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Volumn 25, Issue 4, 2007, Pages 505-517

Identification of Two Distinct Hybrid State Intermediates on the Ribosome

Author keywords

RNA

Indexed keywords

TRANSFER RNA;

EID: 33847051154     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.01.022     Document Type: Article
Times cited : (226)

References (65)
  • 1
    • 0033605751 scopus 로고    scopus 로고
    • Effect of buffer conditions on the position of tRNA on the 70S ribosome as visualized by cryoelectron microscopy
    • Agrawal R.K., Penczek P., Grassucci R.A., Burkhardt N., Nierhaus K.H., and Frank J. Effect of buffer conditions on the position of tRNA on the 70S ribosome as visualized by cryoelectron microscopy. J. Biol. Chem. 274 (1999) 8723-8729
    • (1999) J. Biol. Chem. , vol.274 , pp. 8723-8729
    • Agrawal, R.K.1    Penczek, P.2    Grassucci, R.A.3    Burkhardt, N.4    Nierhaus, K.H.5    Frank, J.6
  • 2
    • 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., and Frank J. EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nat. Struct. Biol. 6 (1999) 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
  • 3
    • 0016355478 scopus 로고
    • A new look at statistical model identification
    • Akaike H. A new look at statistical model identification. IEEE Trans. Auto. Cont. 19 (1974) 716-723
    • (1974) IEEE Trans. Auto. Cont. , vol.19 , pp. 716-723
    • Akaike, H.1
  • 4
    • 0037007466 scopus 로고    scopus 로고
    • Formation of 70S ribosomes: large activation energy is required for the adaptation of exclusively the small ribosomal subunit
    • Blaha G., Burkhardt N., and Nierhaus K. Formation of 70S 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.3
  • 8
    • 0014422075 scopus 로고
    • Translocation in protein synthesis: a hybrid structure model
    • Bretscher M.S. Translocation in protein synthesis: a hybrid structure model. Nature 218 (1968) 675-677
    • (1968) Nature , vol.218 , pp. 675-677
    • Bretscher, M.S.1
  • 11
    • 33644798018 scopus 로고    scopus 로고
    • The hybrid state of tRNA binding is an authentic translation elongation intermediate
    • Dorner S., Brunelle J.L., Sharma D., and Green R. The hybrid state of tRNA binding is an authentic translation elongation intermediate. Nat. Struct. Mol. Biol. 13 (2006) 234-241
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 234-241
    • Dorner, S.1    Brunelle, J.L.2    Sharma, D.3    Green, R.4
  • 12
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank J., and 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
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H., Sligar S.G., and Wolynes P.G. The energy landscapes and motions of proteins. Science 254 (1991) 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 14
    • 0033571249 scopus 로고    scopus 로고
    • Major rearrangements in the 70S ribosomal 3D structure caused by a conformational switch in 16S ribosomal RNA
    • Gabashvili I.S., Agrawal R.K., Grassucci R., Squires C.L., Dahlberg A.E., and Frank J. Major rearrangements in the 70S ribosomal 3D structure caused by a conformational switch in 16S ribosomal RNA. EMBO J. 18 (1999) 6501-6507
    • (1999) EMBO J. , vol.18 , pp. 6501-6507
    • Gabashvili, I.S.1    Agrawal, R.K.2    Grassucci, R.3    Squires, C.L.4    Dahlberg, A.E.5    Frank, J.6
  • 15
    • 0037633360 scopus 로고    scopus 로고
    • Gene replacement without selection: regulated suppression of amber mutations in Escherichia coli
    • Herring C.D., Glasner J.D., and Blattner F.R. Gene replacement without selection: regulated suppression of amber mutations in Escherichia coli. Gene 331 (2003) 153-163
    • (2003) Gene , vol.331 , pp. 153-163
    • Herring, C.D.1    Glasner, J.D.2    Blattner, F.R.3
