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Volumn 46, Issue 2, 2013, Pages 133-180

Structure of viruses: A short history

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[No Author keywords available]

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EID: 84881075013     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583513000012     Document Type: Review
Times cited : (85)

References (310)
  • 2
    • 0018818719 scopus 로고
    • Structure of southern bean mosaic virus at 2.8 A resolution
    • DOI 10.1038/286033a0
    • ABAD-ZAPATERO, C., ABDEL-MEGUID, S. S., JOHNSON, J. E., LESLIE, A. G. W., RAYMENT, I., ROSSMANN, M. G., SUCK, D. & TSUKIHARA, T. (1980). Structure of southern bean mosaic virus at 2-8 Å resolution. Nature 286, 33-39. (Pubitemid 10061063)
    • (1980) Nature , vol.286 , Issue.5768 , pp. 33-39
    • Abad-Zapatero, C.1    Adel-Meguid, S.S.2    Johnson, J.E.3
  • 5
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution
    • DOI 10.1038/337709a0
    • ACHARYA, R., FRY, E., STUART, D., FOX, G., ROWLANDS, D. & BROWN, F. (1989). The three-dimensional structure of foot-and-mouth disease virus at 2-9 Å resolution. Nature 337, 709-716. (Pubitemid 19064726)
    • (1989) Nature , vol.337 , Issue.6209 , pp. 709-716
    • Acharya, R.1    Fry, E.2    Stuart, D.3    Fox, G.4    Rowlands, D.5    Brown, F.6
  • 6
    • 0021257186 scopus 로고
    • Cryo-electron microscopy of viruses
    • ADRIAN, M., DUBOCHET, J., LEPAULT, J. & MCDOWALL, A. W. (1984). Cryo-electron microscopy of viruses. Nature 308, 32-36. (Pubitemid 14130928)
    • (1984) Nature , vol.308 , Issue.5954 , pp. 32-36
    • Adrian, M.1    Dubochet, J.2    Lepault, J.3    McDowall, A.W.4
  • 8
    • 0032534013 scopus 로고    scopus 로고
    • Functional implications of the structure of the murine parvovirus, minute virus of mice
    • AGBANDJE-MCKENNA, M., LLAMAS-SAIZ, A. L., WANG, F., TATTERSALL, P. & ROSSMANN, M. G. (1998). Functional implications of the structure of the murine parvovirus, minute virus of mice. Structure 6, 1369-1381. (Pubitemid 28541881)
    • (1998) Structure , vol.6 , Issue.11 , pp. 1369-1381
    • Agbandje-McKenna, M.1    Llamas-Saiz, A.L.2    Wang, F.3    Tattersall, P.4    Rossmann, M.G.5
  • 12
    • 66749084492 scopus 로고    scopus 로고
    • The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate
    • AKSYUK, A. A., LEIMAN, P. G., SHNEIDER, M. M., MESYANZHINOV, V. V. & ROSSMANN, M. G. (2009b). The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate. Structure 17, 800-808.
    • (2009) Structure , vol.17 , pp. 800-808
    • Aksyuk, A.A.1    Leiman, P.G.2    Shneider, M.M.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 13
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • DOI 10.1128/JVI.75.9.4268-4275.2001
    • ALLISON, S. L., SCHALICH, J., STIASNY, K., MANDL, C.W. & HEINZ, F. X. (2001). Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. Journal of Virology 75, 4268-4275. (Pubitemid 32410139)
    • (2001) Journal of Virology , vol.75 , Issue.9 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 14
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • ALLISON, S. L., SCHALICH, J., STIASNY, K., MANDL, C. W., KUNZ, C. & HEINZ, F. X. (1995). Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. Journal of Virology 69, 695-700.
    • (1995) Journal of Virology , vol.69 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 15
    • 0032989258 scopus 로고    scopus 로고
    • Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E
    • ALLISON, S. L., STIASNY, K., STADLER, K., MANDL, C.W. & HEINZ, F. X. (1999). Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E. Journal of Virology 73, 5605-5612. (Pubitemid 29274844)
    • (1999) Journal of Virology , vol.73 , Issue.7 , pp. 5605-5612
    • Allison, S.L.1    Stiasny, K.2    Stadler, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 16
    • 20444416951 scopus 로고
    • Determining heavyatom positions using non-crystallographic symmetry
    • ARGOS, P. & ROSSMANN, M. G. (1974). Determining heavyatom positions using non-crystallographic symmetry. Acta Crystallographica Section A 30, 672-677.
    • (1974) Acta Crystallographica Section A , vol.30 , pp. 672-677
    • Argos, P.1    Rossmann, M.G.2
  • 20
    • 0028151167 scopus 로고
    • The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2-9 Å resolution
    • ATHAPPILLY, F. K., MURALI, R., RUX, J. J., CAI, Z. & BURNETT, R. M. (1994). The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2-9 Å resolution. Journal of Molecular Biology 242, 430-455.
    • (1994) Journal of Molecular Biology , vol.242 , pp. 430-455
    • Athappilly, F.K.1    Murali, R.2    Rux, J.J.3    Cai, Z.4    Burnett, R.M.5
  • 21
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • DOI 10.1128/JVI.79.23.14967-14970.2005
    • BAKER, M. L., JIANG, W., RIXON, F. J. & CHIU, W. (2005). Common ancestry of herpesvirus and tailed DNA bacteriophages. Journal of Virology 79, 14967-14970. (Pubitemid 41636294)
    • (2005) Journal of Virology , vol.79 , Issue.23 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 22
    • 0020539720 scopus 로고
    • Polyoma virus 'hexamer' tubes consist of paired pentamers
    • BAKER, T. S., CASPAR, D. L. & MURAKAMI, W. T. (1983). Polyoma virus 'hexamer' tubes consist of paired pentamers. Nature 303, 446-448. (Pubitemid 13094887)
    • (1983) Nature , vol.303 , Issue.5916 , pp. 446-448
    • Baker, T.S.1    Caspar, D.L.D.2    Murakami, W.T.3
  • 23
    • 0026329210 scopus 로고
    • Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and threedimensional image reconstruction
    • BAKER, T. S., NEWCOMB, W. W., OLSON, N. H., COWSERT, L. M., OLSON, C. & BROWN, J. C. (1991). Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and threedimensional image reconstruction. Biophysical Journal 60, 1445-1456.
    • (1991) Biophysical Journal , vol.60 , pp. 1445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 24
    • 27944491964 scopus 로고    scopus 로고
    • What does structure tell us about virus evolution?
    • DOI 10.1016/j.sbi.2005.10.012, PII S0959440X05002009, Catalysis and Regulation/Proteins
    • BAMFORD, D. H., GRIMES, J.M. & STUART, D. I. (2005). What does structure tell us about virus evolution? Current Opinion in Structural Biology 15, 655-663. (Pubitemid 41668522)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.6 , pp. 655-663
    • Bamford, D.H.1    Grimes, J.M.2    Stuart, D.I.3
  • 27
    • 0032516070 scopus 로고    scopus 로고
    • The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand
    • DOI 10.1073/pnas.95.8.4140
    • BELLA, J., KOLATKAR, P. R., MARLOR, C. W., GREVE, J.M. & ROSSMANN, M. G. (1998). The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand. Proceedings of the National Academy of Sciences of the United States of America 95, 4140-4145. (Pubitemid 28207878)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.8 , pp. 4140-4145
    • Bella, J.1    Kolatkar, P.R.2    Marlor, C.W.3    Greve, J.M.4    Rossmann, M.G.5
  • 28
    • 0032806637 scopus 로고    scopus 로고
    • The structure of the two amino-terminal domains of human intercellular adhesion molecule-1 suggests how it functions as a rhinovirus receptor
    • DOI 10.1016/S0168-1702(99)00038-6, PII S0168170299000386
    • BELLA, J., KOLATKAR, P. R., MARLOR, C. W., GREVE, J.M. & ROSSMANN, M. G. (1999). The structure of the two amino-terminal domains of human intercellular adhesion molecule-1 suggests how it functions as a rhinovirus receptor. Virus Research 62, 107-117. (Pubitemid 29393112)
    • (1999) Virus Research , vol.62 , Issue.2 , pp. 107-117
    • Bella, J.1    Kolatkar, P.R.2    Marlor, C.W.3    Greve, J.M.4    Rossmann, M.G.5
  • 29
    • 9744228738 scopus 로고    scopus 로고
    • Does common architecture reveal a viral lineage spanning all three domains of life?
