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Volumn , Issue , 2016, Pages 1390-1406

The ribosome in action: Tuning of translational efficiency and protein folding

Author keywords

mRNA rare codons; protein synthesis and folding; ribosome; translational pausing; tRNA

Indexed keywords

ARGININE; GLYCINE; LYSINE; MESSENGER RNA; PEPTIDE; PROTEIN; TRANSFER RNA;

EID: 84978983295     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2950     Document Type: Review
Times cited : (137)

References (168)
  • 1
    • 84873510362 scopus 로고    scopus 로고
    • Ribosome traffic on mRNAs maps to gene ontology: genome-wide quantification of translation initiation rates and polysome size regulation
    • Ciandrini L, Stansfield I, Romano MC (2013) Ribosome traffic on mRNAs maps to gene ontology: genome-wide quantification of translation initiation rates and polysome size regulation. PLoS Comput Biol 9:e1002866.
    • (2013) PLoS Comput Biol , vol.9
    • Ciandrini, L.1    Stansfield, I.2    Romano, M.C.3
  • 2
    • 84883549935 scopus 로고    scopus 로고
    • Transimulation—protein biosynthesis web service
    • Siwiak M, Zielenkiewicz P (2013) Transimulation—protein biosynthesis web service. PLoS One 8:e73943.
    • (2013) PLoS One , vol.8
    • Siwiak, M.1    Zielenkiewicz, P.2
  • 3
    • 49349113285 scopus 로고    scopus 로고
    • Ribosome collisions and translation efficiency: optimization by codon usage and mRNA destabilization
    • Mitarai N, Sneppen K, Pedersen S (2008) Ribosome collisions and translation efficiency: optimization by codon usage and mRNA destabilization. J Mol Biol 382:236–245.
    • (2008) J Mol Biol , vol.382 , pp. 236-245
    • Mitarai, N.1    Sneppen, K.2    Pedersen, S.3
  • 4
    • 84911468469 scopus 로고    scopus 로고
    • An integrated approach reveals regulatory controls on bacterial translation elongation
    • Subramaniam AR, Zid BM, O'Shea EK (2014) An integrated approach reveals regulatory controls on bacterial translation elongation. Cell 159:1200–1211.
    • (2014) Cell , vol.159 , pp. 1200-1211
    • Subramaniam, A.R.1    Zid, B.M.2    O'Shea, E.K.3
  • 5
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter JD, Sonenberg N (2005) Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature 433:477–480.
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 6
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11:113–127.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 7
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136:731–745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 9
    • 84872543206 scopus 로고    scopus 로고
    • A decade of riboswitches
    • Serganov A, Nudler E (2013) A decade of riboswitches. Cell 152:17–24.
    • (2013) Cell , vol.152 , pp. 17-24
    • Serganov, A.1    Nudler, E.2
  • 10
    • 84877286711 scopus 로고    scopus 로고
    • Regulation of pathogenicity by noncoding RNAs in bacteria
    • Han Y, Liu L, Fang N, Yang R, Zhou D (2013) Regulation of pathogenicity by noncoding RNAs in bacteria. Future Microbiol 8:579–591.
    • (2013) Future Microbiol , vol.8 , pp. 579-591
    • Han, Y.1    Liu, L.2    Fang, N.3    Yang, R.4    Zhou, D.5
  • 11
    • 84937440655 scopus 로고    scopus 로고
    • Roles for synonymous codon usage in protein biogenesis
    • Chaney JL, Clark PL (2015) Roles for synonymous codon usage in protein biogenesis. Annu Rev Biophys 44:143–166.
    • (2015) Annu Rev Biophys , vol.44 , pp. 143-166
    • Chaney, J.L.1    Clark, P.L.2
  • 12
    • 58149199728 scopus 로고    scopus 로고
    • A pause for thought along the co-translational folding pathway
    • Komar AA (2009) A pause for thought along the co-translational folding pathway. Trends Biochem Sci 34:16–24.
    • (2009) Trends Biochem Sci , vol.34 , pp. 16-24
    • Komar, A.A.1
  • 13
    • 84945497191 scopus 로고    scopus 로고
    • Ribosome profiling reveals the what, when, where and how of protein synthesis
    • Brar GA, Weissman JS (2015) Ribosome profiling reveals the what, when, where and how of protein synthesis. Nat Rev Mol Cell Biol 16:651–664.
    • (2015) Nat Rev Mol Cell Biol , vol.16 , pp. 651-664
    • Brar, G.A.1    Weissman, J.S.2
  • 14
    • 84893255169 scopus 로고    scopus 로고
    • Controlling translation elongation efficiency: tRNA regulation of ribosome flux on the mRNA
    • Gorgoni B, Marshall E, McFarland MR, Romano MC, Stansfield I (2014) Controlling translation elongation efficiency: tRNA regulation of ribosome flux on the mRNA. Biochem Soc Trans 42:160–165.
    • (2014) Biochem Soc Trans , vol.42 , pp. 160-165
    • Gorgoni, B.1    Marshall, E.2    McFarland, M.R.3    Romano, M.C.4    Stansfield, I.5
  • 15
    • 84867732569 scopus 로고    scopus 로고
    • Speeding with control: codon usage, tRNAs, and ribosomes
    • Novoa EM, Ribas de Pouplana L (2012) Speeding with control: codon usage, tRNAs, and ribosomes. Trends Genet 28:574–581.
    • (2012) Trends Genet , vol.28 , pp. 574-581
    • Novoa, E.M.1    Ribas de Pouplana, L.2
  • 16
    • 84873419140 scopus 로고    scopus 로고
    • The ribosome as a hub for protein quality control
    • Pechmann S, Willmund F, Frydman J (2013) The ribosome as a hub for protein quality control. Mol Cell 49:411–421.
    • (2013) Mol Cell , vol.49 , pp. 411-421
    • Pechmann, S.1    Willmund, F.2    Frydman, J.3
  • 17
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi Y, Choi PJ, Li GW, Chen H, Babu M, Hearn J, Emili A, Xie XS (2010) Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 329:533–538.
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.W.3    Chen, H.4    Babu, M.5    Hearn, J.6    Emili, A.7    Xie, X.S.8
  • 18
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • Lu P, Vogel C, Wang R, Yao X, Marcotte EM (2007) Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat Biotechnol 25:117–124.
