메뉴 건너뛰기




Volumn 46, Issue , 2017, Pages 140-148

Focused classification and refinement in high-resolution cryo-EM structural analysis of ribosome complexes

Author keywords

[No Author keywords available]

Indexed keywords

RIBOSOME RNA;

EID: 85028352875     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2017.07.007     Document Type: Review
Times cited : (47)

References (88)
  • 2
    • 84855886702 scopus 로고    scopus 로고
    • Termination and post-termination events in eukaryotic translation
    • Jackson, R.J., Hellen, C.U., Pestova, T.V., Termination and post-termination events in eukaryotic translation. Adv Protein Chem Struct Biol 86 (2012), 45–93.
    • (2012) Adv Protein Chem Struct Biol , vol.86 , pp. 45-93
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 3
    • 85018782909 scopus 로고    scopus 로고
    • Structural insights into the mechanism of scanning and start codon recognition in eukaryotic translation initiation
    • Hinnebusch, A.G., Structural insights into the mechanism of scanning and start codon recognition in eukaryotic translation initiation. Trends Biochem Sci 42 (2017), 589–611.
    • (2017) Trends Biochem Sci , vol.42 , pp. 589-611
    • Hinnebusch, A.G.1
  • 4
    • 85028320552 scopus 로고    scopus 로고
    • Structure sorting of multiple macromolecular states in heterogeneous cryo-EM samples by 3D multivariate statistical analysis. edn Special Issue on Multivariate Statistical Analysis [Edited by: Open Journal of Statistics; :820–836. vol 5].
    • Klaholz BP: Structure sorting of multiple macromolecular states in heterogeneous cryo-EM samples by 3D multivariate statistical analysis. edn Special Issue on Multivariate Statistical Analysis [Edited by: Open Journal of Statistics; 2015:820–836. vol 5].
    • (2015)
    • Klaholz, B.P.1
  • 5
    • 77957292751 scopus 로고    scopus 로고
    • Methods for three-dimensional reconstruction of heterogeneous assemblies
    • Orlova, E.V., Saibil, H.R., Methods for three-dimensional reconstruction of heterogeneous assemblies. Methods Enzymol 482 (2010), 321–341.
    • (2010) Methods Enzymol , vol.482 , pp. 321-341
    • Orlova, E.V.1    Saibil, H.R.2
  • 6
    • 85011590448 scopus 로고    scopus 로고
    • Structural study of heterogeneous biological samples by cryoelectron microscopy and image processing
    • White, H.E., Ignatiou, A., Clare, D.K., Orlova, E.V., Structural study of heterogeneous biological samples by cryoelectron microscopy and image processing. Biomed Res Int, 2017, 2017, 1032432.
    • (2017) Biomed Res Int , vol.2017 , pp. 1032432
    • White, H.E.1    Ignatiou, A.2    Clare, D.K.3    Orlova, E.V.4
  • 8
    • 84912566327 scopus 로고    scopus 로고
    • Cryo-EM enters a new era
    • Kühlbrandt, W., Cryo-EM enters a new era. Elife, 3, 2014, e03678.
    • (2014) Elife , vol.3 , pp. e03678
    • Kühlbrandt, W.1
  • 10
    • 84888064039 scopus 로고    scopus 로고
    • Quantitative characterization of electron detectors for transmission electron microscopy
    • Ruskin, R.S., Yu, Z., Grigorieff, N., Quantitative characterization of electron detectors for transmission electron microscopy. J Struct Biol 184 (2013), 385–393.
    • (2013) J Struct Biol , vol.184 , pp. 385-393
    • Ruskin, R.S.1    Yu, Z.2    Grigorieff, N.3
  • 14
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • Zheng, S.Q., Palovcak, E., Armache, J.P., Verba, K.A., Cheng, Y., Agard, D.A., MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat Methods 14 (2017), 331–332.
