메뉴 건너뛰기




Volumn 483, Issue C, 2010, Pages 161-177

Multiparticle Cryo-EM of Ribosomes

Author keywords

[No Author keywords available]

Indexed keywords

MOCIMYCIN; RIBOSOME PROTEIN;

EID: 77957255312     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)83008-3     Document Type: Chapter
Times cited : (45)

References (41)
  • 1
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: Preparing the next generation of molecular biologists. Cell 1998, 92:291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 2
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • Allen G.S., Zavialov A., Gursky R., Ehrenberg M., Frank J. The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 2005, 121:703-712.
    • (2005) Cell , vol.121 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 3
    • 33845449481 scopus 로고    scopus 로고
    • SIGNATURE: A single-particle selection system for molecular electron microscopy
    • Chen J.Z., Grigorieff N. SIGNATURE: A single-particle selection system for molecular electron microscopy. J. Struct. Biol. 2007, 157:168-173.
    • (2007) J. Struct. Biol. , vol.157 , pp. 168-173
    • Chen, J.Z.1    Grigorieff, N.2
  • 7
    • 77449108419 scopus 로고    scopus 로고
    • Single-particle reconstruction of biological macromolecules in electron microscopy-30 years
    • Frank J. Single-particle reconstruction of biological macromolecules in electron microscopy-30 years. Q. Rev. Biophys. 2009, 42:139-158.
    • (2009) Q. Rev. Biophys. , vol.42 , pp. 139-158
    • Frank, J.1
  • 8
    • 33845346092 scopus 로고    scopus 로고
    • The ribosome and the mechanism of protein synthesis
    • Frank J., Spahn C.M.T. The ribosome and the mechanism of protein synthesis. Rep. Prog. Phys. 2006, 69:1383-1417.
    • (2006) Rep. Prog. Phys. , vol.69 , pp. 1383-1417
    • Frank, J.1    Spahn, C.M.T.2
  • 9
    • 0026045381 scopus 로고
    • Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: The distribution of ribosomal RNA
    • Frank J., Penczek P.A., Grassucci R.A., Srivastava S. Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: The distribution of ribosomal RNA. J. Cell Biol. 1991, 115:597-605.
    • (1991) J. Cell Biol. , vol.115 , pp. 597-605
    • Frank, J.1    Penczek, P.A.2    Grassucci, R.A.3    Srivastava, S.4
  • 10
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P.A., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 1996, 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.A.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 13
    • 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. 2004, 147:283-290.
    • (2004) J. Struct. Biol. , vol.147 , pp. 283-290
    • Gao, H.1    Valle, M.2    Ehrenberg, M.3    Frank, J.4
  • 14
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M., Becker T., Pool M.R., Spahn C.M.T., Grassucci R.A., Frank J., Beckmann R. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 2004, 427:806-814.
    • (2004) Nature , vol.427 , pp. 806-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.T.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 15
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • Hellen C.U.T., Sarnow P. Internal ribosome entry sites in eukaryotic mRNA molecules. Genes Dev. 2001, 15:1593-1612.
    • (2001) Genes Dev. , vol.15 , pp. 1593-1612
    • Hellen, C.U.T.1    Sarnow, P.2
  • 17
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell J.A., Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 2003, 142:334-347.
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 19
    • 58749105833 scopus 로고    scopus 로고
    • Flexible fitting of high-resolution X-ray structures into cryoelectron microscopy maps using biased molecular dynamics simulations
    • Orzechowski M., Tama F. Flexible fitting of high-resolution X-ray structures into cryoelectron microscopy maps using biased molecular dynamics simulations. Biophys. J. 2008, 95:5692-5705.
    • (2008) Biophys. J. , vol.95 , pp. 5692-5705