    • (2007) Nat Biotechnol , vol.25 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 21
    • 84899881726 scopus 로고    scopus 로고
    • Transcript level and sequence determinants of protein abundance and noise in Escherichia coli
    • Guimaraes JC, Rocha M, Arkin AP (2014) Transcript level and sequence determinants of protein abundance and noise in Escherichia coli. Nucleic Acids Res 42:4791–4799.
    • (2014) Nucleic Acids Res , vol.42 , pp. 4791-4799
    • Guimaraes, J.C.1    Rocha, M.2    Arkin, A.P.3
  • 22
    • 84890795845 scopus 로고    scopus 로고
    • Protein synthesis rate is the predominant regulator of protein expression during differentiation
    • Kristensen AR, Gsponer J, Foster LJ (2013) Protein synthesis rate is the predominant regulator of protein expression during differentiation. Mol Syst Biol 9:689.
    • (2013) Mol Syst Biol , vol.9 , pp. 689
    • Kristensen, A.R.1    Gsponer, J.2    Foster, L.J.3
  • 26
    • 33845790070 scopus 로고    scopus 로고
    • Correlation of mRNA expression and protein abundance affected by multiple sequence features related to translational efficiency in Desulfovibrio vulgaris: a quantitative analysis
    • Nie L, Wu G, Zhang W (2006) Correlation of mRNA expression and protein abundance affected by multiple sequence features related to translational efficiency in Desulfovibrio vulgaris: a quantitative analysis. Genetics 174:2229–2243.
    • (2006) Genetics , vol.174 , pp. 2229-2243
    • Nie, L.1    Wu, G.2    Zhang, W.3
  • 27
    • 62549134121 scopus 로고    scopus 로고
    • Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
    • Ingolia NT, Ghaemmaghami S, Newman JR, Weissman JS (2009) Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling. Science 324:218–223.
    • (2009) Science , vol.324 , pp. 218-223
    • Ingolia, N.T.1    Ghaemmaghami, S.2    Newman, J.R.3    Weissman, J.S.4
  • 28
    • 84959149884 scopus 로고    scopus 로고
    • Improved ribosome-footprint and mRNA measurements provide insights into dynamics and regulation of yeast translation
    • Weinberg DE, Shah P, Eichhorn SW, Hussmann JA, Plotkin JB, Bartel DP (2016) Improved ribosome-footprint and mRNA measurements provide insights into dynamics and regulation of yeast translation. Cell Rep 14:1787–1799.
    • (2016) Cell Rep , vol.14 , pp. 1787-1799
    • Weinberg, D.E.1    Shah, P.2    Eichhorn, S.W.3    Hussmann, J.A.4    Plotkin, J.B.5    Bartel, D.P.6
  • 29
    • 84886302057 scopus 로고    scopus 로고
    • Causes and effects of N-terminal codon bias in bacterial genes
    • Goodman DB, Church GM, Kosuri S (2013) Causes and effects of N-terminal codon bias in bacterial genes. Science 342:475–479.
    • (2013) Science , vol.342 , pp. 475-479
    • Goodman, D.B.1    Church, G.M.2    Kosuri, S.3
  • 30
    • 84902193122 scopus 로고    scopus 로고
    • The scanning mechanism of eukaryotic translation initiation
    • Hinnebusch AG (2014) The scanning mechanism of eukaryotic translation initiation. Annu Rev Biochem 83:779–812.
    • (2014) Annu Rev Biochem , vol.83 , pp. 779-812
    • Hinnebusch, A.G.1
  • 31
    • 84911480225 scopus 로고    scopus 로고
    • Predicting translation initiation rates for designing synthetic biology
    • Reeve B, Hargest T, Gilbert C, Ellis T (2014) Predicting translation initiation rates for designing synthetic biology. Front Bioeng Biotechnol 2:1.
    • (2014) Front Bioeng Biotechnol , vol.2 , pp. 1
    • Reeve, B.1    Hargest, T.2    Gilbert, C.3    Ellis, T.4
  • 32
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • Salis HM, Mirsky EA, Voigt CA (2009) Automated design of synthetic ribosome binding sites to control protein expression. Nat Biotechnol 27:946–950.
    • (2009) Nat Biotechnol , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 34
    • 0024210037 scopus 로고
    • What constitutes the signal for the initiation of protein synthesis on Escherichia coli mRNAs?
    • Dreyfus M (1988) What constitutes the signal for the initiation of protein synthesis on Escherichia coli mRNAs? J Mol Biol 204:79–94.
    • (1988) J Mol Biol , vol.204 , pp. 79-94
    • Dreyfus, M.1
  • 35
    • 84862658718 scopus 로고    scopus 로고
    • Kinetic control of translation initiation in bacteria
    • Milon P, Rodnina MV (2012) Kinetic control of translation initiation in bacteria. Crit Rev Biochem Mol Biol 47:334–348.
    • (2012) Crit Rev Biochem Mol Biol , vol.47 , pp. 334-348
    • Milon, P.1    Rodnina, M.V.2
  • 37
    • 33645965566 scopus 로고    scopus 로고
    • Unfolding of mRNA secondary structure by the bacterial translation initiation complex
    • Studer SM, Joseph S (2006) Unfolding of mRNA secondary structure by the bacterial translation initiation complex. Mol Cell 22:105–115.
    • (2006) Mol Cell , vol.22 , pp. 105-115
    • Studer, S.M.1    Joseph, S.2
  • 38
    • 44949260971 scopus 로고    scopus 로고
    • Kinetic checkpoint at a late step in translation initiation
    • Milon P, Konevega AL, Gualerzi CO, Rodnina MV (2008) Kinetic checkpoint at a late step in translation initiation. Mol Cell 30:712–720.
    • (2008) Mol Cell , vol.30 , pp. 712-720
    • Milon, P.1    Konevega, A.L.2    Gualerzi, C.O.3    Rodnina, M.V.4
  • 39
    • 84932113188 scopus 로고    scopus 로고
    • Translation initiation factor 3 regulates switching between different modes of ribosomal subunit joining. J
    • MacDougall DD, Gonzalez RL Jr. (2015) Translation initiation factor 3 regulates switching between different modes of ribosomal subunit joining. J Mol Biol 427:1801–1818.
