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Volumn 34, Issue 1, 2009, Pages 16-24

A pause for thought along the co-translational folding pathway

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA;

EID: 58149199728     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.10.002     Document Type: Review
Times cited : (271)

References (95)
  • 1
    • 46549084254 scopus 로고    scopus 로고
    • Protein misfolding and disease: from the test tube to the organism
    • Luheshi L.M., et al. Protein misfolding and disease: from the test tube to the organism. Curr. Opin. Chem. Biol. 12 (2008) 25-31
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 25-31
    • Luheshi, L.M.1
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • Jaenicke R., and Lilie H. Folding and association of oligomeric and multimeric proteins. Adv. Protein Chem. 53 (2000) 329-401
    • (2000) Adv. Protein Chem. , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 5
    • 33846916730 scopus 로고    scopus 로고
    • Malleability of protein folding pathways: a simple reason for complex behaviour
    • Lindberg M.O., and Oliveberg M. Malleability of protein folding pathways: a simple reason for complex behaviour. Curr. Opin. Struct. Biol. 17 (2007) 21-29
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 21-29
    • Lindberg, M.O.1    Oliveberg, M.2
  • 6
    • 0025876740 scopus 로고
    • Protein folding: local structures, domains, subunits, and assemblies
    • Jaenicke R. Protein folding: local structures, domains, subunits, and assemblies. Biochemistry 30 (1991) 3147-3161
    • (1991) Biochemistry , vol.30 , pp. 3147-3161
    • Jaenicke, R.1
  • 7
    • 33644878610 scopus 로고    scopus 로고
    • The REFOLD database: a tool for the optimization of protein expression and refolding
    • Chow M.K., et al. The REFOLD database: a tool for the optimization of protein expression and refolding. Nucleic Acids Res. 34 (2006) D207-D212
    • (2006) Nucleic Acids Res. , vol.34
    • Chow, M.K.1
  • 8
    • 0030347863 scopus 로고    scopus 로고
    • Revisiting the Anfinsen cage
    • Ellis R.J. Revisiting the Anfinsen cage. Fold. Des. 1 (1996) R9-R15
    • (1996) Fold. Des. , vol.1
    • Ellis, R.J.1
  • 9
    • 0035238206 scopus 로고    scopus 로고
    • Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells
    • Naylor D.J., and Hartl F.U. Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells. Biochem. Soc. Symp. 68 (2001) 45-68
    • (2001) Biochem. Soc. Symp. , vol.68 , pp. 45-68
    • Naylor, D.J.1    Hartl, F.U.2
  • 10
    • 1342281633 scopus 로고    scopus 로고
    • The protein folding 'speed limit'
    • Kubelka J., et al. The protein folding 'speed limit'. Curr. Opin. Struct. Biol. 14 (2004) 76-88
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 76-88
    • Kubelka, J.1
  • 11
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70 (2001) 603-647
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 12
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B., et al. Molecular chaperones and protein quality control. Cell 125 (2006) 443-451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1
  • 13
    • 0000433760 scopus 로고
    • Ribosome-bound β-galactosidase
    • Cowie D.B., et al. Ribosome-bound β-galactosidase. Proc. Natl. Acad. Sci. U. S. A. 47 (1961) 114-122
    • (1961) Proc. Natl. Acad. Sci. U. S. A. , vol.47 , pp. 114-122
    • Cowie, D.B.1
  • 15
    • 0000098759 scopus 로고
    • Induced enzyme formed on bacterial polyribosomes
    • Kiho Y., and Rich A. Induced enzyme formed on bacterial polyribosomes. Proc. Natl. Acad. Sci. U. S. A. 51 (1964) 111-118
    • (1964) Proc. Natl. Acad. Sci. U. S. A. , vol.51 , pp. 111-118
    • Kiho, Y.1    Rich, A.2
  • 16
    • 0015293032 scopus 로고
    • β-Galactosidase: immunological activity of ribosome-bound, growing polypeptide chains
