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References from Reversing the relative time courses of the peptide bond reaction with oligopeptides of different lengths and charged amino acid distributions in the ribosome exit tunnel. Local targets link to admitted publications; unresolved targets remain external evidence.
Kinetics of biopolymerization on nucleic acid templates
10.1002/bip.1968.360060102 · 1968 · External reference
10.1002/bip.1969.360070508
10.1002/bip.1969.360070508 · External reference
10.5936/csbj.201204002
10.5936/csbj.201204002 · External reference
Predictive biophysical modeling and understanding of the dynamics of mRNA translation and its evolution
2016 · External reference
10.1371/journal.pgen.1007166
10.1371/journal.pgen.1007166 · External reference
10.1093/nar/gku646
10.1093/nar/gku646 · External reference
Trade-offs between tRNA abundance and mRNA secondary structure support smoothing of translation elongation rate
10.1093/nar/gkv199 · 2015 · External reference
10.1016/j.cell.2012.01.050
10.1016/j.cell.2012.01.050 · External reference
Adaptation of codon usage to tRNA I34 modification controls translation kinetics and proteome landscape
2020 · External reference
10.1186/1471-2164-16-s10-s5
10.1186/1471-2164-16-s10-s5 · External reference
10.1080/15476286.2016.1172755
10.1080/15476286.2016.1172755 · External reference
10.1371/journal.pbio.1001508
10.1371/journal.pbio.1001508 · External reference
10.1038/nature06716
10.1038/nature06716 · External reference
Direct measurement of the mechanical work during translocation by the ribosome
10.7554/elife.03406 · 2014 · External reference
10.1016/j.molcel.2019.07.024
10.1016/j.molcel.2019.07.024 · External reference
10.1101/gr.175893.114
10.1101/gr.175893.114 · External reference
10.1073/pnas.0809211106
10.1073/pnas.0809211106 · External reference
Totally asymmetric exclusion process with extended objects: a model for protein synthesis
10.1103/physreve.68.021910 · 2003 · External reference
10.1016/j.cell.2013.05.049
10.1016/j.cell.2013.05.049 · External reference
A model for competition for ribosomes in the cell
10.1098/rsif.2015.1062 · 2016 · External reference
Mixed population of competing totally asymmetric simple exclusion processes with a shared reservoir of particles
10.1103/physreve.85.011142 · 2012 · External reference
10.1073/pnas.0801795105
10.1073/pnas.0801795105 · External reference
What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome?
10.1021/bi0509806 · 2005 · External reference
10.1074/jbc.m805316200
10.1074/jbc.m805316200 · External reference
Mechanism of peptide bond formation on the ribosome
10.1017/s003358350600429x · 2006 · External reference
Translation in prokaryotes
10.1101/cshperspect.a032664 · 2018 · External reference
10.1016/j.molcel.2007.03.015
10.1016/j.molcel.2007.03.015 · External reference
Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome
10.1093/emboj/17.24.7490 · 1998 · External reference
10.1073/pnas.0402488101
10.1073/pnas.0402488101 · External reference
10.1016/j.molcel.2005.09.006
10.1016/j.molcel.2005.09.006 · External reference
10.1073/pnas.0504043102
10.1073/pnas.0504043102 · External reference
Analysis of predictions for the catalytic mechanism of ribosomal peptidyl transfer
10.1021/bi0605383 · 2006 · External reference
The transition state for peptide bond formation reveals the ribosome as a water trap
10.1073/pnas.0914192107 · 2010 · External reference
A structural view on the mechanism of ribosome-catalyzed peptide bond formation
10.1016/j.bbagrm.2009.06.006 · 2009 · External reference
10.1038/nsmb.2871
10.1038/nsmb.2871 · External reference
Ribosome exit tunnel electrostatics
10.1103/physreve.105.014409 · 2022 · External reference
10.1063/1.1749604
10.1063/1.1749604 · External reference
The development of transition state theory
10.1021/j100238a002 · 1983 · External reference
Unresolved reference
2005 · External reference
10.1016/j.jmb.2007.06.038
10.1016/j.jmb.2007.06.038 · External reference
10.1016/j.jmb.2008.08.089
10.1016/j.jmb.2008.08.089 · External reference
10.1016/j.csbj.2023.07.016 · Admitted local publication
10.1021/cr400313x
10.1021/cr400313x · External reference
10.1126/science.347575
10.1126/science.347575 · External reference
10.1146/annurev.biochem.72.121801.161542
10.1146/annurev.biochem.72.121801.161542 · External reference
10.1021/cr200399q
10.1021/cr200399q · External reference
10.1007/978-4-431-55052-5_4
10.1007/978-4-431-55052-5_4 · 2014 · External reference
10.1146/annurev-biochem-061516-044432
10.1146/annurev-biochem-061516-044432 · External reference
Co-translational folding trajectory of the HEMK helical domain
10.1021/acs.biochem.8b00293 · 2020 · External reference
10.7554/elife.60895
10.7554/elife.60895 · External reference
10.1126/science.aaf0899
10.1126/science.aaf0899 · External reference
10.1093/nar/gkz106
10.1093/nar/gkz106 · External reference