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Volumn 520, Issue 7549, 2015, Pages 640-645

Structure of the human 80S ribosome

Author keywords

[No Author keywords available]

Indexed keywords

RIBOSOME RNA; TRANSFER RNA; RIBOSOME PROTEIN;

EID: 84928786981     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14427     Document Type: Article
Times cited : (373)

References (60)
  • 1
    • 84877310529 scopus 로고    scopus 로고
    • Structures of the human and Drosophila 80S ribosome
    • Anger, A. M. et al. Structures of the human and Drosophila 80S ribosome. Nature 497, 80-85 (2013).
    • (2013) Nature , vol.497 , pp. 80-85
    • Anger, A.M.1
  • 2
    • 83855162728 scopus 로고    scopus 로고
    • The structure of the eukaryotic ribosome at 3.0A? Resolution
    • Ben-Shem, A. et al. The structure of the eukaryotic ribosome at 3.0A? resolution. Science 334, 1524-1529 (2011).
    • (2011) Science , vol.334 , pp. 1524-1529
    • Ben-Shem, A.1
  • 3
    • 79951510534 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
    • Rabl, J., Leibundgut, M., Ataide, S. F., Haag, A. & Ban, N. Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 331, 730-736 (2011).
    • (2011) Science , vol.331 , pp. 730-736
    • Rabl, J.1    Leibundgut, M.2    Ataide, S.F.3    Haag, A.4    Ban, N.5
  • 4
    • 81555219350 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6
    • Klinge, S., Voigts-Hoffmann, F., Leibundgut, M., Arpagaus, S. & Ban, N. Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6. Science 334, 941-948 (2011).
    • (2011) Science , vol.334 , pp. 941-948
    • Klinge, S.1    Voigts-Hoffmann, F.2    Leibundgut, M.3    Arpagaus, S.4    Ban, N.5
  • 5
    • 4644247805 scopus 로고    scopus 로고
    • Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes: The IRES functions as an RNA-based translation factor
    • Spahn, C. M. et al. Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes: the IRES functions as an RNA-based translation factor. Cell 118, 465-475 (2004).
    • (2004) Cell , vol.118 , pp. 465-475
    • Spahn, C.M.1
  • 6
    • 27644484907 scopus 로고    scopus 로고
    • Structure of the hepatitisC virus IRES bound to the human 80S ribosome: Remodeling of the HCV IRES
    • Boehringer, D., Thermann, R., Ostareck-Lederer, A., Lewis, J. D.&Stark, H. Structure of the hepatitisC virus IRES bound to the human 80S ribosome: remodeling of the HCV IRES. Structure 13, 1695-1706 (2005).
    • (2005) Structure , vol.13 , pp. 1695-1706
    • Boehringer, D.1    Thermann, R.2    Ostareck-Lederer, A.3    Lewis, J.D.4    Stark, H.5
  • 7
    • 41549119061 scopus 로고    scopus 로고
    • Structure of the mammalian 80S ribosome at 8.7A? Resolution
    • Chandramouli, P. et al. Structure of the mammalian 80S ribosome at 8.7A? resolution. Structure 16, 535-548 (2008).
    • (2008) Structure , vol.16 , pp. 535-548
    • Chandramouli, P.1
  • 8
    • 84903310310 scopus 로고    scopus 로고
    • Structure of the mammalian ribosome-Sec61 complex to 3.4A? Resolution
    • Voorhees, R. M., Fernandez, I. S., Scheres, S. H. & Hegde, R. S. Structure of the mammalian ribosome-Sec61 complex to 3.4A? resolution. Cell 157, 1632-1643 (2014).
    • (2014) Cell , vol.157 , pp. 1632-1643
    • Voorhees, R.M.1    Fernandez, I.S.2    Scheres, S.H.3    Hegde, R.S.4
  • 9
    • 84897000112 scopus 로고    scopus 로고
    • Structure of the yeast mitochondrial large ribosomal subunit
    • Amunts, A. et al. Structure of the yeast mitochondrial large ribosomal subunit. Science 343, 1485-1489 (2014).