    • Hamlin J., and Zabin I. β-Galactosidase: immunological activity of ribosome-bound, growing polypeptide chains. Proc. Natl. Acad. Sci. U. S. A. 69 (1972) 412-416
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 412-416
    • Hamlin, J.1    Zabin, I.2
  • 17
    • 0018647555 scopus 로고
    • Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides
    • Bergman L.W., and Kuehl W.M. Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides. J. Biol. Chem. 254 (1979) 5690-5694
    • (1979) J. Biol. Chem. , vol.254 , pp. 5690-5694
    • Bergman, L.W.1    Kuehl, W.M.2
  • 18
    • 0018679846 scopus 로고
    • Formation of an intrachain disulfide bond on nascent immunoglobulin light chains
    • Bergman L.W., and Kuehl W.M. Formation of an intrachain disulfide bond on nascent immunoglobulin light chains. J. Biol. Chem. 254 (1979) 8869-8876
    • (1979) J. Biol. Chem. , vol.254 , pp. 8869-8876
    • Bergman, L.W.1    Kuehl, W.M.2
  • 19
    • 0018590219 scopus 로고
    • Co-translational modification of nascent immunoglobulin heavy and light chains
    • Bergman L.W., and Kuehl W.M. Co-translational modification of nascent immunoglobulin heavy and light chains. J. Supramol. Struct. 11 (1979) 9-24
    • (1979) J. Supramol. Struct. , vol.11 , pp. 9-24
    • Bergman, L.W.1    Kuehl, W.M.2
  • 20
    • 0031468437 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • Fedorov A.N., and Baldwin T.O. Cotranslational protein folding. J. Biol. Chem. 272 (1997) 32715-32718
    • (1997) J. Biol. Chem. , vol.272 , pp. 32715-32718
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 21
    • 0030929725 scopus 로고    scopus 로고
    • Cotranslational folding of globin
    • Komar A.A., et al. Cotranslational folding of globin. J. Biol. Chem. 272 (1997) 10646-10651
    • (1997) J. Biol. Chem. , vol.272 , pp. 10646-10651
    • Komar, A.A.1
  • 23
    • 0035385082 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • Kolb V.A. Cotranslational protein folding. Mol. Biol. (Mosk.) 35 (2001) 682-690
    • (2001) Mol. Biol. (Mosk.) , vol.35 , pp. 682-690
    • Kolb, V.A.1
  • 24
    • 14544282996 scopus 로고    scopus 로고
    • The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer
    • Johnson A.E. The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer. FEBS Lett. 579 (2005) 916-920
    • (2005) FEBS Lett. , vol.579 , pp. 916-920
    • Johnson, A.E.1
  • 25
    • 85034953206 scopus 로고    scopus 로고
    • Komar, A.A. (2008) Protein translation rates and protein misfolding: is there any link? In Protein Misfolding: New Research (O'Doherty C.B. and Byrne, A.C. eds) Nova Science Publishers (in press)
    • Komar, A.A. (2008) Protein translation rates and protein misfolding: is there any link? In Protein Misfolding: New Research (O'Doherty C.B. and Byrne, A.C. eds) Nova Science Publishers (in press)
  • 26
    • 0037147191 scopus 로고    scopus 로고
    • Coordinated nonvectorial folding in a newly synthesized multidomain protein
    • Jansens A., et al. Coordinated nonvectorial folding in a newly synthesized multidomain protein. Science 298 (2002) 2401-2403
    • (2002) Science , vol.298 , pp. 2401-2403
    • Jansens, A.1
  • 27
    • 0037399205 scopus 로고    scopus 로고
    • The chemistry of protein synthesis and voyage through the ribosomal tunnel
    • Jenni S., and Ban N. The chemistry of protein synthesis and voyage through the ribosomal tunnel. Curr. Opin. Struct. Biol. 13 (2003) 212-219
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 212-219
    • Jenni, S.1    Ban, N.2
  • 28
    • 0030025303 scopus 로고    scopus 로고
    • Enzymatic activity of the ribosome-bound nascent polypeptide
    • Makeyev E.V., et al. Enzymatic activity of the ribosome-bound nascent polypeptide. FEBS Lett. 378 (1996) 166-170
    • (1996) FEBS Lett. , vol.378 , pp. 166-170
    • Makeyev, E.V.1
  • 29
