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Volumn 326, Issue 3, 2003, Pages 887-897

Localization of the trigger factor binding site on the ribosomal 50 S subunit

Author keywords

50 S subunit; Neutron scattering; Ribosome; Spin contrast variation; Trigger factor

Indexed keywords

BIOLOGICAL FACTOR; TRIGGER FACTOR; UNCLASSIFIED DRUG;

EID: 0037459119     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01436-5     Document Type: Article
Times cited : (43)

References (57)
  • 1
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, U.1
  • 2
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • Bukau B., Deuerling E., Pfund C., Craig E.A. Getting newly synthesized proteins into shape. Cell. 101:2000;119-122.
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 3
    • 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
  • 4
    • 0023387587 scopus 로고
    • Trigger factor: A soluble protein that folds pro-OmpA into a membrane-assembly-competent form
    • Crooke E., Wickner W. Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form. Proc. Natl Acad. Sci. USA. 84:1987;5216-5220.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5216-5220
    • Crooke, E.1    Wickner, W.2
  • 5
    • 0024022420 scopus 로고
    • ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes
    • Crooke E., Brundage L., Rice M., Wickner W. ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes. EMBO J. 7:1988;1831-1835.
    • (1988) EMBO J. , vol.7 , pp. 1831-1835
    • Crooke, E.1    Brundage, L.2    Rice, M.3    Wickner, W.4
  • 6
    • 0024295389 scopus 로고
    • ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle
    • Crooke E., Guthrie B., Lecker S., Lill R., Wickner W. ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle. Cell. 54:1988;1003-1011.
    • (1988) Cell , vol.54 , pp. 1003-1011
    • Crooke, E.1    Guthrie, B.2    Lecker, S.3    Lill, R.4    Wickner, W.5
  • 7
    • 0025003789 scopus 로고
    • Trigger factor depletion or overproduction causes defective cell division but does not block protein export
    • Guthrie B., Wickner W. Trigger factor depletion or overproduction causes defective cell division but does not block protein export. J. Bacteriol. 172:1990;5555-5562.
    • (1990) J. Bacteriol. , vol.172 , pp. 5555-5562
    • Guthrie, B.1    Wickner, W.2
  • 8
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller G., Rucknagel K.P., Nierhaus K.H., Schmid F.X., Fischer G., Rahfeld J.U. 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
  • 9
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides
    • Valent Q.A., Kendall D.A., High S., Kusters R., Oudega B., Luirink J. Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 14:1995;5494-5505.
    • (1995) EMBO J. , vol.14 , pp. 5494-5505
    • Valent, Q.A.1    Kendall, D.A.2    High, S.3    Kusters, R.4    Oudega, B.5    Luirink, J.6
  • 10
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains
    • Hesterkamp T., Hauser S., Lutcke H., Bukau B. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc. Natl Acad. Sci. USA. 93:1996;4437-4441.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4437-4441
    • Hesterkamp, T.1    Hauser, S.2    Lutcke, H.3    Bukau, B.4
  • 11
    • 0031554922 scopus 로고    scopus 로고
    • Modular structure of the trigger factor required for high activity in protein folding
    • Zarnt T., Tradler T., Stoller G., Scholz C., Schmid F.X., Fischer G. Modular structure of the trigger factor required for high activity in protein folding. J. Mol. Biol. 271:1997;827-837.
    • (1997) J. Mol. Biol. , vol.271 , pp. 827-837
    • Zarnt, T.1    Tradler, T.2    Stoller, G.3    Scholz, C.4    Schmid, F.X.5    Fischer, G.6
  • 12
    • 0028789790 scopus 로고
    • Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family
    • Callebaut I., Mornon J.P. Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family. FEBS Letters. 374:1995;211-215.
    • (1995) FEBS Letters , vol.374 , pp. 211-215
    • Callebaut, I.1    Mornon, J.P.2
  • 13
    • 0029935818 scopus 로고    scopus 로고
    • Identification of the prolyl isomerase domain of Escherichia coli trigger factor
    • Hesterkamp T., Bukau B. Identification of the prolyl isomerase domain of Escherichia coli trigger factor. FEBS Letters. 385:1996;67-71.