    • (2017) Nat Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1    Palovcak, E.2    Armache, J.P.3    Verba, K.A.4    Cheng, Y.5    Agard, D.A.6
  • 17
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres, S.H., Beam-induced motion correction for sub-megadalton cryo-EM particles. Elife, 3, 2014, e03665.
    • (2014) Elife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 18
    • 84923447206 scopus 로고    scopus 로고
    • Alignment of direct detection device micrographs using a robust Optical Flow approach
    • Abrishami, V., Vargas, J., Li, X., Cheng, Y., Marabini, R., Sorzano, C., Carazo, J.M., Alignment of direct detection device micrographs using a robust Optical Flow approach. J Struct Biol 189 (2015), 163–176.
    • (2015) J Struct Biol , vol.189 , pp. 163-176
    • Abrishami, V.1    Vargas, J.2    Li, X.3    Cheng, Y.4    Marabini, R.5    Sorzano, C.6    Carazo, J.M.7
  • 19
    • 4344605740 scopus 로고    scopus 로고
    • Dynamics of EF-G interaction with the ribosome explored by classification of a heterogeneous cryo-EM dataset
    • Gao, H., Valle, M., Ehrenberg, M., Frank, J., Dynamics of EF-G interaction with the ribosome explored by classification of a heterogeneous cryo-EM dataset. J Struct Biol 147 (2004), 283–290.
    • (2004) J Struct Biol , vol.147 , pp. 283-290
    • Gao, H.1    Valle, M.2    Ehrenberg, M.3    Frank, J.4
  • 21
    • 1542378898 scopus 로고    scopus 로고
    • Visualization of release factor 3 on the ribosome during termination of protein synthesis
    • Klaholz, B.P., Myasnikov, A.G., Van Heel, M., Visualization of release factor 3 on the ribosome during termination of protein synthesis. Nature 427 (2004), 862–865.
    • (2004) Nature , vol.427 , pp. 862-865
    • Klaholz, B.P.1    Myasnikov, A.G.2    Van Heel, M.3
  • 22
    • 84930274128 scopus 로고    scopus 로고
    • Efficient estimation of three-dimensional covariance and its application in the analysis of heterogeneous samples in cryo-electron microscopy
    • Liao, H.Y., Hashem, Y., Frank, J., Efficient estimation of three-dimensional covariance and its application in the analysis of heterogeneous samples in cryo-electron microscopy. Structure 23 (2015), 1129–1137.
    • (2015) Structure , vol.23 , pp. 1129-1137
    • Liao, H.Y.1    Hashem, Y.2    Frank, J.3
  • 23
    • 41649087227 scopus 로고    scopus 로고
    • Detection and separation of heterogeneity in molecular complexes by statistical analysis of their two-dimensional projections
    • Elad, N., Clare, D.K., Saibil, H.R., Orlova, E.V., Detection and separation of heterogeneity in molecular complexes by statistical analysis of their two-dimensional projections. J Struct Biol 162 (2008), 108–120.
    • (2008) J Struct Biol , vol.162 , pp. 108-120
    • Elad, N.1    Clare, D.K.2    Saibil, H.R.3    Orlova, E.V.4
  • 24
    • 33646042904 scopus 로고    scopus 로고
    • A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation
    • Penczek, P.A., Frank, J., Spahn, C.M., A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation. J Struct Biol 154 (2006), 184–194.
    • (2006) J Struct Biol , vol.154 , pp. 184-194
    • Penczek, P.A.1    Frank, J.2    Spahn, C.M.3
  • 25
    • 33947328020 scopus 로고    scopus 로고
    • Bootstrap resampling for voxel-wise variance analysis of three-dimensional density maps derived by image analysis of two-dimensional crystals
    • Cheng, A., Yeager, M., Bootstrap resampling for voxel-wise variance analysis of three-dimensional density maps derived by image analysis of two-dimensional crystals. J Struct Biol 158 (2007), 19–32.