    • 0028849478 scopus 로고
    • Folding of an enzyme into an active conformation while bound as peptidyl-tRNA to the ribosome
    • Kudlicki W., et al. Folding of an enzyme into an active conformation while bound as peptidyl-tRNA to the ribosome. Biochemistry 34 (1995) 14284-14287
    • (1995) Biochemistry , vol.34 , pp. 14284-14287
    • Kudlicki, W.1
  • 30
    • 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 C.A., et al. Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116 (2004) 725-736
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1
  • 31
    • 28544449949 scopus 로고    scopus 로고
    • Folding zones inside the ribosomal exit tunnel
    • Lu J., and Deutsch C. Folding zones inside the ribosomal exit tunnel. Nat. Struct. Mol. Biol. 12 (2005) 1123-1129
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1123-1129
    • Lu, J.1    Deutsch, C.2
  • 32
    • 0023053308 scopus 로고
    • Stereochemical analysis of ribosomal transpeptidation. Conformation of nascent peptide
    • Lim V.I., and Spirin A.S. Stereochemical analysis of ribosomal transpeptidation. Conformation of nascent peptide. J. Mol. Biol. 188 (1986) 565-574
    • (1986) J. Mol. Biol. , vol.188 , pp. 565-574
    • Lim, V.I.1    Spirin, A.S.2
  • 33
    • 30044447928 scopus 로고    scopus 로고
    • Ribosome exit tunnel can entropically stabilize alpha-helices
    • Ziv G., et al. Ribosome exit tunnel can entropically stabilize alpha-helices. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 18956-18961
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18956-18961
    • Ziv, G.1
  • 35
    • 33745628037 scopus 로고    scopus 로고
    • The geometry of the ribosomal polypeptide exit tunnel
    • Voss N.R., et al. The geometry of the ribosomal polypeptide exit tunnel. J. Mol. Biol. 360 (2006) 893-906
    • (2006) J. Mol. Biol. , vol.360 , pp. 893-906
    • Voss, N.R.1
  • 36
    • 1842766175 scopus 로고    scopus 로고
    • Three-dimensional structures of translating ribosomes by Cryo-EM
    • Gilbert R.J., et al. Three-dimensional structures of translating ribosomes by Cryo-EM. Mol. Cell 14 (2004) 57-66
    • (2004) Mol. Cell , vol.14 , pp. 57-66
    • Gilbert, R.J.1
  • 37
    • 0345862088 scopus 로고    scopus 로고
    • The role of cotranslation in protein folding: a lattice model study
    • Morrissey M.P., et al. The role of cotranslation in protein folding: a lattice model study. Polymer 45 (2004) 557-571
    • (2004) Polymer , vol.45 , pp. 557-571
    • Morrissey, M.P.1
  • 38
    • 0029422261 scopus 로고
    • Circular permutation of polypeptide chains: implications for protein folding and stability
    • Heinemann U., and Hahn M. Circular permutation of polypeptide chains: implications for protein folding and stability. Prog. Biophys. Mol. Biol. 64 (1995) 121-143
    • (1995) Prog. Biophys. Mol. Biol. , vol.64 , pp. 121-143
    • Heinemann, U.1    Hahn, M.2
  • 39
    • 33646555833 scopus 로고    scopus 로고
    • Protein translocation through a tunnel induces changes in folding kinetics: a lattice model study
    • Contreras Martínez L.M., et al. Protein translocation through a tunnel induces changes in folding kinetics: a lattice model study. Biotechnol. Bioeng. 94 (2006) 105-117
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 105-117
    • Contreras Martínez, L.M.1
  • 40
    • 33747884282 scopus 로고    scopus 로고
    • Modelling sequential protein folding under kinetic control
    • Huard F.P., et al. Modelling sequential protein folding under kinetic control. Bioinformatics 22 (2006) e203-e210
    • (2006) Bioinformatics , vol.22
    • Huard, F.P.1
  • 41
    • 0024117032 scopus 로고
    • Ribosome pausing and stacking during translation of a eukaryotic mRNA
    • Wolin S.L., and Walter P. Ribosome pausing and stacking during translation of a eukaryotic mRNA. EMBO J. 7 (1988) 3559-3569
