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Volumn 44, Issue D1, 2016, Pages D396-D403

EMDataBank unified data resource for 3DEM

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CONTROLLED STUDY; DATA ANALYSIS; DATA BASE; DATA PROCESSING; ELECTRON MICROSCOPY; EMDATABANK; INFORMATION CENTER; NONHUMAN; PRIORITY JOURNAL; PROTEIN DATA BANK; THREE DIMENSIONAL ELECTRON MICROSCOPY; VALIDATION STUDY; CHEMISTRY; FACTUAL DATABASE; MACROMOLECULE; MOLECULAR MODEL; PROTEIN DATABASE; THREE DIMENSIONAL IMAGING;

EID: 84976884440     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv1126     Document Type: Article
Times cited : (242)

References (62)
  • 2
    • 84929687804 scopus 로고    scopus 로고
    • Cryo-EM: A unique tool for the visualization of macromolecular complexity
    • Nogales, E. and Scheres, S.H. (2015) Cryo-EM: a unique tool for the visualization of macromolecular complexity. Mol Cell, 58, 677-689.
    • (2015) Mol Cell , vol.58 , pp. 677-689
    • Nogales, E.1    Scheres, S.H.2
  • 3
    • 84939268956 scopus 로고    scopus 로고
    • Overview and future of single particle electron cryomicroscopy
    • Henderson, R. (2015) Overview and future of single particle electron cryomicroscopy. Arch. Biochem. Biophys., 581, 19-24.
    • (2015) Arch. Biochem. Biophys. , vol.581 , pp. 19-24
    • Henderson, R.1
  • 4
    • 84897000286 scopus 로고    scopus 로고
    • Biochemistry. The resolution revolution
    • Kuhlbrandt, W. (2014) Biochemistry. The resolution revolution. Science, 343, 1443-1444.
    • (2014) Science , vol.343 , pp. 1443-1444
    • Kuhlbrandt, W.1
  • 5
    • 84899868547 scopus 로고    scopus 로고
    • Structures of viral membrane proteins by high-resolution cryoEM
    • Zhou, Z.H. (2014) Structures of viral membrane proteins by high-resolution cryoEM. Curr. Opin. Virol., 5, 111-119.
    • (2014) Curr. Opin. Virol. , vol.5 , pp. 111-119
    • Zhou, Z.H.1
  • 6
    • 84930646533 scopus 로고    scopus 로고
    • Cryo-electron microscopy and the amazing race to atomic resolution
    • Binshtein, E. and Ohi, M.D. (2015) Cryo-electron microscopy and the amazing race to atomic resolution. Biochemistry, 54, 3133-3141.
    • (2015) Biochemistry , vol.54 , pp. 3133-3141
    • Binshtein, E.1    Ohi, M.D.2
  • 7
    • 84899908212 scopus 로고    scopus 로고
    • Finding the right fit: Chiseling structures out of cryo-electron microscopy maps
    • Villa, E. and Lasker, K. (2014) Finding the right fit: chiseling structures out of cryo-electron microscopy maps. Curr. Opin. Struct. Biol., 25, 118-125.
    • (2014) Curr. Opin. Struct. Biol. , vol.25 , pp. 118-125
    • Villa, E.1    Lasker, K.2
  • 8
    • 84857925824 scopus 로고    scopus 로고
    • Constructing and validating initial calpha models from subnanometer resolution density maps with pathwalking
    • Baker, M.R., Rees, I., Ludtke, S.J., Chiu, W. and Baker, M.L. (2012) Constructing and validating initial Calpha models from subnanometer resolution density maps with pathwalking. Structure, 20, 450-463.
    • (2012) Structure , vol.20 , pp. 450-463
    • Baker, M.R.1    Rees, I.2    Ludtke, S.J.3    Chiu, W.4    Baker, M.L.5
  • 11
    • 77957263900 scopus 로고    scopus 로고
    • Unified data resource for cryo-EM
    • Lawson, C.L. (2010) Unified data resource for cryo-EM. Methods Enzymol., 483, 73-90.
    • (2010) Methods Enzymol. , vol.483 , pp. 73-90
    • Lawson, C.L.1
  • 12
    • 33846036096 scopus 로고    scopus 로고
    • The worldwide protein data bank (wwPDB): Ensuring a single, uniform archive of PDB data
    • Berman, H., Henrick, K., Nakamura, H. and Markley, J.L. (2007) The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data. Nucleic Acids Res., 35, D301-D303.
    • (2007) Nucleic Acids Res. , vol.35 , pp. D301-D303
    • Berman, H.1    Henrick, K.2    Nakamura, H.3    Markley, J.L.4
  • 13
    • 84862803501 scopus 로고    scopus 로고
    • Direct electron detection yields cryo-EM reconstructions at resolutions beyond 3/4 nyquist frequency
    • Bammes, B.E., Rochat, R.H., Jakana, J., Chen, D.H. and Chiu, W. (2012) Direct electron detection yields cryo-EM reconstructions at resolutions beyond 3/4 Nyquist frequency. J. Struct. Biol., 177, 589-601.
    • (2012) J. Struct. Biol. , vol.177 , pp. 589-601