    • (2007) J Struct Biol , vol.158 , pp. 19-32
    • Cheng, A.1    Yeager, M.2
  • 28
    • 85028344986 scopus 로고
    • Bootstrap methods: another look at the jackknife [Edited by: The Annals of Statistics; :1–26. vol 7].
    • Efron B: Bootstrap methods: another look at the jackknife [Edited by: The Annals of Statistics; 1979:1–26. vol 7].
    • (1979)
    • Efron, B.1
  • 29
    • 84873993676 scopus 로고    scopus 로고
    • Dynamics in cryo EM reconstructions visualized with maximum-likelihood derived variance maps
    • Wang, Q., Matsui, T., Domitrovic, T., Zheng, Y., Doerschuk, P.C., Johnson, J.E., Dynamics in cryo EM reconstructions visualized with maximum-likelihood derived variance maps. J Struct Biol 181 (2013), 195–206.
    • (2013) J Struct Biol , vol.181 , pp. 195-206
    • Wang, Q.1    Matsui, T.2    Domitrovic, T.3    Zheng, Y.4    Doerschuk, P.C.5    Johnson, J.E.6
  • 30
    • 84883447961 scopus 로고    scopus 로고
    • Likelihood-based classification of cryo-EM images using FREALIGN
    • Lyumkis, D., Brilot, A.F., Theobald, D.L., Grigorieff, N., Likelihood-based classification of cryo-EM images using FREALIGN. J Struct Biol 183 (2013), 377–388.
    • (2013) J Struct Biol , vol.183 , pp. 377-388
    • Lyumkis, D.1    Brilot, A.F.2    Theobald, D.L.3    Grigorieff, N.4
  • 31
    • 0031704540 scopus 로고    scopus 로고
    • A maximum-likelihood approach to single-particle image refinement
    • Sigworth, F.J., A maximum-likelihood approach to single-particle image refinement. J Struct Biol 122 (1998), 328–339.
    • (1998) J Struct Biol , vol.122 , pp. 328-339
    • Sigworth, F.J.1
  • 32
    • 84973518493 scopus 로고    scopus 로고
    • Processing of structurally heterogeneous cryo-EM data in RELION
    • Scheres, S.H., Processing of structurally heterogeneous cryo-EM data in RELION. Methods Enzymol 579 (2016), 125–157.
    • (2016) Methods Enzymol , vol.579 , pp. 125-157
    • Scheres, S.H.1
  • 33
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
    • Bai, X.C., Fernandez, I.S., McMullan, G., Scheres, S.H., Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. Elife, 2, 2013, e00461.
    • (2013) Elife , vol.2 , pp. e00461
    • Bai, X.C.1    Fernandez, I.S.2    McMullan, G.3    Scheres, S.H.4
  • 36
    • 85006765705 scopus 로고    scopus 로고
    • Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution
    • Hilal, T., Yamamoto, H., Loerke, J., Bürger, J., Mielke, T., Spahn, C.M., Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution. Nat Commun, 7, 2016, 13521.
    • (2016) Nat Commun , vol.7 , pp. 13521
    • Hilal, T.1    Yamamoto, H.2    Loerke, J.3    Bürger, J.4    Mielke, T.5    Spahn, C.M.6
  • 37
    • 84992125329 scopus 로고    scopus 로고
    • Structures and stabilization of kinetoplastid-specific split rRNAs revealed by comparing leishmanial and human ribosomes
    • Zhang, X., Lai, M., Chang, W., Yu, I., Ding, K., Mrazek, J., Ng, H.L., Yang, O.O., Maslov, D.A., Zhou, Z.H., Structures and stabilization of kinetoplastid-specific split rRNAs revealed by comparing leishmanial and human ribosomes. Nat Commun, 7, 2016, 13223.
