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Volumn 482, Issue 7386, 2012, Pages 501-506

Structural basis of highly conserved ribosome recycling in eukaryotes and archaea

Author keywords

[No Author keywords available]

Indexed keywords

ABCE1 PROTEIN; ADENOSINE TRIPHOSPHATASE; PELOTA PROTEIN; RIBOSOME RNA; TRANSLATION TERMINATION FACTOR; UNCLASSIFIED DRUG;

EID: 84857396073     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10829     Document Type: Article
Times cited : (194)

References (57)
  • 1
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • Winzeler, E. A. et al. Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285, 901-906 (1999).
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.A.1
  • 2
    • 31144451118 scopus 로고    scopus 로고
    • Growth and cell survival are unevenly impaired in pixie mutant wing discs
    • Coelho, C. M. et al. Growth and cell survival are unevenly impaired in pixie mutant wing discs. Development 132, 5411-5424 (2005).
    • (2005) Development , vol.132 , pp. 5411-5424
    • Coelho, C.M.1
  • 3
    • 0344234330 scopus 로고    scopus 로고
    • Effects of depletion and overexpression of the Trypanosoma brucei ribonuclease L inhibitor homologue
    • Estevez, A. M., Haile, S., Steinbuchel, M.,Quijada, L. & Clayton, C. Effects of depletion and overexpression of the Trypanosoma brucei ribonuclease L inhibitor homologue. Mol. Biochem. Parasitol. 133, 137-141 (2004).
    • (2004) Mol. Biochem. Parasitol. , vol.133 , pp. 137-141
    • Estevez, A.M.1    Haile, S.2    Steinbuchel, M.3    Quijada, L.4    Clayton, C.5
  • 4
    • 74749098978 scopus 로고    scopus 로고
    • The role of ABCE1 in eukaryotic posttermination ribosomal recycling
    • Pisarev, A. V. et al. The role of ABCE1 in eukaryotic posttermination ribosomal recycling. Mol. Cell 37, 196-210 (2010).
    • (2010) Mol. Cell , vol.37 , pp. 196-210
    • Pisarev, A.V.1
  • 5
    • 79955626576 scopus 로고    scopus 로고
    • Dissociation by Pelota Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
    • Pisareva, V. P., Skabkin, M. A.,Hellen, C. U., Pestova, T. V. & Pisarev, A. V. Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes. EMBO J. 30, 1804-1817 (2011).
    • (2011) EMBO J. , vol.30 , pp. 1804-1817
    • Pisareva, V.P.1    Skabkin, M.A.2    Hellen, C.U.3    Pestova, T.V.4    Pisarev, A.V.5
  • 6
    • 43149119755 scopus 로고    scopus 로고
    • X-ray structure of the completeABCenzyme ABCE1 from Pyrococcus abyssi
    • Karcher, A., Schele,A. & Hopfner, K.-P. X-ray structure of the completeABCenzyme ABCE1 from Pyrococcus abyssi. J. Biol. Chem. 283, 7962-7971 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 7962-7971
    • Karcher, A.1    Schele, A.2    Hopfner, K.-P.3
  • 7
    • 17044401303 scopus 로고    scopus 로고
    • X-ray structure of RLI, an essential twin cassette ABC ATPase involved in ribosome biogenesis and HIV capsid assembly
    • Karcher, A., Buttner, K., Martens, B., Jansen, R. P. & Hopfner, K. P. X-ray structure of RLI, an essential twin cassette ABC ATPase involved in ribosome biogenesis and HIV capsid assembly. Structure 13, 649-659 (2005).
    • (2005) Structure , vol.13 , pp. 649-659
    • Karcher, A.1    Buttner, K.2    Martens, B.3    Jansen, R.P.4    Hopfner, K.P.5
  • 8
    • 79952750280 scopus 로고    scopus 로고
    • Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1
    • Barthelme, D. et al. Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1. Proc. Natl. Acad. Sci. USA 108, 3228-3233 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3228-3233
    • Barthelme, D.1
  • 9
    • 34347209921 scopus 로고    scopus 로고
    • Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette proteinABCE1
    • Barthelme, D. et al. Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette proteinABCE1. J. Biol. Chem. 282, 14598-14607 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 14598-14607
    • Barthelme, D.1
  • 10
    • 4744350877 scopus 로고    scopus 로고
    • The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly
    • Dong, J. et al. The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly. J. Biol. Chem. 279, 42157-42168 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 42157-42168
    • Dong, J.1
  • 11
    • 34447531011 scopus 로고    scopus 로고
    • The essential Drosophila ATP-binding cassette domain protein, Pixie, binds the 40S ribosome in an ATP-dependent manner and is required for translation initiation
    • Andersen, D. & Leevers, S. The essential Drosophila ATP-binding cassette domain protein, Pixie, binds the 40S ribosome in an ATP-dependent manner and is required for translation initiation. J. Biol. Chem. 282, 14752-14760 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 14752-14760