    • (1988) EMBO J. , vol.7 , pp. 3559-3569
    • Wolin, S.L.1    Walter, P.2
  • 42
    • 0026047846 scopus 로고
    • Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model
    • Krasheninnikov I.A., et al. Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a cotranslational protein-folding model. J. Protein Chem. 10 (1991) 445-454
    • (1991) J. Protein Chem. , vol.10 , pp. 445-454
    • Krasheninnikov, I.A.1
  • 43
    • 0032699491 scopus 로고    scopus 로고
    • Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation
    • Komar A.A., et al. Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. FEBS Lett. 462 (1999) 387-391
    • (1999) FEBS Lett. , vol.462 , pp. 387-391
    • Komar, A.A.1
  • 44
    • 0016195149 scopus 로고
    • Gel chromatographic analysis of nascent globin chains. Evidence of nonuniform size distribution
    • Protzel A., and Morris A.J. Gel chromatographic analysis of nascent globin chains. Evidence of nonuniform size distribution. J. Biol. Chem. 249 (1974) 4594-4600
    • (1974) J. Biol. Chem. , vol.249 , pp. 4594-4600
    • Protzel, A.1    Morris, A.J.2
  • 45
    • 0028880533 scopus 로고
    • Kinetics of translation of γ B crystallin and its circularly permutated variant in an in vitro cell-free system: possible relations to codon distribution and protein folding
    • Komar A.A., and Jaenicke R. Kinetics of translation of γ B crystallin and its circularly permutated variant in an in vitro cell-free system: possible relations to codon distribution and protein folding. FEBS Lett. 376 (1995) 195-198
    • (1995) FEBS Lett. , vol.376 , pp. 195-198
    • Komar, A.A.1    Jaenicke, R.2
  • 46
    • 0032245666 scopus 로고    scopus 로고
    • Heelprinting analysis of in vivo ribosome pause sites
    • Hollingsworth M.J., et al. Heelprinting analysis of in vivo ribosome pause sites. Methods Mol. Biol. 77 (1998) 153-165
    • (1998) Methods Mol. Biol. , vol.77 , pp. 153-165
    • Hollingsworth, M.J.1
  • 47
    • 34548446795 scopus 로고    scopus 로고
    • Halting a cellular production line: responses to ribosomal pausing during translation
    • Buchan J.R., and Stansfield I. Halting a cellular production line: responses to ribosomal pausing during translation. Biol. Cell 99 (2007) 475-487
    • (2007) Biol. Cell , vol.99 , pp. 475-487
    • Buchan, J.R.1    Stansfield, I.2
  • 48
    • 0023762645 scopus 로고
    • Codon usage patterns in Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogaster and Homo sapiens; a review of the considerable within-species diversity
    • Sharp P.M., et al. Codon usage patterns in Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogaster and Homo sapiens; a review of the considerable within-species diversity. Nucleic Acids Res. 16 (1988) 8207-8211
    • (1988) Nucleic Acids Res. , vol.16 , pp. 8207-8211
    • Sharp, P.M.1
  • 49
    • 0021958933 scopus 로고
    • Codon usage and tRNA content in unicellular and multicellular organisms
    • Ikemura T. Codon usage and tRNA content in unicellular and multicellular organisms. Mol. Biol. Evol. 2 (1985) 13-34
    • (1985) Mol. Biol. Evol. , vol.2 , pp. 13-34
    • Ikemura, T.1
  • 50
    • 0031762232 scopus 로고    scopus 로고
    • Enhanced expression of the yeast Ure2 protein in Escherichia coli: the effect of synonymous codon substitutions at a selected place in the gene
    • Komar A.A., et al. Enhanced expression of the yeast Ure2 protein in Escherichia coli: the effect of synonymous codon substitutions at a selected place in the gene. Biol. Chem. 379 (1998) 1295-1300
    • (1998) Biol. Chem. , vol.379 , pp. 1295-1300
    • Komar, A.A.1
  • 51
    • 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 (1987) 413-417
    • (1987) J. Mol. Biol. , vol.193 , pp. 413-417
    • Purvis, I.J.1
  • 52
    • 0024257727 scopus 로고