    • (1996) FEBS Letters , vol.385 , pp. 67-71
    • Hesterkamp, T.1    Bukau, B.2
  • 14
    • 0029962123 scopus 로고    scopus 로고
    • An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity
    • Stoller G., Tradler T., Rucknagel K.P., Rahfeld J.U., Fischer G. An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity. FEBS Letters. 384:1996;117-122.
    • (1996) FEBS Letters , vol.384 , pp. 117-122
    • Stoller, G.1    Tradler, T.2    Rucknagel, K.P.3    Rahfeld, J.U.4    Fischer, G.5
  • 15
    • 0023766740 scopus 로고
    • The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane
    • Lill R., Crooke E., Guthrie B., Wickner W. The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane. Cell. 54:1988;1013-1018.
    • (1988) Cell , vol.54 , pp. 1013-1018
    • Lill, R.1    Crooke, E.2    Guthrie, B.3    Wickner, W.4
  • 16
    • 0030881913 scopus 로고    scopus 로고
    • The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
    • Hesterkamp T., Deuerling E., Bukau B. The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J. Biol. Chem. 272:1997;21865-21871.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21865-21871
    • Hesterkamp, T.1    Deuerling, E.2    Bukau, B.3
  • 18
    • 0031029046 scopus 로고    scopus 로고
    • Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
    • Scholz C., Stoller G., Zarnt T., Fischer G., Schmid F.X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16:1997;54-58.
    • (1997) EMBO J. , vol.16 , pp. 54-58
    • Scholz, C.1    Stoller, G.2    Zarnt, T.3    Fischer, G.4    Schmid, F.X.5
  • 19
    • 0041172666 scopus 로고    scopus 로고
    • Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions
    • Gothel S.F., Scholz C., Schmid F.X., Marahiel M.A. Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions. Biochemistry. 37:1998;13392-13399.
    • (1998) Biochemistry , vol.37 , pp. 13392-13399
    • Gothel, S.F.1    Scholz, C.2    Schmid, F.X.3    Marahiel, M.A.4
  • 20
    • 0032476656 scopus 로고    scopus 로고
    • A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon W.R., Gibson C.M., Caparon M.G. A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J. 17:1998;6263-6275.
    • (1998) EMBO J. , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 21
    • 0033918740 scopus 로고    scopus 로고
    • Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor
    • Huang G.C., Li Z.Y., Zhou J.M., Fischer G. Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor. Protein Sci. 9:2000;1254-1261.
    • (2000) Protein Sci. , vol.9 , pp. 1254-1261
    • Huang, G.C.1    Li, Z.Y.2    Zhou, J.M.3    Fischer, G.4
  • 22
    • 0035812938 scopus 로고    scopus 로고
    • The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli
    • Li Z.Y., Liu C.P., Zhu L.Q., Jing G.Z., Zhou J.M. The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli. FEBS Letters. 506:2001;108-112.
    • (2001) FEBS Letters , vol.506 , pp. 108-112
    • Li, Z.Y.1    Liu, C.P.2    Zhu, L.Q.3    Jing, G.Z.4    Zhou, J.M.5
  • 23
    • 0028849206 scopus 로고
    • Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins
    • Kandror O., Sherman M., Rhode M., Goldberg A.L. Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J. 14:1995;6021-6027.
    • (1995) EMBO J. , vol.14 , pp. 6021-6027
    • Kandror, O.1    Sherman, M.2    Rhode, M.3    Goldberg, A.L.4
  • 24
    • 0031026329 scopus 로고    scopus 로고
    • Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides
    • Kandror O., Sherman M., Moerschell R., Goldberg A.L. Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides. J. Biol. Chem. 272:1997;1730-1734.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1730-1734
    • Kandror, O.1    Sherman, M.2    Moerschell, R.3    Goldberg, A.L.4
  • 25
    • 0024672180 scopus 로고
    • Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism
    • Bukau B., Walker G.C. Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism. J. Bacteriol. 171:1989;2337-2346.