    • DOI 10.1016/j.molcel.2004.11.016, PII S1097276504007099
    • BENSON, S. D., BAMFORD, J. K. H., BAMFORD, D.H. & BURNETT, R. M. (2004). Does common architecture reveal a viral lineage spanning all three domains of life ? Molecular Cell 16, 673-685. (Pubitemid 39586527)
    • (2004) Molecular Cell , vol.16 , Issue.5 , pp. 673-685
    • Benson, S.D.1    Bamford, J.K.H.2    Bamford, D.H.3    Burnett, R.M.4
  • 30
    • 0018126959 scopus 로고
    • Isolation and characterization of precursors in T4 baseplate assembly the complex of gene 10 and gene 11 products
    • BERGET, P. B. & KING, J. (1978). Isolation and characterization of precursors in T4 baseplate assembly. The complex of gene 10 and gene 11 products. Journal of Molecular Biology 124, 469-486. (Pubitemid 9034593)
    • (1978) Journal of Molecular Biology , vol.124 , Issue.3 , pp. 469-486
    • Berget, P.B.1    King, J.2
  • 31
    • 0343097602 scopus 로고
    • Structure types of protein crystals from virus-infected plants
    • BERNAL, J.D. & FANKUCHEN, I. (1937). Structure types of protein crystals from virus-infected plants. Nature 139, 923-924.
    • (1937) Nature , vol.139 , pp. 923-924
    • Bernal, J.D.1    Fankuchen, I.2
  • 32
    • 0000500338 scopus 로고
    • X-Ray and crystallographic studies of plant virus preparations: I. Introduction and preparation of specimens. II. Modes of aggregation of the virus particles. III. (1) the structure of the particles and (2) biological implications
    • BERNAL, J.D. & FANKUCHEN, I. (1941). X-Ray and crystallographic studies of plant virus preparations: I. Introduction and preparation of specimens. II. Modes of aggregation of the virus particles. III. (1) The structure of the particles and (2) biological implications. Journal of General Physiology 25, 111-165.
    • (1941) Journal of General Physiology , vol.25 , pp. 111-165
    • Bernal, J.D.1    Fankuchen, I.2
  • 33
    • 0018223550 scopus 로고
    • Protein disk of tobacco mosaic virus at 2.8 Å resolution showing the interactions within and between subunits
    • BLOOMER, A. C., CHAMPNESS, J. N., BRICOGNE, G., STADEN, R. & KLUG, A. (1978). Protein disk of tobacco mosaic virus at 2-8 Å resolution showing the interactions within and between subunits. Nature 276, 362-368. (Pubitemid 9096463)
    • (1978) Nature , vol.276 , Issue.5686 , pp. 362-368
    • Bloomer, A.C.1    Champness, J.N.2    Bricogne, G.3
  • 34
    • 35148838173 scopus 로고    scopus 로고
    • Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus-receptor-membrane complex at 30 Å resolution
    • DOI 10.1016/j.jsb.2007.08.009, PII S1047847707001967
    • BOSTINA, M., BUBECK, D., SCHWARTZ, C., NICASTRO, D., FILMAN, D. J. & HOGLE, J. M. (2007). Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus-receptormembrane complex at 30 A ̊ resolution. Journal of Structural Biology 160, 200-210. (Pubitemid 47539198)
    • (2007) Journal of Structural Biology , vol.160 , Issue.2 , pp. 200-210
    • Bostina, M.1    Bubeck, D.2    Schwartz, C.3    Nicastro, D.4    Filman, D.J.5    Hogle, J.M.6
  • 35
    • 78650670078 scopus 로고    scopus 로고
    • Poliovirus RNA is released from the capsid near a twofold symmetry axis
    • BOSTINA, M., LEVY, H., FILMAN, D. J. & HOGLE, J.M. (2011). Poliovirus RNA is released from the capsid near a twofold symmetry axis. Journal of Virology 83, 776-783.
    • (2011) Journal of Virology , vol.83 , pp. 776-783
    • Bostina, M.1    Levy, H.2    Filman, D.J.3    Hogle, J.M.4
  • 38
    • 33646835810 scopus 로고
    • A negative staining method for high resolution electron microscopy of viruses
    • BRENNER, S. & HORNE, R. W. (1959). A negative staining method for high resolution electron microscopy of viruses. Biochimica et Biophysica Acta 34, 103-110.
    • (1959) Biochimica et Biophysica Acta , vol.34 , pp. 103-110
    • Brenner, S.1    Horne, R.W.2
  • 39
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • DOI 10.1038/sj.emboj.7600064
    • BRESSANELLI, S., STIASNY, K., ALLISON, S. L., STURA, E. A., DUQUERROY, S., LESCAR, J., HEINZ, F.X. & REY, F.A. (2004). Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO Journal 23, 728-738. (Pubitemid 38425440)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 728-738
    • Bressanelli, S.1    Stiasny, K.2    Allison, S.L.3    Stura, E.A.4    Duquerroy, S.5    Lescar, J.6    Heinz, F.X.7    Rey, F.A.8
  • 40
    • 0036407156 scopus 로고    scopus 로고
    • The molecular biology of West Nile virus: A new invader of the Western hemisphere
    • DOI 10.1146/annurev.micro.56.012302.160654
    • BRINTON, M. A. (2002). The molecular biology of West Nile virus: a new invader of the western hemisphere. Annual Review of Microbiology 56, 371-402. (Pubitemid 35217460)
    • (2002) Annual Review of Microbiology , vol.56 , pp. 371-402
    • Brinton, M.A.1
  • 41
    • 84862908674 scopus 로고    scopus 로고
    • Herpesvirus capsid assembly: Insights from structural analysis
    • BROWN, J.C. & NEWCOMB, W. W. (2011). Herpesvirus capsid assembly: insights from structural analysis. Current Opinion in Virology 1, 142-149.
    • (2011) Current Opinion in Virology , vol.1 , pp. 142-149
    • Brown, J.C.1    Newcomb, W.W.2
  • 43
    • 0015948244 scopus 로고
    • Structure determination of crystalline lobster D-glyceraldehyde-3- phosphate dehydrogenase
    • BUEHNER, M., FORD, G. C., MORAS, D., OLSEN, K.W. & ROSSMANN, M. G. (1974). Structure determination of crystalline lobster D-glyceraldehyde-3- phosphate dehydrogenase. Journal of Molecular Biology 82, 563-585.
    • (1974) Journal of Molecular Biology , vol.82 , pp. 563-585
    • Buehner, M.1    Ford, G.C.2    Moras, D.3    Olsen, K.W.4    Rossmann, M.G.5
  • 44
    • 0001422785 scopus 로고    scopus 로고
    • Flaviviruses
    • (EDS. D. M. Knipe & P. M. Howley), Philadelphia: Lippincott Williams & Wilkins
    • BURKE, D. S. & MONATH, T. P. (2001). Flaviviruses. In Fields Virology (EDS. D. M. Knipe & P. M. Howley), pp. 1043-1125. Philadelphia: Lippincott Williams & Wilkins.
