ETF1 Antibody

1. Report molecular dynamics free energy calculations on termination complexes, where relative eRF1 binding free energies to different cognate and near-cognate codons are evaluated. The simulations show a high and uniform discrimination against the near-cognate codons, that differ from the cognate ones by a single nucleotide, and reveal the structural mechanisms behind the precise decoding by eRF1. PMID: 29127299
2. The GTS loop forms a switch that is key for the multiple codon recognition capability of eRF1. PMID: 26725946
3. New information has been presented on architecture of the eRF1 binding site on mammalian ribosome at various translation termination steps and on conformational rearrangements induced by binding of the release factors. PMID: 26655225
4. cryo-electron microscopy (cryo-EM) structures at 3.5-3.8 A resolution of ribosomal complexes containing eRF1 interacting with each of the three stop codons in the A-site PMID: 26245381
5. We characterized a region of the eRF1 N-terminal domain, the P1 pocket, that we had previously shown to be involved in termination efficiency. We identified two residues, arginine 65 and lysine 109, as critical for recognition of the three stop codons. PMID: 25735746
6. C4 lysyl hydroxylation of eRF1 is required for optimal translational termination PMID: 24486019
7. The role of the 41 invariant and conserved N-domain residues in stop codon decoding by human eRF1 was determined. PMID: 23435318
8. This work provides mechanistic insight into the coordination between GTP hydrolysis by eRF3 and subsequent peptide release by eRF1. PMID: 23091004
9. Authors propose that structural variability in the GTS loop may underline the switching between omnipotency and unipotency of eRF1, implying the direct access of the GTS loop to the stop codon. PMID: 22383581
10. The NMR data show that the N-domain of human eRF1 exists in two conformational states. PMID: 22517631
11. Molecular modeling of eRF1 in the 80S termination complex showed that eRF1 fragments neighboring guanines and adenines of stop signals are compatible with different N domain conformations of eRF1. PMID: 21602268
12. By molecular modeling, the eRF1 molecule can be fitted to the A site proximal to the P-site-bound tRNA and to a stop codon in mRNA via a large conformational change to one of its three domains. PMID: 20688868
13. Data show that depleting eRF1 increased the Gag-Pol to Gag ratio in cells infected with replication-competent virus. PMID: 20418372
14. bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1 PMID: 11779511
15. The invariant uridine of stop codons contacts the conserved NIKSR loop in the ribosome PMID: 12356746
16. codon dependence of human eRF1 binding to the mRNA-ribosome complex PMID: 12909007
17. the intracellular concentration of the eukaryotic release factor 1 (eRF1) is a critical parameter influencing the efficiency of amino acid incorporation by nonsense suppression PMID: 15716307
18. Glu55 and Tyr125 residues in the N domain of eRF1 are important for eRF1's decoding function. PMID: 16282590
19. we describe a novel complex that contains the NMD factors SMG-1 and Upf1, and the translation termination release factors eRF1 and eRF3 (SURF). PMID: 16452507
20. Results shows eRF1 promotes GTP binding by eRF3. PMID: 16797113
21. Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes PMID: 19140327
22. Molecular dynamics simulations show that there is no structural effect on the free RF1 release factor caused by methylation of glutamine185, suggesting that its role is intimately associated with the ribosome environment. PMID: 19265422

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HGNC: 3477

OMIM: 600285

KEGG: hsa:2107

STRING: 9606.ENSP00000353741

UniGene: Hs.483494