    • (2014) Science , vol.343 , pp. 1485-1489
    • Amunts, A.1
  • 10
    • 84922065877 scopus 로고    scopus 로고
    • The complete structure of the large subunit of the mammalian mitochondrial ribosome
    • Greber, B. J. et al. The complete structure of the large subunit of the mammalian mitochondrial ribosome. Nature 515, 283-286 (2014).
    • (2014) Nature , vol.515 , pp. 283-286
    • Greber, B.J.1
  • 11
    • 84909594483 scopus 로고    scopus 로고
    • Structure of the large ribosomal subunit from human mitochondria
    • Brown, A. et al. Structure of the large ribosomal subunit from human mitochondria. Science 346, 718-722 (2014).
    • (2014) Science , vol.346 , pp. 718-722
    • Brown, A.1
  • 12
    • 84887252893 scopus 로고    scopus 로고
    • Influence of electron dose rate on electron counting images recorded with the K2 camera
    • Li, X., Zheng, S. Q., Egami, K., Agard, D. A.& Cheng, Y. Influence of electron dose rate on electron counting images recorded with the K2 camera. J. Struct. Biol. 184, 251-260 (2013).
    • (2013) J. Struct. Biol. , vol.184 , pp. 251-260
    • Li, X.1    Zheng, S.Q.2    Egami, K.3    Agard, D.A.4    Cheng, Y.5
  • 13
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM. Nature Methods 10, 584-590 (2013).
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 14
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures tonearatomic resolution from thirty thousand cryo-EM particles
    • Bai, X.C., Fernandez, I.S., McMullan, G.&Scheres, S. H. Ribosome structures tonearatomic resolution from thirty thousand cryo-EM particles. eLife 2, e00461 (2013).
    • (2013) ELife , vol.2 , pp. e00461
    • Bai, X.C.1    Fernandez, I.S.2    McMullan, G.3    Scheres, S.H.4
  • 15
    • 84898979617 scopus 로고    scopus 로고
    • Purification characterization and crystallization of the human 80S ribosome
    • Khatter, H. et al.Purification, characterization and crystallization of the human 80S ribosome. Nucleic Acids Res. 42, e49 (2014).
    • (2014) Nucleic Acids Res , vol.42 , pp. e49
    • Khatter, H.1
  • 16
    • 33746414364 scopus 로고    scopus 로고
    • Considerations for the refinement of low-resolution crystal structures
    • DeLaBarre, B. & Brunger, A. T. Considerations for the refinement of low-resolution crystal structures. Acta Crystallogr. D 62, 923-932 (2006).
    • (2006) Acta Crystallogr. D , vol.62 , pp. 923-932
    • Delabarre, B.1    Brunger, A.T.2
  • 17
    • 84924785638 scopus 로고    scopus 로고
    • FEM: Feature-enhanced map
    • Afonine, P. V. et al. FEM: feature-enhanced map. Acta Crystallogr. D 71, 646-666 (2015).
    • (2015) Acta Crystallogr. D , vol.71 , pp. 646-666
    • Afonine, P.V.1
  • 18
    • 78649426085 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic ribosome
    • Ben-Shem, A., Jenner, L., Yusupova, G. & Yusupov, M. Crystal structure of the eukaryotic ribosome. Science 330, 1203-1209 (2010).
    • (2010) Science , vol.330 , pp. 1203-1209
    • Ben-Shem, A.1    Jenner, L.2    Yusupova, G.3    Yusupov, M.4
  • 19
    • 42949126723 scopus 로고    scopus 로고
    • Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation
    • Fei, J., Kosuri, P., MacDougall, D. D. & Gonzalez, R. L. Jr. Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation. Mol. Cell 30, 348-359 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 348-359
    • Fei, J.1    Kosuri, P.2    MacDougall, D.D.3    Gonzalez, R.L.4
  • 20
    • 62449216538 scopus 로고    scopus 로고
    • Following movement of the L1 stalk between three functional states in single ribosomes
    • Cornish, P. V. et al. Following movement of the L1 stalk between three functional states in single ribosomes. Proc. Natl Acad. Sci. USA 106, 2571-2576 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 2571-2576
    • Cornish, P.V.1
  • 21
    • 84875116452 scopus 로고    scopus 로고
    • Crystal structure of 70S ribosome with both cognate tRNAs in the e and P sites representing an authentic elongation complex
    • Feng, S., Chen, Y. & Gao, Y. G. Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex. PLoS ONE 8, e58829 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e58829
    • Feng, S.1    Chen, Y.2    Gao, Y.G.3
  • 22
    • 0037963475 scopus 로고    scopus 로고
    • Locking and unlocking of ribosomal motions
    • Valle, M. et al. Locking and unlocking of ribosomal motions. Cell 114, 123-134 (2003).
