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Volumn 5, Issue , 2014, Pages

Erratum: Protruding knob-like proteins violate local symmetries in an icosahedral marine virus (Nature Communications (2014) 5 (4278) doi: 10.1038/ncomms5278);Protruding knob-like proteins violate local symmetries in an icosahedral marine virus

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; KNOB LIKE PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84903700691     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7040     Document Type: Erratum
Times cited : (20)

References (51)
  • 1
    • 34548792911 scopus 로고    scopus 로고
    • Marine viruses - Major players in the global ecosystem
    • DOI 10.1038/nrmicro1750, PII NRMICRO1750
    • Suttle, C. A. Marine viruses-major players in the global ecosystem. Nat. Rev. Microbiol. 5, 801-812 (2007). (Pubitemid 47423768)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.10 , pp. 801-812
    • Suttle, C.A.1
  • 2
    • 66149151286 scopus 로고    scopus 로고
    • Viruses manipulate the marine environment
    • Rohwer, F. & Thurber, R. V. Viruses manipulate the marine environment. Nature 459, 207-212 (2009).
    • (2009) Nature , vol.459 , pp. 207-212
    • Rohwer, F.1    Thurber, R.V.2
  • 3
    • 79959842126 scopus 로고    scopus 로고
    • Genomic island variability facilitates Prochlorococcus-virus coexistence
    • Avrani, S., Wurtzel, O., Sharon, I., Sorek, R. & Lindell, D. Genomic island variability facilitates Prochlorococcus-virus coexistence. Nature 474, 604-608 (2011).
    • (2011) Nature , vol.474 , pp. 604-608
    • Avrani, S.1    Wurtzel, O.2    Sharon, I.3    Sorek, R.4    Lindell, D.5
  • 4
    • 0034682335 scopus 로고    scopus 로고
    • Lateral gene transfer and the nature of bacterial innovation
    • DOI 10.1038/35012500
    • Ochman, H., Lawrence, J. G. & Groisman, E. A. Lateral gene transfer and the nature of bacterial innovation. Nature 405, 299-304 (2000). (Pubitemid 30337055)
    • (2000) Nature , vol.405 , Issue.6784 , pp. 299-304
    • Ochman, H.1    Lawrence, J.G.2    Grolsman, E.A.3
  • 5
    • 79551715241 scopus 로고    scopus 로고
    • Intracellular assembly of cyanophage Syn5 proceeds through a scaffold-containing procapsid
    • Raytcheva, D. A., Haase-Pettingell, C., Piret, J. M. & King, J. A. Intracellular assembly of cyanophage Syn5 proceeds through a scaffold-containing procapsid. J. Virol. 85, 2406-2415 (2011).
    • (2011) J. Virol. , vol.85 , pp. 2406-2415
    • Raytcheva, D.A.1    Haase-Pettingell, C.2    Piret, J.M.3    King, J.A.4
  • 7
    • 77954384340 scopus 로고    scopus 로고
    • Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus
    • Liu, X. et al. Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus. Nat. Struct. Mol. Biol. 17, 830-836 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 830-836
    • Liu, X.1
  • 8
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999). (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 9
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther, R. A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. Roy. Soc. 261, 221-230 (1971).
    • (1971) Phil. Trans. Roy. Soc. , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 10
    • 34548643898 scopus 로고    scopus 로고
    • Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-path Simulated Annealing optimization algorithm
    • DOI 10.1016/j.jsb.2007.06.009, PII S1047847707001426
    • Liu, X., Jiang, W., Jakana, J. & Chiu, W. Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a multi-path simulated annealing optimization algorithm. J. Struct. Biol. 160, 11-27 (2007). (Pubitemid 47405231)
    • (2007) Journal of Structural Biology , vol.160 , Issue.1 , pp. 11-27
    • Liu, X.1    Jiang, W.2    Jakana, J.3    Chiu, W.4
  • 11
    • 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
  • 12
    • 14844325731 scopus 로고    scopus 로고
    • Electron cryomicroscopy of biological machines at subnanometer resolution
    • DOI 10.1016/j.str.2004.12.016
    • Chiu, W., Baker, M. L., Jiang, W., Dougherty, M. & Schmid, M. F. Electron cryomicroscopy of biological machines at subnanometer resolution. Structure 13, 363-372 (2005). (Pubitemid 40342875)
    • (2005) Structure , vol.13 , Issue.3 , pp. 363-372
    • Chiu, W.1    Baker, M.L.2    Jiang, W.3    Dougherty, M.4    Schmid, M.F.5
  • 13
    • 77957282828 scopus 로고    scopus 로고
    • Analyses of subnanometer resolution cryo-EM density maps
    • Baker, M. L., Baker, M. R., Hryc, C. F. & Dimaio, F. Analyses of subnanometer resolution cryo-EM density maps. Methods Enzymol. 483, 1-29 (2010).