    • Orzechowski, M.1    Tama, F.2
  • 20
    • 0028393194 scopus 로고
    • The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles
    • Penczek P.A., Grassucci R.A., Frank J. The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles. Ultramicroscopy 1994, 53:251-270.
    • (1994) Ultramicroscopy , vol.53 , pp. 251-270
    • Penczek, P.A.1    Grassucci, R.A.2    Frank, J.3
  • 21
    • 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.T. A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation. J. Struct. Biol. 2006, 154:184-194.
    • (2006) J. Struct. Biol. , vol.154 , pp. 184-194
    • Penczek, P.A.1    Frank, J.2    Spahn, C.M.T.3
  • 23
    • 33845335508 scopus 로고    scopus 로고
    • Structural basis for ribosome recruitment and manipulation by a viral IRES RNA
    • Pfingsten J.S., Costantino D., Kieft J.S. Structural basis for ribosome recruitment and manipulation by a viral IRES RNA. Science 2006, 314:1450-1454.
    • (2006) Science , vol.314 , pp. 1450-1454
    • Pfingsten, J.S.1    Costantino, D.2    Kieft, J.S.3
  • 25
    • 0035782663 scopus 로고    scopus 로고
    • Fourier amplitude decay of electron cryomicroscopic images of single particles and effects on structure determination
    • Saad A., Ludtke S.J., Jakana J., Rixon F.J., Tsuruta H., Chiu W. Fourier amplitude decay of electron cryomicroscopic images of single particles and effects on structure determination. J. Struct. Biol. 2001, 133:32-42.
    • (2001) J. Struct. Biol. , vol.133 , pp. 32-42
    • Saad, A.1    Ludtke, S.J.2    Jakana, J.3    Rixon, F.J.4    Tsuruta, H.5    Chiu, W.6
  • 27
    • 70350654363 scopus 로고    scopus 로고
    • What recent ribosome structures have revealed about the mechanism of translation
    • Schmeing T.M., Ramakrishnan V. What recent ribosome structures have revealed about the mechanism of translation. Nature 2009, 461:1234-1242.
    • (2009) Nature , vol.461 , pp. 1234-1242
    • Schmeing, T.M.1    Ramakrishnan, V.2
  • 32
    • 70349884311 scopus 로고    scopus 로고
    • Exploring conformational modes of macromolecular assemblies by multiparticle cryo-EM
    • Spahn C.M.T., Penczek P.A. Exploring conformational modes of macromolecular assemblies by multiparticle cryo-EM. Curr. Opin. Struct. Biol. 2009, 19:623-631.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 623-631
    • Spahn, C.M.T.1    Penczek, P.A.2
  • 34
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco L.G., Villa E., Mitra K., Frank J., Schulten K. Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 2008, 16:673-683.
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 38
    • 0026566945 scopus 로고
    • A brief look at imaging and contrast transfer
    • Wade R.H. A brief look at imaging and contrast transfer. Ultramicroscopy 1992, 46:145-156.
    • (1992) Ultramicroscopy , vol.46 , pp. 145-156
    • Wade, R.H.1
  • 39
    • 0017541997 scopus 로고
    • Electron microscopic transfer functions for partially coherent axial illumination and chromatic defocus spread
    • Wade R.H., Frank J. Electron microscopic transfer functions for partially coherent axial illumination and chromatic defocus spread. Optik 1977, 49:81-92.
    • (1977) Optik , vol.49 , pp. 81-92
    • Wade, R.H.1    Frank, J.2
  • 40
    • 63449135082 scopus 로고    scopus 로고
    • An all-atom structure-based potential for proteins: Bridging minimal models with all-atom empirical forcefields
    • Whitford P.C., Noel J.K., Gosavi S., Schug A., Sanbonmatsu K.Y., Onuchic J.N. An all-atom structure-based potential for proteins: Bridging minimal models with all-atom empirical forcefields. Proteins 2009, 75:430-441.
    • (2009) Proteins , vol.75 , pp. 430-441
    • Whitford, P.C.1    Noel, J.K.2    Gosavi, S.3    Schug, A.4    Sanbonmatsu, K.Y.5    Onuchic, J.N.6
  • 41
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., McCammon J.A. Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 1999, 125:185-195.
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.