메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages

Structural basis of GM-CSF and IL-2 sequestration by the viral decoy receptor GIF

Author keywords

[No Author keywords available]

Indexed keywords

DECOY RECEPTOR GIF; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 2; UNCLASSIFIED DRUG; VIRAL PROTEIN; GIF PROTEIN, ORF VIRUS; MULTIPROTEIN COMPLEX; PROTEIN BINDING;

EID: 84994432322     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms13228     Document Type: Article
Times cited : (15)

References (80)
  • 2
    • 30144433012 scopus 로고    scopus 로고
    • Viral strategies for evading antiviral cellular immune responses of the host
    • Iannello, A. et al. Viral strategies for evading antiviral cellular immune responses of the host. J. Leukoc. Biol. 79, 16-35 (2006).
    • (2006) J. Leukoc. Biol , vol.79 , pp. 16-35
    • Iannello, A.1
  • 3
    • 0037271850 scopus 로고    scopus 로고
    • Viral mimicry of cytokines, chemokines and their receptors
    • Alcami, A. Viral mimicry of cytokines, chemokines and their receptors. Nat. Rev. Immunol. 3, 36-50 (2003).
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 36-50
    • Alcami, A.1
  • 4
    • 84867411780 scopus 로고    scopus 로고
    • Subversion of cytokine networks by virally encoded decoy receptors
    • Epperson, M. L., Lee, C. A. & Fremont, D. H. Subversion of cytokine networks by virally encoded decoy receptors. Immunol. Rev. 250, 199-215 (2012).
    • (2012) Immunol. Rev , vol.250 , pp. 199-215
    • Epperson, M.L.1    Lee, C.A.2    Fremont, D.H.3
  • 5
    • 84959542315 scopus 로고    scopus 로고
    • Immune modulation by virus-encoded chemokine binding proteins
    • Heidarieh, H., Hernaez, B. & Alcami, A. Immune modulation by virus-encoded chemokine binding proteins. Virus Res. 209, 67-75 (2015).
    • (2015) Virus Res , vol.209 , pp. 67-75
    • Heidarieh, H.1    Hernaez, B.2    Alcami, A.3
  • 6
    • 0029930262 scopus 로고    scopus 로고
    • Cytolytic activity and associated serine protease expression by skin and afferent lymph CD8+ T cells during orf virus reinfection
    • Haig, D. M., Hutchinson, G., Thomson, J., Yirrell, D. & Reid, H. W. Cytolytic activity and associated serine protease expression by skin and afferent lymph CD8+ T cells during orf virus reinfection. J. Gen. Virol. 77, 953-961 (1996).
    • (1996) J. Gen. Virol , vol.77 , pp. 953-961
    • Haig, D.M.1    Hutchinson, G.2    Thomson, J.3    Yirrell, D.4    Reid, H.W.5
  • 9
    • 38049005984 scopus 로고    scopus 로고
    • Giant and recurrent orf virus infection in a renal transplant recipient treated with imiquimod
    • Ara, M. et al. Giant and recurrent orf virus infection in a renal transplant recipient treated with imiquimod. J. Am. Acad. Dermatol. 58, S39-S40 (2008).
    • (2008) J. Am. Acad. Dermatol , vol.58 , pp. S39-S40
    • Ara, M.1
  • 10
    • 33847186307 scopus 로고    scopus 로고
    • Antiviral activity of HPMPC (cidofovir) against orf virus infected lambs
    • Scagliarini, A. et al. Antiviral activity of HPMPC (cidofovir) against orf virus infected lambs. Antiviral Res. 73, 169-174 (2007).
    • (2007) Antiviral Res , vol.73 , pp. 169-174
    • Scagliarini, A.1
  • 12
    • 84995132680 scopus 로고
    • The B and T cell responses to Orf virus infection of ovine skin
    • Jenkinson, D. M., Hutchison, G. & Reid, H. W. The B and T cell responses to Orf virus infection of ovine skin. Vet. Dermatol. 3, 57-64 (1992).