    • (2016) Nat Commun , vol.7 , pp. 13223
    • Zhang, X.1    Lai, M.2    Chang, W.3    Yu, I.4    Ding, K.5    Mrazek, J.6    Ng, H.L.7    Yang, O.O.8    Maslov, D.A.9    Zhou, Z.H.10
  • 38
    • 84975221229 scopus 로고    scopus 로고
    • Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosome
    • Study illustrating the strength of particle sorting to address multiple structural states simulateneously of an IRES mRNA moving through the ribosome.
    • Abeyrathne, P.D., Koh, C.S., Grant, T., Grigorieff, N., Korostelev, A.A., Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosome. Elife, 5, 2016 Study illustrating the strength of particle sorting to address multiple structural states simulateneously of an IRES mRNA moving through the ribosome.
    • (2016) Elife , vol.5
    • Abeyrathne, P.D.1    Koh, C.S.2    Grant, T.3    Grigorieff, N.4    Korostelev, A.A.5
  • 40
    • 84940478899 scopus 로고    scopus 로고
    • Structural basis for stop codon recognition in eukaryotes
    • Brown, A., Shao, S., Murray, J., Hegde, R.S., Ramakrishnan, V., Structural basis for stop codon recognition in eukaryotes. Nature 524 (2015), 493–496.
    • (2015) Nature , vol.524 , pp. 493-496
    • Brown, A.1    Shao, S.2    Murray, J.3    Hegde, R.S.4    Ramakrishnan, V.5
  • 42
    • 84988556853 scopus 로고    scopus 로고
    • Large-scale movements of IF3 and tRNA during bacterial translation initiation
    • 133–144.e113
    • Hussain, T., Llácer, J.L., Wimberly, B.T., Kieft, J.S., Ramakrishnan, V., Large-scale movements of IF3 and tRNA during bacterial translation initiation. Cell, 167, 2016 133–144.e113.
    • (2016) Cell , vol.167
    • Hussain, T.1    Llácer, J.L.2    Wimberly, B.T.3    Kieft, J.S.4    Ramakrishnan, V.5
  • 44
    • 84928786981 scopus 로고    scopus 로고
    • Structure of the human 80S ribosome
    • First high-resolution structure of the cytosolic human ribosome with visualisation of nucleotide and amino acid side-chains.
    • Khatter, H., Myasnikov, A.G., Natchiar, S.K., Klaholz, B.P., Structure of the human 80S ribosome. Nature 520 (2015), 640–645 First high-resolution structure of the cytosolic human ribosome with visualisation of nucleotide and amino acid side-chains.
    • (2015) Nature , vol.520 , pp. 640-645
    • Khatter, H.1    Myasnikov, A.G.2    Natchiar, S.K.3    Klaholz, B.P.4
  • 46
    • 84978511982 scopus 로고    scopus 로고
    • 2.8-Å cryo-EM structure of the large ribosomal subunit from the eukaryotic parasite leishmania
    • Visualisation of rRNA modifications in the leishmanial parasite ribosome.
    • Shalev-Benami, M., Zhang, Y., Matzov, D., Halfon, Y., Zackay, A., Rozenberg, H., Zimmerman, E., Bashan, A., Jaffe, C.L., Yonath, A., et al. 2.8-Å cryo-EM structure of the large ribosomal subunit from the eukaryotic parasite leishmania. Cell Rep 16 (2016), 288–294 Visualisation of rRNA modifications in the leishmanial parasite ribosome.
    • (2016) Cell Rep , vol.16 , pp. 288-294
    • Shalev-Benami, M.1    Zhang, Y.2    Matzov, D.3    Halfon, Y.4    Zackay, A.5    Rozenberg, H.6    Zimmerman, E.7    Bashan, A.8    Jaffe, C.L.9    Yonath, A.10
  • 47
    • 84928560614 scopus 로고    scopus 로고
    • Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM
    • Fischer, N., Neumann, P., Konevega, A.L., Bock, L.V., Ficner, R., Rodnina, M.V., Stark, H., Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM. Nature 520 (2015), 567–570.
