eIF4E (Phospho_Ser209) Antibody
- Known as:
- eIF4E (Phospho_Ser209) Antibody
- Catalog number:
- E011233-1
- Product Quantity:
- 50ug
- Category:
- Antibodies
- Supplier:
- EnoGene
- Gene target:
- eIF4E (Phospho_Ser209) Antibody
Related genes to: eIF4E (Phospho_Ser209) Antibody
- Gene:
- EIF4E NIH gene
- Name:
- eukaryotic translation initiation factor 4E
- Previous symbol:
- EIF4EL1, EIF4F
- Synonyms:
- EIF4E1
- Chromosome:
- 4q23
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-09
- Date modifiied:
- 2015-08-25
Related products to: eIF4E (Phospho_Ser209) Antibody
Related articles to: eIF4E (Phospho_Ser209) Antibody
- Sweet potato feathery mottle virus (SPFMV), a member of the Potyviridae family and Potyvirus genus, severely affects the yield and quality of sweet potato. Internal ribosome entry site (IRES) elements were first identified in animal RNA viruses and have since been identified in plant RNA viruses and eukaryotic mRNAs. Herein, we show that the 5' untranslated region (UTR) of SPFMV possesses IRES activity and contains the complete IRES sequence. Furthermore, the 3'UTR can synergistically enhance the cap-independent translation efficiency of the 5'UTR. Within the 5'UTR of SPFMV, three stem-loop structures, H1, H2, and H3, play critical roles in cap-independent translation. The top loop of H1 interacts with the 3'UTR through RNA-RNA interaction between GUG and CAC, thereby enhancing IRES activity of the 5'UTR. The top loops of H2 and H3 serve as binding sites for eukaryotic translation initiation factor 4E (eIF4E) or its complex, while their stem structures provide essential structural support. in conclusion, we discovered a unique three-stem-loop IRES element within the SPFMV 5'UTR, providing a potential target for the prevention and control of sweet potato virus disease caused by SPFMV. - Source: PubMed
Publication date: 2026/09/26
Liu LongjunLv XiaomeiLiu MinjunGeng Guowei - Per- and polyfluoroalkyl substances (PFAS) have been associated with thyroid dysfunction, but their relationship with papillary thyroid carcinoma (PTC) and relevant molecular processes remains unclear. We integrated bioinformatics analyses, a hospital-based case-control study, and in vitro experiments to investigate associations between PFAS exposure and PTC and to explore potentially relevant post-transcriptional RNA regulatory processes. Transcriptomic data, PFAS-associated genes, and mG-associated genes were integrated to identify candidate genes. Among 24 overlapping candidates, 21 remained differentially expressed between PTC and normal thyroid tissues after false discovery rate correction, and EIF4E, NCBP1, and AGO2 were identified as candidate hub genes. The case-control study included 60 patients with newly diagnosed PTC and 60 controls. Serum concentrations of 17 PFAS were measured, and individual and mixture associations with PTC status were evaluated using logistic regression, weighted quantile sum regression, quantile g-computation, and Bayesian kernel machine regression. Higher concentrations of several PFAS were associated with lower odds of PTC, although the findings were not fully consistent across analytical models. In vitro, high concentrations of PFOA and PFOS reduced relative thyroid-cell viability, whereas wound-healing responses were variable and did not show a consistent enhancement. PFOA and PFOS exposure was also accompanied by altered EIF4E and NCBP1 mRNA expression, respectively. Overall, these findings support an association between PFAS exposure and PTC and identify mG-associated post-transcriptional regulatory candidates, particularly EIF4E and NCBP1, that may contribute to PFAS-related thyroid cellular responses and warrant further mechanistic investigation. - Source: PubMed
Publication date: 2026/09/17
Yan YuxinSun HongguangCong MeiliQi XinxinZhang ShileiLiu Tao - In recent years, the eIF4E protein family has been actively studied as one of the major susceptibility factors for Solanaceae plants in relation to potyvirus infections. This makes eIF4E an attractive target for genome editing to generate resistant varieties. The viral protein VPg interacts with eIF4E family proteins. Measuring the in vitro affinity of VPg for different eIF4E isoforms has traditionally been difficult. The main reason for this is the high aggregation propensity of VPg. To overcome this, we used protein engineering to generate a chimeric construct based on a fluorescent protein. This approach greatly facilitated the measurement of affinity between two proteins using surface plasmon resonance (SPR). Our results confirm that the α1-α2 hairpin of PVY VPg is involved in complex formation with eIF4E. These findings provide new insights into the molecular mechanism of this protein-protein interaction. - Source: PubMed
Publication date: 2026/09/15
Kolesnikova VictoriaMikhailina AlisaLekontseva NataliaNikonov OlegNikonov StanislavAndreytsev VladimirMaksimov EugenePhat Do TienLe Ngoc ThuNikonova Ekaterina - Anaplastic thyroid cancer (ATC) is a highly aggressive malignancy with limited therapeutic options and poor prognosis. This study aimed to identify effective targeted agents and evaluate their therapeutic potential in combination with paclitaxel. - Source: PubMed
Publication date: 2026/09/22
Jie RanShen Xiawei - Excessive unnecessary protein accumulation in cardiomyocyte is a leading contributor for pathological cardiac hypertrophy and has been found closely regulated by the mTORC1 (mechanistic target of rapamycin complex 1) signaling and lysosome transmembrane proteins. However, the precise regulatory mechanism stratifying mTORC1 signaling and the specific functions of lysosomal proteins in protein homeostasis of cardiomyocytes remain largely unidentified. - Source: PubMed
Publication date: 2026/09/22
Hu YufengLi WeiHu ManliTian SongZhou SiyiLiu JiayiCheng XuZhang ChangjiangZuo YingjieZhang JiaxingLiu DianyuHu YangChen YuanbaoLi XinLuo LeiYang HailongBai LanLiu HuiFerdinandy PéterChiong MarioTroncoso Mayarling FranciscaWen JinyingCai JingjingZhang Xiao-JingShe Zhi-GangZhang XinLi Hongliang