    • (1992) Vet. Dermatol , vol.3 , pp. 57-64
    • Jenkinson, D.M.1    Hutchison, G.2    Reid, H.W.3
  • 13
    • 0029988505 scopus 로고    scopus 로고
    • Phenotypic characterisation of the dendritic cells accumulating in ovine dermis following primary and secondary orf virus infections
    • Lear, A., Hutchison, G., Reid, H. W., Norval, M. & Haig, D. M. Phenotypic characterisation of the dendritic cells accumulating in ovine dermis following primary and secondary orf virus infections. Eur. J. Dermatol. 6, 135-140 (1996).
    • (1996) Eur. J. Dermatol , vol.6 , pp. 135-140
    • Lear, A.1    Hutchison, G.2    Reid, H.W.3    Norval, M.4    Haig, D.M.5
  • 14
    • 0036711438 scopus 로고    scopus 로고
    • Immunity and counter-immunity during infection with the parapoxvirus orf virus
    • Haig, D. M. & McInnes, C. J. Immunity and counter-immunity during infection with the parapoxvirus orf virus. Virus Res. 88, 3-16 (2002).
    • (2002) Virus Res , vol.88 , pp. 3-16
    • Haig, D.M.1    McInnes, C.J.2
  • 15
    • 0032744451 scopus 로고    scopus 로고
    • Immunomodulation by virulence proteins of the parapoxvirus orf virus
    • Haig, D. M. & Fleming, S. Immunomodulation by virulence proteins of the parapoxvirus orf virus. Vet. Immunol. mmunopathol. 72, 81-86 (1999).
    • (1999) Vet. Immunol. Mmunopathol , vol.72 , pp. 81-86
    • Haig, D.M.1    Fleming, S.2
  • 16
    • 0345598122 scopus 로고    scopus 로고
    • Analysis of an orf virus chemokine-binding protein: Shifting ligand specificities among a family of poxvirus viroceptors
    • Seet, B. T. et al. Analysis of an orf virus chemokine-binding protein: shifting ligand specificities among a family of poxvirus viroceptors. Proc. Natl Acad. Sci. USA 100, 15137-15142 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15137-15142
    • Seet, B.T.1
  • 17
    • 0036891259 scopus 로고    scopus 로고
    • A comparison of the anti-inflammatory and immuno-stimulatory activities of orf virus and ovine interleukin-10
    • Haig, D. M. et al. A comparison of the anti-inflammatory and immuno-stimulatory activities of orf virus and ovine interleukin-10. Virus Res. 90, 303-316 (2002).
    • (2002) Virus Res , vol.90 , pp. 303-316
    • Haig, D.M.1
  • 18
    • 0027979253 scopus 로고
    • Homologs of vascular endothelial growth factor are encoded by the poxvirus orf virus
    • Lyttle, D. J., Fraser, K. M., Fleming, S. B., Mercer, A. A. & Robinson, A. J. Homologs of vascular endothelial growth factor are encoded by the poxvirus orf virus. J. Virol. 68, 84-92 (1994).
    • (1994) J. Virol , vol.68 , pp. 84-92
    • Lyttle, D.J.1    Fraser, K.M.2    Fleming, S.B.3    Mercer, A.A.4    Robinson, A.J.5
  • 19
    • 0031916702 scopus 로고    scopus 로고
    • The orf virus OV20.0L gene product is involved in interferon resistance and inhibits an interferon-inducible, double-stranded RNAdependent kinase
    • Haig, D. M. et al. The orf virus OV20.0L gene product is involved in interferon resistance and inhibits an interferon-inducible, double-stranded RNAdependent kinase. Immunology 93, 335-340 (1998).