  • 16
    • 0037159243 scopus 로고    scopus 로고
    • Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the Ribosome
    • Katunin V.I., Savelsbergh A., Rodnina M.V., and Wintermeyer W. Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the Ribosome. Biochemistry 41 (2002) 12806-12812
    • (2002) Biochemistry , vol.41 , pp. 12806-12812
    • Katunin, V.I.1    Savelsbergh, A.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 17
    • 0033231562 scopus 로고    scopus 로고
    • Base-pairing between 23S rRNA and tRNA in the ribosomal A site
    • Kim D.F., and 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
  • 18
    • 33845958586 scopus 로고    scopus 로고
    • The A site finger in 23S rRNA acts as a functional attenuator for translocation
    • Komoda T., Sato N.S., Phelps S.S., Namba N., Joseph S., and Suzuki T. The A site finger in 23S rRNA acts as a functional attenuator for translocation. J. Biol. Chem. 281 (2006) 32303-32309
    • (2006) J. Biol. Chem. , vol.281 , pp. 32303-32309
    • Komoda, T.1    Sato, N.S.2    Phelps, S.S.3    Namba, N.4    Joseph, S.5    Suzuki, T.6
  • 19
    • 0015372559 scopus 로고
    • Natural-abundance carbon-13 Fourier-transform nuclear magnetic resonance spectra and spin lattice relaxation times of unfractionated yeast transfer-RNA
    • Komoroski R.A., and Allerhand A. Natural-abundance carbon-13 Fourier-transform nuclear magnetic resonance spectra and spin lattice relaxation times of unfractionated yeast transfer-RNA. Proc. Natl. Acad. Sci. USA 69 (1972) 1804-1808
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1804-1808
    • Komoroski, R.A.1    Allerhand, A.2
  • 20
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev A., Trakhanov S., Laurberg M., and Noller H.F. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell 126 (2006) 1065-1077
    • (2006) Cell , vol.126 , pp. 1065-1077
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noller, H.F.4
  • 21
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • McKinney S.A., Joo C., and Ha T. Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys. J. 91 (2006) 1941-1951
    • (2006) Biophys. J. , vol.91 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 22
    • 33746831687 scopus 로고    scopus 로고
    • Maximum likelihood estimation of molecular motor kinetics from staircase dwell-time sequences
    • Milescu L.S., Yildiz A., Selvin P.R., and Sachs F. Maximum likelihood estimation of molecular motor kinetics from staircase dwell-time sequences. Biophys. J. 91 (2006) 1156-1168
    • (2006) Biophys. J. , vol.91 , pp. 1156-1168
    • Milescu, L.S.1    Yildiz, A.2    Selvin, P.R.3    Sachs, F.4
  • 23
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed D., and 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
  • 24
    • 0043268903 scopus 로고    scopus 로고
    • The structural basis of large ribosomal subunit function
    • Moore P.B., and Steitz T.A. The structural basis of large ribosomal subunit function. Annu. Rev. Biochem. 72 (2003) 813-850
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 813-850
    • Moore, P.B.1    Steitz, T.A.2
  • 25
    • 0034757629 scopus 로고    scopus 로고
    • PH-dependent conformational flexibility within the ribosomal peptidyl transferase center
    • Muth G.W., Chen L., Kosek A.B., and Strobel S.A. PH-dependent conformational flexibility within the ribosomal peptidyl transferase center. RNA 7 (2001) 1403-1415
    • (2001) RNA , vol.7 , pp. 1403-1415
    • Muth, G.W.1    Chen, L.2    Kosek, A.B.3    Strobel, S.A.4
  • 26
    • 33646557329 scopus 로고    scopus 로고
    • A mechanical explanation of RNA pseudoknot function in programmed ribosomal frameshifting
