메뉴 건너뛰기




Volumn 11, Issue 1, 2003, Pages 91-102

Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDYLTRANSFERASE; PUROMYCIN; RIBOSOME RNA; TRANSFER RNA;

EID: 0037249473     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00009-1     Document Type: Article
Times cited : (246)

References (64)
  • 1
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Bailey S. The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 2
    • 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
  • 3
    • 0035847360 scopus 로고    scopus 로고
    • Mechanism of ribosomal peptide bond formation
    • Barta A., Dorner S., Polacek N. Mechanism of ribosomal peptide bond formation. Science. 291:2001;203.
    • (2001) Science , vol.291 , pp. 203
    • Barta, A.1    Dorner, S.2    Polacek, N.3
  • 4
    • 0035964256 scopus 로고    scopus 로고
    • A conformational change in the ribosomal peptidyltransferase center upon active/inactive transition
    • Bayfield M.A., Dahlberg A.E., Schulmeister U., Dorner S., Barta A. A conformational change in the ribosomal peptidyltransferase center upon active/inactive transition. Proc. Natl. Acad. Sci. USA. 98:2001;10096-10101.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10096-10101
    • Bayfield, M.A.1    Dahlberg, A.E.2    Schulmeister, U.3    Dorner, S.4    Barta, A.5
  • 5
    • 0021094219 scopus 로고
    • Cooperative effects in the peptidyltransferase center of Escherichia coli ribosomes
    • Bourd S.B., Kukhanova M.K., Gottikh B.P., Krayevsky A.A. Cooperative effects in the peptidyltransferase center of Escherichia coli ribosomes. Eur. J. Biochem. 135:1983;465-470.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 465-470
    • Bourd, S.B.1    Kukhanova, M.K.2    Gottikh, B.P.3    Krayevsky, A.A.4
  • 7
    • 0017330920 scopus 로고
    • Identification of binding sites on the E. coli ribosome by affinity labeling, Adv
    • Cooperman B.S. Identification of binding sites on the E. coli ribosome by affinity labeling, Adv. Exp. Med. Biol. 86A:1977;595-609.
    • (1977) Exp. Med. Biol. , vol.86 A , pp. 595-609
    • Cooperman, B.S.1
  • 8
    • 0003792548 scopus 로고
    • E.F. Gale, E. Cundliffe, P.E. Reynolds, M.H. Richmond, and M. H. Waring, eds. (London, NY, Sydney, Toronto: Wiley)
    • Cundliffe, E. (1981). Antibiotic inhibitors of ribosome function, E.F. Gale, E. Cundliffe, P.E. Reynolds, M.H. Richmond, and M. H. Waring, eds. (London, NY, Sydney, Toronto: Wiley).
    • (1981) Antibiotic Inhibitors of Ribosome Function
    • Cundliffe, E.1
  • 9
    • 0002331708 scopus 로고
    • Recognition sites for antibiotics within rRNA
    • W.E. Function and Evolution, A.E. Hill, R.A. Dahlberg, P.B. Garrett, D. Moore, Schlessinger, & J.R. Warner. Washington, DC: ASM. 479-90.pp
    • Cundliffe E. Recognition sites for antibiotics within rRNA. Function and Evolution W.E., Hill A.E., Dahlberg R.A., Garrett P.B., Moore D., Schlessinger, Warner J.R. The Ribosome. Structure:1990;ASM, Washington, DC. 479-90.pp.
    • (1990) The Ribosome: Structure
    • Cundliffe, E.1
  • 10
    • 0017918842 scopus 로고
    • Sequence at the site of attachment of an affinity-label derivative of puromycin on 23S ribosomal RNA of E. coli ribosomes
    • Eckerman D.J., Symons R.H. Sequence at the site of attachment of an affinity-label derivative of puromycin on 23S ribosomal RNA of E. coli ribosomes. Eur. J. Biochem. 82:1978;225-234.
    • (1978) Eur. J. Biochem. , vol.82 , pp. 225-234
    • Eckerman, D.J.1    Symons, R.H.2
  • 11
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank J., Agrawal R.K. A ratchet-like inter-subunit reorganization of the ribosome during translocation. Nature. 406:2000;318-322.
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 13
    • 0002963789 scopus 로고
    • The peptidyltransferase center
    • Processing Evolution, R.A. Function, A.E. Zimmermann and, & Dahlberg. Boca Raton: CRC Press. 327-355.pp
    • Garrett R.A., Rodriguez-Fonseca C. The peptidyltransferase center. Evolution Processing, Function R.A., Zimmermann and A.E., Dahlberg Ribosomal RNA. Structure:1995;CRC Press, Boca Raton. 327-355.pp.
