eEF2 Antibody (C-term)
- Known as:
- eEF2 Antibody (C-terminus)
- Catalog number:
- AJ1250b
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- eEF2 Antibody (C-term)
Related genes to: eEF2 Antibody (C-term)
- Gene:
- EEF2 NIH gene
- Name:
- eukaryotic translation elongation factor 2
- Previous symbol:
- EF2
- Synonyms:
- EEF-2
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-03-11
- Date modifiied:
- 2015-09-11
Related products to: eEF2 Antibody (C-term)
Related articles to: eEF2 Antibody (C-term)
- Periodontitis, a common chronic inflammatory disease, causes connective tissue degradation, alveolar bone resorption, and tooth loss. G protein coupled receptor class C group 5 member A (GPRC5A) regulates chronic inflammation in several diseases, but its role in periodontitis remains unclear. This study investigated GPRC5A expression and function in periodontitis. In human tissues, GPRC5A expression was assessed by immunohistochemistry and quantitative real-time PCR (qRT-PCR). In vivo, adeno associated virus (AAV) mediated GPRC5A silencing was applied in a murine periodontitis model. In vitro, mechanistic studies used small interfering RNA (siRNA) knockdown, co-immunoprecipitation (Co-IP), mass spectrometry, and western blot in periodontal ligament cells (PDLCs). GPRC5A was upregulated in inflamed periodontal tissues, and its downregulation reduced alveolar bone loss and periodontitis severity in mice. GPRC5A knockdown suppressed inflammatory cytokine production and NF-κB activation in lipopolysaccharide (LPS) stimulated PDLCs. β-arrestin 2 (ARRB2) expression paralleled GPRC5A changes, and mass spectrometry/Co-IP identified eukaryotic elongation factor 2 (EEF2) as an ARRB2 binding partner. GPRC5A silencing reduced LPS induced ARRB2 expression and EEF2 phosphorylation. These data suggest a possible mechanistic link that GPRC5A downregulation mitigates periodontitis through the ARRB2‑EEF2 pathway, though direct evidence of causality is still needed. - Source: PubMed
Publication date: 2026/06/11
Hu YuhanLiu RunxuanChen XinxiaoShang Lingling - Translation is accompanied by the rotation of the small and large ribosomal subunits relative to each other. Here, we use single-molecule Förster resonance energy transfer between fluorophores introduced into ribosomal proteins uS15 and eL30 to follow the intersubunit dynamics of Saccharomyces cerevisiae ribosomes. Similar to their bacterial counterparts, yeast ribosomes are observed to sample two predominant FRET states corresponding to the nonrotated (NR) and rotated (R) conformations. Our data yield further evidence that intersubunit rotation is coupled to tRNA transitions between the classical and hybrid binding states. The elongation cycle, which comprises tRNA binding, peptide transfer, and mRNA-tRNA translocation, is accompanied by switching from NR to R, and then back to the NR conformation. We find that fungal elongation factor 3 (eEF3) stabilizes the NR conformation of the ribosome. Our data are consistent with the model suggesting that eEF3 facilitates E-site tRNA release at the late step of mRNA-tRNA translocation, following the reverse intersubunit rotation induced by the universally conserved elongation factor 2 (eEF2). Our uS15-eL30 smFRET assay provides the basis for investigating eukaryotic mechanisms of translation regulation, including ribosome pausing, stalling, and frameshifting. - Source: PubMed
Das AnanyaGrove Amy KIvanov Aleksandr VWakabayashi HironaoErmolenko Dmitri N - Newcastle disease (ND) caused by Newcastle disease virus (NDV) infection is a highly contagious avian disease that causes substantial threat to the global poultry industry. Emodin (EMO), a member of the free anthraquinone compounds derived from traditional Chinese medicines, is known for its antibacterial, antiviral, antitumor, and antioxidant activity. However, the anti-NDV activity and potential mechanism of action of EMO remains unknown. In this study, EMO was found to exert a remarkable anti-NDV activity in a dose- and phase-dependent manner. In addition, EMO restricted NDV replication mainly