    • Namy O., Moran S.J., Stuart D.I., Gilbert R.J.C., and Brierley I. A mechanical explanation of RNA pseudoknot function in programmed ribosomal frameshifting. Nature 441 (2006) 244-247
    • (2006) Nature , vol.441 , pp. 244-247
    • Namy, O.1    Moran, S.J.2    Stuart, D.I.3    Gilbert, R.J.C.4    Brierley, I.5
  • 29
    • 18844413446 scopus 로고    scopus 로고
    • Structural insights into translational fidelity
    • Ogle J.M., and Ramakrishnan V. Structural insights into translational fidelity. Annu. Rev. Biochem. 74 (2005) 129-177
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 129-177
    • Ogle, J.M.1    Ramakrishnan, V.2
  • 31
    • 33745044746 scopus 로고    scopus 로고
    • Rapid ribosomal translocation depends on the conserved 18-55 base pair in P-site transfer RNA
    • Pan D., Kirillov S., Zhang C., Hou Y., and Cooperman B.S. Rapid ribosomal translocation depends on the conserved 18-55 base pair in P-site transfer RNA. Nat. Struct. Mol. Biol. 13 (2006) 354-359
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 354-359
    • Pan, D.1    Kirillov, S.2    Zhang, C.3    Hou, Y.4    Cooperman, B.S.5
  • 32
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • Pape T., Wintermeyer W., and 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
  • 33
    • 0018855288 scopus 로고
    • "Two out of three" codon reading leading to mistranslation in vivo
    • Parker J., and Friesen J.D. "Two out of three" codon reading leading to mistranslation in vivo. Mol. Gen. Genet. 177 (1980) 439-445
    • (1980) Mol. Gen. Genet. , vol.177 , pp. 439-445
    • Parker, J.1    Friesen, J.D.2
  • 34
    • 0029873397 scopus 로고    scopus 로고
    • Rate of translation of natural mRNAs in an optimized in vitro system
    • Pavlov M.Y., and Ehrenberg M. Rate of translation of natural mRNAs in an optimized in vitro system. Arch. Biochem. Biophys. 328 (1996) 9-16
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 9-16
    • Pavlov, M.Y.1    Ehrenberg, M.2
  • 35
    • 1542285356 scopus 로고    scopus 로고
    • Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling
    • Qin F. Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling. Biophys. J. 86 (2004) 1488-1501
    • (2004) Biophys. J. , vol.86 , pp. 1488-1501
    • Qin, F.1
  • 36
    • 0030061670 scopus 로고    scopus 로고
    • Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events
    • Qin F., Auerbach A., and Sachs F. Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events. Biophys. J. 70 (1996) 264-280
    • (1996) Biophys. J. , vol.70 , pp. 264-280
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 37
    • 0030956174 scopus 로고    scopus 로고
    • Maximum likelihood estmation of aggregated Markov processes
    • Qin F., Auerbach A., and Sachs F. Maximum likelihood estmation of aggregated Markov processes. Proc. R. Soc. Lond. B. Biol. Sci. 264 (1997) 375-383
    • (1997) Proc. R. Soc. Lond. B. Biol. Sci. , vol.264 , pp. 375-383
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 38
    • 33646379375 scopus 로고    scopus 로고
    • Conformational changes associated with receptor-stimulated guanine nucleotide exchange in a heterotrimeric G-protein α-subunit
    • Ridge K.D., Abdulaev N.G., Zhang C., Ngo T., Brabazon D.M., and Marino J.P. Conformational changes associated with receptor-stimulated guanine nucleotide exchange in a heterotrimeric G-protein α-subunit. J. Biol. Chem. 281 (2006) 7635-7648
    • (2006) J. Biol. Chem. , vol.281 , pp. 7635-7648
    • Ridge, K.D.1    Abdulaev, N.G.2    Zhang, C.3    Ngo, T.4    Brabazon, D.M.5    Marino, J.P.6
  • 39
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina M.V., Savelsbergh A., Katunin V.I., and Wintermeyer W. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385 (1997) 37-41
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 40
    • 0029085929 scopus 로고