    • (1995) Ribosomal RNA: Structure
    • Garrett, R.A.1    Rodriguez-Fonseca, C.2
  • 14
    • 0014027460 scopus 로고
    • Sparsomycin, an inhibitor of aminoacyl transfer to polypeptide
    • Goldberg I.H., Mitsugi K. Sparsomycin, an inhibitor of aminoacyl transfer to polypeptide. Biochem. Biophys. Res. Commun. 23:1966;453-459.
    • (1966) Biochem. Biophys. Res. Commun. , vol.23 , pp. 453-459
    • Goldberg, I.H.1    Mitsugi, K.2
  • 15
    • 0031566952 scopus 로고    scopus 로고
    • Mutations at nucleotides G2251 and U2585 of 23S rRNA perturb the peptidyltransferase center of the ribosome
    • Green R., Samaha R.R., Noller H.F. Mutations at nucleotides G2251 and U2585 of 23S rRNA perturb the peptidyltransferase center of the ribosome. J. Mol. Biol. 266:1997;40-50.
    • (1997) J. Mol. Biol. , vol.266 , pp. 40-50
    • Green, R.1    Samaha, R.R.2    Noller, H.F.3
  • 16
    • 0032502997 scopus 로고    scopus 로고
    • Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA
    • Green R., Switzer C., Noller H.F. Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA. Science. 280:1998;286-289.
    • (1998) Science , vol.280 , pp. 286-289
    • Green, R.1    Switzer, C.2    Noller, H.F.3
  • 17
    • 0027225783 scopus 로고
    • A compilation of large subunit (23S and 23S-like) ribosomal RNA structures: 1993
    • Gutell R.R., Gray M.W., Schnare M.N. A compilation of large subunit (23S and 23S-like) ribosomal RNA structures. 1993 Nucleic Acids Res. 21:1993;3055-3074.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3055-3074
    • Gutell, R.R.1    Gray, M.W.2    Schnare, M.N.3
  • 18
    • 0023821349 scopus 로고
    • [3H]-p-azidopuromycin photoaffinity labeling of E. coli ribosomes: Evidence for site-specific interaction at U-2504 and G-2502 in domain V of 23S ribosomal RNA
    • Hall C.C., Johnson D., Cooperman B.S. -p-azidopuromycin photoaffinity labeling of E. coli ribosomes. evidence for site-specific interaction at U-2504 and G-2502 in domain V of 23S ribosomal RNA Biochemistry. 27:1988;3983-3990. [3H].
    • (1988) Biochemistry , vol.27 , pp. 3983-3990
    • Hall, C.C.1    Johnson, D.2    Cooperman, B.S.3
  • 21
    • 0023579725 scopus 로고
    • Decoding at the ribosomal A site: Antibiotics, misreading and energy of aminoacyl-tRNA binding
    • Hornig H., Woolley P., Luhrmann R. Decoding at the ribosomal A site. antibiotics, misreading and energy of aminoacyl-tRNA binding Biochimie. 69:1987;803-813.
    • (1987) Biochimie , vol.69 , pp. 803-813
    • Hornig, H.1    Woolley, P.2    Luhrmann, R.3
  • 22
    • 0023139432 scopus 로고
    • 23S ribosomal RNA mutations in halobacteria conferring resistance to the anti-80S ribosome targeted antibiotic anisomycin
    • Hummel H., Bock A. 23S ribosomal RNA mutations in halobacteria conferring resistance to the anti-80S ribosome targeted antibiotic anisomycin. Nucleic Acids Res. 15:1987;2431-2443.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 2431-2443
    • Hummel, H.1    Bock, A.2
  • 23
    • 0033231562 scopus 로고    scopus 로고
    • Base-pairing between 23S rRNA and tRNA in the ribosomal A site
    • Kim D.F., Green R. Base-pairing between 23S rRNA and tRNA in the ribosomal A site. Mol. Cell. 4:1999;859-864.
    • (1999) Mol. Cell , vol.4 , pp. 859-864
    • Kim, D.F.1    Green, R.2
  • 24
    • 0030904329 scopus 로고    scopus 로고
    • Movement of the 3′-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics
    • Kirillov S., Porse B.T., Vester B., Woolley P., Garrett R.A. Movement of the 3′-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics. FEBS Lett. 406:1997;223-233.
