메뉴 건너뛰기




Volumn 270, Issue 12, 2003, Pages 2543-2556

On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes: Delivered on 20 October 2002 at the 28th FEBS meeting in Istanbul

Author keywords

Elongation arrest; Peptide bond formation; Ribosomes; Translocation; Tunnel gating

Indexed keywords

CARBON; CARBONYL DERIVATIVE; HYDROGEN; NUCLEOTIDE; PEPTIDE; PEPTIDYLTRANSFERASE; PROTEIN; RNA; SOLVENT; TRANSFER RNA;

EID: 0037636310     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03634.x     Document Type: Conference Paper
Times cited : (57)

References (76)
  • 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. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289, 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
    • 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. (2000) The structural basis of ribosome activity in peptide bond synthesis. Science 289, 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
  • 4
    • 0036342198 scopus 로고    scopus 로고
    • The structures of four macrolide antibiotics bound to the large ribosomal subunit
    • Hansen, J.L., Ippolito, J.A., Ban, N., Nissen, P., Moore, P.B. & Steitz, T.A. (2002) The structures of four macrolide antibiotics bound to the large ribosomal subunit. Mol. Cell. 10, 117-128.
    • (2002) Mol. Cell. , vol.10 , pp. 117-128
    • Hansen, J.L.1    Ippolito, J.A.2    Ban, N.3    Nissen, P.4    Moore, P.B.5    Steitz, T.A.6
  • 9
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schluenzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., Yonath, A. & Franceschi, F. (2001) Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413, 814-821.
    • (2001) Nature , vol.413 , pp. 814-821
    • Schluenzen, F.1    Zarivach, R.2    Harms, J.3    Bashan, A.4    Tocilj, A.5    Albrecht, R.6    Yonath, A.7    Franceschi, F.8
  • 11
    • 0023645140 scopus 로고
    • Destabilization of codon-anticodon interaction in the ribosomal exit site
    • Lill, R. & Wintermeyer, W. (1987) Destabilization of codon-anticodon interaction in the ribosomal exit site. J. Mol. Biol. 196, 137-148.
    • (1987) J. Mol. Biol. , vol.196 , pp. 137-148
    • Lill, R.1    Wintermeyer, W.2
  • 13
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed, D. & Noller, H.F. (1989) Intermediate states in the movement of transfer RNA in the ribosome. Nature 342, 142-148.
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 15
    • 0036082654 scopus 로고    scopus 로고
    • The search and its outcome: High-resolution structures of ribosomal particles from mesophilic, thermophilic, and halophilic bacteria at various functional states
    • Yonath, A. (2002) The search and its outcome: high-resolution structures of ribosomal particles from mesophilic, thermophilic, and halophilic bacteria at various functional states. Annu. Rev. Biophys. Biomol. Struct. 31, 257-273.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 257-273
    • Yonath, A.1
  • 17
    • 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. (1998) Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA. Science 280, 286-289.
    • (1998) Science , vol.280 , pp. 286-289
    • Green, R.1    Switzer, C.2    Noller, H.F.3
  • 18
    • 0025811850 scopus 로고
    • Sites of interaction of the CCA end of peptidyl-t-RNA with 23S rRna
    • Moazed, D. & Noller, H.F. (1991) Sites of interaction of the CCA end of peptidyl-t-RNA with 23S rRna. Proc. Natl Acad. Sci. USA 88, 3725-3728.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3725-3728
    • Moazed, D.1    Noller, H.F.2
  • 19
    • 0026639881 scopus 로고
    • Unusual resistance of peptidyl transferase to protein extraction procedures
    • Noller, H.F., Hoffarth, V. & Zimniak, L. (1992) Unusual resistance of peptidyl transferase to protein extraction procedures. Science 256, 1416-1419.
    • (1992) Science , vol.256 , pp. 1416-1419
    • Noller, H.F.1    Hoffarth, V.2    Zimniak, L.3
  • 20