    • Role of the rare codon clusters in defining the boundaries of polypeptide chain regions with identical secondary structures in the process of co-translational folding of proteins
    • Krasheninnikov I.A., et al. Role of the rare codon clusters in defining the boundaries of polypeptide chain regions with identical secondary structures in the process of co-translational folding of proteins. Dokl. Akad. Nauk SSSR 303 (1988) 995-999
    • (1988) Dokl. Akad. Nauk SSSR , vol.303 , pp. 995-999
    • Krasheninnikov, I.A.1
  • 53
    • 0028079904 scopus 로고
    • The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase
    • Crombie T., et al. The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase. Eur. J. Biochem. 226 (1994) 657-664
    • (1994) Eur. J. Biochem. , vol.226 , pp. 657-664
    • Crombie, T.1
  • 54
    • 0036295371 scopus 로고    scopus 로고
    • Silent mutations affect in vivo protein folding in Escherichia coli
    • Cortazzo P., et al. Silent mutations affect in vivo protein folding in Escherichia coli. Biochem. Biophys. Res. Commun. 293 (2002) 537-541
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 537-541
    • Cortazzo, P.1
  • 55
    • 0024547216 scopus 로고
    • Frequency of using codons in mRNA and coding of the domain structure of proteins
    • Krasheninnikov I.A., et al. Frequency of using codons in mRNA and coding of the domain structure of proteins. Dokl. Akad. Nauk SSSR 305 (1989) 1006-1012
    • (1989) Dokl. Akad. Nauk SSSR , vol.305 , pp. 1006-1012
    • Krasheninnikov, I.A.1
  • 56
    • 0024617266 scopus 로고
    • Role of the code redundancy in determining cotranslational protein folding
    • Krasheninnikov I.A., et al. Role of the code redundancy in determining cotranslational protein folding. Biokhimiia 54 (1989) 187-200
    • (1989) Biokhimiia , vol.54 , pp. 187-200
    • Krasheninnikov, I.A.1
  • 57
    • 0030018101 scopus 로고    scopus 로고
    • Ribosome-mediated translational pause and protein domain organization
    • Thanaraj T.A., and Argos P. Ribosome-mediated translational pause and protein domain organization. Protein Sci. 5 (1996) 1594-1612
    • (1996) Protein Sci. , vol.5 , pp. 1594-1612
    • Thanaraj, T.A.1    Argos, P.2
  • 58
    • 0029908504 scopus 로고    scopus 로고
    • Protein secondary structural types are differentially coded on messenger RNA
    • Thanaraj T.A., and Argos P. Protein secondary structural types are differentially coded on messenger RNA. Protein Sci. 5 (1996) 1973-1983
    • (1996) Protein Sci. , vol.5 , pp. 1973-1983
    • Thanaraj, T.A.1    Argos, P.2
  • 59
    • 0030577349 scopus 로고    scopus 로고
    • Non-random usage of 'degenerate' codons is related to protein three-dimensional structure
    • Adzhubei A.A., et al. Non-random usage of 'degenerate' codons is related to protein three-dimensional structure. FEBS Lett. 399 (1996) 78-82
    • (1996) FEBS Lett. , vol.399 , pp. 78-82
    • Adzhubei, A.A.1
  • 60
    • 0031697801 scopus 로고    scopus 로고
    • The relationship between synonymous codon usage and protein structure
    • Xie T., and Ding D. The relationship between synonymous codon usage and protein structure. FEBS Lett. 434 (1998) 93-96
    • (1998) FEBS Lett. , vol.434 , pp. 93-96
    • Xie, T.1    Ding, D.2
  • 61
    • 0032493780 scopus 로고    scopus 로고
    • Specific correlations between relative synonymous codon usage and protein secondary structure
    • Oresic M., and Shalloway D. Specific correlations between relative synonymous codon usage and protein secondary structure. J. Mol. Biol. 281 (1998) 31-48
    • (1998) J. Mol. Biol. , vol.281 , pp. 31-48
    • Oresic, M.1    Shalloway, D.2
  • 62
    • 0034708361 scopus 로고    scopus 로고
    • Studies on the relationships between the synonymous codon usage and protein secondary structural units