    • (1997) FEBS Lett. , vol.406 , pp. 223-233
    • Kirillov, S.1    Porse, B.T.2    Vester, B.3    Woolley, P.4    Garrett, R.A.5
  • 25
    • 0032818296 scopus 로고    scopus 로고
    • Peptidyltransferase antibiotics perturb the relative positioning of the 3′-terminal adenosine of P/P'-site-bound tRNA and 23S rRNA in the ribosome
    • Kirillov S.V., Porse B.T., Garrett R.A. Peptidyltransferase antibiotics perturb the relative positioning of the 3′-terminal adenosine of P/P'-site-bound tRNA and 23S rRNA in the ribosome. RNA. 5:1999;1003-1013.
    • (1999) RNA , vol.5 , pp. 1003-1013
    • Kirillov, S.V.1    Porse, B.T.2    Garrett, R.A.3
  • 26
    • 0026008858 scopus 로고
    • Biochemical and kinetic characteristics of the interaction of the antitumor antibiotic sparsomycin with prokaryotic and eukaryotic ribosomes
    • Lazaro E., van den Broek L.A., San Felix A., Ottenheijm H.C., Ballesta J.P. Biochemical and kinetic characteristics of the interaction of the antitumor antibiotic sparsomycin with prokaryotic and eukaryotic ribosomes. Biochemistry. 30:1991;9642-9648.
    • (1991) Biochemistry , vol.30 , pp. 9642-9648
    • Lazaro, E.1    Van den Broek, L.A.2    San Felix, A.3    Ottenheijm, H.C.4    Ballesta, J.P.5
  • 27
    • 0030590237 scopus 로고    scopus 로고
    • A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23S RNA
    • Lazaro E., Rodriguez-Fonseca C., Porse B., Urena D., Garrett R.A., Ballesta J.P. A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23S RNA. J. Mol. Biol. 261:1996;231-238.
    • (1996) J. Mol. Biol. , vol.261 , pp. 231-238
    • Lazaro, E.1    Rodriguez-Fonseca, C.2    Porse, B.3    Urena, D.4    Garrett, R.A.5    Ballesta, J.P.6
  • 28
    • 0023645140 scopus 로고
    • Destabilization of codon-anticodon interaction in the ribosomal exit site
    • Lill R., Wintermeyer W. Destabilization of codon-anticodon interaction in the ribosomal exit site. J. Mol. Biol. 196:1987;137-148.
    • (1987) J. Mol. Biol. , vol.196 , pp. 137-148
    • Lill, R.1    Wintermeyer, W.2
  • 29
    • 0025892855 scopus 로고
    • Chloramphenicol resistance mutations in the single 23S rRNA gene of the archaeon H. halobium
    • Mankin A.S., Garrett R.A. Chloramphenicol resistance mutations in the single 23S rRNA gene of the archaeon H. halobium. J. Bacteriol. 173:1991;3559-3563.
    • (1991) J. Bacteriol. , vol.173 , pp. 3559-3563
    • Mankin, A.S.1    Garrett, R.A.2
  • 30
    • 0014430218 scopus 로고
    • The inactivation and reactivation of ribosomal-peptidyltransferase of E. coli
    • Miskin R., Zamir A., Elson D. The inactivation and reactivation of ribosomal-peptidyltransferase of E. coli. Biochem. Biophys. Res. Commun. 33:1968;551-557.
    • (1968) Biochem. Biophys. Res. Commun. , vol.33 , pp. 551-557
    • Miskin, R.1    Zamir, A.2    Elson, D.3
  • 31
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed D., Noller H.F. Intermediate states in the movement of transfer RNA in the ribosome. Nature. 342:1989;142-148.
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 32
    • 0025811850 scopus 로고
    • Sites of interaction of the CCAa end of peptidyl-transfer RNA with 23S ribosomal-RNA
    • Moazed D., Noller H.F. Sites of interaction of the CCAa end of peptidyl-transfer RNA with 23S ribosomal-RNA. Proc. Natl. Acad. Sci. USA. 88:1991;3725-3728.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3725-3728
    • Moazed, D.1    Noller, H.F.2
  • 33
    • 0014360492 scopus 로고
    • Ribosome-catalyzed peptidyl transfer: Substrate specificity at the P-site
    • Monro R.E., Cerna J., Marcker K.A. Ribosome-catalyzed peptidyl transfer. substrate specificity at the P-site Proc. Natl. Acad. Sci. USA. 61:1968;1042-1049.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 1042-1049
    • Monro, R.E.1    Cerna, J.2    Marcker, K.A.3
  • 34
    • 0014691601 scopus 로고
    • Action of sparsomycin on ribosome-catalysed peptidyl transfer
    • Monro R.E., Celma M.L., Vazquez D. Action of sparsomycin on ribosome-catalysed peptidyl transfer. Nature. 222:1969;356-358.