    • (2003) Cell , vol.114 , pp. 123-134
    • Valle, M.1
  • 23
    • 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, 318-322 (2000).
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 24
    • 84903950561 scopus 로고    scopus 로고
    • Regulation of the mammalian elongation cycle by subunit rolling: A eukaryotic-specific ribosomerearrangement
    • Budkevich, T. V. et al. Regulation of the mammalian elongation cycle by subunit rolling: a eukaryotic-specific ribosomerearrangement. Cell 158, 121-131 (2014).
    • (2014) Cell , vol.158 , pp. 121-131
    • Budkevich, T.V.1
  • 25
    • 81755173676 scopus 로고    scopus 로고
    • Structure and dynamics of the mammalian ribosomal pretranslocation complex
    • Budkevich, T. et al. Structure and dynamics of the mammalian ribosomal pretranslocation complex. Mol. Cell 44, 214-224 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 214-224
    • Budkevich, T.1
  • 26
    • 84878909556 scopus 로고    scopus 로고
    • Coordinated conformational and compositional dynamics drive ribosome translocation
    • Chen, J., Petrov, A., Tsai, A., O'Leary, S. E.&Puglisi, J. D.Coordinated conformational and compositional dynamics drive ribosome translocation. Nature Struct. Mol. Biol. 20, 718-727 (2013).
    • (2013) Nature Struct. Mol. Biol. , vol.20 , pp. 718-727
    • Chen, J.1    Petrov, A.2    Tsai, A.3    O'Leary, S.E.4    Puglisi, J.D.5
  • 27
    • 0035010211 scopus 로고    scopus 로고
    • Geometric nomenclature and classification of RNA base pairs
    • Leontis, N. B. & Westhof, E. Geometric nomenclature and classification of RNA base pairs. RNA 7, 499-512 (2001).
    • (2001) RNA , vol.7 , pp. 499-512
    • Leontis, N.B.1    Westhof, E.2
  • 28
    • 0036711448 scopus 로고    scopus 로고
    • O hydrogen bonds in the nuclear receptor RARgamma-A potential tool for drug selectivity
    • Klaholz, B. & Moras, D. C.-H. O hydrogen bonds in the nuclear receptor RARgamma-a potential tool for drug selectivity. Structure 10, 1197-1204 (2002).
    • (2002) Structure , vol.10 , pp. 1197-1204
    • Klaholz, B.1    Moras, D.C.-H.2
  • 29
    • 39749109971 scopus 로고    scopus 로고
    • NMR detection of bifurcated hydrogen bonds in large proteins
    • Liu, A. et al. NMR detection of bifurcated hydrogen bonds in large proteins. J. Am. Chem. Soc. 130, 2428-2429 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2428-2429
    • Liu, A.1
  • 30
    • 0037019829 scopus 로고    scopus 로고
    • Ohydrogen bonds at protein-protein interfaces
    • Jiang, L.&Lai, L. C. H.Ohydrogen bonds at protein-protein interfaces. J. Biol. Chem. 277, 37732-37740 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 37732-37740
    • Jiang, L.1    Lai, L.C.H.2
  • 31
    • 27644491082 scopus 로고    scopus 로고
    • Structures of the bacterial ribosome at 3.5A? Resolution
    • Schuwirth, B. S. et al. Structures of the bacterial ribosome at 3.5A? resolution. Science 310, 827-834 (2005).
    • (2005) Science , vol.310 , pp. 827-834
    • Schuwirth, B.S.1
  • 32
    • 0032881809 scopus 로고    scopus 로고
    • X-ray crystal structures of 70S ribosome functional complexes
    • Cate, J. H., Yusupov, M. M., Yusupova, G. Z., Earnest, T. N.& Noller, H. F. X-ray crystal structures of 70S ribosome functional complexes. Science 285, 2095-2104 (1999).