    • (2001) Fields Virology , pp. 1043-1125
    • Burke, D.S.1    Monath, T.P.2
  • 47
    • 0004161721 scopus 로고    scopus 로고
    • (ED. R. Calendar). New York: Oxford University Press
    • CALENDAR, R. (2006). The Bacteriophages (ED. R. Calendar). New York: Oxford University Press.
    • (2006) The Bacteriophages
    • Calendar, R.1
  • 49
    • 36949079814 scopus 로고
    • Structure of bushy stunt virus
    • CASPAR, D. L. D. (1956). Structure of bushy stunt virus. Nature 177, 475-476.
    • (1956) Nature , vol.177 , pp. 475-476
    • Caspar, D.L.D.1
  • 51
    • 0016892556 scopus 로고
    • The structure of the protein disk of tobacco mosaic virus to 5 A ̊ resolution
    • CHAMPNESS, J. N., BLOOMER, A. C., BRICOGNE, G., BUTLER, P.G. & KLUG, A. (1976). The structure of the protein disk of tobacco mosaic virus to 5 A ̊ resolution. Nature 259, 20-24.
    • (1976) Nature , vol.259 , pp. 20-24
    • Champness, J.N.1    Bloomer, A.C.2    Bricogne, G.3    Butler, P.G.4    Klug, A.5
  • 52
    • 0000080575 scopus 로고    scopus 로고
    • Structural refinement of the DNA-containing capsid of canine parvovirus using RSRef, a resolution-dependent stereochemically restrained real-space refinement method
    • CHAPMAN, M. S. & ROSSMANN, M. G. (1996). Structural refinement of the DNA-containing capsid of canine parvovirus using RSRef, a resolution-dependent stereochemically restrained real-space refinement method. Acta Crystallographica Section D: Biological Crystallography 52, 129-142. (Pubitemid 126512691)
    • (1996) Acta Crystallographica Section D: Biological Crystallography , vol.52 , Issue.1 , pp. 129-142
    • Chapman, M.S.1    Rossmann, M.G.2
  • 53
    • 0001121111 scopus 로고
    • Ab initio phase determination for spherical viruses: Parameter determination for spherical-shell models
    • CHAPMAN, M. S., TSAO, J. & ROSSMANN, M. G. (1992). Ab initio phase determination for spherical viruses: parameter determination for spherical-shell models. Acta Crystallogaphica Section A 48, 301-312.
    • (1992) Acta Crystallogaphica Section A , vol.48 , pp. 301-312
    • Chapman, M.S.1    Tsao, J.2    Rossmann, M.G.3
  • 57
    • 0026419333 scopus 로고
    • Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion
    • CHOI, H. K., TONG, L., MINOR, W., DUMAS, P., BOEGE, U., ROSSMANN, M.G. & WENGLER, G. (1991). Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. Nature 354, 37-43. (Pubitemid 21896775)
    • (1991) Nature , vol.354 , Issue.6348 , pp. 37-43
    • Choi, H.K.1    Tong, L.2    Minor, W.3    Dumas, P.4    Boege, U.5    Rossmann, M.G.6    Wengler, G.7
  • 60
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic site in influenza virus neuraminidase
    • COLMAN, P. M., VARGHESE, J.N. & LAVER, W. G. (1983). Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303, 41-44. (Pubitemid 13125071)
    • (1983) Nature , vol.303 , Issue.5912 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 61
    • 0001295606 scopus 로고
    • T4 tail structure and function
    • (ED. J. D. Karam), Washington, DC: American Society for Microbiology
    • COOMBS, D.H. & ARISAKA, F. (1994). T4 tail structure and function. In Molecular Biology of Bacteriophage T4 (ED. J. D. Karam), pp. 259-281. Washington, DC: American Society for Microbiology.
    • (1994) Molecular Biology of Bacteriophage T4 , pp. 259-281
    • Coombs, D.H.1    Arisaka, F.2
  • 62
    • 36949077319 scopus 로고
    • Structure of small viruses
    • CRICK, F. H. C. &WATSON, J. D. (1956). Structure of small viruses. Nature 177, 473-475.
    • (1956) Nature , vol.177 , pp. 473-475
    • Crick, F.H.C.1    Watson, J.D.2
  • 63
    • 0002534092 scopus 로고
    • Virus structure: General principles
    • (EDS. G. E. W. Wolstenholme, E. C. P. Millar and Ciba Foundation), London: J. & A. Churchill
    • CRICK, F.H. C. & WATSON, J. D. (1957). Virus structure: general principles. In Ciba Foundation Symposium on the Nature of Viruses (EDS. G. E. W. Wolstenholme, E. C. P. Millar and Ciba Foundation), pp. 5-13. London: J. & A. Churchill.
    • (1957) Ciba Foundation Symposium on the Nature of Viruses , pp. 5-13
    • Crick, F.H.C.1    Watson, J.D.2
  • 64
    • 0542431418 scopus 로고
    • X-ray crystallographic measurements on a single crystal of a tobacco necrosis virus derivative
    • CROWFOOT, D. & SCHMIDT, G. M. J. (1945). X-ray crystallographic measurements on a single crystal of a tobacco necrosis virus derivative. Nature 155, 504-505.
    • (1945) Nature , vol.155 , pp. 504-505
    • Crowfoot, D.1    Schmidt, G.M.J.2
  • 65
    • 0014930077 scopus 로고
    • Three-dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • CROWTHER, R. A., AMOS, L. A., FINCH, J. T., DEROSIER, D. J. & KLUG, A. (1970). Three-dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature 226, 421-425.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    Derosier, D.J.4    Klug, A.5
  • 66
    • 0017757241 scopus 로고
    • Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4
    • DOI 10.1016/0022-2836(77)90081-X
    • CROWTHER, R. A., LENK, E. V., KIKUCHI, Y. & KING, J. (1977). Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4. Journal of Molecular Biology 116, 489-523. (Pubitemid 8204725)
    • (1977) Journal of Molecular Biology , vol.116 , Issue.3 , pp. 489-523
    • Crowther, R.A.1    Lenk, E.V.2    Kikuchi, Y.3    King, J.4
  • 67
    • 31144445030 scopus 로고    scopus 로고
    • West nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection
    • DOI 10.1128/JVI.80.3.1290-1301.2006
    • DAVIS, C. W., NGUYEN, H. Y., HANNA, S. L., SÁNCHEZ, M. D., DOMS, R.W. & PIERSON, T. C. (2006). West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection. Journal of Virology 80, 1290-1301. (Pubitemid 43134086)
    • (2006) Journal of Virology , vol.80 , Issue.3 , pp. 1290-1301
    • Davis, C.W.1    Nguyen, H.-Y.2    Hanna, S.L.3    Sanchez, M.D.4    Doms, R.W.5    Pierson, T.C.6
  • 68
    • 0034663762 scopus 로고    scopus 로고
    • Crystal structure of the matrix protein VP40 from Ebola virus
    • DESSEN, A., VOLCHKOV, V., DOLNIK, O., KLENK, H.-D. & WEISSENHORN, W. (2000). Crystal structure of the matrix protein VP40 from Ebola virus. EMBO Journal 19, 4228-4236. (Pubitemid 30623733)
    • (2000) EMBO Journal , vol.19 , Issue.16 , pp. 4228-4236
    • Dessen, A.1    Volchkov, V.2    Dolnik, O.3    Klenk, H.-D.4    Weissenhorn, W.5
  • 72
    • 3142611054 scopus 로고    scopus 로고
    • West Nile virus core protein: Tetramer structure and ribbon formation
    • DOI 10.1016/j.str.2004.04.024, PII S0969212604002059
    • DOKLAND, T., WALSH, M., MACKENZIE, J. M., KHROMYKH, A. A., EE, K.-H. & WANG, S. (2004). West Nile virus core protein: tetramer structure and ribbon formation. Structure 12, 1157-1163. (Pubitemid 38900758)
    • (2004) Structure , vol.12 , Issue.7 , pp. 1157-1163
    • Dokland, T.1    Walsh, M.2    Mackenzie, J.M.3    Khromykh, A.A.4    Ee, K.-H.5    Wang, S.6
  • 73
    • 0036148234 scopus 로고    scopus 로고
    • The VP1 unique region of parvovirus B19 and its constituent phospholipase A2-like activity
    • DOI 10.1128/JVI.76.4.2014-2018.2002
    • DORSCH, S., LIEBISCH, G., KAUFMANN, B., VON LANDENBERG, P., HOFFMANN, J. H., DROBNIK, W. & MODROW, S. (2002). The VP1 unique region of parvovirus B19 and its constituent phospholipase A2-like activity. Journal of Virology 76, 2014-2018. (Pubitemid 34094651)
    • (2002) Journal of Virology , vol.76 , Issue.4 , pp. 2014-2018
    • Dorsch, S.1    Liebisch, G.2    Kaufmann, B.3    Von Landenberg, P.4    Hoffmann, J.H.5    Drobnik, W.6    Modrow, S.7
  • 75
    • 0001044165 scopus 로고
    • Pathways in T4 morphogenesis
    • (EDS. J. D. Karam, J. W. Drake, K. N. Kreuzer, G. Mosig, D. H. Hall, F. A. Eiserling, L. W. Black, E. K. Spicer, E. Kutter, C. Carlson & E. S. Miller),. Washington, DC: American Society for Microbiology
    • EISERLING, F.A. & BLACK, L. W. (1994). Pathways in T4 morphogenesis. In Molecular Biology of Bacteriophage T4 (EDS. J. D. Karam, J. W. Drake, K. N. Kreuzer, G. Mosig, D. H. Hall, F. A. Eiserling, L. W. Black, E. K. Spicer, E. Kutter, C. Carlson & E. S. Miller), pp. 209-212. Washington, DC: American Society for Microbiology.