    • (2015) Mol Biol , vol.427 , pp. 1801-1818
    • MacDougall, D.D.1    Gonzalez, R.L.2
  • 40
    • 84964589294 scopus 로고    scopus 로고
    • Directional transition from initiation to elongation in bacterial translation
    • Goyal A, Belardinelli R, Maracci C, Milon P, Rodnina MV (2015) Directional transition from initiation to elongation in bacterial translation. Nucleic Acids Res 43:10700–10712.
    • (2015) Nucleic Acids Res , vol.43 , pp. 10700-10712
    • Goyal, A.1    Belardinelli, R.2    Maracci, C.3    Milon, P.4    Rodnina, M.V.5
  • 41
    • 34548788950 scopus 로고    scopus 로고
    • Structured mRNAs regulate translation initiation by binding to the platform of the ribosome
    • Marzi S, Myasnikov AG, Serganov A, Ehresmann C, Romby P, Yusupov M, Klaholz BP (2007) Structured mRNAs regulate translation initiation by binding to the platform of the ribosome. Cell 130:1019–1031.
    • (2007) Cell , vol.130 , pp. 1019-1031
    • Marzi, S.1    Myasnikov, A.G.2    Serganov, A.3    Ehresmann, C.4    Romby, P.5    Yusupov, M.6    Klaholz, B.P.7
  • 42
    • 33751103912 scopus 로고    scopus 로고
    • Structural basis for messenger RNA movement on the ribosome
    • Yusupova G, Jenner L, Rees B, Moras D, Yusupov M (2006) Structural basis for messenger RNA movement on the ribosome. Nature 444:391–394.
    • (2006) Nature , vol.444 , pp. 391-394
    • Yusupova, G.1    Jenner, L.2    Rees, B.3    Moras, D.4    Yusupov, M.5
  • 45
    • 84860730931 scopus 로고    scopus 로고
    • Multiple activities of RNA-binding proteins S1 and Hfq
    • Hajnsdorf E, Boni IV (2012) Multiple activities of RNA-binding proteins S1 and Hfq. Biochimie 94:1544–1553.
    • (2012) Biochimie , vol.94 , pp. 1544-1553
    • Hajnsdorf, E.1    Boni, I.V.2
  • 46
    • 77957240693 scopus 로고    scopus 로고
    • Multifactorial determinants of protein expression in prokaryotic open reading frames
    • Allert M, Cox JC, Hellinga HW (2010) Multifactorial determinants of protein expression in prokaryotic open reading frames. J Mol Biol 402:905–918.
    • (2010) J Mol Biol , vol.402 , pp. 905-918
    • Allert, M.1    Cox, J.C.2    Hellinga, H.W.3
  • 47
    • 33745943856 scopus 로고    scopus 로고
    • How initiation factors maximize the accuracy of tRNA selection in initiation of bacterial protein synthesis
    • Antoun A, Pavlov MY, Lovmar M, Ehrenberg M (2006) How initiation factors maximize the accuracy of tRNA selection in initiation of bacterial protein synthesis. Mol Cell 23:183–193.
    • (2006) Mol Cell , vol.23 , pp. 183-193
    • Antoun, A.1    Pavlov, M.Y.2    Lovmar, M.3    Ehrenberg, M.4
  • 48
    • 64849114915 scopus 로고    scopus 로고
    • Coding-sequence determinants of gene expression in Escherichia coli
    • Kudla G, Murray AW, Tollervey D, Plotkin JB (2009) Coding-sequence determinants of gene expression in Escherichia coli. Science 324:255–258.
    • (2009) Science , vol.324 , pp. 255-258
    • Kudla, G.1    Murray, A.W.2    Tollervey, D.3    Plotkin, J.B.4
  • 49
    • 77649245858 scopus 로고    scopus 로고
    • Translation efficiency is determined by both codon bias and folding energy
    • Tuller T, Waldman YY, Kupiec M, Ruppin E (2010) Translation efficiency is determined by both codon bias and folding energy. Proc Natl Acad Sci USA 107:3645–3650.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3645-3650
    • Tuller, T.1    Waldman, Y.Y.2    Kupiec, M.3    Ruppin, E.4
  • 50
    • 23244446620 scopus 로고    scopus 로고
    • Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis
    • Underwood KA, Swartz JR, Puglisi JD (2005) Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis. Biotechnol Bioeng 91:425–435.
    • (2005) Biotechnol Bioeng , vol.91 , pp. 425-435
    • Underwood, K.A.1    Swartz, J.R.2    Puglisi, J.D.3
  • 53
    • 34047223024 scopus 로고    scopus 로고
    • Posttranscriptional expression regulation: what determines translation rates?
    • Brockmann R, Beyer A, Heinisch JJ, Wilhelm T (2007) Posttranscriptional expression regulation: what determines translation rates? PLoS Comput Biol 3:e57.
    • (2007) PLoS Comput Biol , vol.3
    • Brockmann, R.1    Beyer, A.2    Heinisch, J.J.3    Wilhelm, T.4
  • 54
    • 79954456859 scopus 로고    scopus 로고
    • Determinants of translation efficiency and accuracy
    • Gingold H, Pilpel Y (2011) Determinants of translation efficiency and accuracy. Mol Syst Biol 7:481.
    • (2011) Mol Syst Biol , vol.7 , pp. 481
    • Gingold, H.1    Pilpel, Y.2
  • 55
    • 84879345901 scopus 로고    scopus 로고
    • Rate-limiting steps in yeast protein translation
    • Shah P, Ding Y, Niemczyk M, Kudla G, Plotkin JB (2013) Rate-limiting steps in yeast protein translation. Cell 153:1589–1601.
    • (2013) Cell , vol.153 , pp. 1589-1601
    • Shah, P.1    Ding, Y.2    Niemczyk, M.3    Kudla, G.4    Plotkin, J.B.5
  • 56
    • 84899550455 scopus 로고    scopus 로고
    • Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources
    • Li GW, Burkhardt D, Gross C, Weissman JS (2014) Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. Cell 157:624–635.
    • (2014) Cell , vol.157 , pp. 624-635
    • Li, G.W.1    Burkhardt, D.2    Gross, C.3    Weissman, J.S.4
  • 57
    • 84927693301 scopus 로고    scopus 로고
    • High-precision analysis of translational pausing by ribosome profiling in bacteria lacking EFP
    • Woolstenhulme CJ, Guydosh NR, Green R, Buskirk AR (2015) High-precision analysis of translational pausing by ribosome profiling in bacteria lacking EFP. Cell Rep 11:13–21.