    • (1998) Immunology , vol.93 , pp. 335-340
    • Haig, D.M.1
  • 20
    • 0033958428 scopus 로고    scopus 로고
    • Orf virus encodes a novel secreted protein inhibitor of granulocyte-macrophage colony-stimulating factor and interleukin-2
    • Deane, D. et al. Orf virus encodes a novel secreted protein inhibitor of granulocyte-macrophage colony-stimulating factor and interleukin-2. J. Virol. 74, 1313-1320 (2000).
    • (2000) J. Virol , vol.74 , pp. 1313-1320
    • Deane, D.1
  • 21
    • 46249090513 scopus 로고    scopus 로고
    • Colony-stimulating factors in inflammation and autoimmunity
    • Hamilton, J. A. Colony-stimulating factors in inflammation and autoimmunity. Nat. Rev. Immunol. 8, 533-544 (2008).
    • (2008) Nat. Rev. Immunol , vol.8 , pp. 533-544
    • Hamilton, J.A.1
  • 22
    • 4744357460 scopus 로고    scopus 로고
    • Overview of interleukin-2 function, production and clinical applications
    • Gaffen, S. L. & Liu, K. D. Overview of interleukin-2 function, production and clinical applications. Cytokine 28, 109-123 (2004).
    • (2004) Cytokine , vol.28 , pp. 109-123
    • Gaffen, S.L.1    Liu, K.D.2
  • 23
    • 84857646605 scopus 로고    scopus 로고
    • The role of interleukin-2 during homeostasis and activation of the immune system
    • Boyman, O. & Sprent, J. The role of interleukin-2 during homeostasis and activation of the immune system. Nat. Rev. Immunol. 12, 180-190 (2012).
    • (2012) Nat. Rev. Immunol , vol.12 , pp. 180-190
    • Boyman, O.1    Sprent, J.2
  • 24
    • 0031964453 scopus 로고    scopus 로고
    • Blockade of chemokine activity by a soluble chemokine binding protein from vaccinia virus
    • Alcami, A., Symons, J. A., Collins, P. D., Williams, T. J. & Smith, G. L. Blockade of chemokine activity by a soluble chemokine binding protein from vaccinia virus. J. Immunol. 160, 624-633 (1998).
    • (1998) J. Immunol , vol.160 , pp. 624-633
    • Alcami, A.1    Symons, J.A.2    Collins, P.D.3    Williams, T.J.4    Smith, G.L.5
  • 25
    • 0342506481 scopus 로고    scopus 로고
    • Poxvirus genomes encode a secreted, soluble protein that preferentially inhibits beta chemokine activity yet lacks sequence homology to known chemokine receptors
    • Smith, C. A. et al. Poxvirus genomes encode a secreted, soluble protein that preferentially inhibits beta chemokine activity yet lacks sequence homology to known chemokine receptors. Virology 236, 316-327 (1997).
    • (1997) Virology , vol.236 , pp. 316-327
    • Smith, C.A.1
  • 26
    • 0001917235 scopus 로고    scopus 로고
    • The T1/35kDa family of poxvirus-secreted proteins bind chemokines and modulate leukocyte influx into virus-infected tissues
    • Graham, K. A. et al. The T1/35kDa family of poxvirus-secreted proteins bind chemokines and modulate leukocyte influx into virus-infected tissues. Virology 229, 12-24 (1997).
    • (1997) Virology , vol.229 , pp. 12-24
    • Graham, K.A.1
  • 27
    • 38949213433 scopus 로고    scopus 로고
    • Structure and function of A41, a vaccinia virus chemokine binding protein
    • Bahar, M. W. et al. Structure and function of A41, a vaccinia virus chemokine binding protein. PLoS Pathog. 4, e5 (2008).