by affecting the production of viral proteins, but not by inhibiting the viral RNA synthesis and transcription. Moreover, the EMO treatment-induced reduction of viral proteins was correlated well with the increased phosphorylation level of eukaryotic elongation factor 2 (eEF2) in NDV-infected cells, which was further confirmed by inhibition of eEF2 kinase (eEF2K) activity with pharmacological inhibitors NH125 and A-484954, respectively. Meanwhile, multiple signaling cascades, including p38 MAPK, mTORC1/p70 S6K, and ERK1/2/p90 RSK1, were found to regulate the phosphorylation levels and activities of eEF2K and eEF2 by which EMO reduced viral protein production and inhibited NDV replication. Furthermore, molecular docking combined with protein-protein interaction analysis showed that EMO could form stable hydrogen bond structures with the NDV N protein at the Lys32 and Leu225 residues, and attenuate its interaction with eIF4E to decrease the production of viral proteins. These findings reveal the anti-NDV effect and the underlying mechanism of EMO, offering a potential natural compound for the development of antiviral strategies against NDV. - Source: PubMed
Publication date: 2026/05/25
Wu WenjieXia RongjingMa SiHu ZengleiDuan Zhiqiang - We utilized the nedicistrovirus (NediV) intergenic region (IGR) internal ribosomal entry site (IRES)-mediated, initiation factor-independent translation initiation system and determined high-resolution structures of 80S ribosome complexes with the NediV IRES in various functional states, including binary complexes, aminoacyl-transfer RNA (tRNA)-bound complexes, and complexes with elongation factor eEF2. In binary complexes, the NediV IRES primarily occupies the ribosomal P site, exhibiting conformational flexibility and engaging the ribosome at multiple interaction sites. Upon translocation, the IRES undergoes structural rearrangements, including destabilization of its PKI domain, facilitating the transition to canonical elongation. Crucially, we captured an eEF2-bound complex, along with an eEF1A-bound failed decoding complex featuring a mismatched tRNA, the latter representing the first instance of a canonical elongation complex visualized in the presence of a natural, hydrolysable nucleotide and without the addition of any trapping agents. These findings provide a comprehensive structural overview of IGR IRES-mediated translation initiation and its transition to elongation, revealing key mechanistic details of viral translation and proofreading. - Source: PubMed
De SwastikAltomare Clara GAbaeva Irina SDadhwal PrikshatGarg PriyankaAcosta-Reyes FranciscoBrown Zuben PPestova Tatyana VHellen Christopher U TFrank Joachim - Digital PCR (dPCR) enables absolute, precise nucleic acid quantification without the need for standard curves. Still, technical variability across the sample life cycle remains a challenge in complex multi-organ preclinical studies. This study evaluated the necessity of internal reference genes (i.e., housekeeping genes; HKGs) for normalizing reverse transcription (RT)-dPCR data from recombinant adeno-associated virus (rAAV) studies in mice and non-human primates (NHPs). HKGs were ranked using statistical analysis and further evaluated with the BestKeeper and geNorm algorithms. In mice, , , and were identified as the most stable HKGs. Normalization to a single HKG () consistently and markedly reduced transgene-expression variability across tissues. In NHPs, and demonstrated the highest stability. Importantly, multiplexing HKGs allowed to differentiate technical from biological variation, thereby mitigating common assay pitfalls. Collectively, these findings underscore that normalization is essential for reliable inter- and intra-group comparability in RT-dPCR. We strongly recommend multiplexing at least two medium-expression, validated HKGs to derive a robust normalization factor, thereby significantly improving accuracy in complex preclinical settings. - Source: PubMed
Publication date: 2026/04/16
Mackeben KlausMüller SarahDolim KimberlyOtteneder Michael BRos FrancescaFakhiri Julia