    • (2015) Nature , vol.520 , pp. 567-570
    • Fischer, N.1    Neumann, P.2    Konevega, A.L.3    Bock, L.V.4    Ficner, R.5    Rodnina, M.V.6    Stark, H.7
  • 48
    • 84903310310 scopus 로고    scopus 로고
    • Structure of the mammalian ribosome-Sec61 complex to 3.4 Å resolution
    • Voorhees, R.M., Fernández, I.S., Scheres, S.H., Hegde, R.S., Structure of the mammalian ribosome-Sec61 complex to 3.4 Å resolution. Cell 157 (2014), 1632–1643.
    • (2014) Cell , vol.157 , pp. 1632-1643
    • Voorhees, R.M.1    Fernández, I.S.2    Scheres, S.H.3    Hegde, R.S.4
  • 49
    • 84890445788 scopus 로고    scopus 로고
    • Ribosome-targeting antibiotics and mechanisms of bacterial resistance
    • Wilson, D.N., Ribosome-targeting antibiotics and mechanisms of bacterial resistance. Nat Rev Microbiol 12 (2014), 35–48.
    • (2014) Nat Rev Microbiol , vol.12 , pp. 35-48
    • Wilson, D.N.1
  • 50
    • 85000480334 scopus 로고    scopus 로고
    • The pathway to GTPase activation of elongation factor SelB on the ribosome
    • High-resolution cryo-EM visualisation of rRNA modifications in the E. coli ribosome.
    • Fischer, N., Neumann, P., Bock, L.V., Maracci, C., Wang, Z., Paleskava, A., Konevega, A.L., Schröder, G.F., Grubmüller, H., Ficner, R., et al. The pathway to GTPase activation of elongation factor SelB on the ribosome. Nature 540 (2016), 80–85 High-resolution cryo-EM visualisation of rRNA modifications in the E. coli ribosome.
    • (2016) Nature , vol.540 , pp. 80-85
    • Fischer, N.1    Neumann, P.2    Bock, L.V.3    Maracci, C.4    Wang, Z.5    Paleskava, A.6    Konevega, A.L.7    Schröder, G.F.8    Grubmüller, H.9    Ficner, R.10
  • 51
    • 85019880566 scopus 로고    scopus 로고
    • Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome
    • Jomaa, A., Fu, Y.H., Boehringer, D., Leibundgut, M., Shan, S.O., Ban, N., Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome. Nat Commun, 8, 2017, 15470.
    • (2017) Nat Commun , vol.8 , pp. 15470
    • Jomaa, A.1    Fu, Y.H.2    Boehringer, D.3    Leibundgut, M.4    Shan, S.O.5    Ban, N.6
  • 52
    • 84955516320 scopus 로고    scopus 로고
    • Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon
    • Jomaa, A., Boehringer, D., Leibundgut, M., Ban, N., Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon. Nat Commun, 7, 2016, 10471.
    • (2016) Nat Commun , vol.7 , pp. 10471
    • Jomaa, A.1    Boehringer, D.2    Leibundgut, M.3    Ban, N.4
  • 58
    • 0037363075 scopus 로고    scopus 로고
    • Does the ribosome translate cancer?
    • Ruggero, D., Pandolfi, P.P., Does the ribosome translate cancer?. Nat Rev Cancer 3 (2003), 179–192.
    • (2003) Nat Rev Cancer , vol.3 , pp. 179-192
    • Ruggero, D.1    Pandolfi, P.P.2
  • 59
    • 9244243139 scopus 로고    scopus 로고
    • Ribosomal crystallography: initiation, peptide bond formation, and amino acid polymerization are hampered by antibiotics
    • Yonath, A., Bashan, A., Ribosomal crystallography: initiation, peptide bond formation, and amino acid polymerization are hampered by antibiotics. Annu Rev Microbiol 58 (2004), 233–251.
