Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus

• Main Authors: Tang, X, Zhu, Y, Baker, S.L, Bowler, M.W, Chen, B.J, Chen, C, Hogg, J.R, Goff, S.P, Song, H
• Other Authors: BIOCHEMISTRY
• Format: Article
• Published: Nature Publishing Group 2020
• Subjects: peptidyl release factor 1; peptidyl release factor 3; protein; ribonuclease H; RNA directed DNA polymerase; unclassified drug; Etf1 protein, mouse; Gag protein; messenger RNA; peptide-chain-release factor 3; protein binding; translation termination factor; crystal structure; human immunodeficiency virus; machinery; peptide; virus; Article; carboxy terminal sequence; controlled study; host; Human immunodeficiency virus; Moloney murine leukemia virus; nonhuman; nonsense mediated mRNA decay; protein interaction; stop codon; animal; calorimetry; chemistry; HEK293 cell line; HeLa cell line; human; metabolism; mouse; mutation; protein domain; translation termination; Animals; Calorimetry; Codon, Terminator; Fusion Proteins, gag-pol; HEK293 Cells; HeLa Cells; HIV Reverse Transcriptase; Humans; Mice; Mutation; Nonsense Mediated mRNA Decay; Peptide Chain Termination, Translational; Peptide Termination Factors; Protein Binding; Protein Domains; Ribonuclease H; RNA, Messenger; RNA-Directed DNA Polymerase
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/174953
• Institution: National University of Singapore

10.1038/ncomms12070