    • (1989) J. Bacteriol. , vol.171 , pp. 2337-2346
    • Bukau, B.1    Walker, G.C.2
  • 26
    • 0032541496 scopus 로고    scopus 로고
    • Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli
    • Hesterkamp T., Bukau B. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17:1998;4818-4828.
    • (1998) EMBO J. , vol.17 , pp. 4818-4828
    • Hesterkamp, T.1    Bukau, B.2
  • 27
    • 0033549770 scopus 로고    scopus 로고
    • Trigger factor and DnaK cooperate in folding of newly synthesized proteins
    • Deuerling E., Schulze-Specking A., Tomoyasu T., Mogk A., Bukau B. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature. 400:1999;693-696.
    • (1999) Nature , vol.400 , pp. 693-696
    • Deuerling, E.1    Schulze-Specking, A.2    Tomoyasu, T.3    Mogk, A.4    Bukau, B.5
  • 28
    • 0033032592 scopus 로고    scopus 로고
    • Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
    • Teter S.A., Houry W.A., Ang D., Tradler T., Rockabrand D., Fischer G., et al. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell. 97:1999;755-765.
    • (1999) Cell , vol.97 , pp. 755-765
    • Teter, S.A.1    Houry, W.A.2    Ang, D.3    Tradler, T.4    Rockabrand, D.5    Fischer, G.6
  • 29
    • 0004491398 scopus 로고    scopus 로고
    • Prolyl isomerases in a minimal cell. Catalysis of protein folding by trigger factor from Mycoplasma genitalium
    • Bang H., Pecht A., Raddatz G., Scior T., Solbach W., Brune K., Pahl A. Prolyl isomerases in a minimal cell. Catalysis of protein folding by trigger factor from Mycoplasma genitalium. Eur. J. Biochem. 267:2000;3270-3280.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3270-3280
    • Bang, H.1    Pecht, A.2    Raddatz, G.3    Scior, T.4    Solbach, W.5    Brune, K.6    Pahl, A.7
  • 31
    • 0026533909 scopus 로고
    • Inter-protein distances within the large subunit from Escherichia coli ribosomes
    • May R.P., Nowotny V., Nowotny P., Voss H., Nierhaus K.H. Inter-protein distances within the large subunit from Escherichia coli ribosomes. EMBO J. 11:1992;373-378.
    • (1992) EMBO J. , vol.11 , pp. 373-378
    • May, R.P.1    Nowotny, V.2    Nowotny, P.3    Voss, H.4    Nierhaus, K.H.5
  • 33
    • 0000595376 scopus 로고    scopus 로고
    • Localisation of proteins and tRNA molecules in the 70 S ribosome of the E. coli bacteria with polarized neutron scattering
    • Willumeit R., Burkhardt N., Wadzack J., Nierhaus K.H., Stuhrmann H.B. Localisation of proteins and tRNA molecules in the 70 S ribosome of the E. coli bacteria with polarized neutron scattering. J. Appl. Crystallog. 30:1997;1125-1131.
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1125-1131
    • Willumeit, R.1    Burkhardt, N.2    Wadzack, J.3    Nierhaus, K.H.4    Stuhrmann, H.B.5
  • 34
    • 0344404198 scopus 로고    scopus 로고
    • Small angle scattering in ribosomal structure research: Localisation of the messenger RNA within the ribosomal elongation states
    • Jünemann R., Burkhardt N., Wadzack J., Schmitt M., Willumeit R., Stuhrmann H.B., Nierhaus K.H. Small angle scattering in ribosomal structure research: localisation of the messenger RNA within the ribosomal elongation states. Biol. Chem. 379:1998;807-818.