    • (1994) Molecular Biology of Bacteriophage T4 , pp. 209-212
    • Eiserling, F.A.1    Black, L.W.2
  • 76
    • 0037236396 scopus 로고    scopus 로고
    • Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus
    • DOI 10.1099/vir.0.18723-0
    • ELSHUBER, S., ALLISON, S. L., HEINZ, F. X. & MANDL, C.W. (2003). Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus. Journal of General Virology 84, 183-191. (Pubitemid 36113564)
    • (2003) Journal of General Virology , vol.84 , Issue.1 , pp. 183-191
    • Elshuber, S.1    Allison, S.L.2    Heinz, F.X.3    Mandl, C.W.4
  • 78
    • 0024316730 scopus 로고
    • Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus
    • FILMAN, D. J., SYED, R., CHOW, M., MACADAM, A. J., MINOR, P.D. & HOGLE, J. M. (1989). Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus. EMBO Journal 18, 1567-1579. (Pubitemid 19274384)
    • (1989) EMBO Journal , vol.8 , Issue.5 , pp. 1567-1579
    • Filman, D.J.1    Syed, R.2    Chow, M.3    Macadam, A.J.4    Minor, P.D.5    Hogle, J.M.6
  • 79
    • 2642675374 scopus 로고
    • Structure of poliomyelitis virus
    • FINCH, J. T. & KLUG, A. (1959). Structure of poliomyelitis virus. Nature 183, 1709-1714.
    • (1959) Nature , vol.183 , pp. 1709-1714
    • Finch, J.T.1    Klug, A.2
  • 80
    • 33646712345 scopus 로고    scopus 로고
    • Cryo-EM structure of a bacteriophage T4 gp24 bypass mutant: The evolution of pentameric vertex proteins in icosahedral viruses
    • DOI 10.1016/j.jsb.2006.01.008, PII S1047847706000220
    • FOKINE, A., BATTISTI, A. J., KOSTYUCHENKO, V. A., BLACK, L.W. & ROSSMANN, M. G. (2006). Cryo-EM structure of a bacteriophage T4 gp24 bypass mutant: the evolution of pentameric vertex proteins in icosahedral viruses. Journal of Structural Biology 154, 255-259. (Pubitemid 43737263)
    • (2006) Journal of Structural Biology , vol.154 , Issue.3 , pp. 255-259
    • Fokine, A.1    Battisti, A.J.2    Kostyuchenko, V.A.3    Black, L.W.4    Rossmann, M.G.5
  • 84
    • 0006757280 scopus 로고
    • Tobacco mosaic virus: Application of the method of isomorphous replacement to the determination of the helical parameters and radial density distribution
    • FRANKLIN, R. E. & HOLMES, K. C. (1958). Tobacco mosaic virus: application of the method of isomorphous replacement to the determination of the helical parameters and radial density distribution. Acta Crystallographica 11, 213-220.
    • (1958) Acta Crystallographica , vol.11 , pp. 213-220
    • Franklin, R.E.1    Holmes, K.C.2
  • 85
    • 29544432024 scopus 로고
    • X-ray diffraction studies of the structure and morphology of tobacco mosaic virus
    • (EDS. G. E. W. Wolstenholme, E. C. P. Millar and Ciba Foundation), London: J. & A. Churchill
    • FRANKLIN, R. E., KLUG, A. & HOLMES, K. C. (1957). X-ray diffraction studies of the structure and morphology of tobacco mosaic virus. In Ciba Foundation Symposium on the Nature of Viruses (EDS. G. E. W. Wolstenholme, E. C. P. Millar and Ciba Foundation), pp. 39-55. London: J. & A. Churchill.
    • (1957) Ciba Foundation Symposium on the Nature of Viruses , pp. 39-55
    • Franklin, R.E.1    Klug, A.2    Holmes, K.C.3
  • 86
    • 84862830238 scopus 로고    scopus 로고
    • Structure and cell biology of archaeal virus STIV
    • FU, C.Y. & JOHNSON, J. E. (2012). Structure and cell biology of archaeal virus STIV. Current Opinion in Virology 2, 122-127.
    • (2012) Current Opinion in Virology , vol.2 , pp. 122-127
    • Fu, C.Y.1    Johnson, J.E.2
  • 88
    • 0023666171 scopus 로고
    • The T=4 envelope of Sindbis virus is organized by interactions with a complementary T=3 capsid
    • FULLER, S. D. (1987). The T=4 envelope of Sindbis virus is organized by interactions with a complementary T=3 capsid. Cell 48, 923-934.
    • (1987) Cell , vol.48 , pp. 923-934
    • Fuller, S.D.1
  • 89
    • 0023053018 scopus 로고
    • Structure determination of Panulirus interruptus haemocyanin at 3-2 Å resolution. Successful phase extension by sixfold density averaging
    • GAYKEMA, W. P., VOLBEDA, A. & HOL, W. G. (1986). Structure determination of Panulirus interruptus haemocyanin at 3-2 Å resolution. Successful phase extension by sixfold density averaging. Journal of Molecular Biology 187, 255-275.
    • (1986) Journal of Molecular Biology , vol.187 , pp. 255-275
    • Gaykema, W.P.1    Volbeda, A.2    Hol, W.G.3
  • 90
    • 0036149164 scopus 로고    scopus 로고
    • Molecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein
    • GIBBONS, D. L. & KIELIAN, M. (2002). Molecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein. Journal of Virology 76, 1194-1205. (Pubitemid 34066423)
    • (2002) Journal of Virology , vol.76 , Issue.3 , pp. 1194-1205
    • Gibbons, D.L.1    Kielian, M.2
  • 94
    • 0027081630 scopus 로고
    • The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein
    • DOI 10.1016/0042-6822(92)90267-S
    • GUIRAKHOO, F., BOLIN, R. A. & ROEHRIG, J. T. (1992). The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein. Virology 191, 921-931. (Pubitemid 23022496)
    • (1992) Virology , vol.191 , Issue.2 , pp. 921-931
    • Guirakhoo, F.1    Bolin, R.A.2    Roehrig, J.T.3
  • 95
    • 0025855266 scopus 로고
    • Fusion activity of flaviviruses: Comparison of mature and immature (prM-containing) tick-borne encephalitis virions
    • GUIRAKHOO, F., HEINZ, F. X., MANDL, C. W., HOLZMANN, H. & KUNZ, C. (1991). Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions. Journal of General Virology 72, 1323-1329.