    • (2008) PLoS Pathog , vol.4 , pp. e5
    • Bahar, M.W.1
  • 28
    • 0033607216 scopus 로고    scopus 로고
    • Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus
    • Carfi, A., Smith, C. A., Smolak, P. J., McGrew, J. & Wiley, D. C. Structure of a soluble secreted chemokine inhibitor vCCI (p35) from cowpox virus. Proc. Natl Acad. Sci. USA 96, 12379-12383 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12379-12383
    • Carfi, A.1    Smith, C.A.2    Smolak, P.J.3    McGrew, J.4    Wiley, D.C.5
  • 29
    • 33749011677 scopus 로고    scopus 로고
    • Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta
    • Zhang, L. et al. Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta. Proc. Natl Acad. Sci. USA 103, 13985-13990 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 13985-13990
    • Zhang, L.1
  • 30
    • 33746215102 scopus 로고    scopus 로고
    • Structural determinants of chemokine binding by an Ectromelia virus-encoded decoy receptor
    • Arnold, P. L. & Fremont, D. H. Structural determinants of chemokine binding by an Ectromelia virus-encoded decoy receptor. J. Virol. 80, 7439-7449 (2006).
    • (2006) J. Virol , vol.80 , pp. 7439-7449
    • Arnold, P.L.1    Fremont, D.H.2
  • 31
    • 84936847326 scopus 로고    scopus 로고
    • Structures of Orf virus chemokine binding protein in complex with host chemokines reveal clues to broad binding specificity
    • Counago, R. M. et al. Structures of Orf virus chemokine binding protein in complex with host chemokines reveal clues to broad binding specificity. Structure 23, 1199-1213 (2015).
    • (2015) Structure , vol.23 , pp. 1199-1213
    • Counago, R.M.1
  • 32
    • 48449102092 scopus 로고    scopus 로고
    • The structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation
    • Hansen, G. et al. The structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation. Cell 134, 496-507 (2008).
    • (2008) Cell , vol.134 , pp. 496-507
    • Hansen, G.1
  • 33
    • 84980002167 scopus 로고    scopus 로고
    • Conformational changes in the GM-CSF receptor suggest a molecular mechanism for affinity conversion and receptor signaling
    • Broughton, S. E. et al. Conformational changes in the GM-CSF receptor suggest a molecular mechanism for affinity conversion and receptor signaling. Structure 24, 1271-1281 (2016).
    • (2016) Structure , vol.24 , pp. 1271-1281
    • Broughton, S.E.1
  • 34
    • 0033607540 scopus 로고    scopus 로고
    • Molecular determinants of the granulocyte-macrophage colony-stimulating factor receptor complex assembly
    • Haman, A. et al. Molecular determinants of the granulocyte-macrophage colony-stimulating factor receptor complex assembly. J. Biol. Chem. 274, 34155-34163 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 34155-34163
    • Haman, A.1
  • 35
    • 0030960120 scopus 로고    scopus 로고
    • Crucial role of the residue R280 at the F0-G0 loop of the human granulocyte/macrophage colony-stimulating factor receptor alpha chain for ligand recognition
    • Rajotte, D. et al. Crucial role of the residue R280 at the F0-G0 loop of the human granulocyte/macrophage colony-stimulating factor receptor alpha chain for ligand recognition. J. Exp. Med. 185, 1939-1950 (1997).
    • (1997) J. Exp. Med , vol.185 , pp. 1939-1950
    • Rajotte, D.1
  • 36
    • 35848929278 scopus 로고    scopus 로고
    • Cowpox virus exploits the endoplasmic reticulum retention pathway to inhibit MHC class i transport to the cell surface
    • Byun, M., Wang, X., Pak, M., Hansen, T. H. & Yokoyama, W. M. Cowpox virus exploits the endoplasmic reticulum retention pathway to inhibit MHC class I transport to the cell surface. Cell Host Microbe 2, 306-315 (2007).