    • (2010) Methods Enzymol. , vol.483 , pp. 1-29
    • Baker, M.L.1    Baker, M.R.2    Hryc, C.F.3    Dimaio, F.4
  • 14
    • 0034703226 scopus 로고    scopus 로고
    • Topologically linked protein rings in the bacteriophage HK97 capsid
    • Wikoff, W. R. et al. Topologically linked protein rings in the bacteriophage HK97 capsid. Science 289, 2129-2133 (2000).
    • (2000) Science , vol.289 , pp. 2129-2133
    • Wikoff, W.R.1
  • 15
    • 84880659509 scopus 로고    scopus 로고
    • Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling
    • Baker, M. L. et al. Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling. Proc. Natl Acad. Sci. USA 110, 12301-12306 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 12301-12306
    • Baker, M.L.1
  • 17
    • 84862871445 scopus 로고    scopus 로고
    • Gorgon and pathwalking: Macromolecular modeling tools for subnanometer resolution density maps
    • Baker, M. L., Baker, M. R., Hryc, C. F., Ju, T. & Chiu, W. Gorgon and pathwalking: macromolecular modeling tools for subnanometer resolution density maps. Biopolymers 97, 655-668 (2012).
    • (2012) Biopolymers , vol.97 , pp. 655-668
    • Baker, M.L.1    Baker, M.R.2    Hryc, C.F.3    Ju, T.4    Chiu, W.5
  • 18
    • 79959919131 scopus 로고    scopus 로고
    • CLICK-topologyindependent comparison of biomolecular 3D structures
    • Nguyen, M. N., Tan, K. P. & Madhusudhan, M. S. CLICK- topologyindependent comparison of biomolecular 3D structures. Nucleic Acids Res. 39, W24-W28 (2011).
    • (2011) Nucleic Acids Res. , vol.39
    • Nguyen, M.N.1    Tan, K.P.2    Madhusudhan, M.S.3
  • 19
    • 77952581453 scopus 로고    scopus 로고
    • Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions
    • Pintilie, G. D., Zhang, J., Goddard, T. D., Chiu, W. & Gossard, D. C. Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions. J. Struct. Biol. 170, 427-438 (2010).
    • (2010) J. Struct. Biol. , vol.170 , pp. 427-438
    • Pintilie, G.D.1    Zhang, J.2    Goddard, T.D.3    Chiu, W.4    Gossard, D.C.5
  • 20
    • 84893481998 scopus 로고    scopus 로고
    • Two novel proteins of Cyanophage Syn5 compose its unusual horn structure
    • Raytcheva, D. A., Haase-Pettingell, C., Piret, J. & King, J. A. Two novel proteins of Cyanophage Syn5 compose its unusual horn structure. J. Virol. 88, 2047-2055 (2014).
    • (2014) J. Virol. , vol.88 , pp. 2047-2055
    • Raytcheva, D.A.1    Haase-Pettingell, C.2    Piret, J.3    King, J.A.4
  • 21
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K. & Jones, D. T. The PSIPRED protein structure prediction server. Bioinformatics 16, 404-405 (2000). (Pubitemid 30417087)
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 22
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole, C., Barber, J. D. & Barton, G. J. The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 36, W197-W201 (2008).
    • (2008) Nucleic Acids Res. , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 23
    • 0032619552 scopus 로고    scopus 로고
    • Protein identification and analysis tools in the ExPASy server
    • Wilkins, M. R. et al. Protein identification and analysis tools in the ExPASy server. Methods Mol. Biol. 112, 531-552 (1999).