    • (1969) Nature , vol.222 , pp. 356-358
    • Monro, R.E.1    Celma, M.L.2    Vazquez, D.3
  • 35
    • 0001349638 scopus 로고
    • Molecular mechanisms of the ribosomal peptidyl transferase center
    • Nierhaus K.H., Schulze H., Cooperman B.S. Molecular mechanisms of the ribosomal peptidyl transferase center. Biochem. Int. 1:1980;185-192.
    • (1980) Biochem. Int. , vol.1 , pp. 185-192
    • Nierhaus, K.H.1    Schulze, H.2    Cooperman, B.S.3
  • 36
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A. The structural basis of ribosome activity in peptide bond synthesis. Science. 289:2000;920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 37
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyltransferase to protein extraction procedures
    • Noller H.F., Hoffarth V., Zimniak L. Unusual resistance of peptidyltransferase to protein extraction procedures. Science. 256:1992;1416-1419.
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 39
    • 0025679294 scopus 로고
    • Movement of tRNA but not the nascent peptide during peptide bond formation on ribosomes
    • Odom O.W., Picking W.D., Hardesty B. Movement of tRNA but not the nascent peptide during peptide bond formation on ribosomes. Biochemistry. 29:1990;10734-10744.
    • (1990) Biochemistry , vol.29 , pp. 10734-10744
    • Odom, O.W.1    Picking, W.D.2    Hardesty, B.3
  • 40
    • 0031581856 scopus 로고    scopus 로고
    • Mapping to nucleotide resolution of pseudouridine residues in large subunit ribosomal RNAs from representative eukaryotes, prokaryotes, archaebacteria, mitochondria, and chloroplasts
    • Ofengand J., Bakin A. Mapping to nucleotide resolution of pseudouridine residues in large subunit ribosomal RNAs from representative eukaryotes, prokaryotes, archaebacteria, mitochondria, and chloroplasts. J. Mol Biol. 266:1997;246-268.
    • (1997) J. Mol Biol. , vol.266 , pp. 246-268
    • Ofengand, J.1    Bakin, A.2
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallogr. Pt A. 276:1997;307-326.
    • (1997) Macromolecular Crystallogr. Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • Pape T., Wintermeyer W., Rodnina M. Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome. EMBO J. 18:1999;3800-3807.
    • (1999) EMBO J. , vol.18 , pp. 3800-3807
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.3
  • 43
    • 0003291306 scopus 로고
    • Inhibitors of protein synthesis
    • H. Weissbach, & S. Pestka. New York: Academic Press. 467-553.pp
    • Pestka S. Inhibitors of protein synthesis. Weissbach H., Pestka S. Molecular Mechanisms of Protein Biosynthesis. 1977;Academic Press, New York. 467-553.pp.
    • (1977) Molecular Mechanisms of Protein Biosynthesis
    • Pestka, S.1
  • 44
    • 0035942753 scopus 로고    scopus 로고
    • Ribosomal peptidyltransferase can withstand mutations at the putative catalytic nucleotide
    • Polacek N., Gaynor M., Yassin A., Mankin A.S. Ribosomal peptidyltransferase can withstand mutations at the putative catalytic nucleotide. Nature. 411:2001;498-501.
    • (2001) Nature , vol.411 , pp. 498-501
    • Polacek, N.1    Gaynor, M.2    Yassin, A.3    Mankin, A.S.4
  • 45
    • 0029011424 scopus 로고
    • Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenesis approach
    • Porse B.T., Garrett R.A. Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenesis approach. J. Mol. Biol. 249:1995;1-10.
    • (1995) J. Mol. Biol. , vol.249 , pp. 1-10
    • Porse, B.T.1    Garrett, R.A.2
  • 46
    • 0033529799 scopus 로고    scopus 로고
    • Direct crosslinking of the antitumor antibiotic sparsomycin, and its derivatives, to A2602 in the peptidyltransferase center of 23S-like rRNA within ribosome-tRNA complexes
    • Porse B.T., Kirillov S.V., Awayez M.J., Ottenheijm H.C., Garrett R.A. Direct crosslinking of the antitumor antibiotic sparsomycin, and its derivatives, to A2602 in the peptidyltransferase center of 23S-like rRNA within ribosome-tRNA complexes. Proc. Natl. Acad. Sci. USA. 96:1999;9003-9008.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9003-9008
    • Porse, B.T.1    Kirillov, S.V.2    Awayez, M.J.3    Ottenheijm, H.C.4    Garrett, R.A.5
  • 48
    • 0028924641 scopus 로고
    • Fine structure of the peptidyl transferase centre on 23S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes
    • Rodriguez-Fonseca C., Amils R., Garrett R.A. Fine structure of the peptidyl transferase centre on 23S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes. J. Mol. Biol. 247:1995;224-235.