    • (2015) Cell Rep , vol.11 , pp. 13-21
    • Woolstenhulme, C.J.1    Guydosh, N.R.2    Green, R.3    Buskirk, A.R.4
  • 58
    • 84953284492 scopus 로고    scopus 로고
    • Understanding biases in ribosome profiling experiments reveals signatures of translation dynamics in yeast
    • Hussmann JA, Patchett S, Johnson A, Sawyer S, Press WH (2015) Understanding biases in ribosome profiling experiments reveals signatures of translation dynamics in yeast. PLoS Genet 11:e1005732.
    • (2015) PLoS Genet , vol.11
    • Hussmann, J.A.1    Patchett, S.2    Johnson, A.3    Sawyer, S.4    Press, W.H.5
  • 59
    • 84927635725 scopus 로고    scopus 로고
    • Determinants of the rate of mRNA translocation in bacterial protein synthesis
    • Borg A, Ehrenberg M (2015) Determinants of the rate of mRNA translocation in bacterial protein synthesis. J Mol Biol 427:1835–1847.
    • (2015) J Mol Biol , vol.427 , pp. 1835-1847
    • Borg, A.1    Ehrenberg, M.2
  • 60
    • 84871921644 scopus 로고    scopus 로고
    • EF-P is essential for rapid synthesis of proteins containing consecutive proline residues
    • Doerfel LK, Wohlgemuth I, Kothe C, Peske F, Urlaub H, Rodnina MV (2013) EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science 339:85–88.
    • (2013) Science , vol.339 , pp. 85-88
    • Doerfel, L.K.1    Wohlgemuth, I.2    Kothe, C.3    Peske, F.4    Urlaub, H.5    Rodnina, M.V.6
  • 61
    • 37549003962 scopus 로고    scopus 로고
    • Peptidyl-prolyl-tRNA at the ribosomal P-site reacts poorly with puromycin
    • Muto H, Ito K (2008) Peptidyl-prolyl-tRNA at the ribosomal P-site reacts poorly with puromycin. Biochem Biophys Res Commun 366:1043–1047.
    • (2008) Biochem Biophys Res Commun , vol.366 , pp. 1043-1047
    • Muto, H.1    Ito, K.2
  • 62
    • 57749116022 scopus 로고    scopus 로고
    • Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates
    • Wohlgemuth I, Brenner S, Beringer M, Rodnina MV (2008) Modulation of the rate of peptidyl transfer on the ribosome by the nature of substrates. J Biol Chem 283:32229–32235.
    • (2008) J Biol Chem , vol.283 , pp. 32229-32235
    • Wohlgemuth, I.1    Brenner, S.2    Beringer, M.3    Rodnina, M.V.4
  • 64
    • 84875465945 scopus 로고    scopus 로고
    • Positively charged residues are the major determinants of ribosomal velocity
    • Charneski CA, Hurst LD (2013) Positively charged residues are the major determinants of ribosomal velocity. PLoS Biol 11:e1001508.
    • (2013) PLoS Biol , vol.11
    • Charneski, C.A.1    Hurst, L.D.2
  • 65
  • 66
    • 78149280508 scopus 로고    scopus 로고
    • Optimization of speed and accuracy of decoding in translation
    • Wohlgemuth I, Pohl C, Rodnina MV (2010) Optimization of speed and accuracy of decoding in translation. Embo J 29:3701–3709.
    • (2010) Embo J , vol.29 , pp. 3701-3709
    • Wohlgemuth, I.1    Pohl, C.2    Rodnina, M.V.3
  • 68
    • 46149104347 scopus 로고    scopus 로고
    • Different aa-tRNAs are selected uniformly on the ribosome
    • Ledoux S, Uhlenbeck OC (2008) Different aa-tRNAs are selected uniformly on the ribosome. Mol Cell 31:114–123.
    • (2008) Mol Cell , vol.31 , pp. 114-123
    • Ledoux, S.1    Uhlenbeck, O.C.2
  • 69
    • 33845995459 scopus 로고    scopus 로고
    • Codon reading by tRNAAla with modified uridine in the wobble position
    • Kothe U, Rodnina MV (2007) Codon reading by tRNAAla with modified uridine in the wobble position. Mol Cell 25:167–174.
    • (2007) Mol Cell , vol.25 , pp. 167-174
    • Kothe, U.1    Rodnina, M.V.2
  • 70
    • 31544454704 scopus 로고    scopus 로고
    • A uniform response to mismatches in codon-anticodon complexes ensures ribosomal fidelity
    • Gromadski KB, Daviter T, Rodnina MV (2006) A uniform response to mismatches in codon-anticodon complexes ensures ribosomal fidelity. Mol Cell 21:369–377.
    • (2006) Mol Cell , vol.21 , pp. 369-377
    • Gromadski, K.B.1    Daviter, T.2    Rodnina, M.V.3
  • 71
    • 0842267211 scopus 로고    scopus 로고
    • Kinetic determinants of high-fidelity tRNA discrimination on the ribosome
    • Gromadski KB, Rodnina MV (2004) Kinetic determinants of high-fidelity tRNA discrimination on the ribosome. Mol Cell 13:191–200.
    • (2004) Mol Cell , vol.13 , pp. 191-200
    • Gromadski, K.B.1    Rodnina, M.V.2
  • 73
    • 84924192559 scopus 로고    scopus 로고
    • Emerging roles of tRNA in adaptive translation, signalling dynamics and disease
    • Kirchner S, Ignatova Z (2015) Emerging roles of tRNA in adaptive translation, signalling dynamics and disease. Nat Rev Genet 16:98–112.
    • (2015) Nat Rev Genet , vol.16 , pp. 98-112
    • Kirchner, S.1    Ignatova, Z.2
  • 76
    • 84962533940 scopus 로고    scopus 로고
    • Codon usage and 3' UTR length determine maternal mRNA stability in zebrafish
    • Mishima Y, Tomari Y (2016) Codon usage and 3' UTR length determine maternal mRNA stability in zebrafish. Mol Cell 61:874–885.