    • (1999) Methods Mol. Biol. , vol.112 , pp. 531-552
    • Wilkins, M.R.1
  • 24
    • 3242885293 scopus 로고    scopus 로고
    • The PredictProtein server
    • DOI 10.1093/nar/gkh377
    • Rost, B., Yachdav, G. & Liu, J. The PredictProtein server. Nucleic Acids Res. 32, W321-W326 (2004). (Pubitemid 39004075)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Rost, B.1    Yachdav, G.2    Liu, J.3
  • 25
    • 33846061281 scopus 로고    scopus 로고
    • Identification of Secondary Structure Elements in Intermediate-Resolution Density Maps
    • DOI 10.1016/j.str.2006.11.008, PII S0969212606004722
    • Baker, M. L., Ju, T. & Chiu, W. Identification of secondary structure elements in intermediate-resolution density maps. Structure 15, 7-19 (2007). (Pubitemid 46073771)
    • (2007) Structure , vol.15 , Issue.1 , pp. 7-19
    • Baker, M.L.1    Ju, T.2    Chiu, W.3
  • 29
    • 0037271850 scopus 로고    scopus 로고
    • Viral mimicry of cytokines, chemokines and their receptors
    • DOI 10.1038/nri980
    • Alcami, A. Viral mimicry of cytokines, chemokines and their receptors. Nat. Rev. Immunol. 3, 36-50 (2003). (Pubitemid 37328698)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.1 , pp. 36-50
    • Alcami, A.1
  • 30
    • 77954368167 scopus 로고    scopus 로고
    • Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages
    • Sathaliyawala, T. et al. Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages. Mol. Microbiol. 77, 444-455 (2010).
    • (2010) Mol. Microbiol. , vol.77 , pp. 444-455
    • Sathaliyawala, T.1
  • 31
    • 79961196704 scopus 로고    scopus 로고
    • Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage
    • Fokine, A. et al. Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage. J. Virol. 85, 8141-8148 (2011).
    • (2011) J. Virol. , vol.85 , pp. 8141-8148
    • Fokine, A.1
  • 32
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar, D. L. D. & Klug, A. Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27, 1-24 (1962).
    • (1962) Cold Spring Harb. Symp. Quant. Biol. , vol.27 , pp. 1-24
    • Caspar, D.L.D.1    Klug, A.2
  • 33
    • 84876549863 scopus 로고    scopus 로고
    • Assembly stability and dynamics of virus capsids
    • Mateu, M. G. Assembly, stability and dynamics of virus capsids. Arch. Biochem. Biophys. 531, 65-79 (2012).
    • (2012) Arch. Biochem. Biophys. , vol.531 , pp. 65-79
    • Mateu, M.G.1
  • 34
    • 27244438043 scopus 로고    scopus 로고
    • Mechanical properties of viral capsids
    • Zandi, R. & Reguera, D. Mechanical properties of viral capsids. Phys. Rev. E 72, 021917 (2005).
    • (2005) Phys. Rev. e , vol.72 , pp. 021917
    • Zandi, R.1    Reguera, D.2
  • 36
    • 33646353426 scopus 로고    scopus 로고
    • Highly Discriminatory Binding of Capsid-Cementing Proteins in Bacteriophage L
    • DOI 10.1016/j.str.2006.03.010, PII S0969212606001778
    • Tang, L., Gilcrease, E. B., Casjens, S. R. & Johnson, J. E. Highly discriminatory binding of capsid-cementing proteins in bacteriophage L. Structure 14, 837-845 (2006). (Pubitemid 43674099)
    • (2006) Structure , vol.14 , Issue.5 , pp. 837-845
    • Tang, L.1    Gilcrease, E.B.2    Casjens, S.R.3    Johnson, J.E.4
  • 37
    • 0034608199 scopus 로고    scopus 로고
    • Molecular architecture of bacteriophage T4 capsid: Vertex structure and bimodal binding of the stabilizing accessory protein, Soc
    • DOI 10.1006/viro.2000.0321
    • Iwasaki, K. et al. Molecular architecture of bacteriophage T4 capsid: vertex structure and bimodal binding of the stabilizing accessory protein, Soc. Virol. 271, 321-333 (2000). (Pubitemid 30461310)
    • (2000) Virology , vol.271 , Issue.2 , pp. 321-333
    • Iwasaki, K.1    Trus, B.L.2    Wingfield, P.T.3    Cheng, N.4    Campusano, G.5    Rao, V.B.6    Steven, A.C.7
  • 38
    • 84861540383 scopus 로고    scopus 로고
    • Latest insights on adenovirus structure and assembly
    • San Martín, C. Latest insights on adenovirus structure and assembly. Viruses 4, 847-877 (2012).