    • (1995) J. Mol. Biol. , vol.247 , pp. 224-235
    • Rodriguez-Fonseca, C.1    Amils, R.2    Garrett, R.A.3
  • 50
    • 0029085929 scopus 로고
    • A base pair between tRNA and 23S rRNA in the peptidyltransferase centre of the ribosome
    • Samaha R.R., Green R., Noller H.F. A base pair between tRNA and 23S rRNA in the peptidyltransferase centre of the ribosome. Nature. 377:1995;309-314.
    • (1995) Nature , vol.377 , pp. 309-314
    • Samaha, R.R.1    Green, R.2    Noller, H.F.3
  • 53
    • 0021876968 scopus 로고
    • Characterization and crystallization of ribosomal particles from Halobacterium marismortui
    • Shevack A., Gewitz H.S., Hennemann B., Yonath A., Wittmann H.G. Characterization and crystallization of ribosomal particles from Halobacterium marismortui. FEBS Lett. 184:1985;68-71.
    • (1985) FEBS Lett. , vol.184 , pp. 68-71
    • Shevack, A.1    Gewitz, H.S.2    Hennemann, B.3    Yonath, A.4    Wittmann, H.G.5
  • 54
    • 0001457849 scopus 로고
    • Action of puromycin in polyadenylic acid-directed polylysine synthesis
    • Smith J.D., Traut R.R., Blackburn G.M., Monro R.E. Action of puromycin in polyadenylic acid-directed polylysine synthesis. J. Mol. Biol. 13:1965;617-628.
    • (1965) J. Mol. Biol. , vol.13 , pp. 617-628
    • Smith, J.D.1    Traut, R.R.2    Blackburn, G.M.3    Monro, R.E.4
  • 56
    • 0030590258 scopus 로고    scopus 로고
    • Mutations in the peptidyltransferase center of 23S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation
    • Tan G.T., DeBlasio A., Mankin A.S. Mutations in the peptidyltransferase center of 23S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation. J. Mol. Biol. 261:1996;222-230.
    • (1996) J. Mol. Biol. , vol.261 , pp. 222-230
    • Tan, G.T.1    DeBlasio, A.2    Mankin, A.S.3
  • 57
    • 0026693196 scopus 로고
    • Mechanism of action of sparsomycin in protein synthesis
    • Theocharis D.A., Coutsogeorgopoulos C. Mechanism of action of sparsomycin in protein synthesis. Biochemistry. 31:1992;5861-5868.
    • (1992) Biochemistry , vol.31 , pp. 5861-5868
    • Theocharis, D.A.1    Coutsogeorgopoulos, C.2
  • 59
    • 0002445013 scopus 로고
    • The puromycin reaction and its relationship to protein synthesis
    • Traut R.R., Monro R.E. The puromycin reaction and its relationship to protein synthesis. J. Mol. Biol. 10:1964;63-72.
    • (1964) J. Mol. Biol. , vol.10 , pp. 63-72
    • Traut, R.R.1    Monro, R.E.2
  • 60
    • 19244385826 scopus 로고
    • Inhibitors of protein biosynthesis
    • Vazquez D. Inhibitors of protein biosynthesis. Mol. Biol. Biochem. Biophys. 30:1979;1-312.
    • (1979) Mol. Biol. Biochem. Biophys. , vol.30 , pp. 1-312
    • Vazquez, D.1
  • 61
    • 0024114860 scopus 로고
    • The importance of highly conserved nucleotides in the binding region of chloramphenicol at the peptidyltransfer center of E. coli 23S ribosomal RNA
    • Vester B., Garrett R.A. The importance of highly conserved nucleotides in the binding region of chloramphenicol at the peptidyltransfer center of E. coli 23S ribosomal RNA. EMBO J. 7:1988;3577-3588.
    • (1988) EMBO J. , vol.7 , pp. 3577-3588
    • Vester, B.1    Garrett, R.A.2
  • 62
    • 0032498266 scopus 로고    scopus 로고
    • Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing
    • Wilson K.S., Noller H.F. Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing. Cell. 92:1998;131-139.
    • (1998) Cell , vol.92 , pp. 131-139
    • Wilson, K.S.1    Noller, H.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.