    • (2016) Mol Cell , vol.61 , pp. 874-885
    • Mishima, Y.1    Tomari, Y.2
  • 77
    • 62049083910 scopus 로고    scopus 로고
    • Transient ribosomal attenuation coordinates protein synthesis and co-translational folding
    • Zhang G, Hubalewska M, Ignatova Z (2009) Transient ribosomal attenuation coordinates protein synthesis and co-translational folding. Nat Struct Mol Biol 16:274–280.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 274-280
    • Zhang, G.1    Hubalewska, M.2    Ignatova, Z.3
  • 78
    • 0021731777 scopus 로고
    • Escherichia coli ribosomes translate in vivo with variable rate
    • Pedersen S (1984) Escherichia coli ribosomes translate in vivo with variable rate. Embo J 3:2895–2898.
    • (1984) Embo J , vol.3 , pp. 2895-2898
    • Pedersen, S.1
  • 79
    • 0024405193 scopus 로고
    • Codon usage determines translation rate in Escherichia coli
    • Sorensen MA, Kurland CG, Pedersen S (1989) Codon usage determines translation rate in Escherichia coli. J Mol Biol 207:365–377.
    • (1989) J Mol Biol , vol.207 , pp. 365-377
    • Sorensen, M.A.1    Kurland, C.G.2    Pedersen, S.3
  • 80
    • 0029162727 scopus 로고
    • Codon pair utilization biases influence translational elongation step times
    • Irwin B, Heck JD, Hatfield GW (1995) Codon pair utilization biases influence translational elongation step times. J Biol Chem 270:22801–22806.
    • (1995) J Biol Chem , vol.270 , pp. 22801-22806
    • Irwin, B.1    Heck, J.D.2    Hatfield, G.W.3
  • 81
    • 0024284197 scopus 로고
    • The AGG codon is translated slowly in E. coli even at very low expression levels
    • Bonekamp F, Jensen KF (1988) The AGG codon is translated slowly in E. coli even at very low expression levels. Nucleic Acids Res 16:3013–3024.
    • (1988) Nucleic Acids Res , vol.16 , pp. 3013-3024
    • Bonekamp, F.1    Jensen, K.F.2
  • 82
    • 0022536971 scopus 로고
    • Effect of distribution of unfavourable codons on the maximum rate of gene expression by an heterologous organism
    • Varenne S, Lazdunski C (1986) Effect of distribution of unfavourable codons on the maximum rate of gene expression by an heterologous organism. J Theor Biol 120:99–110.
    • (1986) J Theor Biol , vol.120 , pp. 99-110
    • Varenne, S.1    Lazdunski, C.2
  • 84
    • 0032699491 scopus 로고    scopus 로고
    • Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation
    • Komar AA, Lesnik T, Reiss C (1999) Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. FEBS Lett 462:387–391.
    • (1999) FEBS Lett , vol.462 , pp. 387-391
    • Komar, A.A.1    Lesnik, T.2    Reiss, C.3
  • 85
    • 78649656286 scopus 로고    scopus 로고
    • Control of translation efficiency in yeast by codon-anticodon interactions
    • Letzring DP, Dean KM, Grayhack EJ (2010) Control of translation efficiency in yeast by codon-anticodon interactions. Rna 16:2516–2528.
    • (2010) Rna , vol.16 , pp. 2516-2528
    • Letzring, D.P.1    Dean, K.M.2    Grayhack, E.J.3
  • 86
    • 0024962419 scopus 로고
    • Rates of aminoacyl-tRNA selection at 29 sense codons in vivo
    • Curran JF, Yarus M (1989) Rates of aminoacyl-tRNA selection at 29 sense codons in vivo. J Mol Biol 209:65–77.
    • (1989) J Mol Biol , vol.209 , pp. 65-77
    • Curran, J.F.1    Yarus, M.2
  • 87
    • 84903457409 scopus 로고    scopus 로고
    • The effects of codon context on in vivo translation speed
    • Chevance FF, Le Guyon S, Hughes KT (2014) The effects of codon context on in vivo translation speed. PLoS Genet 10:e1004392.
    • (2014) PLoS Genet , vol.10
    • Chevance, F.F.1    Le Guyon, S.2    Hughes, K.T.3
  • 88
    • 84892981871 scopus 로고    scopus 로고
    • Expanding Anfinsen's principle: contributions of synonymous codon selection to rational protein design
    • Sander IM, Chaney JL, Clark PL (2014) Expanding Anfinsen's principle: contributions of synonymous codon selection to rational protein design. J Am Chem Soc 136:858–861.
    • (2014) J Am Chem Soc , vol.136 , pp. 858-861
    • Sander, I.M.1    Chaney, J.L.2    Clark, P.L.3
  • 89
    • 84860231100 scopus 로고    scopus 로고
    • The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria
    • Li GW, Oh E, Weissman JS (2012) The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria. Nature 484:538–541.
    • (2012) Nature , vol.484 , pp. 538-541
    • Li, G.W.1    Oh, E.2    Weissman, J.S.3
  • 91
    • 84906235471 scopus 로고    scopus 로고
    • The effect of tRNA levels on decoding times of mRNA codons
    • Dana A, Tuller T (2014) The effect of tRNA levels on decoding times of mRNA codons. Nucleic Acids Res 42:9171–9181.
    • (2014) Nucleic Acids Res , vol.42 , pp. 9171-9181
    • Dana, A.1    Tuller, T.2
  • 94
    • 84958213278 scopus 로고    scopus 로고
    • Redefining the translational status of 80S monosomes
    • Heyer EE, Moore MJ (2016) Redefining the translational status of 80S monosomes. Cell 164:757–769.
    • (2016) Cell , vol.164 , pp. 757-769
    • Heyer, E.E.1    Moore, M.J.2
  • 95
    • 84925553022 scopus 로고    scopus 로고
    • Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo
    • Pechmann S, Chartron JW, Frydman J (2014) Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo. Nat Struct Mol Biol 21:1100–1105.
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 1100-1105
    • Pechmann, S.1    Chartron, J.W.2    Frydman, J.3
  • 96
    • 79957870201 scopus 로고    scopus 로고
    • Coupling between codon usage, translation and protein export in Escherichia coli
    • Zalucki YM, Beacham IR, Jennings MP (2011) Coupling between codon usage, translation and protein export in Escherichia coli. Biotechnol J 6:660–667.