    • (2007) Cell Host Microbe , vol.2 , pp. 306-315
    • Byun, M.1    Wang, X.2    Pak, M.3    Hansen, T.H.4    Yokoyama, W.M.5
  • 37
    • 79960617916 scopus 로고    scopus 로고
    • Structural principles within the human-virus protein-protein interaction network
    • Franzosa, E. A. & Xia, Y. Structural principles within the human-virus protein-protein interaction network. Proc. Natl Acad. Sci. USA 108, 10538-10543 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 10538-10543
    • Franzosa, E.A.1    Xia, Y.2
  • 38
    • 27944505913 scopus 로고    scopus 로고
    • Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors
    • Wang, X., Rickert, M. & Garcia, K. C. Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors. Science 310, 1159-1163 (2005).
    • (2005) Science , vol.310 , pp. 1159-1163
    • Wang, X.1    Rickert, M.2    Garcia, K.C.3
  • 39
    • 84862776988 scopus 로고    scopus 로고
    • Exploiting a natural conformational switch to engineer an interleukin-2 'superkine
    • Levin, A. M. et al. Exploiting a natural conformational switch to engineer an interleukin-2 'superkine'. Nature 484, 529-533 (2012).
    • (2012) Nature , vol.484 , pp. 529-533
    • Levin, A.M.1
  • 40
    • 84941585430 scopus 로고    scopus 로고
    • Structural conservation and functional diversity of the poxvirus immune evasion (PIE) domain superfamily
    • Nelson, C. A., Epperson, M. L., Singh, S., Elliott, J. I. & Fremont, D. H. Structural conservation and functional diversity of the poxvirus immune evasion (PIE) domain superfamily. Viruses 7, 4878-4898 (2015).
    • (2015) Viruses , vol.7 , pp. 4878-4898
    • Nelson, C.A.1    Epperson, M.L.2    Singh, S.3    Elliott, J.I.4    Fremont, D.H.5
  • 41
    • 84866109628 scopus 로고    scopus 로고
    • Allosteric competitive inactivation of hematopoietic CSF-1 signaling by the viral decoy receptor BARF1
    • Elegheert, J. et al. Allosteric competitive inactivation of hematopoietic CSF-1 signaling by the viral decoy receptor BARF1. Nat. Struct. Mol. Biol. 19, 938-947 (2012).
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 938-947
    • Elegheert, J.1
  • 42
    • 70350754207 scopus 로고    scopus 로고
    • Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein
    • Yang, Z., West, A. P. & Bjorkman, P. J. Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein. Nat. Struct. Mol. Biol. 16, 1189-1191 (2009).
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 1189-1191
    • Yang, Z.1    West, A.P.2    Bjorkman, P.J.3
  • 43
    • 33645819161 scopus 로고    scopus 로고
    • A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus
    • Alejo, A. et al. A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus. Proc. Natl Acad. Sci. USA 103, 5995-6000 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 5995-6000
    • Alejo, A.1
  • 44
    • 79960963198 scopus 로고    scopus 로고
    • Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor
    • Xue, X. et al. Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor. PLoS Pathog. 7, e1002162 (2011).
    • (2011) PLoS Pathog , vol.7
    • Xue, X.1
  • 46
    • 18744401050 scopus 로고    scopus 로고
    • Structural basis of chemokine sequestration by a herpesvirus decoy receptor
    • Alexander, J. M. et al. Structural basis of chemokine sequestration by a herpesvirus decoy receptor. Cell 111, 343-356 (2002).
    • (2002) Cell , vol.111 , pp. 343-356
    • Alexander, J.M.1
  • 47
    • 33846164793 scopus 로고    scopus 로고
    • Properties of the recombinant TNF-binding proteins from variola, monkeypox, and cowpox viruses are different
    • Gileva, I. P. et al. Properties of the recombinant TNF-binding proteins from variola, monkeypox, and cowpox viruses are different. Biochim. Biophys. Acta 1764, 1710-1718 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1710-1718
    • Gileva, I.P.1
  • 48
    • 70350754207 scopus 로고    scopus 로고
    • Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein
    • Yang, Z., West, Jr. A. P. & Bjorkman, P. J. Crystal structure of TNFalpha complexed with a poxvirus MHC-related TNF binding protein. Nat. Struct. Mol. Biol. 16, 1189-1191 (2009).