    • (1991) Journal of General Virology , vol.72 , pp. 1323-1329
    • Guirakhoo, F.1    Heinz, F.X.2    Mandl, C.W.3    Holzmann, H.4    Kunz, C.5
  • 96
    • 66149137648 scopus 로고    scopus 로고
    • The structural analysis of eight different FAb interacting with parvovirus capsids reveals alternative mechanisms of neutralization and binding to host range variant capsids
    • HAFENSTEIN, S., BOWMAN, V. D., SUN, T., NELSON, C. D. S., PALERMO, L., CHIPMAN, P. R., BATTISTI, A. J., PARRISH, C. R. & ROSSMANN, M. G. (2009). The structural analysis of eight different FAb interacting with parvovirus capsids reveals alternative mechanisms of neutralization and binding to host range variant capsids. Journal of Virology 83, 5556-5566.
    • (2009) Journal of Virology , vol.83 , pp. 5556-5566
    • Hafenstein, S.1    Bowman, V.D.2    Sun, T.3    Nelson, C.D.S.4    Palermo, L.5    Chipman, P.R.6    Battisti, A.J.7    Parrish, C.R.8    Rossmann, M.G.9
  • 98
    • 0035840794 scopus 로고    scopus 로고
    • The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein: Interfaces can rotate in the oligomeric structures of M1
    • DOI 10.1006/viro.2001.1119
    • HARRIS, A., FOROUHAR, F., QIU, S., SHA, B. & LUO, M. (2001). The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1. Virology 289, 34-44. (Pubitemid 33016235)
    • (2001) Virology , vol.289 , Issue.1 , pp. 34-44
    • Harris, A.1    Forouhar, F.2    Qiu, S.3    Sha, B.4    Luo, M.5
  • 99
    • 0002685998 scopus 로고
    • A point-focusing camera for single-crystal diffraction
    • HARRISON, S. C. (1968). A point-focusing camera for single-crystal diffraction. Journal of Applied Crystallography 1, 84-90.
    • (1968) Journal of Applied Crystallography , vol.1 , pp. 84-90
    • Harrison, S.C.1
  • 100
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • DOI 10.1038/nsmb.1456, PII NSMB1456
    • HARRISON, S. C. (2008). Viral membrane fusion. Nature Structural and Molecular Biology 15, 690-698. (Pubitemid 351932011)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.7 , pp. 690-698
    • Harrison, S.C.1
  • 102
    • 0018225178 scopus 로고
    • Tomato bushy stunt virus at 2.9 Å resolution
    • HARRISON, S. C., OLSON, A. J., SCHUTT, C. E., WINKLER, F.K. & BRICOGNE, G. (1978). Tomato bushy stunt virus at 2-9 Å resolution. Nature 276, 368-373. (Pubitemid 9096464)
    • (1978) Nature , vol.276 , Issue.5686 , pp. 368-373
    • Harrison, S.C.1    Olson, A.J.2    Schutt, C.E.3
  • 105
    • 0009541353 scopus 로고
    • Morphogenesis of the isometric phages
    • (EDS. D. T. Denhardt, D. Dressler & D. S. Ray), Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • HAYASHI, M. A. (1978). Morphogenesis of the isometric phages. In Cold Spring Harbor Monograph: The Single- Stranded DNA Phages, vol. 8 (EDS. D. T. Denhardt, D. Dressler & D. S. Ray), pp. 531-547. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1978) Cold Spring Harbor Monograph: The Single- Stranded DNA Phages , vol.8 , pp. 531-547
    • Hayashi, M.A.1
  • 106
    • 0038548251 scopus 로고    scopus 로고
    • Efficacy and safety of oral pleconaril for treatment of colds due to picornaviruses in adults: Results of 2 double-blind, randomized, placebo-controlled trials
    • DOI 10.1086/375069
    • HAYDEN, F. G., HERRINGTON, D. T., COATS, T. L., KIM, K. H., COOPER, E. C., VILLANO, S. A., LIU, S., HUDSON, S., PEVEAR, D. C., COLLETT, M. & MCKINLAY, M. A. (2003). Efficacy and safety of oral pleconaril for treatment of picornavirus colds in adults: results of two double-blind, randomized, placebocontrolled trials. Clinical Infectious Diseases 36, 1523-1532. (Pubitemid 36783334)
    • (2003) Clinical Infectious Diseases , vol.36 , Issue.12 , pp. 1523-1532
    • Hayden, F.G.1    Herrington, D.T.2    Coats, T.L.3    Kim, K.4    Cooper, E.C.5    Villano, S.A.6    Liu, S.7    Hudson, S.8    Pevear, D.C.9    Collett, M.10    McKinlay, M.11
  • 109
    • 0028278395 scopus 로고
    • Structural changes and functional control of the tick-borne encephalitis virus glycoprotein e by the heterodimeric association with protein prM
    • HEINZ, F. X., STIASNY, K., PüSCHNER-AUER, G., HOLZMANN, H., ALLISON, S. L., MANDL, C.W. & KUNZ, C. (1994). Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM. Virology 198, 109-117.
    • (1994) Virology , vol.198 , pp. 109-117
    • Heinz, F.X.1    Stiasny, K.2    Püschner-Auer, G.3    Holzmann, H.4    Allison, S.L.5    Mandl, C.W.6    Kunz, C.7
  • 110
    • 0020046189 scopus 로고
    • Amino acid sequence of southern bean mosaic virus coat protein and its relation to the three-dimensional structure of the virus
    • DOI 10.1016/0042-6822(82)90071-X
    • HERMODSON, M. A., ABAD-ZAPATERO, C., ABDEL-MEGUID, S. S., PUNDAK, S., ROSSMANN, M.G. & TREMAINE, J.H. (1982). Amino acid sequence of southern bean mosaic virus coat protein and its relation to the three-dimensional structure of the virus. Virology 119, 133-149. (Pubitemid 12100686)
    • (1982) Virology , vol.119 , Issue.1 , pp. 133-149
    • Hermodson, M.A.1    Abad-Zapatero, C.2    Abdel-Meguid, S.S.3
  • 111
    • 0036403802 scopus 로고    scopus 로고
    • Poliovirus cell entry: Common structural themes in viral cell entry pathways
    • DOI 10.1146/annurev.micro.56.012302.160757
    • HOGLE, J. M. (2002). Poliovirus cell entry: common structural themes in viral cell entry pathways. Annual Review of Microbiology 56, 677-702. (Pubitemid 35217471)
    • (2002) Annual Review of Microbiology , vol.56 , pp. 677-702
    • Hogle, J.M.1
  • 112
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 Å resolution
    • HOGLE, J. M., CHOW, M. & FILMAN, D. J. (1985). Threedimensional structure of poliovirus at 2-9 Å resolution. Science 229, 1358-1365. (Pubitemid 16222374)
    • (1985) Science , vol.229 , Issue.4720 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 113
    • 0016661329 scopus 로고
    • Structure of tobacco mosaic virus at 6-7 Å resolution
    • HOLMES, K. C., STUBBS, G. J., MANDELKOW, E. & GALLWITZ, U. (1975). Structure of tobacco mosaic virus at 6-7 Å resolution. Nature 254, 192-196.