    • 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. (1990) Movement of tRNA but not the nascent peptide during peptide bond formation on ribosomes. Biochemistry 29, 10734-10744.
    • (1990) Biochemistry , vol.29 , pp. 10734-10744
    • Odom, O.W.1    Picking, W.D.2    Hardesty, B.3
  • 21
    • 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. (1995) Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenesis approach. J. Mol. Biol. 249, 1-10.
    • (1995) J. Mol. Biol. , vol.249 , pp. 1-10
    • Porse, B.T.1    Garrett, R.A.2
  • 23
    • 19244385826 scopus 로고
    • Inhibitors of protein biosynthesis
    • Vazquez, D. (1979) Inhibitors of protein biosynthesis. Mol. Biol. Biochem. Biophys. 30, 1-312.
    • (1979) Mol. Biol. Biochem. Biophys. , vol.30 , pp. 1-312
    • Vazquez, D.1
  • 24
    • 0017330920 scopus 로고
    • Identification of binding sites on the E. coli ribosome by affinity labeling
    • Cooperman, B.S. (1977) Identification of binding sites on the E. coli ribosome by affinity labeling. Adv. Exp Med. Biol. 86A, 595-609.
    • (1977) Adv. Exp Med. Biol. , vol.86 A , pp. 595-609
    • Cooperman, B.S.1
  • 27
    • 0001349638 scopus 로고
    • Molecular mechanisms of the ribosomal peptidyl transferase center
    • Nierhaus, K.H., Schulze, H. & Cooperman, B.S. (1980) Molecular mechanisms of the ribosomal peptidyl transferase center. Biochem. Int. 1, 185-192.
    • (1980) Biochem. Int. , vol.1 , pp. 185-192
    • Nierhaus, K.H.1    Schulze, H.2    Cooperman, B.S.3
  • 28
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • Pape, T., Wintermeyer, W. & Rodnina, M. (1999) Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome. EMBO J. 18, 3800-3807.
    • (1999) EMBO J. , vol.18 , pp. 3800-3807
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.3
  • 29
    • 0035942753 scopus 로고    scopus 로고
    • Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide
    • Polacek, N., Gaynor, M., Yassin, A. & Mankin, A.S. (2001) Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide. Nature 411, 498-501.
    • (2001) Nature , vol.411 , pp. 498-501
    • Polacek, N.1    Gaynor, M.2    Yassin, A.3    Mankin, A.S.4
  • 30
    • 0029085929 scopus 로고
    • A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome
    • Samaha, R.R., Green, R. & Noller, H.F. (1995) A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome. Nature 377, 309-314.
    • (1995) Nature , vol.377 , pp. 309-314
    • Samaha, R.R.1    Green, R.2    Noller, H.F.3
  • 31
    • 0032488946 scopus 로고    scopus 로고
    • Molecular movement inside the translational engine
    • Wilson, K.S. & Noller, H.F. (1998) Molecular movement inside the translational engine. Cell 92, 337-349.
    • (1998) Cell , vol.92 , pp. 337-349
    • Wilson, K.S.1    Noller, H.F.2
  • 32
    • 0035847360 scopus 로고    scopus 로고
    • Mechanism of ribosomal peptide bond formation
    • Barta, A., Dorner, S. & Polacek, N. (2001) Mechanism of ribosomal peptide bond formation. Science 291, 203.
    • (2001) Science , vol.291 , pp. 203
    • Barta, A.1    Dorner, S.2    Polacek, N.3
  • 33
    • 0035964256 scopus 로고    scopus 로고
    • A conformational change in the ribosomal peptidyl transferase center upon active/inactive transition
    • Bayfield, M.A., Dahlberg, A.E., Schulmeister, U., Dorner, S. & Barta, A. (2001) A conformational change in the ribosomal peptidyl transferase center upon active/inactive transition. Proc. Natl Acad. Sci. USA 98, 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
  • 34
    • 0037015029 scopus 로고    scopus 로고
    • Evidence against stabilization of the transition state oxyanion by a pKa-perturbed RNA base in the peptidyl transferase center
    • Parnell, K.M., Seila, A.C. & Strobel, S.A. (2002) Evidence against stabilization of the transition state oxyanion by a pKa-perturbed RNA base in the peptidyl transferase center. Proc. Natl Acad. Sci. USA 99, 11658-11663.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11658-11663