    • (1999) Science , vol.285 , pp. 2095-2104
    • Cate, J.H.1    Yusupov, M.M.2    Yusupova, G.Z.3    Earnest, T.N.4    Noller, H.F.5
  • 33
    • 0035805213 scopus 로고    scopus 로고
    • Crystal structure of the ribosome at 5.5A? Resolution
    • Yusupov, M. M. et al. Crystal structure of the ribosome at 5.5A? resolution. Science 292, 883-896 (2001).
    • (2001) Science , vol.292 , pp. 883-896
    • Yusupov, M.M.1
  • 34
    • 28344456738 scopus 로고    scopus 로고
    • Accessibility of 18S rRNA in human 40S subunits and 80S ribosomes at physiological magnesiumion concentrations-implications for the study of ribosome dynamics
    • Shenvi, C. L., Dong, K. C., Friedman, E. M., Hanson, J. A. & Cate, J. H. Accessibility of 18S rRNA in human 40S subunits and 80S ribosomes at physiological magnesiumion concentrations-implications for the study of ribosome dynamics. RNA 11, 1898-1908 (2005).
    • (2005) RNA , vol.11 , pp. 1898-1908
    • Shenvi, C.L.1    Dong, K.C.2    Friedman, E.M.3    Hanson, J.A.4    Cate, J.H.5
  • 35
    • 0021905817 scopus 로고
    • Effects of cations and cosolvents on eukaryotic ribosomal subunit conformation
    • Moore, M. N. & Spremulli, L. L. Effects of cations and cosolvents on eukaryotic ribosomal subunit conformation. Biochemistry 24, 191-196 (1985).
    • (1985) Biochemistry , vol.24 , pp. 191-196
    • Moore, M.N.1    Spremulli, L.L.2
  • 36
    • 0019327875 scopus 로고
    • Reversible dissociation of wheat germ ribosomal subunits: Cation-dependent equilibria and thermodynamic parameters
    • Sperrazza, J. M., Russell, D. W. & Spremulli, L. L. Reversible dissociation of wheat germ ribosomal subunits: cation-dependent equilibria and thermodynamic parameters. Biochemistry 19, 1053-1058 (1980).
    • (1980) Biochemistry , vol.19 , pp. 1053-1058
    • Sperrazza, J.M.1    Russell, D.W.2    Spremulli, L.L.3
  • 37
    • 69249112231 scopus 로고    scopus 로고
    • Structures of the ribosome in intermediate states of ratcheting
    • Zhang, W., Dunkle, J. A. & Cate, J. H. Structures of the ribosome in intermediate states of ratcheting. Science 325, 1014-1017 (2009).
    • (2009) Science , vol.325 , pp. 1014-1017
    • Zhang, W.1    Dunkle, J.A.2    Cate, J.H.3
  • 38
    • 79956303529 scopus 로고    scopus 로고
    • Structures of thebacterial ribosome in classical and hybrid states of tRNA binding
    • Dunkle, J. A. et al. Structures of thebacterial ribosome in classical and hybrid states of tRNA binding. Science 332, 981-984 (2011).
    • (2011) Science , vol.332 , pp. 981-984
    • Dunkle, J.A.1
  • 39
    • 84879663355 scopus 로고    scopus 로고
    • Elongation factorG bound to the ribosome in an intermediate state of translocation
    • Tourigny, D. S., Fernandez, I. S., Kelley, A. C.&Ramakrishnan, V. Elongation factorG bound to the ribosome in an intermediate state of translocation. Science 340, 1235490 (2013).
    • (2013) Science , vol.340 , pp. 1235490
    • Tourigny, D.S.1    Fernandez, I.S.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 40
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • Selmer, M. et al. Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313, 1935-1942 (2006).
    • (2006) Science , vol.313 , pp. 1935-1942
    • Selmer, M.1
  • 41
    • 84908546298 scopus 로고    scopus 로고
    • Structural basis for the inhibition of the eukaryotic ribosome
    • Garreau de Loubresse, N. et al. Structural basis for the inhibition of the eukaryotic ribosome. Nature 513, 517-522 (2014).