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 1189-1191
    • Yang, Z.1    West, A.P.2    Bjorkman, P.J.3
  • 49
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • Aricescu, A. R., Lu, W. & Jones, E. Y. A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr. D Biol. Crystallogr. 62, 1243-1250 (2006).
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 50
    • 63449093707 scopus 로고    scopus 로고
    • Efficient production of bioactive recombinant human Flt3 ligand in E. Coli
    • Verstraete, K. et al. Efficient production of bioactive recombinant human Flt3 ligand in E. coli. Protein J. 28, 57-65 (2009).
    • (2009) Protein J , vol.28 , pp. 57-65
    • Verstraete, K.1
  • 51
    • 76449099287 scopus 로고    scopus 로고
    • Xds. Acta Crystallogr
    • Kabsch, W. Xds. Acta Crystallogr. D Biol. Crystallogr. 66, 125-132 (2010).
    • (2010) D Biol. Crystallogr , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 52
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 53
    • 0029805606 scopus 로고    scopus 로고
    • Refined crystal structure and mutagenesis of human granulocyte-macrophage colony-stimulating factor
    • Rozwarski, D. A., Diederichs, K., Hecht, R., Boone, T. & Karplus, P. A. Refined crystal structure and mutagenesis of human granulocyte-macrophage colony-stimulating factor. Proteins 26, 304-313 (1996).
    • (1996) Proteins , vol.26 , pp. 304-313
    • Rozwarski, D.A.1    Diederichs, K.2    Hecht, R.3    Boone, T.4    Karplus, P.A.5
  • 54
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 55
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong, M. et al. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 103, 8060-8065 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8060-8065
    • Strong, M.1
  • 56
    • 14844321328 scopus 로고    scopus 로고
    • Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT
    • Blanc, E. et al. Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT. Acta Crystallogr. D Biol. Crystallogr. 60, 2210-2221 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2210-2221
    • Blanc, E.1
  • 57
    • 40649128835 scopus 로고    scopus 로고
    • Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin
    • Howarth, M. & Ting, A. Y. Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin. Nat. Protoc. 3, 534-545 (2008).
    • (2008) Nat. Protoc , vol.3 , pp. 534-545
    • Howarth, M.1    Ting, A.Y.2
  • 58
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 59
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 60
    • 84928379119 scopus 로고    scopus 로고
    • A primer to single-particle cryo-electron microscopy
    • Cheng, Y., Grigorieff, N., Penczek, P. A. & Walz, T. A primer to single-particle cryo-electron microscopy. Cell 161, 438-449 (2015).
    • (2015) Cell , vol.161 , pp. 438-449
    • Cheng, Y.1    Grigorieff, N.2    Penczek, P.A.3    Walz, T.4
  • 63
    • 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. 142, 334-347 (2003).
    • (2003) J. Struct. Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 64
    • 43049111744 scopus 로고    scopus 로고
    • Fast projection matching for cryo-electron microscopy image reconstruction
    • Estrozi, L. F. & Navaza, J. Fast projection matching for cryo-electron microscopy image reconstruction. J. Struct. Biol. 162, 324-334 (2008).
    • (2008) J. Struct. Biol , vol.162 , pp. 324-334
    • Estrozi, L.F.1    Navaza, J.2
  • 65
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • Eswar, N. et al. Comparative protein structure modeling using Modeller. Curr. Protoc. Bioinformatics Chapter 5, 6 (2006).
    • (2006) Curr. Protoc. Bioinformatics Chapter , vol.5 , pp. 6
    • Eswar, N.1
  • 66
    • 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
  • 68
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux tres petits angles: applications a l'etude de phenomenes ultramicroscopiques
    • Guinier, A. La diffraction des rayons X aux tres petits angles: applications a l'etude de phenomenes ultramicroscopiques. Ann. Phys. 12, 161-237 (1939).