    • Parnell, K.M.1    Seila, A.C.2    Strobel, S.A.3
  • 36
    • 0037321497 scopus 로고    scopus 로고
    • After the ribosome structures: How does peptidyl transferase work?
    • Moore, P.B. & Steitz, T.A. (2003) After the ribosome structures: how does peptidyl transferase work? RNA 9, 155-159.
    • (2003) RNA , vol.9 , pp. 155-159
    • Moore, P.B.1    Steitz, T.A.2
  • 37
    • 0036671344 scopus 로고    scopus 로고
    • Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome
    • Katunin, V.I., Muth, G.W., Strobel, S.A., Wintermeyer, W. & Rodnina, M.V. (2002) Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome. Mol. Cell. 10, 339-346.
    • (2002) Mol. Cell. , vol.10 , pp. 339-346
    • Katunin, V.I.1    Muth, G.W.2    Strobel, S.A.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 39
    • 0037428220 scopus 로고    scopus 로고
    • Ringlike structure of the Deinococcus radiodurans genome: A key to radioresistance?
    • Levin-Zaidman, S., Englander, J., Shimoni, E., Sharma, A.K., Minton, K.W. & Minsky, A. (2003) Ringlike structure of the Deinococcus radiodurans genome: a key to radioresistance? Science 299, 254-256.
    • (2003) Science , vol.299 , pp. 254-256
    • Levin-Zaidman, S.1    Englander, J.2    Shimoni, E.3    Sharma, A.K.4    Minton, K.W.5    Minsky, A.6
  • 40
    • 0014430218 scopus 로고
    • The inactivation and reactivation of ribosomal-peptidyl transferase of E. coli
    • Miskin, R., Zamir, A. & Elson, D. (1968) The inactivation and reactivation of ribosomal-peptidyl transferase of E. coli. Biochem. Biophys. Res. Commun. 33, 551-557.
    • (1968) Biochem. Biophys. Res. Commun. , vol.33 , pp. 551-557
    • Miskin, R.1    Zamir, A.2    Elson, D.3
  • 41
    • 0033231562 scopus 로고    scopus 로고
    • Base-pairing between 23S rRNA and tRNA in the ribosomal A site
    • Kim, D.F. & Green, R. (1999) Base-pairing between 23S rRNA and tRNA in the ribosomal A site. Mol. Cell. 4, 859-864.
    • (1999) Mol. Cell. , vol.4 , pp. 859-864
    • Kim, D.F.1    Green, R.2
  • 43
    • 0014027460 scopus 로고
    • Sparsomycin, an inhibitor of aminoacyl transfer to polypeptide
    • Goldberg, I.H. & Mitsugi, K. (1966) Sparsomycin, an inhibitor of aminoacyl transfer to polypeptide. Biochem. Biophys. Res. Commun. 23, 453-459.
    • (1966) Biochem. Biophys. Res. Commun. , vol.23 , pp. 453-459
    • Goldberg, I.H.1    Mitsugi, K.2
  • 44
    • 0033529799 scopus 로고    scopus 로고
    • Direct crosslinking of the antitumor antibiotic sparsomycin, and its derivatives, to A2602 in the peptidyl transferase center of 23S-like rRNA within ribosome-tRNA complexes
    • Porse, B.T., Kirillov, S.V., Awayez, M.J., Ottenheijm, H.C. & Garrett, R.A. (1999) Direct crosslinking of the antitumor antibiotic sparsomycin, and its derivatives, to A2602 in the peptidyl transferase center of 23S-like rRNA within ribosome-tRNA complexes. Proc. Natl Acad. Sci. USA 96, 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
  • 45
    • 0030590258 scopus 로고    scopus 로고
    • Mutations in the peptidyl transferase center of 23 S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation
    • Tan, G.T., DeBlasio, A. & Mankin, A.S. (1996) Mutations in the peptidyl transferase center of 23 S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation. J. Mol. Biol. 261, 222-230.
    • (1996) J. Mol. Biol. , vol.261 , pp. 222-230
    • Tan, G.T.1    DeBlasio, A.2    Mankin, A.S.3
  • 46
    • 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. (1991) Biochemical and kinetic characteristics of the interaction of the antitumor antibiotic sparsomycin with prokaryotic and eukaryotic ribosomes. Biochemistry 30, 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
  • 47
    • 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 rRNA
    • Lazaro, E., Rodriguez-Fonseca, C., Porse, B., Urena, D., Garrett, R.A. & Ballesta, J.P. (1996) A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23S rRNA. J. Mol. Biol. 261, 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
