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Volumn 9, Issue 1, 1999, Pages 111-114

Co-translational folding

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PEPTIDE; RIBOSOME PROTEIN; RIBOSOME RNA;

EID: 0032825283     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80014-1     Document Type: Article
Times cited : (60)

References (26)
  • 1
    • 0031468437 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • Fedorov AN, Baldwin TO 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
  • 2
    • 0028849478 scopus 로고
    • Folding of an enzyme into an active conformation while bound as peptidyl-tRNA to the ribosome
    • Kudlicki W, Chirgwin JM, Kramer G, Hardesty B 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    Chirgwin, J.M.2    Kramer, G.3    Hardesty, B.4
  • 3
    • 0030025303 scopus 로고    scopus 로고
    • Enzymatic activity of the ribosome-bound nascent polypeptide
    • Makeyev EV, Kolb VA, Spirin AS Enzymatic activity of the ribosome-bound nascent polypeptide. FEBS Lett. 376:1996;166-170.
    • (1996) FEBS Lett , vol.376 , pp. 166-170
    • Makeyev, E.V.1    Kolb, V.A.2    Spirin, A.S.3
  • 5
    • 0032525163 scopus 로고    scopus 로고
    • Different conformations of nascent peptides on ribosomes
    • •], demonstrates that nascent peptides are folded in or on the ribosome.
    • •], demonstrates that nascent peptides are folded in or on the ribosome.
    • (1998) J Mol Biol , vol.278 , pp. 713-723
    • Tsalkova, T.1    Odom, O.W.2    Kramer, G.3    Hardesty, B.4
  • 6
    • 0027322659 scopus 로고
    • GroEL and GroES increase the specific enzymatic activity of newly synthesized rhodanese if present during in vitro transcription/translation
    • Tsalkova T, Zardeneta G, Kudlicki W, Kramer G, Horowitz P, Hardesty B GroEL and GroES increase the specific enzymatic activity of newly synthesized rhodanese if present during in vitro transcription/translation. Biochemistry. 32:1993;3377-3380.
    • (1993) Biochemistry , vol.32 , pp. 3377-3380
    • Tsalkova, T.1    Zardeneta, G.2    Kudlicki, W.3    Kramer, G.4    Horowitz, P.5    Hardesty, B.6
  • 7
    • 0028346454 scopus 로고
    • Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNA
    • Kudlicki W, Odom OW, Kramer G, Hardesty B Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNA. J Biol Chem. 269:1994;16549-16553.
    • (1994) J Biol Chem , vol.269 , pp. 16549-16553
    • Kudlicki, W.1    Odom, O.W.2    Kramer, G.3    Hardesty, B.4
  • 8
    • 0027988581 scopus 로고
    • Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese: Analysis by fluorescence
    • Kudlicki W, Odom OW, Kramer G, Hardesty B Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese: analysis by fluorescence. J Mol Biol. 244:1994;319-331.
    • (1994) J Mol Biol , vol.244 , pp. 319-331
    • Kudlicki, W.1    Odom, O.W.2    Kramer, G.3    Hardesty, B.4
  • 10
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • Eggers DK, Welch WJ, Hansen WJ Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol Biol Cell. 8:1997;1159-1173.
    • (1997) Mol Biol Cell , vol.8 , pp. 1159-1173
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 11
    • 0031895718 scopus 로고    scopus 로고
    • Preparation and application of chaperone-deficient Escherichia coli cell-free translation systems
    • Kramer G, Zhang T, Kudlicki W, Hardesty B Preparation and application of chaperone-deficient Escherichia coli cell-free translation systems. Methods Enzymol. 290:1998;18-26.
    • (1998) Methods Enzymol , vol.290 , pp. 18-26
    • Kramer, G.1    Zhang, T.2    Kudlicki, W.3    Hardesty, B.4
  • 12
    • 0030903131 scopus 로고    scopus 로고
    • Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
    • Vickery LE, Silberg JJ, Dennis TT Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli. Protein Sci. 6:1997;1047-1056.
    • (1997) Protein Sci , vol.6 , pp. 1047-1056
    • Vickery, L.E.1    Silberg, J.J.2    Dennis, T.T.3
  • 13
    • 0029863755 scopus 로고    scopus 로고
    • GroEL binds to and unfolds rhodanese posttranslationally
    • Reid BG, Flynn GC GroEL binds to and unfolds rhodanese posttranslationally. J Biol Chem. 271:1996;7212-7217.
    • (1996) J Biol Chem , vol.271 , pp. 7212-7217
    • Reid, B.G.1    Flynn, G.C.2
  • 14
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton WA, Horwich AL GroEL-mediated protein folding. Protein Sci. 6:1997;743-760.
    • (1997) Protein Sci , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 15
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of chaperonin proteins in protein folding in vivo
    • Lorimer GH A quantitative assessment of the role of chaperonin proteins in protein folding in vivo. FASEB J. 10:1996;5-9.
    • (1996) FASEB J , vol.10 , pp. 5-9
    • Lorimer, G.H.1
  • 16
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt K, Hendrick JP, Houry WA, Hartl FU In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 90:1997;491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 17
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer WJ, Hartl FU 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
  • 18
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller G, Rucknagel KP, Nierhaus KH, Schmid FX, Fischer G, Rahfeld JU A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J. 14:1995;4939-4948.
    • (1995) EMBO J , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rucknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.U.6
  • 21
    • 0030048409 scopus 로고    scopus 로고
    • In vitro protein folding by ribosomes from Escherichia coli, wheat germ and rat liver. The role of the 50S particle and its 23S rRNA
    • Das B, Chattopadhhyay S, Bera AK, Dasgupta C In vitro protein folding by ribosomes from Escherichia coli, wheat germ and rat liver. The role of the 50S particle and its 23S rRNA. Eur J Biochem. 235:1996;613-621.
    • (1996) Eur J Biochem , vol.235 , pp. 613-621
    • Das, B.1    Chattopadhhyay, S.2    Bera, A.K.3    Dasgupta, C.4
  • 24
    • 0032519376 scopus 로고    scopus 로고
    • The path of the growing peptide chain through the 23 S rRNA in the 50S ribosomal subunit; A comparative cross-linking study with three different peptide families
    • This paper describes the progression of the nascent peptide through the ribosome.
    • Choi KM, Brimacombe R The path of the growing peptide chain through the 23 S rRNA in the 50S ribosomal subunit; a comparative cross-linking study with three different peptide families. Nucleic Acids Res. 26:1998;887-895. This paper describes the progression of the nascent peptide through the ribosome.
    • (1998) Nucleic Acids Res , vol.26 , pp. 887-895
    • Choi, K.M.1    Brimacombe, R.2
  • 25
    • 0025820393 scopus 로고
    • Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese
    • Mendoza J, Rogers E, Lorimer G, Horowitz PM Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J Biol Chem. 266:1991;13044-13049.
    • (1991) J Biol Chem , vol.266 , pp. 13044-13049
    • Mendoza, J.1    Rogers, E.2    Lorimer, G.3    Horowitz, P.M.4
  • 26
    • 0031590293 scopus 로고    scopus 로고
    • Do molecular chaperones have to be proteins?
    • Ellis RJ Do molecular chaperones have to be proteins? Biochem Biophys Res Commun. 238:1997;687-692.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 687-692
    • Ellis, R.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.