    • Andersen, D.1    Leevers, S.2
  • 12
    • 84855501083 scopus 로고    scopus 로고
    • Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast
    • Shoemaker, C. J. & Green, R. Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast. Proc. Natl Acad. Sci. USA 108, E1392-E1398 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108
    • Shoemaker, C.J.1    Green, R.2
  • 13
    • 77649240878 scopus 로고    scopus 로고
    • The iron-sulphur protein RNase L inhibitor functions in translation termination
    • Khoshnevis, S. et al. The iron-sulphur protein RNase L inhibitor functions in translation termination. EMBO Rep. 11, 214-219 (2010).
    • (2010) EMBO Rep. , vol.11 , pp. 214-219
    • Khoshnevis, S.1
  • 14
    • 33645277360 scopus 로고    scopus 로고
    • Endonucleolytic cleavage of eukaryoticmRNAs with stalls in translation elongation
    • Doma, M. & Parker, R. Endonucleolytic cleavage of eukaryoticmRNAs with stalls in translation elongation. Nature 440, 561-564 (2006).
    • (2006) Nature , vol.440 , pp. 561-564
    • Doma, M.1    Parker, R.2
  • 15
    • 58149178746 scopus 로고    scopus 로고
    • Evolution of nonstop, no-go and nonsensemediated mRNA decay and their termination factor-derived components
    • Atkinson, G., Baldauf, S. & Hauryliuk, V. Evolution of nonstop, no-go and nonsensemediated mRNA decay and their termination factor-derived components. BMC Evol. Biol. 8, 290 (2008).
    • (2008) BMC Evol. Biol. , vol.8 , pp. 290
    • Atkinson, G.1    Baldauf, S.2    Hauryliuk, V.3
  • 16
    • 34748898889 scopus 로고    scopus 로고
    • Structural and functional insights into Dom34, a key component of no-go mRNA decay
    • Lee, H. H. et al. Structural and functional insights into Dom34, a key component of no-go mRNA decay. Mol. Cell 27, 938-950 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 938-950
    • Lee, H.H.1
  • 17
    • 0037155592 scopus 로고    scopus 로고
    • An mRNA surveillance mechanism that eliminates transcripts lacking termination codons
    • Frischmeyer, P. et al. An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science 295, 2258-2261 (2002).
    • (2002) Science , vol.295 , pp. 2258-2261
    • Frischmeyer, P.1
  • 18
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation ofmRNAs lacking a termination codon
    • van Hoof, A., Frischmeyer, P. A., Dietz, H. C. & Parker, R. Exosome-mediated recognition and degradation ofmRNAs lacking a termination codon. Science 295, 2262-2264 (2002).
    • (2002) Science , vol.295 , pp. 2262-2264
    • Van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 19
    • 79958809003 scopus 로고    scopus 로고
    • Structure of the no-gomRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome
    • Becker, T. et al. Structure of the no-gomRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome. Nature Struct. Mol. Biol. 18, 715-720 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 715-720
    • Becker, T.1
  • 20
    • 77957935294 scopus 로고    scopus 로고
    • Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay
    • Shoemaker, C. J., Eyler, D. E. & Green, R. Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay. Science 330, 369-372 (2010).
    • (2010) Science , vol.330 , pp. 369-372
    • Shoemaker, C.J.1    Eyler, D.E.2    Green, R.3
  • 21
    • 0141866883 scopus 로고    scopus 로고
    • Translation termination factor eRF3 mediates mRNA decay throughthe regulationof deadenylation
    • Hosoda, N. et al. Translation termination factor eRF3 mediates mRNA decay throughthe regulationof deadenylation. J. Biol. Chem.278,38287-38291(2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 38287-38291
    • Hosoda, N.1
  • 22
    • 33947268903 scopus 로고    scopus 로고
    • A highly productive system for cell-free protein synthesis using a lysate of the hyperthermophilic archaeon.Thermococcus kodakaraensis
    • Endoh, T., Kanai, T. & Imanaka, T. A highly productive system for cell-free protein synthesis using a lysate of the hyperthermophilic archaeon, Thermococcus kodakaraensis. Appl. Microbiol. Biotechnol. 74, 1153-1161 (2007).
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 1153-1161
    • Endoh, T.1    Kanai, T.2    Imanaka, T.3
  • 23
    • 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
  • 24
    • 78650532579 scopus 로고    scopus 로고
    • Localization of eukaryote-specific ribosomal proteins in a 5.5-A? cryo-EM map of the 80S eukaryotic ribosome
    • Armache, J. P. et al. Localization of eukaryote-specific ribosomal proteins in a 5.5-A? cryo-EM map of the 80S eukaryotic ribosome. Proc. Natl Acad. Sci. USA 107, 19754-19759 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19754-19759