    • Gupta S.K., et al. Studies on the relationships between the synonymous codon usage and protein secondary structural units. Biochem. Biophys. Res. Commun. 269 (2000) 692-696
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 692-696
    • Gupta, S.K.1
  • 63
    • 0034736516 scopus 로고    scopus 로고
    • Second codon positions of genes and the secondary structures of proteins. Relationships and implications for the origin of the genetic code
    • Chiusano M.L., et al. Second codon positions of genes and the secondary structures of proteins. Relationships and implications for the origin of the genetic code. Gene 261 (2000) 63-69
    • (2000) Gene , vol.261 , pp. 63-69
    • Chiusano, M.L.1
  • 64
    • 0036908375 scopus 로고    scopus 로고
    • Distribution of rare triplets along mRNA and their relation to protein folding
    • Makhoul C.H., and Trifonov E.N. Distribution of rare triplets along mRNA and their relation to protein folding. J. Biomol. Struct. Dyn. 20 (2002) 413-420
    • (2002) J. Biomol. Struct. Dyn. , vol.20 , pp. 413-420
    • Makhoul, C.H.1    Trifonov, E.N.2
  • 65
    • 0842307105 scopus 로고    scopus 로고
    • The relationship between synonymous codon usage and protein structure in Escherichia coli and Homo sapiens
    • Gu W., et al. The relationship between synonymous codon usage and protein structure in Escherichia coli and Homo sapiens. Biosystems 73 (2004) 89-97
    • (2004) Biosystems , vol.73 , pp. 89-97
    • Gu, W.1
  • 66
    • 34548709778 scopus 로고    scopus 로고
    • Synonymous codon usage in different protein secondary structural classes of human genes: implication for increased non-randomness of GC3 rich genes towards protein stability
    • Mukhopadhyay P., et al. Synonymous codon usage in different protein secondary structural classes of human genes: implication for increased non-randomness of GC3 rich genes towards protein stability. J. Biosci. 32 (2007) 947-963
    • (2007) J. Biosci. , vol.32 , pp. 947-963
    • Mukhopadhyay, P.1
  • 67
    • 0035816546 scopus 로고    scopus 로고
    • A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates
    • Clark P.L., and King J. A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates. J. Biol. Chem. 276 (2001) 25411-25420
    • (2001) J. Biol. Chem. , vol.276 , pp. 25411-25420
    • Clark, P.L.1    King, J.2
  • 68
    • 52949153256 scopus 로고    scopus 로고
    • Cotranslational folding promotes β-helix formation and avoids aggregation in vivo
    • Evans M.S., et al. Cotranslational folding promotes β-helix formation and avoids aggregation in vivo. J. Mol. Biol. 383 (2008) 683-692
    • (2008) J. Mol. Biol. , vol.383 , pp. 683-692
    • Evans, M.S.1
  • 69
    • 0032983520 scopus 로고    scopus 로고
    • Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    • Frydman J., et al. Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nat. Struct. Biol. 6 (1999) 697-705
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 697-705
    • Frydman, J.1
  • 70
    • 33846021292 scopus 로고    scopus 로고
    • Tissue-specific differences in human transfer RNA expression
    • Dittmar K.A., et al. Tissue-specific differences in human transfer RNA expression. PLoS Genet. 2 (2006) e221
    • (2006) PLoS Genet. , vol.2
    • Dittmar, K.A.1
  • 71
    • 44349120609 scopus 로고    scopus 로고
    • Analysis of the distribution of functionally relevant rare codons
    • Widmann M., et al. Analysis of the distribution of functionally relevant rare codons. BMC Genomics 9 (2008) 207
    • (2008) BMC Genomics , vol.9 , pp. 207
    • Widmann, M.1
  • 72
    • 17344384932 scopus 로고    scopus 로고
    • Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity
    • Sánchez I.E., et al. Fast folding of the two-domain semliki forest virus capsid protein explains co-translational proteolytic activity. J. Mol. Biol. 338 (2004) 159-167
    • (2004) J. Mol. Biol. , vol.338 , pp. 159-167