    • (2014) Nature , vol.513 , pp. 517-522
    • Garreau De Loubresse, N.1
  • 42
    • 35549002147 scopus 로고    scopus 로고
    • Messenger RNA conformations in the ribosomal e site revealed by X-ray crystallography
    • Jenner, L., Rees, B., Yusupov, M. & Yusupova, G. Messenger RNA conformations in the ribosomal E site revealed by X-ray crystallography. EMBO Rep. 8, 846-850 (2007).
    • (2007) EMBO Rep , vol.8 , pp. 846-850
    • Jenner, L.1    Rees, B.2    Yusupov, M.3    Yusupova, G.4
  • 43
    • 78650434685 scopus 로고    scopus 로고
    • A flexible loop in yeast ribosomal protein L11 coordinates P-site tRNA binding
    • Rhodin, M. H. & Dinman, J. D. A flexible loop in yeast ribosomal protein L11 coordinates P-site tRNA binding. Nucleic Acids Res. 38, 8377-8389 (2010).
    • (2010) Nucleic Acids Res , vol.38 , pp. 8377-8389
    • Rhodin, M.H.1    Dinman, J.D.2
  • 44
    • 84905655144 scopus 로고    scopus 로고
    • Structure of the mammalian 80S initiation complex with initiation factor5BonHCV-IRESRNA
    • Yamamoto, H. et al. Structure of the mammalian 80S initiation complex with initiation factor5BonHCV-IRESRNA.Nature Struct. Mol. Biol. 21, 721-727(2014).
    • (2014) Nature Struct. Mol. Biol. , vol.21 , pp. 721-727
    • Yamamoto, H.1
  • 45
    • 84902193122 scopus 로고    scopus 로고
    • The scanning mechanism of eukaryotic translation initiation
    • Hinnebusch, A. G. The scanning mechanism of eukaryotic translation initiation. Annu. Rev. Biochem. 83, 779-812 (2014).
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 779-812
    • Hinnebusch, A.G.1
  • 46
    • 0035912725 scopus 로고    scopus 로고
    • Molecular mechanisms of translation initiation in eukaryotes
    • Pestova, T. V. et al. Molecular mechanisms of translation initiation in eukaryotes. Proc. Natl Acad. Sci. USA 98, 7029-7036 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7029-7036
    • Pestova, T.V.1
  • 47
    • 84859593945 scopus 로고    scopus 로고
    • A new understanding of the decoding principle on the ribosome
    • Demeshkina, N., Jenner, L., Westhof, E., Yusupov, M. & Yusupova, G. A new understanding of the decoding principle on the ribosome. Nature 484, 256-259 (2012).
    • (2012) Nature , vol.484 , pp. 256-259
    • Demeshkina, N.1    Jenner, L.2    Westhof, E.3    Yusupov, M.4    Yusupova, G.5
  • 48
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for highresolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for highresolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 49
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determinationof local defocus and specimen tilt in electron microscopy
    • Mindell, J. A.&Grigorieff, N. Accurate determinationof local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 50
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 51
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen, S. et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24-35 (2013).
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1
  • 52
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J.Mol. Biol. 333, 721-745 (2003).
    • (2003) J.Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 53
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • van Heel, M. & Schatz, M. Fourier shell correlation threshold criteria. J. Struct. Biol. 151, 250-262 (2005).
    • (2005) J. Struct. Biol. , vol.151 , pp. 250-262
    • Van Heel, M.1    Schatz, M.2
  • 54
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63-65 (2014).
    • (2014) Nature Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 55
    • 4444221565 scopus 로고    scopus 로고
    • UCSFChimera-A visualization systemfor exploratory research and analysis
    • Pettersen, E. F. et al.UCSFChimera-a visualization systemfor exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 57
    • 84897964300 scopus 로고    scopus 로고
    • A new system for naming ribosomal proteins
    • Ban, N. et al. A new system for naming ribosomal proteins. Curr. Opin. Struct. Biol. 24, 165-169 (2014).
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 165-169
    • Ban, N.1
  • 58
    • 84860273177 scopus 로고    scopus 로고
    • Towards automated crystallographic structure refinement with phenix.refine
    • Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr. D 68, 352-367 (2012).
    • (2012) Acta Crystallogr. D , vol.68 , pp. 352-367
    • Afonine, P.V.1
  • 59
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • Selmer, M. et al. Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313, 1935-1942 (2006).
    • (2006) Science , vol.313 , pp. 1935-1942
    • Selmer, M.1


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