    • A base pair between tRNA and 23S rRNA in the peptidyl transferase center of the ribosome
    • Samaha R.R., Green R., and Noller H.F. A base pair between tRNA and 23S rRNA in the peptidyl transferase center 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
  • 41
    • 0034949816 scopus 로고    scopus 로고
    • Codon and base biases after the initiation codon of the open reading frames in the Escherichia coli genome and their influence on the translation efficiency
    • Sato T., Terabe M., Watanabe H., Gojobori T., Hori-Takemoto C., and Miura K. Codon and base biases after the initiation codon of the open reading frames in the Escherichia coli genome and their influence on the translation efficiency. J. Biochem. (Tokyo) 129 (2001) 851-860
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 851-860
    • Sato, T.1    Terabe, M.2    Watanabe, H.3    Gojobori, T.4    Hori-Takemoto, C.5    Miura, K.6
  • 42
    • 28544452248 scopus 로고    scopus 로고
    • An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • Schmeing T.M., Huang K.S., Strobel S.A., and Steitz T.A. An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature 438 (2005) 520-524
    • (2005) Nature , vol.438 , pp. 520-524
    • Schmeing, T.M.1    Huang, K.S.2    Strobel, S.A.3    Steitz, T.A.4
  • 46
    • 0033762347 scopus 로고    scopus 로고
    • Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome
    • Semenkov Y.P., Rodnina M.V., and Wintermeyer W. Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome. Nat. Struct. Biol. 7 (2000) 1027-1031
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1027-1031
    • Semenkov, Y.P.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 47
    • 0026548529 scopus 로고
    • Puromycin reaction for the A site-bound peptidyl-tRNA
    • Semenkov Y., Shapkina T., Makhno V., and Kirillov S. Puromycin reaction for the A site-bound peptidyl-tRNA. FEBS Lett. 296 (1992) 207-210
    • (1992) FEBS Lett. , vol.296 , pp. 207-210
    • Semenkov, Y.1    Shapkina, T.2    Makhno, V.3    Kirillov, S.4
  • 48
    • 0039993541 scopus 로고
    • Escherichia coli formylmethionine tRNA: mutations in GGG-CCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop
    • Seong B.L., and RajBhandary U.L. Escherichia coli formylmethionine tRNA: mutations in GGG-CCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop. Proc. Natl. Acad. Sci. USA 84 (1987) 334-338
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 334-338
    • Seong, B.L.1    RajBhandary, U.L.2
  • 49
    • 0346362324 scopus 로고    scopus 로고
    • EF-G-independent reactivity of a pre-translocation-state ribosome complex with the aminoacyl tRNA substrate puromycin supports an intermediate (hybrid) state of tRNA binding
    • Sharma D., Southworth D.R., and Green R. EF-G-independent reactivity of a pre-translocation-state ribosome complex with the aminoacyl tRNA substrate puromycin supports an intermediate (hybrid) state of tRNA binding. RNA 10 (2004) 102-113
    • (2004) RNA , vol.10 , pp. 102-113
    • Sharma, D.1    Southworth, D.R.2    Green, R.3
  • 50
    • 0014425341 scopus 로고
    • On the mechanism of ribosome function. The hypothesis of locking-unlocking of subparticles
    • Spirin A.S. On the mechanism of ribosome function. The hypothesis of locking-unlocking of subparticles. Dokl. Akad. Nauk SSSR 179 (1968) 1467-1470
    • (1968) Dokl. Akad. Nauk SSSR , vol.179 , pp. 1467-1470
    • Spirin, A.S.1
  • 51
    • 0037459218 scopus 로고    scopus 로고
    • Rapid kinetic analysis of EF-G-dependent mRNA translocation in the ribosome
    • Studer S.M., Feinberg J.S., and Joseph S. Rapid kinetic analysis of EF-G-dependent mRNA translocation in the ribosome. J. Mol. Biol. 327 (2003) 369-381
    • (2003) J. Mol. Biol. , vol.327 , pp. 369-381