    • (2011) Biotechnol J , vol.6 , pp. 660-667
    • Zalucki, Y.M.1    Beacham, I.R.2    Jennings, M.P.3
  • 97
    • 63349088915 scopus 로고    scopus 로고
    • Biased codon usage in signal peptides: a role in protein export
    • Zalucki YM, Beacham IR, Jennings MP (2009) Biased codon usage in signal peptides: a role in protein export. Trends Microbiol 17:146–150.
    • (2009) Trends Microbiol , vol.17 , pp. 146-150
    • Zalucki, Y.M.1    Beacham, I.R.2    Jennings, M.P.3
  • 98
    • 43249083239 scopus 로고    scopus 로고
    • Signal sequence-independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel
    • Bornemann T, Jockel J, Rodnina MV, Wintermeyer W (2008) Signal sequence-independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel. Nat Struct Mol Biol 15:494–499.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 494-499
    • Bornemann, T.1    Jockel, J.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 99
    • 84873570699 scopus 로고    scopus 로고
    • Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding
    • Pechmann S, Frydman J (2013) Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding. Nat Struct Mol Biol 20:237–243.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 237-243
    • Pechmann, S.1    Frydman, J.2
  • 101
    • 77649198142 scopus 로고    scopus 로고
    • A universal trend of reduced mRNA stability near the translation-initiation site in prokaryotes and eukaryotes
    • Gu W, Zhou T, Wilke CO (2010) A universal trend of reduced mRNA stability near the translation-initiation site in prokaryotes and eukaryotes. PLoS Comput Biol 6:e1000664.
    • (2010) PLoS Comput Biol , vol.6
    • Gu, W.1    Zhou, T.2    Wilke, C.O.3
  • 102
    • 84942284143 scopus 로고    scopus 로고
    • Trade-offs between tRNA abundance and mRNA secondary structure support smoothing of translation elongation rate
    • Gorochowski TE, Ignatova Z, Bovenberg RA, Roubos JA (2015) Trade-offs between tRNA abundance and mRNA secondary structure support smoothing of translation elongation rate. Nucleic Acids Res 43:3022–3032.
    • (2015) Nucleic Acids Res , vol.43 , pp. 3022-3032
    • Gorochowski, T.E.1    Ignatova, Z.2    Bovenberg, R.A.3    Roubos, J.A.4
  • 105
    • 84871918588 scopus 로고    scopus 로고
    • Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches
    • Ude S, Lassak J, Starosta AL, Kraxenberger T, Wilson DN, Jung K (2013) Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches. Science 339:82–85.
    • (2013) Science , vol.339 , pp. 82-85
    • Ude, S.1    Lassak, J.2    Starosta, A.L.3    Kraxenberger, T.4    Wilson, D.N.5    Jung, K.6
  • 110
    • 0037072794 scopus 로고    scopus 로고
    • Proline residues at the C terminus of nascent chains induce SsrA tagging during translation termination
    • Hayes CS, Bose B, Sauer RT (2002) Proline residues at the C terminus of nascent chains induce SsrA tagging during translation termination. J Biol Chem 277:33825–33832.
    • (2002) J Biol Chem , vol.277 , pp. 33825-33832
    • Hayes, C.S.1    Bose, B.2    Sauer, R.T.3
  • 113
    • 84878912996 scopus 로고    scopus 로고
    • Arrest peptides: cis-acting modulators of translation
    • Ito K, Chiba S (2013) Arrest peptides: cis-acting modulators of translation. Annu Rev Biochem 82:171–202.
    • (2013) Annu Rev Biochem , vol.82 , pp. 171-202
    • Ito, K.1    Chiba, S.2
  • 114
    • 77249145819 scopus 로고    scopus 로고
    • Divergent stalling sequences sense and control cellular physiology
    • Ito K, Chiba S, Pogliano K (2010) Divergent stalling sequences sense and control cellular physiology. Biochem Biophys Res Commun 393:1–5.
    • (2010) Biochem Biophys Res Commun , vol.393 , pp. 1-5
    • Ito, K.1    Chiba, S.2    Pogliano, K.3
  • 115
    • 84957548841 scopus 로고    scopus 로고
    • Translation regulation via nascent polypeptide-mediated ribosome stalling
    • Wilson DN, Arenz S, Beckmann R (2016) Translation regulation via nascent polypeptide-mediated ribosome stalling. Curr Opin Struct Biol 37:123–133.
    • (2016) Curr Opin Struct Biol , vol.37 , pp. 123-133
    • Wilson, D.N.1    Arenz, S.2    Beckmann, R.3
  • 119
    • 33947501707 scopus 로고    scopus 로고
    • Peptide bond formation destabilizes Shine-Dalgarno interaction on the ribosome
    • Uemura S, Dorywalska M, Lee TH, Kim HD, Puglisi JD, Chu S (2007) Peptide bond formation destabilizes Shine-Dalgarno interaction on the ribosome. Nature 446:454–457.
    • (2007) Nature , vol.446 , pp. 454-457
    • Uemura, S.1    Dorywalska, M.2    Lee, T.H.3    Kim, H.D.4    Puglisi, J.D.5    Chu, S.6
  • 120
    • 84958115189 scopus 로고    scopus 로고
    • Clarifying the translational pausing landscape in bacteria by ribosome profiling
    • Mohammad F, Woolstenhulme CJ, Green R, Buskirk AR (2016) Clarifying the translational pausing landscape in bacteria by ribosome profiling. Cell Rep 14:686–694.
    • (2016) Cell Rep , vol.14 , pp. 686-694
    • Mohammad, F.1    Woolstenhulme, C.J.2    Green, R.3    Buskirk, A.R.4
  • 121
    • 84873601673 scopus 로고    scopus 로고
    • Good codons, bad transcript: large reductions in gene expression and fitness arising from synonymous mutations in a key enzyme
    • Agashe D, Martinez-Gomez NC, Drummond DA, Marx CJ (2013) Good codons, bad transcript: large reductions in gene expression and fitness arising from synonymous mutations in a key enzyme. Mol Biol E 30:549–560.