    • Bammes, B.E.1    Rochat, R.H.2    Jakana, J.3    Chen, D.H.4    Chiu, W.5
  • 14
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X., Mooney, P., Zheng, S., Booth, C.R., Braunfeld, M.B., Gubbens, S., Agard, D.A. and Cheng, Y. (2013) Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods, 10, 584-590.
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.8
  • 15
    • 84923368907 scopus 로고    scopus 로고
    • How cryo-EM is revolutionizing structural biology
    • Bai, X.C., McMullan, G. and Scheres, S.H. (2015) How cryo-EM is revolutionizing structural biology. Trends Biochem. Sci., 40, 49-57.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 49-57
    • Bai, X.C.1    McMullan, G.2    Scheres, S.H.3
  • 16
    • 84924617498 scopus 로고    scopus 로고
    • 2.8 Å resolution reconstruction of the thermoplasma acidophilum 20S proteasome using cryo-electron microscopy
    • Campbell, M.G., Veesler, D., Cheng, A., Potter, C.S. and Carragher, B. (2015) 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy. Elife, 4, doi:10.7554/eLife.06380.
    • (2015) Elife , vol.4
    • Campbell, M.G.1    Veesler, D.2    Cheng, A.3    Potter, C.S.4    Carragher, B.5
  • 17
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor
    • Bartesaghi, A., Merk, A., Banerjee, S., Matthies, D., Wu, X., Milne, J.L. and Subramaniam, S. (2015) 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor. Science, 348, 1147-1151.
    • (2015) Science , vol.348 , pp. 1147-1151
    • Bartesaghi, A.1    Merk, A.2    Banerjee, S.3    Matthies, D.4    Wu, X.5    Milne, J.L.6    Subramaniam, S.7
  • 19
    • 84905080837 scopus 로고    scopus 로고
    • Cryo-EM structure of the plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine
    • Wong, W., Bai, X.C., Brown, A., Fernandez, I.S., Hanssen, E., Condron, M., Tan, Y.H., Baum, J. and Scheres, S.H. (2014) Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine. Elife, 3, doi:10.7554/eLife.03080.
    • (2014) Elife , vol.3
    • Wong, W.1    Bai, X.C.2    Brown, A.3    Fernandez, I.S.4    Hanssen, E.5    Condron, M.6    Tan, Y.H.7    Baum, J.8    Scheres, S.H.9
  • 20
    • 76549094484 scopus 로고    scopus 로고
    • Structure of intact thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor
    • Lau, W.C. and Rubinstein, J.L. (2010) Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor. Proc. Natl. Acad. Sci. U.S.A., 107, 1367-1372.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1367-1372
    • Lau, W.C.1    Rubinstein, J.L.2
  • 23
    • 84939262583 scopus 로고    scopus 로고
    • Three-dimensional reconstruction methods in single particle analysis from transmission electron microscopy data
    • Carazo, J.M., Sorzano, C.O., Oton, J., Marabini, R. and Vargas, J. (2015) Three-dimensional reconstruction methods in Single Particle Analysis from transmission electron microscopy data. Arch. Biochem. Biophys., 581, 39-48.
    • (2015) Arch. Biochem. Biophys. , vol.581 , pp. 39-48
    • Carazo, J.M.1    Sorzano, C.O.2    Oton, J.3    Marabini, R.4    Vargas, J.5
  • 24
    • 84878527131 scopus 로고    scopus 로고
    • Structural biology in situ - The potential of subtomogram averaging
    • Briggs, J.A. (2013) Structural biology in situ-the potential of subtomogram averaging. Curr. Opin. Struct. Biol., 23, 261-267.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 261-267
    • Briggs, J.A.1
  • 25
    • 84939260439 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of helical polymers
    • Egelman, E.H. (2015) Three-dimensional reconstruction of helical polymers. Arch. Biochem. Biophys., 581, 54-58.
    • (2015) Arch. Biochem. Biophys. , vol.581 , pp. 54-58
    • Egelman, E.H.1
  • 26
    • 84872075769 scopus 로고    scopus 로고
    • Introduction to electron crystallography
    • Kuhlbrandt, W. (2013) Introduction to electron crystallography. Methods Mol. Biol., 955, 1-16.
    • (2013) Methods Mol. Biol. , vol.955 , pp. 1-16
    • Kuhlbrandt, W.1
  • 33
    • 0344120702 scopus 로고    scopus 로고
    • EMDep: A web-based system for the deposition and validation of high-resolution electron microscopy macromolecular structural information
    • Henrick, K., Newman, R., Tagari, M. and Chagoyen, M. (2003) EMDep: a web-based system for the deposition and validation of high-resolution electron microscopy macromolecular structural information. J. Struct. Biol., 144, 228-237.