    • Studer, S.M.1    Feinberg, J.S.2    Joseph, S.3
  • 52
    • 0019257050 scopus 로고
    • Functional studies on ribosomes lacking protein L1 from mutant Escherichia coli
    • Subramanian A.R., and Dabbs E.R. Functional studies on ribosomes lacking protein L1 from mutant Escherichia coli. Eur. J. Biochem. 112 (1980) 425-430
    • (1980) Eur. J. Biochem. , vol.112 , pp. 425-430
    • Subramanian, A.R.1    Dabbs, E.R.2
  • 53
    • 4344716056 scopus 로고    scopus 로고
    • Normal mode based flexible fitting of high-resolution structure into low-resolution experimental data from cryo-EM
    • Tama F., Miyashita O., and Brooks C.L. Normal mode based flexible fitting of high-resolution structure into low-resolution experimental data from cryo-EM. J. Struct. Biol. 147 (2004) 315-326
    • (2004) J. Struct. Biol. , vol.147 , pp. 315-326
    • Tama, F.1    Miyashita, O.2    Brooks, C.L.3
  • 54
    • 23244446620 scopus 로고    scopus 로고
    • Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis
    • Underwood K.A., Swartz J.R., and Puglisi J.D. Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis. Biotechnol. Bioeng. 91 (2005) 425-435
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 425-435
    • Underwood, K.A.1    Swartz, J.R.2    Puglisi, J.D.3
  • 58
    • 0032584643 scopus 로고    scopus 로고
    • An integrated model of the transcription complex in elongation, termination, and editing
    • von Hippel P. An integrated model of the transcription complex in elongation, termination, and editing. Science 281 (1998) 660-665
    • (1998) Science , vol.281 , pp. 660-665
    • von Hippel, P.1
  • 59
    • 4344685227 scopus 로고    scopus 로고
    • Global ribosome motions revealed with elastic network model
    • Wang Y., Rader A.J., Bahar I., and Jernigan R.L. Global ribosome motions revealed with elastic network model. J. Struct. Biol. 147 (2004) 302-314
    • (2004) J. Struct. Biol. , vol.147 , pp. 302-314
    • Wang, Y.1    Rader, A.J.2    Bahar, I.3    Jernigan, R.L.4
  • 60
    • 33748785471 scopus 로고    scopus 로고
    • Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome
    • Wilden B., Savelsbergh A., Rodnina M.V., and Wintermeyer W. Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome. Proc. Natl. Acad. Sci. USA 103 (2006) 13670-13675
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13670-13675
    • Wilden, B.1    Savelsbergh, A.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 62
    • 0037461492 scopus 로고    scopus 로고
    • Single-molecule approach to dispersed kinetics and dynamic disorder: probing conformational fluctuation and enzymatic dynamics
    • Xie X.S. Single-molecule approach to dispersed kinetics and dynamic disorder: probing conformational fluctuation and enzymatic dynamics. J. Chem. Phys. 117 (2002) 11024-11032
    • (2002) J. Chem. Phys. , vol.117 , pp. 11024-11032
    • Xie, X.S.1
  • 63
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin Y.W., and Steitz T.A. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science 298 (2002) 1387-1395
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 64
    • 22244433549 scopus 로고    scopus 로고
    • Antibiotics targeting ribosomes: resistance, selectivity, synergism, and cellular regulation
    • Yonath A. Antibiotics targeting ribosomes: resistance, selectivity, synergism, and cellular regulation. Annu. Rev. Biochem. 74 (2005) 649-679
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 649-679
    • Yonath, A.1
  • 65
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman E.M., Brunelle J.L., Kochaniak A.B., and Green R. The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell 117 (2004) 589-599
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4


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