    • (2013) Mol Biol E , vol.30 , pp. 549-560
    • Agashe, D.1    Martinez-Gomez, N.C.2    Drummond, D.A.3    Marx, C.J.4
  • 122
    • 0028007434 scopus 로고
    • rRNA-mRNA base pairing stimulates a programmed −1 ribosomal frameshift
    • Larsen B, Wills NM, Gesteland RF, Atkins JF (1994) rRNA-mRNA base pairing stimulates a programmed −1 ribosomal frameshift. J Bacteriol 176:6842–6851.
    • (1994) J Bacteriol , vol.176 , pp. 6842-6851
    • Larsen, B.1    Wills, N.M.2    Gesteland, R.F.3    Atkins, J.F.4
  • 123
    • 54249096045 scopus 로고    scopus 로고
    • Electrostatics in the ribosomal tunnel modulate chain elongation rates
    • Lu J, Deutsch C (2008) Electrostatics in the ribosomal tunnel modulate chain elongation rates. J Mol Biol 384:73–86.
    • (2008) J Mol Biol , vol.384 , pp. 73-86
    • Lu, J.1    Deutsch, C.2
  • 124
    • 34547569922 scopus 로고    scopus 로고
    • Mapping the electrostatic potential within the ribosomal exit tunnel
    • Lu J, Kobertz WR, Deutsch C (2007) Mapping the electrostatic potential within the ribosomal exit tunnel. J Mol Biol 371:1378–1391.
    • (2007) J Mol Biol , vol.371 , pp. 1378-1391
    • Lu, J.1    Kobertz, W.R.2    Deutsch, C.3
  • 128
    • 84893351549 scopus 로고    scopus 로고
    • Genome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo
    • Rouskin S, Zubradt M, Washietl S, Kellis M, Weissman JS (2014) Genome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo. Nature 505:701–705.
    • (2014) Nature , vol.505 , pp. 701-705
    • Rouskin, S.1    Zubradt, M.2    Washietl, S.3    Kellis, M.4    Weissman, J.S.5
  • 129
    • 84903197929 scopus 로고    scopus 로고
    • Programmed −1 frame shifting by kinetic partitioning during impeded translocation
    • Caliskan N, Katunin VI, Belardinelli R, Peske F, Rodnina MV (2014) Programmed −1 frame shifting by kinetic partitioning during impeded translocation. Cell 157:1619–1631.
    • (2014) Cell , vol.157 , pp. 1619-1631
    • Caliskan, N.1    Katunin, V.I.2    Belardinelli, R.3    Peske, F.4    Rodnina, M.V.5
  • 130
    • 84898802217 scopus 로고    scopus 로고
    • A frame shifting stimulatory stem loop destabilizes the hybrid state and impedes ribosomal translocation
    • Kim HK, Liu F, Fei J, Bustamante C, Gonzalez RL Jr, Tinoco I Jr (2014) A frame shifting stimulatory stem loop destabilizes the hybrid state and impedes ribosomal translocation. Proc Natl Acad Sci USA 111:5538–5543.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 5538-5543
    • Kim, H.K.1    Liu, F.2    Fei, J.3    Bustamante, C.4    Gonzalez, R.L.5    Tinoco, I.6
  • 133
    • 11844292767 scopus 로고    scopus 로고
    • mRNA helicase activity of the ribosome
    • Takyar S, Hickerson RP, Noller HF (2005) mRNA helicase activity of the ribosome. Cell 120:49–58.
    • (2005) Cell , vol.120 , pp. 49-58
    • Takyar, S.1    Hickerson, R.P.2    Noller, H.F.3
  • 134
    • 79959676389 scopus 로고    scopus 로고
    • The ribosome uses two active mechanisms to unwind messenger RNA during translation
    • Qu X, Wen JD, Lancaster L, Noller HF, Bustamante C, Tinoco I Jr. (2011) The ribosome uses two active mechanisms to unwind messenger RNA during translation. Nature 475:118–121.
    • (2011) Nature , vol.475 , pp. 118-121
    • Qu, X.1    Wen, J.D.2    Lancaster, L.3    Noller, H.F.4    Bustamante, C.5    Tinoco, I.6
  • 135
    • 84866449925 scopus 로고    scopus 로고
    • Prediction of variable translation rate effects on cotranslational protein folding
    • O'Brien EP, Vendruscolo M, Dobson CM (2012) Prediction of variable translation rate effects on cotranslational protein folding. Nat Commun 3:868.
    • (2012) Nat Commun , vol.3 , pp. 868
    • O'Brien, E.P.1    Vendruscolo, M.2    Dobson, C.M.3
  • 136
    • 84872186688 scopus 로고    scopus 로고
    • In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome
    • Ciryam P, Morimoto RI, Vendruscolo M, Dobson CM, O'Brien EP (2013) In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteome. Proc Natl Acad Sci USA 110:E132–E140.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E132-E140
    • Ciryam, P.1    Morimoto, R.I.2    Vendruscolo, M.3    Dobson, C.M.4    O'Brien, E.P.5
  • 137
    • 30044447928 scopus 로고    scopus 로고
    • Ribosome exit tunnel can entropically stabilize alpha-helices
    • Ziv G, Haran G, Thirumalai D (2005) Ribosome exit tunnel can entropically stabilize alpha-helices. Proc Natl Acad Sci USA 102:18956–18961.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18956-18961
    • Ziv, G.1    Haran, G.2    Thirumalai, D.3
  • 138
    • 0035816546 scopus 로고    scopus 로고
    • A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates
    • Clark PL, King J (2001) A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates. J Biol Chem 276:25411–25420.
    • (2001) J Biol Chem , vol.276 , pp. 25411-25420
    • Clark, P.L.1    King, J.2
  • 142
    • 77952694170 scopus 로고    scopus 로고
    • Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy
    • Eichmann C, Preissler S, Riek R, Deuerling E (2010) Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy. Proc Natl Acad Sci USA 107:9111–9116.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9111-9116
    • Eichmann, C.1    Preissler, S.2    Riek, R.3    Deuerling, E.4
  • 145
    • 52949153256 scopus 로고    scopus 로고
    • Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo
    • Evans MS, Sander IM, Clark PL (2008) Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo. J Mol Biol 383:683–692.