    • Sánchez, I.E.1
  • 73
    • 33846504706 scopus 로고    scopus 로고
    • A "silent" polymorphism in the MDR1 gene changes substrate specificity
    • Kimchi-Sarfaty C., et al. A "silent" polymorphism in the MDR1 gene changes substrate specificity. Science 315 (2007) 525-528
    • (2007) Science , vol.315 , pp. 525-528
    • Kimchi-Sarfaty, C.1
  • 74
    • 34548726841 scopus 로고    scopus 로고
    • Silent SNPs; impact on gene function and phenotype
    • Komar A.A. Silent SNPs; impact on gene function and phenotype. Pharmacogenomics 8 (2007) 1075-1080
    • (2007) Pharmacogenomics , vol.8 , pp. 1075-1080
    • Komar, A.A.1
  • 75
    • 48249093081 scopus 로고    scopus 로고
    • Heterologous protein expression is enhanced by harmonizing the codon usage frequencies of the target gene with those of the expression host
    • Angov E., et al. Heterologous protein expression is enhanced by harmonizing the codon usage frequencies of the target gene with those of the expression host. PLoS One 3 (2008) e2189
    • (2008) PLoS One , vol.3
    • Angov, E.1
  • 76
    • 53449096191 scopus 로고    scopus 로고
    • Chain dynamics of nascent polypeptides emerging from the ribosome
    • Ellis J.P., et al. Chain dynamics of nascent polypeptides emerging from the ribosome. ACS Chem. Biol. 3 (2008) 555-566
    • (2008) ACS Chem. Biol. , vol.3 , pp. 555-566
    • Ellis, J.P.1
  • 77
    • 36749052255 scopus 로고    scopus 로고
    • Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy
    • Hsu S.T., et al. Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 16516-16521
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 16516-16521
    • Hsu, S.T.1
  • 78
    • 0020479440 scopus 로고
    • The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds
    • Peters T., and Davidson L.K. The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds. J. Biol. Chem. 257 (1982) 8847-8853
    • (1982) J. Biol. Chem. , vol.257 , pp. 8847-8853
    • Peters, T.1    Davidson, L.K.2
  • 79
    • 0342453116 scopus 로고
    • Extension and folding of nascent peptides on ribosomes
    • Nierhaus K.H., et al. (Ed), Plenum Press
    • Hardesty B., et al. Extension and folding of nascent peptides on ribosomes. In: Nierhaus K.H., et al. (Ed). The Translational Apparatus (1993), Plenum Press 347-358
    • (1993) The Translational Apparatus , pp. 347-358
    • Hardesty, B.1
  • 80
    • 0028300803 scopus 로고
    • In vitro and ribosome-bound folding intermediates of P22 tailspike protein detected with monoclonal antibodies
    • Friguet B., et al. In vitro and ribosome-bound folding intermediates of P22 tailspike protein detected with monoclonal antibodies. J. Biol. Chem. 269 (1994) 15945-15949
    • (1994) J. Biol. Chem. , vol.269 , pp. 15945-15949
    • Friguet, B.1
  • 81
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman J., et al. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370 (1994) 111-117
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1
  • 82
    • 0028094779 scopus 로고
    • Folding of firefly luciferase during translation in a cell-free system
    • Kolb V.A., et al. Folding of firefly luciferase during translation in a cell-free system. EMBO J. 13 (1994) 3631-3637
    • (1994) EMBO J. , vol.13 , pp. 3631-3637
    • Kolb, V.A.1
  • 83
    • 31344479583 scopus 로고    scopus 로고
    • Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family
    • Svetlov M.S., et al. Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family. Protein Sci. 15 (2006) 242-247
    • (2006) Protein Sci. , vol.15 , pp. 242-247
    • Svetlov, M.S.1
  • 84
    • 0033607484 scopus 로고    scopus 로고
    • Process of biosynthetic protein folding determines the rapid formation of native structure
    • Fedorov A.N., and Baldwin T.O. Process of biosynthetic protein folding determines the rapid formation of native structure. J. Mol. Biol. 294 (1999) 579-586