    • (1998) Biol. Chem. , vol.379 , pp. 807-818
    • Jünemann, R.1    Burkhardt, N.2    Wadzack, J.3    Schmitt, M.4    Willumeit, R.5    Stuhrmann, H.B.6    Nierhaus, K.H.7
  • 36
    • 0034640267 scopus 로고    scopus 로고
    • A map of protein-rRNA distribution in the 70 S Escherichia coli ribosome
    • Svergun D.I., Nierhaus K.H. A map of protein-rRNA distribution in the 70 S Escherichia coli ribosome. J. Biol. Chem. 275:2000;14432-14439.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14432-14439
    • Svergun, D.I.1    Nierhaus, K.H.2
  • 37
    • 0026045381 scopus 로고
    • Three dimensional reconstruction of the 70 S Escherichia coli ribosome in ice: The distribution of ribosomal RNA
    • Frank J., Penczek P., Grassucci R., Srivastava S. Three dimensional reconstruction of the 70 S Escherichia coli ribosome in ice: the distribution of ribosomal RNA. J. Cell Biol. 115:1991;597-605.
    • (1991) J. Cell Biol. , vol.115 , pp. 597-605
    • Frank, J.1    Penczek, P.2    Grassucci, R.3    Srivastava, S.4
  • 38
    • 0029402180 scopus 로고
    • A model of the translational apparatus based on a three-dimensional reconstruction of the Escherichia coli ribosome
    • Frank J., Verschoor A., Li Y.H., Zhu J., Lata R.K., Radermacher M., et al. A model of the translational apparatus based on a three-dimensional reconstruction of the Escherichia coli ribosome. Biochem. Cell Biol. 73:1995;757-765.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 757-765
    • Frank, J.1    Verschoor, A.2    Li, Y.H.3    Zhu, J.4    Lata, R.K.5    Radermacher, M.6
  • 39
    • 0037007466 scopus 로고    scopus 로고
    • Formation of 70 S ribosomes: Large activation energy is required for the adaptation of exclusively the small ribosomal subunit
    • Blaha G., Burkhardt N., Nierhaus K.H. Formation of 70 S ribosomes: large activation energy is required for the adaptation of exclusively the small ribosomal subunit. Biophys. Chem. 96:2002;153-161.
    • (2002) Biophys. Chem. , vol.96 , pp. 153-161
    • Blaha, G.1    Burkhardt, N.2    Nierhaus, K.H.3
  • 40
    • 0014202553 scopus 로고
    • Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding
    • Malkin L.I., Rich A. Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding. J. Mol. Biol. 26:1967;329-346.
    • (1967) J. Mol. Biol. , vol.26 , pp. 329-346
    • Malkin, L.I.1    Rich, A.2
  • 41
    • 0014770988 scopus 로고
    • Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes
    • Blobel G., Sabatini D.D. Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes. J. Cell Biol. 45:1970;130-145.
    • (1970) J. Cell Biol. , vol.45 , pp. 130-145
    • Blobel, G.1    Sabatini, D.D.2
  • 42
    • 0343550738 scopus 로고
    • Nascent peptide as sole attachment of polysomes to membranes in bacteria
    • Smith W.P., Tai P.C., Davis B.D. Nascent peptide as sole attachment of polysomes to membranes in bacteria. Proc. Natl Acad. Sci. USA. 75:1978;814-817.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 814-817
    • Smith, W.P.1    Tai, P.C.2    Davis, B.D.3
  • 43
    • 0023053308 scopus 로고
    • Stereochemical analysis of ribosomal transpeptidation. Conformation of nascent peptide
    • Lim V.I., 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
  • 44
    • 0021981137 scopus 로고
    • Stereochemistry of the transpeptidation reaction in the ribosome. The ribosome generates an alpha-helix in the synthesis of the polypeptide chain
    • Lim V.I., Spirin A.S. Stereochemistry of the transpeptidation reaction in the ribosome. The ribosome generates an alpha-helix in the synthesis of the polypeptide chain. Dokl. Akad. Nauk SSSR. 280:1985;235-239.
    • (1985) Dokl. Akad. Nauk SSSR , vol.280 , pp. 235-239
    • Lim, V.I.1    Spirin, A.S.2
  • 45
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289:2000;905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 46
    • 0035977093 scopus 로고    scopus 로고
    • High resolution structure of the large ribosomal subunit from a mesophilic eubacterium
    • Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I., et al. High resolution structure of the large ribosomal subunit from a mesophilic eubacterium. Cell. 107:2001;679-688.
