sheikh WalaaKlishin AlexandrBiziaev NikitaAlkalaeva Elena - PTC124 (Ataluren) is a small molecule drug for the treatment of genetic diseases that has been shown to promote early termination codon read-through. In this study, the binding model of PTC124 to human serum albumin and eukaryotic stop codon recognition factor (eRF1) was established in vitro. In the cell model, the read-through effect of PTC124 on the stop codon was confirmed. Fluorescence analysis showed that PTC124 could spontaneously bind eRF1 and HSA, the binding constants were 3.132 ± 0.643 × 10 and 2.963 ± 0.218 × 10 L/mol (298 K), respectively. Thermodynamic analysis indicated that the binding to eRF1 was driven mainly by hydrophobic interactions, hydrogen bonding, and van der Waals forces, whereas the binding to HSA was driven primarily by hydrogen bonding and van der Waals forces. Structural analysis revealed perturbations in the secondary structure of both HSA and eRF1 induced by PTC124, while the overall native folds of the proteins were maintained. In addition, a binding model of the interaction between PTC124 and eRF1/HSA was established by molecular simulation and STD-NMR. The binding model described in this paper explains the interaction mechanism between PTC124 and its utility and transport targets at the molecular level, which is helpful for the design and synthesis of new molecules related to PTC124 structure and based on its mechanism of action. - Source: PubMed
Publication date: 2025/11/22
Duan RanGuo HanlinPeng ZhengxiongYu XinyuYu JupingTian HongLiu Wei - Black raspberry is known to contain a diverse number of phytochemicals, especially polyphenols which have shown health benefits. These compounds might play a role in alleviating β-amyloid (Aβ)-induced neurotoxicity. In this study, we investigated the effect of black raspberry in reducing Aβ toxicity and improving mitochondrial function in the HT-22 cell model. HT-22 cells were co-cultured together with black raspberry extract (BRE) and Aβ and various markers for apoptosis and mitochondrial function were assessed. BRE treatment significantly improved cell viability, reduced reactive oxygen species (ROS) generation, and enhanced mitochondrial biogenesis via upregulation of PGC-1α and Sirt1 expression. Among the isolated fractions, the ethanol fraction (Et-F1) demonstrated the most potent neuroprotective effect. High-performance liquid chromatography identified rutin as a major compound in Et-F1, though it did not account for the full protective effect. In conclusion, our results suggest that BRE might be used as a natural supplementation for combatting Aβ-associated dementia. - Source: PubMed
Publication date: 2025/09/04
Tandoro YohanesChiu Hui-FangShen You-ChengTsou Sing-HuaLin Chih-LiWang Chin-Kun - Emerging and re-emerging viruses pose a significant threat to global health. Although direct-acting antivirals have shown success, their efficacy is limited by the rapid emergence of drug-resistant viral variants. Hence, there is an urgent need for additional broad spectrum antiviral therapeutic strategies. Here, we identify by phenotypic screening a set of stereochemically defined photoreactive small molecules (photo-stereoprobes) that stereoselectively suppress SARS-CoV-2 replication in human lung epithelial cells. Structure-activity relationship-guided chemical proteomics identified the eukaryotic translation termination factor 1 (ETF1) as a target of the photo-stereoprobes, and this interaction was recapitulated with recombinant purified ETF1. We found that the photo-stereoprobes modulate programmed ribosomal frameshifting mechanisms essential for SARS-CoV-2 infection without causing ETF1 degradation, thus distinguishing the photo-stereoprobes from other known ETF1-directed small molecules. We finally show that the photo-stereoprobes also inhibit the replication of additional viruses with non-canonical ribosomal frameshifting mechanisms. Our findings thus identify a mechanistically distinct class of ETF1 ligands that implicate host translation termination processes as a potential target for antiviral development. - Source: PubMed
Publication date: 2025/08/28
Kim Arthur SMa KevinReinhardt Christopher JLazar Daniel COgasawara DaisukeShaw Teressa Mde la Torre Juan CarlosBailey Adam LMelillo BrunoTeijaro John RCravatt Benjamin F