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- W2180353088 abstract "The regulation of protein synthesis contributes to gene expression in both normal physiology and disease, yet kinetic investigations of the human translation mechanism are currently lacking. Using single-molecule fluorescence imaging methods, we have quantified the nature and timing of structural processes in human ribosomes during single-turnover and processive translation reactions. These measurements reveal that functional complexes exhibit dynamic behaviors and thermodynamic stabilities distinct from those observed for bacterial systems. Structurally defined sub-states of pre- and post-translocation complexes were sensitive to specific inhibitors of the eukaryotic ribosome, demonstrating the utility of this platform to probe drug mechanism. The application of three-color single-molecule fluorescence resonance energy transfer (smFRET) methods further revealed a long-distance allosteric coupling between distal tRNA binding sites within ribosomes bearing three tRNAs, which contributed to the rate of processive translation." @default.
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- W2180353088 date "2015-11-01" @default.
- W2180353088 modified "2023-10-14" @default.
- W2180353088 title "Functional Dynamics within the Human Ribosome Regulate the Rate of Active Protein Synthesis" @default.
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- W2180353088 doi "https://doi.org/10.1016/j.molcel.2015.09.013" @default.
- W2180353088 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4660248" @default.
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- W2180353088 hasPublicationYear "2015" @default.
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