    • (2001) Cell , vol.107 , pp. 679-688
    • Harms, J.1    Schluenzen, F.2    Zarivach, R.3    Bashan, A.4    Gat, S.5    Agmon, I.6
  • 48
    • 0037162838 scopus 로고    scopus 로고
    • Distinct modes of signal recognition particle interaction with the ribosome
    • Pool M.R., Stumm J., Fulga T.A., Sinning I., Dobberstein B. Distinct modes of signal recognition particle interaction with the ribosome. Science. 291:2002;1345-1348.
    • (2002) Science , vol.291 , pp. 1345-1348
    • Pool, M.R.1    Stumm, J.2    Fulga, T.A.3    Sinning, I.4    Dobberstein, B.5
  • 49
    • 0036785913 scopus 로고    scopus 로고
    • Where chaperones and nascent polypeptides meet
    • Albanese V., Frydman J. Where chaperones and nascent polypeptides meet. Nature Struct. Biol. 9:2002;716-718.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 716-718
    • Albanese, V.1    Frydman, J.2
  • 50
    • 0027177825 scopus 로고
    • Large-scale preparation of fully deuterated cell components. Ribosomes from Escherichia coli with high biological activity
    • Vanatalu K., Paalme T., Vilu R., Burkhardt N., Jünemann R., May R., et al. Large-scale preparation of fully deuterated cell components. Ribosomes from Escherichia coli with high biological activity. Eur. J. Biochem. 216:1993;315-321.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 315-321
    • Vanatalu, K.1    Paalme, T.2    Vilu, R.3    Burkhardt, N.4    Jünemann, R.5    May, R.6
  • 51
    • 0024239966 scopus 로고
    • Parameters important for the preparation of E. coli ribosomes and ribosomal subunits highly active in tRNA binding
    • Rheinberger H.-J., Geigenmüller U., Wedde M., Nierhaus K.H. Parameters important for the preparation of E. coli ribosomes and ribosomal subunits highly active in tRNA binding. Methods Enzymol. 164:1988;658-670.
    • (1988) Methods Enzymol. , vol.164 , pp. 658-670
    • Rheinberger, H.-J.1    Geigenmüller, U.2    Wedde, M.3    Nierhaus, K.H.4
  • 54
    • 85031231882 scopus 로고
    • Mechanism of nuclear dynamic polarisation by electron-nucleus dipole coupling in solids
    • G. Shapiro. Springfield, VA: National Technical Information Service
    • Borghini M. Mechanism of nuclear dynamic polarisation by electron-nucleus dipole coupling in solids. Shapiro G. Proceedings of the Second International Conference on Polarized Targets. 1972;National Technical Information Service, Springfield, VA.
    • (1972) Proceedings of the Second International Conference on Polarized Targets
    • Borghini, M.1
  • 55
    • 0024121250 scopus 로고
    • A model for the spatial arrangement of the proteins in the large subunit of the Escherichia coli ribosome
    • Walleczek J., Schuler D., Stöffler-Meilicke M., Brimacombe R., Stöffler G. A model for the spatial arrangement of the proteins in the large subunit of the Escherichia coli ribosome. EMBO J. 7:1988;3571-3576.
    • (1988) EMBO J. , vol.7 , pp. 3571-3576
    • Walleczek, J.1    Schuler, D.2    Stöffler-Meilicke, M.3    Brimacombe, R.4    Stöffler, G.5
  • 56
    • 0029100747 scopus 로고
    • A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome
    • Frank J., Zhu J., Penczek P., Li Y.H., Srivastava S., Verschoor A., et al. A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature. 376:1995;441-444.
    • (1995) Nature , vol.376 , pp. 441-444
    • Frank, J.1    Zhu, J.2    Penczek, P.3    Li, Y.H.4    Srivastava, S.5    Verschoor, A.6


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