    • (2004) Annu Rev Microbiol , vol.58 , pp. 233-251
    • Yonath, A.1    Bashan, A.2
  • 60
    • 33645465733 scopus 로고    scopus 로고
    • Antibiotics and the ribosome
    • Tenson, T., Mankin, A., Antibiotics and the ribosome. Mol Microbiol 59 (2006), 1664–1677.
    • (2006) Mol Microbiol , vol.59 , pp. 1664-1677
    • Tenson, T.1    Mankin, A.2
  • 64
    • 84927930436 scopus 로고    scopus 로고
    • Ribosome. The structure of the human mitochondrial ribosome
    • High-resolution cryo-EM structure of the human ribosome from mitochondria.
    • Amunts, A., Brown, A., Toots, J., Scheres, S.H., Ramakrishnan, V., Ribosome. The structure of the human mitochondrial ribosome. Science 348 (2015), 95–98 High-resolution cryo-EM structure of the human ribosome from mitochondria.
    • (2015) Science , vol.348 , pp. 95-98
    • Amunts, A.1    Brown, A.2    Toots, J.3    Scheres, S.H.4    Ramakrishnan, V.5
  • 67
    • 0034704217 scopus 로고    scopus 로고
    • The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit
    • Brodersen, D.E., Clemons, W.M., Carter, A.P., Morgan-Warren, R.J., Wimberly, B.T., Ramakrishnan, V., The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit. Cell 103 (2000), 1143–1154.
    • (2000) Cell , vol.103 , pp. 1143-1154
    • Brodersen, D.E.1    Clemons, W.M.2    Carter, A.P.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 69
    • 84865837598 scopus 로고    scopus 로고
    • The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA
    • Watkins, N.J., Bohnsack, M.T., The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA. Wiley Interdiscip Rev RNA 3 (2012), 397–414.
    • (2012) Wiley Interdiscip Rev RNA , vol.3 , pp. 397-414
    • Watkins, N.J.1    Bohnsack, M.T.2
  • 70
    • 84942099152 scopus 로고    scopus 로고
    • ‘View from a bridge’: a new perspective on eukaryotic rRNA base modification
    • Sharma, S., Lafontaine, D.L., ‘View from a bridge’: a new perspective on eukaryotic rRNA base modification. Trends Biochem Sci 40 (2015), 560–575.
    • (2015) Trends Biochem Sci , vol.40 , pp. 560-575
    • Sharma, S.1    Lafontaine, D.L.2
  • 71
    • 82355185837 scopus 로고    scopus 로고
    • Comparison of solution conformations and stabilities of modified helix 69 rRNA analogs from bacteria and human
    • Sumita, M., Jiang, J., SantaLucia, J., Chow, C.S., Comparison of solution conformations and stabilities of modified helix 69 rRNA analogs from bacteria and human. Biopolymers 97 (2012), 94–106.
    • (2012) Biopolymers , vol.97 , pp. 94-106
    • Sumita, M.1    Jiang, J.2    SantaLucia, J.3    Chow, C.S.4
  • 72
    • 78649652763 scopus 로고    scopus 로고
    • Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function
    • Demirci, H., Murphy, F., Belardinelli, R., Kelley, A.C., Ramakrishnan, V., Gregory, S.T., Dahlberg, A.E., Jogl, G., Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function. RNA 16 (2010), 2319–2324.
    • (2010) RNA , vol.16 , pp. 2319-2324
    • Demirci, H.1    Murphy, F.2    Belardinelli, R.3    Kelley, A.C.4    Ramakrishnan, V.5    Gregory, S.T.6    Dahlberg, A.E.7    Jogl, G.8
  • 74
    • 84926407700 scopus 로고    scopus 로고
    • Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly
    • Polikanov, Y.S., Melnikov, S.V., Söll, D., Steitz, T.A., Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly. Nat Struct Mol Biol 22 (2015), 342–344.