  • 48
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • Agrawal, R.K., Heagle, A.B., Penczek, P., Grassucci, R.A. & Frank, J. (1999) EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nat. Struct. Biol. 6, 643-647.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 50
    • 0032972963 scopus 로고    scopus 로고
    • Reconstitution of functional 50S ribosomes from in vitro transcripts of Bacillus stearothermophilus 23S rRNA
    • Green, R. & Noller, H.F. (1999) Reconstitution of functional 50S ribosomes from in vitro transcripts of Bacillus stearothermophilus 23S rRNA. Biochemistry 38, 1772-1779.
    • (1999) Biochemistry , vol.38 , pp. 1772-1779
    • Green, R.1    Noller, H.F.2
  • 51
    • 0037245660 scopus 로고    scopus 로고
    • The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination
    • Polacek, N., Gomez, M.J., Ito, K., Xiong, L., Nakamura, Y. & Mankin, A. (2003) The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination. Mol. Cell. 11, 103-112.
    • (2003) Mol. Cell. , vol.11 , pp. 103-112
    • Polacek, N.1    Gomez, M.J.2    Ito, K.3    Xiong, L.4    Nakamura, Y.5    Mankin, A.6
  • 52
    • 0021876968 scopus 로고
    • Characterization and crystallization of ribosomal particles from Halobacterium marismortui
    • Shevack, A., Gewitz, H.S., Hennemann, B., Yonath, A. & Wittmann, H.G. (1985) Characterization and crystallization of ribosomal particles from Halobacterium marismortui. FEBS Lett. 184, 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
  • 53
    • 0035252889 scopus 로고    scopus 로고
    • Ribosome fidelity: tRNA discrimination, proofreading and induced fit
    • Rodnina, M.V. & Wintermeyer, W. (2001) Ribosome fidelity: tRNA discrimination, proofreading and induced fit. Trends Biochem. Sci. 26, 124-130.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 124-130
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 54
    • 0034527174 scopus 로고    scopus 로고
    • The end of the beginning: Structural studies of ribosomal proteins
    • Chandra Sanyal, S. & Liljas, A. (2000) The end of the beginning: structural studies of ribosomal proteins. Curr. Opin. Struct. Biol. 10, 633-636.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 633-636
    • Chandra Sanyal, S.1    Liljas, A.2
  • 55
    • 0018716586 scopus 로고
    • Ribosomes in thiostrepton-resistant mutants of Bacillus megaterium lacking a single 50 S subunit protein
    • Cundliffe, E., Dixon, P., Stark, M., Stoffler, G., Ehrlich, R., Stoffler-Meilicke, M. & Cannon, M. (1979) Ribosomes in thiostrepton-resistant mutants of Bacillus megaterium lacking a single 50 S subunit protein. J. Mol. Biol. 132, 235-252.
    • (1979) J. Mol. Biol. , vol.132 , pp. 235-252
    • Cundliffe, E.1    Dixon, P.2    Stark, M.3    Stoffler, G.4    Ehrlich, R.5    Stoffler-Meilicke, M.6    Cannon, M.7
  • 58
    • 0022588613 scopus 로고
    • Location of exit channel for nascent protein in 80S ribosome
    • Milligan R. A. & Unwin P. N. (1986) Location of exit channel for nascent protein in 80S ribosome. Nature 319, 693-695.
    • (1986) Nature , vol.319 , pp. 693-695
    • Milligan, R.A.1    Unwin, P.N.2
  • 59
    • 0023212383 scopus 로고
    • A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction
    • Yonath, A., Leonard, K.R. & Wittmann, H.G. (1987) A tunnel in the large ribosomal subunit revealed by three-dimensional image reconstruction. Science 236, 813-816.
    • (1987) Science , vol.236 , pp. 813-816
    • Yonath, A.1    Leonard, K.R.2    Wittmann, H.G.3
  • 62
    • 0028963496 scopus 로고
    • Erythromycin resistance by ribosome modification
    • Weisblum, B. (1995) Erythromycin resistance by ribosome modification. Antimicrobial Agents Chemother. 39, 577-585.
    • (1995) Antimicrobial Agents Chemother , vol.39 , pp. 577-585
    • Weisblum, B.1
  • 63
    • 0034115717 scopus 로고    scopus 로고
    • Macrolideketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA
    • Douthwaite, S., Hansen, L.H. & Mauvais, P. (2000) Macrolideketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA. Mol. Microbiol. 36, 183-193.
    • (2000) Mol. Microbiol. , vol.36 , pp. 183-193
    • Douthwaite, S.1    Hansen, L.H.2    Mauvais, P.3
  • 64
    • 0027436439 scopus 로고
    • Adverse effects of macrolide antibacterials
    • Periti, P., Mazzei, T., Mini, E. & Novelli, A. (1993) Adverse effects of macrolide antibacterials. Drug Saf. 9, 346-364.
    • (1993) Drug Saf. , vol.9 , pp. 346-364
    • Periti, P.1    Mazzei, T.2    Mini, E.3    Novelli, A.4
  • 66
    • 0032535124 scopus 로고    scopus 로고
    • The crystal structure of ribosomal protein L22 from Thermus thermophilus: Insights into the mechanism of erythromycin resistance
    • Unge, J., berg, A., Al-Kharadaghi, S., Nilculin, A., Nikonov, S., Davydova, N., Nevskaya, N., Garber, M. & Liljas, A. (1998) The crystal structure of ribosomal protein L22 from Thermus thermophilus: insights into the mechanism of erythromycin resistance. Structure 6, 1577-1586.
    • (1998) Structure , vol.6 , pp. 1577-1586
    • Unge, J.1    Berg, A.2    Al-Kharadaghi, S.3    Nilculin, A.4    Nikonov, S.5    Davydova, N.6    Nevskaya, N.7    Garber, M.8    Liljas, A.9
  • 67
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., Lin, J., Do, H. & Johnson, A.E. (1997) Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90, 31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 68
    • 0034459468 scopus 로고    scopus 로고
    • Upstream open reading frames as regulators of mRNA translation
    • Morris, D.R. & Geballe, A.P. (2000) Upstream open reading frames as regulators of mRNA translation. Mol. Cell Biol. 20, 8635-8642.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 8635-8642
    • Morris, D.R.1    Geballe, A.P.2
  • 69
    • 0032784010 scopus 로고    scopus 로고
    • Signal sequence recognition and protein targeting
    • Stroud, R.M. & Walter, P. (1999) Signal sequence recognition and protein targeting. Curr. Opin. Struct. Biol. 9, 754-759.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 754-759
    • Stroud, R.M.1    Walter, P.2
  • 70
    • 0037040406 scopus 로고    scopus 로고
    • Regulatory nascent peptides in the ribosomal tunnel
    • Tenson, T. & Ehrenberg, M. (2002) Regulatory nascent peptides in the ribosomal tunnel. Cell 108, 591-594.
    • (2002) Cell , vol.108 , pp. 591-594
    • Tenson, T.1    Ehrenberg, M.2
  • 71
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P. & Johnson, A.E. (1994) Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 72
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • Nakatogawa, H. & Ito, K. (2002) The ribosomal exit tunnel functions as a discriminating gate. Cell 108, 629-636.
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 73
    • 0033801865 scopus 로고    scopus 로고
    • Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression
    • Sarker, S., Rudd, K.E. & Oliver, D. (2000) Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression. J. Bacteriol. 182, 5592-5595.
    • (2000) J. Bacteriol. , vol.182 , pp. 5592-5595
    • Sarker, S.1    Rudd, K.E.2    Oliver, D.3
  • 74
    • 0037072627 scopus 로고    scopus 로고
    • Instruction of translating ribosome by nascent peptide
    • Gong, F. & Yanofsky, C. (2002) Instruction of translating ribosome by nascent peptide. Science 297, 1864-1867.
    • (2002) Science , vol.297 , pp. 1864-1867
    • Gong, F.1    Yanofsky, C.2
  • 75
    • 0036384268 scopus 로고    scopus 로고
    • L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin
    • Davydova, N., Streltsov, V., Wilce, M., Liljas, A. & Garber, M. (2002) L22 ribosomal protein and effect of its mutation on ribosome resistance to erythromycin. J. Mol. Biol. 322, 635-644.
    • (2002) J. Mol. Biol. , vol.322 , pp. 635-644
    • Davydova, N.1    Streltsov, V.2    Wilce, M.3    Liljas, A.4    Garber, M.5
  • 76


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.