    • (1975) Nature , vol.254 , pp. 192-196
    • Holmes, K.C.1    Stubbs, G.J.2    Mandelkow, E.3    Gallwitz, U.4
  • 115
    • 0141570405 scopus 로고    scopus 로고
    • Combinations of two capsid regions controlling canine host range determine canine transferrin receptor binding by canine and feline parvoviruses
    • DOI 10.1128/JVI.77.18.10099-10105.2003
    • HUEFFER, K., GOVINDASAMY, L., AGBANDJE-MCKENNA, M. & PARRISH, C. R. (2003). Combinations of two capsid regions controlling canine host range determine canine transferrin receptor binding by canine and feline parvoviruses. Journal of Virology 77, 10099-10105. (Pubitemid 37122091)
    • (2003) Journal of Virology , vol.77 , Issue.18 , pp. 10099-10105
    • Hueffer, K.1    Govindasamy, L.2    Agbandje-McKenna, M.3    Parrish, C.R.4
  • 116
    • 85025343606 scopus 로고
    • The structure of the protein shell of turnip yellow mosaic virus
    • HUXLEY, H.E. & ZUBAY, G. (1960). The structure of the protein shell of turnip yellow mosaic virus. Journal of Molecular Biology 2, 189-196.
    • (1960) Journal of Molecular Biology , vol.2 , pp. 189-196
    • Huxley, H.E.1    Zubay, G.2
  • 117
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • DOI 10.1038/nature04487, PII NATURE04487
    • JIANG, W., CHANG, J., JAKANA, J., WEIGELE, P., KING, J. & CHIU, W. (2006). Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/ injection apparatus. Nature 439, 612-616. (Pubitemid 43185387)
    • (2006) Nature , vol.439 , Issue.7076 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 118
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • DOI 10.1038/nsb891
    • JIANG, W., LI, Z., ZHANG, Z., BAKER, M. L., PREVELIGE JR, P. E. & CHIU, W. (2003). Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nature Structural Biology 10, 131-135. (Pubitemid 36177094)
    • (2003) Nature Structural Biology , vol.10 , Issue.2 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige Jr., P.E.5    Chiu, W.6
  • 119
    • 4644330957 scopus 로고    scopus 로고
    • The functional domains of bacteriophage T4 terminase
    • DOI 10.1074/jbc.M403647200
    • KANAMARU, S., KONDABAGIL, K., ROSSMANN, M.G. & RAO, V. B. (2004). The functional domains of bacteriophage T4 terminase. Journal of Biological Chemistry 279, 40795-40801. (Pubitemid 39287676)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40795-40801
    • Kanamaru, S.1    Kondabagil, K.2    Rossmann, M.G.3    Rao, V.B.4
  • 121
    • 12344292308 scopus 로고    scopus 로고
    • Parvovirus B19 does not bind to membrane-associated globoside in vitro
    • DOI 10.1016/j.virol.2004.11.037, PII S0042682204008128
    • KAUFMANN, B., BAXA, U., CHIPMAN, P. R., ROSSMANN, M. G., MODROW, S. & SECKLER, R. (2005). Parvovirus B19 does not bind to membrane-associated globoside in vitro. Virology 332, 189-198. (Pubitemid 40127240)
    • (2005) Virology , vol.332 , Issue.1 , pp. 189-198
    • Kaufmann, B.1    Baxa, U.2    Chipman, P.R.3    Rossmann, M.G.4    Modrow, S.5    Seckler, R.6
  • 124
    • 47749093965 scopus 로고    scopus 로고
    • Visualization of the externalized VP2 N termini of infectious human parvovirus B19
    • DOI 10.1128/JVI.00512-08
    • KAUFMANN, B., CHIPMAN, P. R., KOSTYUCHENKO, V. A., MODROW, S. & ROSSMANN, M. G. (2008). Visualization of the externalized VP2 N-termini of infectious human parvovirus B19. Journal of Virology 82, 7306-7312. (Pubitemid 352031199)
    • (2008) Journal of Virology , vol.82 , Issue.15 , pp. 7306-7312
    • Kaufmann, B.1    Chipman, P.R.2    Kostyuchenko, V.A.3    Modrow, S.4    Rossmann, M.G.5
  • 127
  • 128
    • 78650608263 scopus 로고    scopus 로고
    • Molecular mechanisms involved in the early steps of flavivirus cell entry
    • KAUFMANN, B. & ROSSMANN, M. G. (2011). Molecular mechanisms involved in the early steps of flavivirus cell entry. Microbes and Infection 13, 1-9.
    • (2011) Microbes and Infection , vol.13 , pp. 1-9
    • Kaufmann, B.1    Rossmann, M.G.2
  • 130
    • 0022777396 scopus 로고
    • W.M. Stanley's crystallization of the tobacco mosaic virus, 1930-1940
    • KAY, L. E. (1986). W. M. Stanley's crystallization of the tobacco mosaic virus, 1930-1940. Isis 77, 450-472.
    • (1986) Isis , vol.77 , pp. 450-472
    • Kay, L.E.1
  • 132
    • 0001266102 scopus 로고
    • A threedimensional model of the myoglobin molecule obtained by X-ray analysis
    • KENDREW, J. C., BODO, G., DINTZIS, H. M., PARRISH, R. G., WYCKOFF, H. & PHILLIPS, D. C. (1958). A threedimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181, 662-666.
    • (1958) Nature , vol.181 , pp. 662-666
    • Kendrew, J.C.1    Bodo, G.2    Dintzis, H.M.3    Parrish, R.G.4    Wyckoff, H.5    Phillips, D.C.6
  • 135
    • 0029108852 scopus 로고
    • Membrane fusion and the alphavirus life cycle
    • KIELIAN, M. (1995). Membrane fusion and the alphavirus life cycle. Advances in Virus Research 45, 113-151.
    • (1995) Advances in Virus Research , vol.45 , pp. 113-151
    • Kielian, M.1
  • 136
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • DOI 10.1038/nrmicro1326, PII N1326
    • KIELIAN, M. & REY, F. A. (2006). Virus membrane-fusion proteins: more than one way to make a hairpin. Nature Reviews Microbiology 4, 67-76. (Pubitemid 43135288)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.1 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 139
    • 0015463581 scopus 로고
    • Interpretation of the rotation function map of satellite tobacco necrosis virus: Octahedral packing of icosahedral particles
    • KLUG, A. (1972). Interpretation of the rotation function map of satellite tobacco necrosis virus: octahedral packing of icosahedral particles. Cold Spring Harbor Symposia on Quantitative Biology 36, 483-487.
    • (1972) Cold Spring Harbor Symposia on Quantitative Biology , vol.36 , pp. 483-487
    • Klug, A.1
  • 140
    • 2742520671 scopus 로고
    • The structure of turnip yellow mosaic virus: X-ray diffraction studies
    • KLUG, A., FINCH, J.T. & FRANKLIN, R. E. (1957). The structure of turnip yellow mosaic virus: X-ray diffraction studies. Biochimica et Biophysica Acta 25, 242-252.
    • (1957) Biochimica et Biophysica Acta , vol.25 , pp. 242-252
    • Klug, A.1    Finch, J.T.2    Franklin, R.E.3
  • 141
    • 0033571522 scopus 로고    scopus 로고
    • Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor
    • DOI 10.1093/emboj/18.22.6249
    • KOLATKAR, P. R., BELLA, J., OLSON, N. H., BATOR, C. M., BAKER, T.S. & ROSSMANN, M. G. (1999). Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor. EMBO Journal 18, 6249-6259. (Pubitemid 29533229)
    • (1999) EMBO Journal , vol.18 , Issue.22 , pp. 6249-6259
    • Kolatkar, P.R.1    Bella, J.2    Olson, N.H.3    Bator, C.M.4    Baker, T.S.5    Rossmann, M.G.6
  • 144
    • 50649097269 scopus 로고    scopus 로고
    • Chapter 30: Togaviridae: The viruses and their replication
    • (EDS. D. M. Knipe & P. M. Howley), Philadelphia, PA: Lippincott Williams & Wilkins
    • KUHN, R. J. (2007). Chapter 30: Togaviridae: the viruses and their replication. In Fields Virology (EDS. D. M. Knipe & P. M. Howley), pp. 1001-1021. Philadelphia, PA: Lippincott Williams & Wilkins.