    • Armache, J.P.1
  • 25
    • 78650546283 scopus 로고    scopus 로고
    • Cryo-EMstructure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution
    • Armache, J. P. et al. Cryo-EMstructure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A? resolution. Proc. Natl Acad. Sci. USA 107, 19748-19753 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19748-19753
    • Armache, J.P.1
  • 26
    • 70350588648 scopus 로고    scopus 로고
    • The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA
    • Schmeing, T. M. et al. The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science 326, 688-694 (2009).
    • (2009) Science , vol.326 , pp. 688-694
    • Schmeing, T.M.1
  • 27
    • 70350602056 scopus 로고    scopus 로고
    • The structure of the ribosome with elongation factor G trapped in the posttranslocational state
    • Gao, Y. G. et al. The structure of the ribosome with elongation factor G trapped in the posttranslocational state. Science 326, 694-699 (2009).
    • (2009) Science , vol.326 , pp. 694-699
    • Gao, Y.G.1
  • 28
    • 34247560812 scopus 로고    scopus 로고
    • Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation
    • Taylor, D. J. et al. Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation. EMBO J. 26, 2421-2431 (2007).
    • (2007) EMBO J. , vol.26 , pp. 2421-2431
    • Taylor, D.J.1
  • 29
    • 1842576803 scopus 로고    scopus 로고
    • Domainmovements of elongationfactor eEF2andthe eukaryotic 80S ribosome facilitate tRNA translocation
    • Spahn, C.M.et al.Domainmovements of elongationfactor eEF2andthe eukaryotic 80S ribosome facilitate tRNA translocation. EMBO J. 23, 1008-1019 (2004).
    • (2004) EMBO J. , vol.23 , pp. 1008-1019
    • Spahn, C.M.1
  • 30
    • 59049096394 scopus 로고    scopus 로고
    • Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis
    • Villa, E. et al. Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proc. Natl Acad. Sci. USA 106, 1063-1068 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1063-1068
    • Villa, E.1
  • 31
    • 33847358277 scopus 로고    scopus 로고
    • Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors
    • Connell, S. R. et al. Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors. Mol. Cell 25, 751-764 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 751-764
    • Connell, S.R.1
  • 32
    • 78049291491 scopus 로고    scopus 로고
    • Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1a complex
    • Kobayashi, K. et al. Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1a complex. Proc. Natl Acad. Sci. USA 107, 17575-17579 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 17575-17579
    • Kobayashi, K.1
  • 33
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conservedGGQmotif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • Frolova, L. et al. Mutations in the highly conservedGGQmotif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5, 1014-1020 (1999).
    • (1999) RNA , vol.5 , pp. 1014-1020
    • Frolova, L.1
  • 34
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • Song, H. et al. The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell 100, 311-321 (2000).
    • (2000) Cell , vol.100 , pp. 311-321
    • Song, H.1
  • 35
    • 0037398027 scopus 로고    scopus 로고
    • Rad50/SMC proteins and ABC transporters: Unifying concepts from high-resolution structures
    • Hopfner, K. P. & Tainer, J. A. Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures. Curr. Opin. Struct. Biol. 13, 249-255 (2003).
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 249-255
    • Hopfner, K.P.1    Tainer, J.A.2
  • 36
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to themotor domain froman ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P. C. et al. ATP binding to themotor domain froman ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1
  • 37
    • 61449341855 scopus 로고    scopus 로고
    • Structure and mechanism of ATP-binding cassette transporters
    • Locher, K. P. Structure and mechanism of ATP-binding cassette transporters. Phil. Trans. R. Soc. Lond. B 364, 239-245 (2009).
    • (2009) Phil. Trans. R. Soc. Lond. B , vol.364 , pp. 239-245
    • Locher, K.P.1
  • 38
    • 35348815020 scopus 로고    scopus 로고
    • Recycling of eukaryotic posttermination ribosomal complexes
    • Pisarev, A. V., Hellen, C. U. & Pestova, T. V. Recycling of eukaryotic posttermination ribosomal complexes. Cell 131, 286-299 (2007).
    • (2007) Cell , vol.131 , pp. 286-299
    • Pisarev, A.V.1    Hellen, C.U.2    Pestova, T.V.3
  • 39
    • 20044391418 scopus 로고    scopus 로고
    • Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria
    • Kispal, G. et al. Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria. EMBO J. 24, 589-598 (2005).
    • (2005) EMBO J. , vol.24 , pp. 589-598
    • Kispal, G.1
  • 40
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • Yarunin, A. et al. Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 24, 580-588 (2005).
    • (2005) EMBO J. , vol.24 , pp. 580-588
    • Yarunin, A.1
  • 41
    • 47049098691 scopus 로고    scopus 로고
    • Complementary roles of initiation factor 1 and ribosomerecycling factor in70S ribosomesplitting
    • Pavlov, M. Y., Antoun, A., Lovmar, M. & Ehrenberg, M. Complementary roles of initiation factor 1 and ribosomerecycling factor in70S ribosomesplitting.EMBOJ. 27, 1706-1717 (2008).
    • (2008) EMBO J. , vol.27 , pp. 1706-1717
    • Pavlov, M.Y.1    Antoun, A.2    Lovmar, M.3    Ehrenberg, M.4
  • 42
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • Beckmann, R. et al. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell 107, 361-372 (2001).
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1
  • 43
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 44
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding, J., Biegert, A. & Lupas, A. N. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-W248 (2005).
    • (2005) Nucleic Acids Res. , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 46
    • 33749533435 scopus 로고    scopus 로고
    • Cell-free protein synthesis at hightemperatures using the lysate of a hyperthermophile
    • Endoh, T. et al. Cell-free protein synthesis at hightemperatures using the lysate of a hyperthermophile. J. Biotechnol. 126, 186-195 (2006).
    • (2006) J. Biotechnol. , vol.126 , pp. 186-195
    • Endoh, T.1
  • 47
    • 37249019159 scopus 로고    scopus 로고
    • Effective approaches for the production of heterologous proteins using the Thermococcus kodakaraensis-based translation system
    • Endoh, T., Kanai, T. & Imanaka, T. Effective approaches for the production of heterologous proteins using the Thermococcus kodakaraensis-based translation system. J. Biotechnol. 133, 177-182 (2008).
    • (2008) J. Biotechnol. , vol.133 , pp. 177-182
    • Endoh, T.1    Kanai, T.2    Imanaka, T.3
  • 48
    • 43749122141 scopus 로고    scopus 로고
    • Structure of yeast Dom34: A protein related to translation termination factor eRF1 and involved in no-go decay
    • Graille, M., Chaillet, M. & van Tilbeurgh, H. Structure of yeast Dom34: a protein related to translation termination factor eRF1 and involved in no-go decay. J. Biol. Chem. 283, 7145-7154 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 7145-7154
    • Graille, M.1    Chaillet, M.2    Van Tilbeurgh, H.3
  • 49
    • 34748898889 scopus 로고    scopus 로고
    • Structural and functional insights into Dom34, a key component of no-go mRNA decay
    • Lee, H. H. et al. Structural and functional insights into Dom34, a key component of no-go mRNA decay. Mol. Cell 27, 938-950 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 938-950
    • Lee, H.H.1
  • 50
    • 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. 157, 168-173 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 168-173
    • Chen, J.Z.1    Grigorieff, N.2
  • 51
    • 71549167617 scopus 로고    scopus 로고
    • Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome
    • Becker, T. et al. Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome. Science 326, 1369-1373 (2009).
    • (2009) Science , vol.326 , pp. 1369-1373
    • Becker, T.1
  • 52
    • 77957801203 scopus 로고    scopus 로고
    • Structure of the Dom34-Hbs1 complex and implications for no-go decay
    • Chen, L. et al. Structure of the Dom34-Hbs1 complex and implications for no-go decay. Nature Struct. Mol. Biol. 17, 1233-1240 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 1233-1240
    • Chen, L.1
  • 53
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 54
    • 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
  • 55
    • 36749078686 scopus 로고    scopus 로고
    • Combining efficient conformational sampling with a deformable elastic networkmodel facilitates structure refinement at low resolution
    • Schroer, G. F., Brunger, A. T. & Levitt, M. Combining efficient conformational sampling with a deformable elastic networkmodel facilitates structure refinement at low resolution. Structure 15, 1630-1641 (2007).
    • (2007) Structure , vol.15 , pp. 1630-1641
    • Schroer, G.F.1    Brunger, A.T.2    Levitt, M.3
  • 56
    • 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 16, 673-683 (2008).
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 57
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781-1802 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.