    • (2015) Nat Struct Mol Biol , vol.22 , pp. 342-344
    • Polikanov, Y.S.1    Melnikov, S.V.2    Söll, D.3    Steitz, T.A.4
  • 78
    • 77956006893 scopus 로고    scopus 로고
    • The three-dimensional organization of polyribosomes in intact human cells
    • Brandt, F., Carlson, L.A., Hartl, F.U., Baumeister, W., Grünewald, K., The three-dimensional organization of polyribosomes in intact human cells. Mol Cell 39 (2010), 560–569.
    • (2010) Mol Cell , vol.39 , pp. 560-569
    • Brandt, F.1    Carlson, L.A.2    Hartl, F.U.3    Baumeister, W.4    Grünewald, K.5
  • 80
    • 84906281181 scopus 로고    scopus 로고
    • Formation of circular polyribosomes on eukaryotic mRNA without cap-structure and poly(A)-tail: a cryo electron tomography study
    • Afonina, Z.A., Myasnikov, A.G., Shirokov, V.A., Klaholz, B.P., Spirin, A.S., Formation of circular polyribosomes on eukaryotic mRNA without cap-structure and poly(A)-tail: a cryo electron tomography study. Nucleic Acids Res 42 (2014), 9461–9469.
    • (2014) Nucleic Acids Res , vol.42 , pp. 9461-9469
    • Afonina, Z.A.1    Myasnikov, A.G.2    Shirokov, V.A.3    Klaholz, B.P.4    Spirin, A.S.5
  • 81
    • 84960488896 scopus 로고    scopus 로고
    • An improved cryo-FIB method for fabrication of frozen hydrated lamella
    • Zhang, J., Ji, G., Huang, X., Xu, W., Sun, F., An improved cryo-FIB method for fabrication of frozen hydrated lamella. J Struct Biol 194 (2016), 218–223.
    • (2016) J Struct Biol , vol.194 , pp. 218-223
    • Zhang, J.1    Ji, G.2    Huang, X.3    Xu, W.4    Sun, F.5
  • 83
    • 85011422346 scopus 로고    scopus 로고
    • Using the Volta phase plate with defocus for cryo-EM single particle analysis
    • High-resolution cryo-EM analysis using contrast-enhancing phase plates.
    • Danev, R., Tegunov, D., Baumeister, W., Using the Volta phase plate with defocus for cryo-EM single particle analysis. Elife, 6, 2017 High-resolution cryo-EM analysis using contrast-enhancing phase plates.
    • (2017) Elife , vol.6
    • Danev, R.1    Tegunov, D.2    Baumeister, W.3
  • 85
    • 84978785861 scopus 로고    scopus 로고
    • An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation
    • First high-resolution cryo electron tomography work in which side-chains can be resolved through sub-tomogram averaging.
    • Schur, F.K., Obr, M., Hagen, W.J., Wan, W., Jakobi, A.J., Kirkpatrick, J.M., Sachse, C., Kräusslich, H.G., Briggs, J.A., An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation. Science 353 (2016), 506–508 First high-resolution cryo electron tomography work in which side-chains can be resolved through sub-tomogram averaging.
    • (2016) Science , vol.353 , pp. 506-508
    • Schur, F.K.1    Obr, M.2    Hagen, W.J.3    Wan, W.4    Jakobi, A.J.5    Kirkpatrick, J.M.6    Sachse, C.7    Kräusslich, H.G.8    Briggs, J.A.9
  • 86
    • 85015268635 scopus 로고    scopus 로고
    • Tools for ligand validation in Coot
    • Emsley, P., Tools for ligand validation in Coot. Acta Crystallogr D: Struct Biol 73 (2017), 203–210.
    • (2017) Acta Crystallogr D: Struct Biol , vol.73 , pp. 203-210
    • Emsley, P.1
  • 88
    • 85028302098 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System Vrp, Schrödinger, LLC.
    • The PyMOL Molecular Graphics System Vrp, Schrödinger, LLC.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.