    • (2003) J. Struct. Biol. , vol.144 , pp. 228-237
    • Henrick, K.1    Newman, R.2    Tagari, M.3    Chagoyen, M.4
  • 39
    • 35648968070 scopus 로고    scopus 로고
    • Visualization software for molecular assemblies
    • Goddard, T.D. and Ferrin, T.E. (2007) Visualization software for molecular assemblies. Curr. Opin. Struct. Biol., 17, 587-595.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 587-595
    • Goddard, T.D.1    Ferrin, T.E.2
  • 42
    • 0347123535 scopus 로고    scopus 로고
    • Structure of the integrin alpha2beta1-binding collagen peptide
    • Emsley, J., Knight, C.G., Farndale, R.W. and Barnes, M.J. (2004) Structure of the integrin alpha2beta1-binding collagen peptide. J. Mol. Biol., 335, 1019-1028.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1019-1028
    • Emsley, J.1    Knight, C.G.2    Farndale, R.W.3    Barnes, M.J.4
  • 45
    • 84887223160 scopus 로고    scopus 로고
    • Replication and validation of cryo-EM structures
    • Glaeser, R.M. (2013) Replication and validation of cryo-EM structures. J. Struct. Biol., 184, 379-380.
    • (2013) J. Struct. Biol. , vol.184 , pp. 379-380
    • Glaeser, R.M.1
  • 46
    • 84887271303 scopus 로고    scopus 로고
    • Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise
    • Henderson, R. (2013) Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise. Proc. Natl. Acad. Sci. U. S. A., 110, 18037-18041.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 18037-18041
    • Henderson, R.1
  • 47
    • 84887297231 scopus 로고    scopus 로고
    • Structure of trimeric HIV-1 envelope glycoproteins
    • Subramaniam, S. (2013) Structure of trimeric HIV-1 envelope glycoproteins. Proc. Natl. Acad. Sci. U.S.A., 110, E4172-E4174.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. E4172-E4174
    • Subramaniam, S.1
  • 48
    • 84887282198 scopus 로고    scopus 로고
    • Finding trimeric HIV-1 envelope glycoproteins in random noise
    • van Heel, M. (2013) Finding trimeric HIV-1 envelope glycoproteins in random noise. Proc. Natl. Acad. Sci. U.S.A., 110, E4175-E4177.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. E4175-E4177
    • Van Heel, M.1
  • 53
    • 84926455488 scopus 로고    scopus 로고
    • The difficulty of a fair comparison (editorial)
    • (2015) The difficulty of a fair comparison (editorial). Nat. Methods, 12, 273.
    • (2015) Nat. Methods , vol.12 , pp. 273
  • 54
    • 77957296661 scopus 로고    scopus 로고
    • Resolution measures in molecular electron microscopy
    • Penczek, P.A. (2010) Resolution measures in molecular electron microscopy. Methods Enzymol., 482, 73-100.
    • (2010) Methods Enzymol. , vol.482 , pp. 73-100
    • Penczek, P.A.1
  • 56
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S.H.W. (2012) RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol., 180, 519-530.
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 57
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: Image processing and molecular modeling for electron microscopy
    • Heymann, J.B. and Belnap, D.M. (2007) Bsoft: image processing and molecular modeling for electron microscopy. J. Struct. Biol., 157, 3-18.
    • (2007) J. Struct. Biol. , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 58
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P.B. and Henderson, R. (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol., 333, 721-745.
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 60
    • 84898601534 scopus 로고    scopus 로고
    • Web server for tilt-pair validation of single particle maps from electron cryomicroscopy
    • Wasilewski, S. and Rosenthal, P.B. (2014) Web server for tilt-pair validation of single particle maps from electron cryomicroscopy. J. Struct. Biol., 186, 122-131.
    • (2014) J. Struct. Biol. , vol.186 , pp. 122-131
    • Wasilewski, S.1    Rosenthal, P.B.2
  • 62
    • 0030831667 scopus 로고    scopus 로고
    • Validation of protein models from calpha coordinates alone
    • Kleywegt, G.J. (1997) Validation of protein models from Calpha coordinates alone. J. Mol. Biol., 273, 371-376.
    • (1997) J. Mol. Biol. , vol.273 , pp. 371-376
    • Kleywegt, G.J.1


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