    • (2007) Fields Virology , pp. 1001-1021
    • Kuhn, R.J.1
  • 145
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: Implications for flavivirus organization, maturation, and fusion
    • DOI 10.1016/S0092-8674(02)00660-8
    • KUHN, R. J., ZHANG, W., ROSSMANN, M. G., PLETNEV, S. V., CORVER, J., LENCHES, E., JONES, C. T., MUKHOPADHYAY, S., CHIPMAN, P. R., STRAUSS, E. G., BAKER, T.S. & STRAUSS, J. H. (2002). Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717-725. (Pubitemid 34241430)
    • (2002) Cell , vol.108 , Issue.5 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossmann, M.G.3    Pletnev, S.V.4    Corver, J.5    Lenches, E.6    Jones7
  • 148
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: Lessons from paramyxovirus F
    • DOI 10.1016/j.sbi.2007.08.016, PII S0959440X07001236
    • LAMB, R.A. & JARDETZKY, T. S. (2007). Structural basis of viral invasion: lessons from paramyxovirus F. Current Opinion in Structural Biology 17, 427-436. (Pubitemid 47451774)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.4 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 149
    • 0027497651 scopus 로고
    • Double-helical RNA in satellite tobacco mosaic virus
    • DOI 10.1038/361179a0
    • LARSON, S. B., KOSZELAK, S., DAY, J., GREENWOOD, A., DODDS, J.A. & MCPHERSON, A. (1993). Double-helical RNA in satellite tobacco mosaic virus. Nature 361, 179-182. (Pubitemid 23031356)
    • (1993) Nature , vol.361 , Issue.6408 , pp. 179-182
    • Larson, S.B.1    Koszelak, S.2    Day, J.3    Greenwood, A.4    Dodds, J.A.5    McPherson, A.6
  • 151
    • 0141918780 scopus 로고    scopus 로고
    • Complementary approaches to structure determination of icosahedral viruses
    • DOI 10.1016/j.sbi.2003.09.007
    • LEE, K.K. & JOHNSON, J. E. (2003). Complementary approaches to structure determination of icosahedral viruses. Current Opinion in Structural Biology 13, 558-569. (Pubitemid 37244111)
    • (2003) Current Opinion in Structural Biology , vol.13 , Issue.5 , pp. 558-569
    • Lee, K.K.1    Johnson, J.E.2
  • 153
    • 4644242580 scopus 로고    scopus 로고
    • Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host
    • DOI 10.1016/j.cell.2004.07.022, PII S0092867404007135
    • LEIMAN, P. G., CHIPMAN, P. R., KOSTYUCHENKO, V. A., MESYANZHINOV, V.V. & ROSSMANN, M. G. (2004). Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell 118, 419-429. (Pubitemid 39485662)
    • (2004) Cell , vol.118 , Issue.4 , pp. 419-429
    • Leiman, P.G.1    Chipman, P.R.2    Kostyuchenko, V.A.3    Mesyanzhinov, V.V.4    Rossmann, M.G.5
  • 155
    • 84864829908 scopus 로고    scopus 로고
    • Structure of AAV-DJ, a retargeted gene therapy vector: Cryo-electron microscopy at 4-5 Å resolution
    • LERCH, T. F., O'DONNELL, J. K., MEYER, N. L., XIE, Q., TAYLOR, K. A., STAGG, S.M. & CHAPMAN, M. S. (2012). Structure of AAV-DJ, a retargeted gene therapy vector: cryo-electron microscopy at 4-5 Å resolution. Structure 20, 1310-1320.
    • (2012) Structure , vol.20 , pp. 1310-1320
    • Lerch, T.F.1    O'Donnell, J.K.2    Meyer, N.L.3    Xie, Q.4    Taylor, K.A.5    Stagg, S.M.6    Chapman, M.S.7
  • 156
    • 0035815282 scopus 로고    scopus 로고
    • The fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
    • DOI 10.1016/S0092-8674(01)00303-8
    • LESCAR, J., ROUSSEL, A., WEIN, M. W., NAVAZA, J., FULLER, S. D., WENGLER, G., WENGLER, G. & REY, F. A. (2001). The fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 105, 137-148. (Pubitemid 32323923)
    • (2001) Cell , vol.105 , Issue.1 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5    Wengler, G.6    Wengler, G.7    Rey, F.A.8
  • 157
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • LI, L., JOSE, J., XIANG, Y., KUHN, R. J. & ROSSMANN, M.G. (2010). Structural changes of envelope proteins during alphavirus fusion. Nature 468, 705-708.
    • (2010) Nature , vol.468 , pp. 705-708
    • Li, Y.1    Jose, J.2    Xiang, Y.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 158
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: Structure and maturation
    • DOI 10.1126/science.1153263
    • LI, L., LOK, S.-M., YU, I.-M., ZHANG, Y., KUHN, R. J., CHEN, J. & ROSSMANN, M. G. (2008). The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 319, 1830-1834. (Pubitemid 351451591)
    • (2008) Science , vol.319 , Issue.5871 , pp. 1830-1834
    • Li, L.1    Lok, S.-M.2    Yu, I.-M.3    Zhang, Y.4    Kuhn, R.J.5    Chen, J.6    Rossmann, M.G.7
  • 160
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • (EDS. D. M. Knipe & P. M. Howley), Philadelphia: Lippincott Williams & Wilkins
    • LINDENBACH, B.D. & RICE, C. M. (2001). Flaviviridae: the viruses and their replication. In Fields Virology (EDS. D. M. Knipe & P. M. Howley), pp. 991-1041. Philadelphia: Lippincott Williams & Wilkins.
    • (2001) Fields Virology , pp. 991-1041
    • Lindenbach, B.D.1    Rice, C.M.2
  • 161
    • 1542676405 scopus 로고    scopus 로고
    • Molecular biology of flaviviruses
    • DOI 10.1016/S0065-3527(03)59002-9, PII S0065352703590029
    • LINDENBACH, B.D. & RICE, C. M. (2003). Molecular biology of flaviviruses. Advances in Virus Research 59, 23-61. (Pubitemid 137639363)
    • (2003) Advances in Virus Research , vol.59 , pp. 23-61
    • Lindenbach, B.D.1    Rice, C.M.2
  • 162
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks
    • LIU, H., JIN, L., KOH, S. B., ATANASOV, I., SCHEIN, S., WU, L. & ZHOU, Z. H. (2010). Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science 329, 1038-1043.