    • (1999) J. Mol. Biol. , vol.294 , pp. 579-586
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 85
    • 0029885416 scopus 로고    scopus 로고
    • Co-translational trimerization of the reovirus cell attachment protein
    • Gilmore R., et al. Co-translational trimerization of the reovirus cell attachment protein. EMBO J. 15 (1996) 2651-2658
    • (1996) EMBO J. , vol.15 , pp. 2651-2658
    • Gilmore, R.1
  • 86
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen W., et al. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 6229-6233
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6229-6233
    • Chen, W.1
  • 87
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels R., et al. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell 11 (2003) 79-90
    • (2003) Mol. Cell , vol.11 , pp. 79-90
    • Daniels, R.1
  • 88
    • 17844369997 scopus 로고    scopus 로고
    • A critical step in the folding of influenza virus HA determined with a novel folding assay
    • Maggioni M.C., et al. A critical step in the folding of influenza virus HA determined with a novel folding assay. Nat. Struct. Mol. Biol. 12 (2005) 258-263
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 258-263
    • Maggioni, M.C.1
  • 89
    • 0029080778 scopus 로고
    • Elongation and folding of nascent ricin chains as peptidyl-tRNA on ribosomes: the effect of amino acid deletions on these processes
    • Kudlicki W., et al. Elongation and folding of nascent ricin chains as peptidyl-tRNA on ribosomes: the effect of amino acid deletions on these processes. J. Mol. Biol. 252 (1995) 203-212
    • (1995) J. Mol. Biol. , vol.252 , pp. 203-212
    • Kudlicki, W.1
  • 90
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer W.J., and Hartl F.U. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 388 (1997) 343-349
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 91
    • 0033203533 scopus 로고    scopus 로고
    • Co-translational folding of an alpha-virus capsid protein in the cytosol of living cells
    • Nicola A.V., et al. Co-translational folding of an alpha-virus capsid protein in the cytosol of living cells. Nat. Cell Biol. 1 (1999) 341-345
    • (1999) Nat. Cell Biol. , vol.1 , pp. 341-345
    • Nicola, A.V.1
  • 92
    • 0034283010 scopus 로고    scopus 로고
    • Cotranslational dimerization of the Rel homology domain of NF-κB1 generates p50-p105 heterodimers and is required for effective p50 production
    • Lin L., et al. Cotranslational dimerization of the Rel homology domain of NF-κB1 generates p50-p105 heterodimers and is required for effective p50 production. EMBO J. 19 (2000) 4712-4722
    • (2000) EMBO J. , vol.19 , pp. 4712-4722
    • Lin, L.1
  • 93
    • 0036479226 scopus 로고    scopus 로고
    • Co-translational folding of caspase-activated DNase with Hsp70, Hsp40, and inhibitor of caspase-activated DNase
    • Sakahira H., and Nagata S. Co-translational folding of caspase-activated DNase with Hsp70, Hsp40, and inhibitor of caspase-activated DNase. J. Biol. Chem. 277 (2002) 3364-3370
    • (2002) J. Biol. Chem. , vol.277 , pp. 3364-3370
    • Sakahira, H.1    Nagata, S.2
  • 94
    • 0038725418 scopus 로고    scopus 로고
    • Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage
    • Land A., et al. Folding of HIV-1 envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation-dependent leader peptide cleavage. FASEB J. 17 (2003) 1058-1067
    • (2003) FASEB J. , vol.17 , pp. 1058-1067
    • Land, A.1
  • 95
    • 26944503059 scopus 로고    scopus 로고
    • Folding of CFTR is predominantly cotranslational
    • Kleizen B., et al. Folding of CFTR is predominantly cotranslational. Mol. Cell 20 (2005) 277-287
    • (2005) Mol. Cell , vol.20 , pp. 277-287
    • Kleizen, B.1


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