    • (1939) Ann. Phys , vol.12 , pp. 161-237
    • Guinier, A.1
  • 69
    • 84876800465 scopus 로고    scopus 로고
    • Accurate assessment of mass, models and resolution by small-angle scattering
    • Rambo, R. P. & Tainer, J. A. Accurate assessment of mass, models and resolution by small-angle scattering. Nature 496, 477-481 (2013).
    • (2013) Nature , vol.496 , pp. 477-481
    • Rambo, R.P.1    Tainer, J.A.2
  • 70
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • Petoukhov, M. V. et al. New developments in the ATSAS program package for small-angle scattering data analysis. J. Appl. Crystallogr. 45, 342-350 (2012).
    • (2012) J. Appl. Crystallogr , vol.45 , pp. 342-350
    • Petoukhov, M.V.1
  • 71
    • 75649147383 scopus 로고    scopus 로고
    • Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale
    • Fischer, H., de Oliveira Neto, M., Napolitano, H. B., Polikarpov, I. & Craievich, a. F. Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale. J. Appl. Crystallogr. 43, 101-109 (2009).
    • (2009) J. Appl. Crystallogr , vol.43 , pp. 101-109
    • Fischer, H.1    De Oliveira Neto, M.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.F.5
  • 72
    • 84859455527 scopus 로고    scopus 로고
    • Structure-based model of allostery predicts coupling between distant sites
    • Weinkam, P., Pons, J. & Sali, A. Structure-based model of allostery predicts coupling between distant sites. Proc. Natl Acad. Sci. USA 103, 6 (2012)
    • (2012) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6
    • Weinkam, P.1    Pons, J.2    Sali, A.3
  • 73
    • 77954280480 scopus 로고    scopus 로고
    • FoXS: A web server for rapid computation and fitting of SAXS profiles
    • Schneidman-Duhovny, D., Hammel, M. & Sali, A. FoXS: a web server for rapid computation and fitting of SAXS profiles. Nucleic Acids Res. 38, W540-W544 (2010).
    • (2010) Nucleic Acids Res , vol.38 , pp. W540-W544
    • Schneidman-Duhovny, D.1    Hammel, M.2    Sali, A.3
  • 74
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky, T. J. et al. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic acids Res. 35, W522-W525 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. W522-W525
    • Dolinsky, T.J.1
  • 75
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A., Sept, D., Joseph, S., Holst, M. J. & McCammon, J. A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Bakern, A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 76
    • 33747829924 scopus 로고    scopus 로고
    • Expresso: Automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee
    • Armougom, F. et al. Expresso: automatic incorporation of structural information in multiple sequence alignments using 3D-Coffee. Nucleic Acids Res. 34, W604-W608 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. W604-W608
    • Armougom, F.1
  • 77
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert, X. & Gouet, P. Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res. 42, W320-W324 (2014).
    • (2014) Nucleic Acids Res , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2
  • 78
    • 84883577718 scopus 로고    scopus 로고
    • Analysis Tool Web Services from the EMBL-EBI
    • McWilliam, H. et al. Analysis Tool Web Services from the EMBL-EBI. Nucleic Acids Res. 41, W597-W600 (2013).
    • (2013) Nucleic Acids Res , vol.41 , pp. W597-W600
    • McWilliam, H.1
  • 79
    • 84863507534 scopus 로고    scopus 로고
    • Geneious Basic: An integrated and extendable desktop software platform for the organization and analysis of sequence data
    • Kearse, M. et al. Geneious Basic: an integrated and extendable desktop software platform for the organization and analysis of sequence data. Bioinformatics 28, 1647-1649 (2012).
    • (2012) Bioinformatics , vol.28 , pp. 1647-1649
    • Kearse, M.1
  • 80
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus, P. A. & Diederichs, K. Linking crystallographic model and data quality. Science 336, 1030-1033 (2012).
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.