    • (2012) Viruses , vol.4 , pp. 847-877
    • San Martín, C.1
  • 39
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks
    • Liu, H. et al. Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science 329, 1038-1043 (2010).
    • (2010) Science , vol.329 , pp. 1038-1043
    • Liu, H.1
  • 40
    • 77956128250 scopus 로고    scopus 로고
    • Crystal structure of human adenovirus at 3.5 A resolution
    • Reddy, V. S., Natchiar, S. K., Stewart, P. L. & Nemerow, G. R. Crystal structure of human adenovirus at 3.5 A resolution. Science 329, 1071-1075 (2010).
    • (2010) Science , vol.329 , pp. 1071-1075
    • Reddy, V.S.1    Natchiar, S.K.2    Stewart, P.L.3    Nemerow, G.R.4
  • 41
    • 79952163890 scopus 로고    scopus 로고
    • Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus
    • Chen, D. H. et al. Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. Proc. Natl Acad. Sci. USA 108, 1355-1360 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 1355-1360
    • Chen, D.H.1
  • 42
    • 84861214424 scopus 로고    scopus 로고
    • How hibernation factors RMF, HPF, and YfiA turn off protein synthesis
    • Polikanov, Y. S., Blaha, G. M. & Steitz, T. A. How hibernation factors RMF, HPF, and YfiA turn off protein synthesis. Science 336, 915 (2012).
    • (2012) Science , vol.336 , pp. 915
    • Polikanov, Y.S.1    Blaha, G.M.2    Steitz, T.A.3
  • 43
    • 0041375471 scopus 로고    scopus 로고
    • Cyanophages infecting the oceanic cyanobacterium Prochlorococcus
    • DOI 10.1038/nature01929
    • Sullivan, M. B., Waterbury, J. B. & Chisholm, S. W. Cyanophages infecting the oceanic cyanobacterium Prochlorococcus. Nature 424, 1047-1051 (2003). (Pubitemid 37064303)
    • (2003) Nature , vol.424 , Issue.6952 , pp. 1047-1051
    • Sullivan, M.B.1    Waterbury, J.B.2    Chisholm, S.W.3
  • 46
    • 0036597231 scopus 로고    scopus 로고
    • Bacteriophages: Evolution of the Majority
    • DOI 10.1006/tpbi.2002.1590
    • Hendrix, R. W. Bacteriophages: evolution of the majority. Theor. Popul. Biol. 61, 471-480 (2002). (Pubitemid 38051050)
    • (2002) Theoretical Population Biology , vol.61 , Issue.4 , pp. 471-480
    • Hendrix, R.W.1
  • 48
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 49
    • 0035906702 scopus 로고    scopus 로고
    • Bridging the information gap: Computational tools for intermediate resolution structure interpretation
    • DOI 10.1006/jmbi.2001.4633
    • Jiang, W., Baker, M. L., Ludtke, S. J. & Chiu, W. Bridging the information gap: computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 308, 1033-1044 (2001). (Pubitemid 32574375)
    • (2001) Journal of Molecular Biology , vol.308 , Issue.5 , pp. 1033-1044
    • Jiang, W.1    Baker, M.L.2    Ludtke, S.J.3    Chiu, W.4
  • 50
    • 84875897533 scopus 로고    scopus 로고
    • Cryo-EM structure of a molluscan hemocyanin suggests its allosteric mechanism
    • Zhang, Q. et al. Cryo-EM structure of a molluscan hemocyanin suggests its allosteric mechanism. Structure 21, 604-613 (2013).
    • (2013) Structure , vol.21 , pp. 604-613
    • Zhang, Q.1
  • 51
    • 79954423522 scopus 로고    scopus 로고
    • Modeling protein structure at near atomic resolutions with Gorgon
    • Baker, M. L. et al. Modeling protein structure at near atomic resolutions with Gorgon. J. Struct. Biol. 174, 360-373 (2011).
    • (2011) J. Struct. Biol. , vol.174 , pp. 360-373
    • Baker, M.L.1


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