    • (2008) J Mol Biol , vol.383 , pp. 683-692
    • Evans, M.S.1    Sander, I.M.2    Clark, P.L.3
  • 146
    • 84947221434 scopus 로고    scopus 로고
    • Operon structure and cotranslational subunit association direct protein assembly in bacteria
    • Shieh YW, Minguez P, Bork P, Auburger JJ, Guilbride DL, Kramer G, Bukau B (2015) Operon structure and cotranslational subunit association direct protein assembly in bacteria. Science 350:678–680.
    • (2015) Science , vol.350 , pp. 678-680
    • Shieh, Y.W.1    Minguez, P.2    Bork, P.3    Auburger, J.J.4    Guilbride, D.L.5    Kramer, G.6    Bukau, B.7
  • 149
    • 84926419545 scopus 로고    scopus 로고
    • Charge-driven dynamics of nascent-chain movement through the SecYEG translocon
    • Ismail N, Hedman R, Linden M, von Heijne G (2015) Charge-driven dynamics of nascent-chain movement through the SecYEG translocon. Nat Struct Mol Biol 22:145–149.
    • (2015) Nat Struct Mol Biol , vol.22 , pp. 145-149
    • Ismail, N.1    Hedman, R.2    Linden, M.3    von Heijne, G.4
  • 150
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead CA, McCormick PJ, Johnson AE (2004) Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116:725–736.
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 151
    • 28544449949 scopus 로고    scopus 로고
    • Folding zones inside the ribosomal exit tunnel
    • Lu J, Deutsch C (2005) Folding zones inside the ribosomal exit tunnel. Nat Struct Mol Biol 12:1123–1129.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1123-1129
    • Lu, J.1    Deutsch, C.2
  • 154
    • 64049105717 scopus 로고    scopus 로고
    • Tertiary interactions within the ribosomal exit tunnel
    • Kosolapov A, Deutsch C (2009) Tertiary interactions within the ribosomal exit tunnel. Nat Struct Mol Biol 16:405–411.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 405-411
    • Kosolapov, A.1    Deutsch, C.2
  • 159
    • 84886662856 scopus 로고    scopus 로고
    • Genetic code-guided protein synthesis and folding in Escherichia coli
    • Hu S, Wang M, Cai G, He M (2013) Genetic code-guided protein synthesis and folding in Escherichia coli. J Biol Chem 288:30855–30861.
    • (2013) J Biol Chem , vol.288 , pp. 30855-30861
    • Hu, S.1    Wang, M.2    Cai, G.3    He, M.4
  • 160
    • 84874683740 scopus 로고    scopus 로고
    • Non-optimal codon usage affects expression, structure and function of clock protein FRQ
    • Zhou M, Guo J, Cha J, Chae M, Chen S, Barral JM, Sachs MS, Liu Y (2013) Non-optimal codon usage affects expression, structure and function of clock protein FRQ. Nature 495:111–115.
    • (2013) Nature , vol.495 , pp. 111-115
    • Zhou, M.1    Guo, J.2    Cha, J.3    Chae, M.4    Chen, S.5    Barral, J.M.6    Sachs, M.S.7    Liu, Y.8
  • 161
    • 84940891331 scopus 로고    scopus 로고
    • Codon usage influences the local rate of translation elongation to regulate co-translational protein folding
    • Yu CH, Dang Y, Zhou Z, Wu C, Zhao F, Sachs MS, Liu Y (2015) Codon usage influences the local rate of translation elongation to regulate co-translational protein folding. Mol Cell 59:744–754.
    • (2015) Mol Cell , vol.59 , pp. 744-754
    • Yu, C.H.1    Dang, Y.2    Zhou, Z.3    Wu, C.4    Zhao, F.5    Sachs, M.S.6    Liu, Y.7
  • 162
    • 80052964856 scopus 로고    scopus 로고
    • Understanding the contribution of synonymous mutations to human disease
    • Sauna ZE, Kimchi-Sarfaty C (2011) Understanding the contribution of synonymous mutations to human disease. Nat Rev Genet 12:683–691.
    • (2011) Nat Rev Genet , vol.12 , pp. 683-691
    • Sauna, Z.E.1    Kimchi-Sarfaty, C.2
  • 164
    • 84958554893 scopus 로고    scopus 로고
    • Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding
    • Nissley DA, Sharma AK, Ahmed N, Friedrich UA, Kramer G, Bukau B, O'Brien EP (2016) Accurate prediction of cellular co-translational folding indicates proteins can switch from post- to co-translational folding. Nat Commun 7:10341.
    • (2016) Nat Commun , vol.7 , pp. 10341
    • Nissley, D.A.1    Sharma, A.K.2    Ahmed, N.3    Friedrich, U.A.4    Kramer, G.5    Bukau, B.6    O'Brien, E.P.7
  • 165
    • 47549097539 scopus 로고    scopus 로고
    • Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution
    • Drummond DA, Wilke CO (2008) Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution. Cell 134:341–352.
    • (2008) Cell , vol.134 , pp. 341-352
    • Drummond, D.A.1    Wilke, C.O.2
  • 166
    • 84957050566 scopus 로고    scopus 로고
    • Physical origins of codon positions that strongly influence cotranslational folding: a framework for controlling nascent-protein folding
    • Sharma AK, Bukau B, O'Brien EP (2016) Physical origins of codon positions that strongly influence cotranslational folding: a framework for controlling nascent-protein folding. J Am Chem Soc 138:1180–1195.
    • (2016) J Am Chem Soc , vol.138 , pp. 1180-1195
    • Sharma, A.K.1    Bukau, B.2    O'Brien, E.P.3
  • 167
    • 84891871414 scopus 로고    scopus 로고
    • Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates
    • O'Brien EP, Vendruscolo M, Dobson CM (2014) Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates. Nat Commun 5:2988.
    • (2014) Nat Commun , vol.5 , pp. 2988
    • O'Brien, E.P.1    Vendruscolo, M.2    Dobson, C.M.3
  • 168
    • 84901289547 scopus 로고    scopus 로고
    • Understanding the influence of codon translation rates on cotranslational protein folding
    • O'Brien EP, Ciryam P, Vendruscolo M, Dobson CM (2014) Understanding the influence of codon translation rates on cotranslational protein folding. Acc Chem Res 47:1536–1544.
    • (2014) Acc Chem Res , vol.47 , pp. 1536-1544
    • O'Brien, E.P.1    Ciryam, P.2    Vendruscolo, M.3    Dobson, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.