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Volumn 3, Issue , 2012, Pages

Erratum: Prediction of variable translation rate effects on cotranslational protein folding (Nature Communications (2012) 3 (868) DOI: 10.1038/ncomms1850);Prediction of variable translation rate effects on cotranslational protein folding

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROTEIN; RIBOSOME PROTEIN;

EID: 84866449925     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2559     Document Type: Erratum
Times cited : (75)

References (36)
  • 1
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl, F. U. & Hayer-Hartl, M. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16, 574-581 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 3
    • 0033203533 scopus 로고    scopus 로고
    • Co-translational folding of an alphavirus capsid protein in the cytosol of living cells
    • Nicola, A. V., Chen, W. & Helenius, A. Co-translational folding of an alphavirus capsid protein in the cytosol of living cells. Nat. Cell Biol. 1, 341-345 (1999). (Pubitemid 129493575)
    • (1999) Nature Cell Biology , vol.1 , Issue.6 , pp. 341-345
    • Nicola, A.V.1    Chen, W.2    Helenius, A.3
  • 5
    • 33746592161 scopus 로고    scopus 로고
    • Molecular simulations of cotranslational protein folding: Fragment stabilities, folding cooperativity, and trapping in the ribosome
    • Elcock, A. H. Molecular simulations of cotranslational protein folding: fragment stabilities, folding cooperativity, and trapping in the ribosome. PLOS Comput. Biol. 2, 824-841 (2006).
    • (2006) PLOS Comput. Biol. , vol.2 , pp. 824-841
    • Elcock, A.H.1
  • 6
  • 7
    • 77950659587 scopus 로고    scopus 로고
    • Cotranslational folding increases GFP folding yield
    • Ugrinov, K. G. & Clark, P. L. Cotranslational folding increases GFP folding yield. Biophys. J. 98, 1312-1320 (2010).
    • (2010) Biophys. J. , vol.98 , pp. 1312-1320
    • Ugrinov, K.G.1    Clark, P.L.2
  • 8
    • 0035816546 scopus 로고    scopus 로고
    • A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates
    • Clark, P. L. & King, J. A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates. J. Biol. Chem. 276, 25411-25420 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 25411-25420
    • Clark, P.L.1    King, J.2
  • 9
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • DOI 10.1038/41024
    • Netzer, W. J. & Hartl, F. U. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 388, 343-9 (1997). (Pubitemid 27334805)
    • (1997) Nature , vol.388 , Issue.6640 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 10
    • 0032699491 scopus 로고    scopus 로고
    • Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation
    • Komar, A. A., Lesnik, T. & Reiss, C. Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. FEBS Lett. 462, 387-391 (1999).
    • (1999) FEBS Lett , vol.462 , pp. 387-391
    • Komar, A.A.1    Lesnik, T.2    Reiss, C.3
  • 11
    • 52949137359 scopus 로고    scopus 로고
    • Synonymous mutations and ribosome stalling can lead to altered folding pathways and distinct minima
    • Tsai, C. J. et al. Synonymous mutations and ribosome stalling can lead to altered folding pathways and distinct minima. J. Mol. Biol. 383, 281-291 (2008).
    • (2008) J. Mol. Biol. , vol.383 , pp. 281-291
    • Tsai, C.J.1
  • 13
    • 0000359208 scopus 로고
    • Kinetic proofreading - New mechanism for reducing errors in biosynthetic processes requiring high specificity
    • Hopfield, J. J. Kinetic proofreading - new mechanism for reducing errors in biosynthetic processes requiring high specificity. Proc. Natl Acad. Sci. USA 71, 4135-4139 (1974).
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4135-4139
    • Hopfield, J.J.1
  • 14
    • 0016793283 scopus 로고
    • Kinetic Amplification of enzyme discrimination
    • Ninio, J. Kinetic Amplification of enzyme discrimination. Biochimie 57, 587-595 (1975).
    • (1975) Biochimie , vol.57 , pp. 587-595
    • Ninio, J.1
  • 15
    • 79952653259 scopus 로고    scopus 로고
    • Ligand-driven vectorial folding of ribosome-bound human CFTR NBD1
    • Khushoo, A., Yang, Z., Johnson, A. E. & Skach, W. R. Ligand-driven vectorial folding of ribosome-bound human CFTR NBD1. Mol. Cell 41, 682-692 (2011).
    • (2011) Mol. Cell , vol.41 , pp. 682-692
    • Khushoo, A.1    Yang, Z.2    Johnson, A.E.3    Skach, W.R.4
  • 16
    • 77951107295 scopus 로고    scopus 로고
    • Real-time tRNA transit on single translating ribosomes at codon resolution
    • Uemura, S. et al. Real-time tRNA transit on single translating ribosomes at codon resolution. Nature 464, 1012-U73 (2010).
    • (2010) Nature , vol.464
    • Uemura, S.1
  • 17
    • 36749052255 scopus 로고    scopus 로고
    • Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy
    • Hsu, S. T. D. et al. Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy. Proc. Natl Acad. Sci. USA 104, 16516-16521 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16516-16521
    • Hsu, S.T.D.1
  • 18
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor-2.1. Evidence for a 2-state transition
    • Jackson, S. E. & Fersht, A. R. Folding of chymotrypsin inhibitor-2.1. Evidence for a 2-state transition. Biochemistry 30, 10428-10435 (1991).
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 19
    • 62049083910 scopus 로고    scopus 로고
    • Transient ribosomal attenuation coordinates protein synthesis and co-translational folding
    • Zhang, G., Hubalewska, M. & Ignatova, Z. Transient ribosomal attenuation coordinates protein synthesis and co-translational folding. Nat. Struct. Mol. Biol. 16, 274-280 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 274-280
    • Zhang, G.1    Hubalewska, M.2    Ignatova, Z.3
  • 20
    • 34948856961 scopus 로고    scopus 로고
    • Ribosome kinetics and aa-tRNA competition determine rate and fidelity of peptide synthesis
    • DOI 10.1016/j.compbiolchem.2007.07.003, PII S1476927107001053
    • Fluitt, A., Pienaar, E. & Vijoen, H. Ribosome kinetics and aa-tRNA competition determine rate and fidelity of peptide synthesis. Comput. Biol. Chem. 31, 335-346 (2007). (Pubitemid 47531990)
    • (2007) Computational Biology and Chemistry , vol.31 , Issue.5-6 , pp. 335-346
    • Fluitt, A.1    Pienaar, E.2    Viljoen, H.3
  • 21
    • 79959676389 scopus 로고    scopus 로고
    • The ribosome uses two active mechanisms to unwind messenger RNA during translation
    • Qu, X. et al. The ribosome uses two active mechanisms to unwind messenger RNA during translation. Nature 475, 118-21 (2011).
    • (2011) Nature , vol.475 , pp. 118-121
    • Qu, X.1
  • 22
    • 68049093016 scopus 로고    scopus 로고
    • Enzymatic transition states and dynamic motion in barrier crossing
    • Schwartz, S. D. & Schramm, V. L. Enzymatic transition states and dynamic motion in barrier crossing. Nat. Chem. Biol. 5, 552-559 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 552-559
    • Schwartz, S.D.1    Schramm, V.L.2
  • 23
    • 0000729781 scopus 로고    scopus 로고
    • Transition path sampling and the calculation of rate constants
    • Dellago, C., Bolhuis, P. G., Csajka, F. S. & Chandler, D. Transition path sampling and the calculation of rate constants. J. Chem. Phys. 108, 1964-1977 (1998). (Pubitemid 128598706)
    • (1998) Journal of Chemical Physics , vol.108 , Issue.5 , pp. 1964-1977
    • Dellago, C.1    Bolhuis, P.G.2    Csajka, F.S.3    Chandler, D.4
  • 24
    • 84857510185 scopus 로고    scopus 로고
    • Single-molecule fluorescence experiments determine protein folding transition path times
    • Chung, H. S., McHale, K., Louis, J. M. & Eaton, W. A. Single-molecule fluorescence experiments determine protein folding transition path times. Science 335, 981-4 (2012).
    • (2012) Science , vol.335 , pp. 981-984
    • Chung, H.S.1    McHale, K.2    Louis, J.M.3    Eaton, W.A.4
  • 25
    • 67849124732 scopus 로고    scopus 로고
    • Protein folding rates and stability: How much is there beyond size?
    • De Sancho, D., Doshi, U. & Munoz, V. Protein folding rates and stability: how much is there beyond size? J. Am. Chem. Soc. 131, 2074-2075 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2074-2075
    • De Sancho, D.1    Doshi, U.2    Munoz, V.3
  • 30
    • 64049105717 scopus 로고    scopus 로고
    • Tertiary interactions within the ribosomal exit tunnel
    • Kosolapov, A. & Deutsch, C. Tertiary interactions within the ribosomal exit tunnel. Nat. Struct. Mol. Biol. 16, 405-411 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 405-411
    • Kosolapov, A.1    Deutsch, C.2
  • 31
    • 0023659927 scopus 로고
    • The efficiency of folding of some proteins is increased by controlled rates of translation in vivo - A hypothesis
    • Purvis, I. J. et al. The efficiency of folding of some proteins is increased by controlled rates of translation in vivo - a hypothesis. J. Mol. Biol. 193, 413-417 (1987).
    • (1987) J. Mol. Biol. , vol.193 , pp. 413-417
    • Purvis, I.J.1
  • 32
    • 0017105938 scopus 로고
    • Polypeptide-chain-elongation rate in escherichia-coli B-R as a function of growth-rate
    • Young, R. & Bremer, H. Polypeptide-chain-elongation rate in escherichia-coli B-R as a function of growth-rate. Biochem. J. 160, 185-194 (1976).
    • (1976) Biochem. J. , vol.160 , pp. 185-194
    • Young, R.1    Bremer, H.2
  • 34
    • 77956521917 scopus 로고    scopus 로고
    • Silent mutations in sight: Co-variations in tRNA abundance as a key to unravel consequences of silent mutations
    • Czech, A., Fedyunin, I., Zhang, G. & Ignatova, Z. Silent mutations in sight: co-variations in tRNA abundance as a key to unravel consequences of silent mutations. Mol. Biosyst. 6, 1767-1772 (2010).
    • (2010) Mol. Biosyst. , vol.6 , pp. 1767-1772
    • Czech, A.1    Fedyunin, I.2    Zhang, G.3    Ignatova, Z.4
  • 35
    • 0023294732 scopus 로고
    • Alternative to the steady-state method: Derivation of reaction rates from first-passage times and pathway probabilities
    • Ninio, J. Alternative to the steady-state method: derivation of reaction rates from first-passage times and pathway probabilities. Proc. Natl Acad. Sci. USA 84, 663-7 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 663-667
    • Ninio, J.1
  • 36
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules.1. The method
    • Kumar, S., Bouzida, D., Swendsen, R. H., Kollman, P. A. & Rosenberg, J. M. The weighted histogram analysis method for free-energy calculations on biomolecules.1. the method. J. Comput. Chem. 13, 1011-1021 (1992).
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5


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