    • (2010) Science , vol.329 , pp. 1038-1043
    • Liu, H.1    Jin, L.2    Koh, S.B.3    Atanasov, I.4    Schein, S.5    Wu, L.6    Zhou, Z.H.7
  • 164
    • 0036094683 scopus 로고    scopus 로고
    • Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum
    • DOI 10.1128/JVI.76.11.5480-5491.2002
    • LORENZ, I. C., ALLISON, S. L., HEINZ, F. X. & HELENIUS, A. (2002). Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum. Journal of Virology 76, 5480-5491. (Pubitemid 34517898)
    • (2002) Journal of Virology , vol.76 , Issue.11 , pp. 5480-5491
    • Lorenz, I.C.1    Allison, S.L.2    Heinz, F.X.3    Helenius, A.4
  • 165
    • 21244462832 scopus 로고    scopus 로고
    • Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals
    • DOI 10.1074/jbc.M504337200
    • LOZACH, P. Y., BURLEIGH, L., STAROPOLI, I., NAVARROSANCHEZ, E., HARRIAGUE, J., VIRELIZIER, J. L., REY, F. A., DESPRES, P., ARENZANA-SEISDEDOS, F. & AMARA, A. (2005). Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals. Journal of Biological Chemistry 280, 23698-23708. (Pubitemid 40884852)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23698-23708
    • Lozach, P.-Y.1    Burleigh, L.2    Staropoli, I.3    Navarro-Sanchez, E.4    Harriague, J.5    Virelizier, J.-L.6    Rey, F.A.7    Despres, P.8    Arenzana-Seisdedos, F.9    Amara, A.10
  • 166
    • 0032930413 scopus 로고    scopus 로고
    • The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependence
    • LU, Y. E., CASSESE, T. & KIELIAN, M. (1999). The cholesterol requirement for Sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependence. Journal of Virology 73, 4272-4278. (Pubitemid 29189873)
    • (1999) Journal of Virology , vol.73 , Issue.5 , pp. 4272-4278
    • Lu, Y.E.1    Cassese, T.2    Kielian, M.3
  • 167
    • 37049180758 scopus 로고
    • The atomic structure of Mengo virus at 3.0 Å resolution
    • LUO, M., VRIEND, G., KAMER, G., MINOR, I., ARNOLD, E., ROSSMANN, M. G., BOEGE, U., SCRABA, D. G., DUKE, G.M. & PALMENBERG, A. C. (1987). The atomic structure of Mengo virus at 3-0 Å resolution. Science 235, 182-191. (Pubitemid 17231335)
    • (1987) Science , vol.235 , Issue.4785 , pp. 182-191
    • Luo, M.1    Vriend, G.2    Kamer, G.3
  • 169
    • 36949067702 scopus 로고
    • Sub-units in southern bean mosaic virus
    • MAGDOFF, B. S. (1960). Sub-units in southern bean mosaic virus. Nature 185, 673-674.
    • (1960) Nature , vol.185 , pp. 673-674
    • Magdoff, B.S.1
  • 170
    • 0002748939 scopus 로고
    • Relationships among structure factors due to identical molecules in different crystallographic environments
    • MAIN, P. & ROSSMANN, M. G. (1966). Relationships among structure factors due to identical molecules in different crystallographic environments. Acta Crystallographica 21, 67-72.
    • (1966) Acta Crystallographica , vol.21 , pp. 67-72
    • Main, P.1    Rossmann, M.G.2
  • 171
    • 4544386863 scopus 로고    scopus 로고
    • Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation
    • DOI 10.1016/j.cell.2004.09.007, PII S0092867404008372
    • MANCINI, E. J., KAINOV, D. E., GRIMES, J. M., TUMA, R., BAMFORD, D.H. & STUART, D. I. (2004). Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation. Cell 118, 743-755. (Pubitemid 39221733)
    • (2004) Cell , vol.118 , Issue.6 , pp. 743-755
    • Mancini, E.J.1    Kainov, D.E.2    Grimes, J.M.3    Tuma, R.4    Bamford, D.H.5    Stuart, D.I.6
  • 176
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • DOI 10.1038/nature02165
    • MODIS, Y., OGATA, S., CLEMENTS, D. & HARRISON, S.C. (2004). Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319. (Pubitemid 38133652)
    • (2004) Nature , vol.427 , Issue.6972 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 177
    • 0037119997 scopus 로고    scopus 로고
    • Atomic model of the papillomavirus capsid
    • MODIS, Y., TRUS, B. L. & HARRISON, S. C. (2002). Atomic model of the papillomavirus capsid. EMBO Journal 21, 4754-4762.
    • (2002) EMBO Journal , vol.21 , pp. 4754-4762
    • Modis, Y.1    Trus, B.L.2    Harrison, S.C.3
  • 180
    • 17044395121 scopus 로고    scopus 로고
    • Conservation of the capsid structure in tailed dsDNA bacteriophages: The pseudo-atomic structure of Q29
    • MORAIS, M. C., CHOI, K. H., KOTI, J. S., CHIPMAN, P. R., ANDERSON, D.L. & ROSSMANN, M. G. (2005). Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudo-atomic structure of Q29. Molecular Cell 18, 149-159.
    • (2005) Molecular Cell , vol.18 , pp. 149-159
    • Morais, M.C.1    Choi, K.H.2    Koti, J.S.3    Chipman, P.R.4    Anderson, D.L.5    Rossmann, M.G.6
  • 181
    • 48149087104 scopus 로고    scopus 로고
    • Defining molecular and domain boundaries in the bacteriophage Q29 DNA packaging motor
    • MORAIS, M. C., KOTI, J. S., BOWMAN, V. D., REYESALDRETE, E., ANDERSON, D.L. & ROSSMANN, M.G. (2008). Defining molecular and domain boundaries in the bacteriophage Q29 DNA packaging motor. Structure 16, 1267-1274.
    • (2008) Structure , vol.16 , pp. 1267-1274
    • Morais, M.C.1    Koti, J.S.2    Bowman, V.D.3    Reyesaldrete, E.4    Anderson, D.L.5    Rossmann, M.G.6
  • 182
    • 34547398145 scopus 로고    scopus 로고
    • T4 and related phages: Structure and development
    • (ED. R. Calendar), New York: Oxford University Press
    • MOSIG, G. & EISERLING, F. (2006). T4 and related phages: structure and development. In The Bacteriophages (ED. R. Calendar), pp. 225-267. New York: Oxford University Press.
    • (2006) The Bacteriophages , pp. 225-267
    • Mosig, G.1    Eiserling, F.2
  • 186
    • 0017113513 scopus 로고
    • Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus
    • NAGAI, Y., KLENK, H.-D. & ROTT, R. (1976). Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology 72, 494-508.
    • (1976) Virology , vol.72 , pp. 494-508
    • Nagai, Y.1    Klenk, H.-D.2    Rott, R.3
  • 189
    • 85025335871 scopus 로고
    • Electron microscope observations on the structure of turnip yellow mosaic virus
    • NIXON, H. L. & GIBBS, A. J. (1960). Electron microscope observations on the structure of turnip yellow mosaic virus. Journal of Molecular Biology 2, 197-200.
    • (1960) Journal of Molecular Biology , vol.2 , pp. 197-200
    • Nixon, H.L.1    Gibbs, A.J.2
  • 194
    • 36949066642 scopus 로고
    • Structure of haemoglobin. A three-dimensional Fourier synthesis at 5-5-Å resolution, obtained by X-ray analysis
    • PERUTZ, M. F., ROSSMANN, M. G., CULLIS, A. F., MUIRHEAD, H., WILL, G. & NORTH, A. C. T. (1960). Structure of haemoglobin. A three-dimensional Fourier synthesis at 5-5-Å resolution, obtained by X-ray analysis. Nature 185, 416-422.
    • (1960) Nature , vol.185 , pp. 416-422
    • Perutz, M.F.1    Rossmann, M.G.2    Cullis, A.F.3    Muirhead, H.4    Will, G.5    North, A.C.T.6
  • 195
    • 0035815301 scopus 로고    scopus 로고
    • Locations of carbohydrate sites on alphavirus glycoproteins show that E1 forms an icosahedral scaffold
    • DOI 10.1016/S0092-8674(01)00302-6
    • PLETNEV, S. V., ZHANG, W., MUKHOPADHYAY, S., FISHER, B. R., HERNANDEZ, R., BROWN, D. T., BAKER, T. S., ROSSMANN, M.G. & KUHN, R. J. (2001). Locations of carbohydrate sites on alphavirus glycoproteins show that E1 forms an icosahedral scaffold. Cell 105, 127-136. (Pubitemid 32323922)
    • (2001) Cell , vol.105 , Issue.1 , pp. 127-136
    • Pletnev, S.V.1    Zhang, W.2    Mukhopadhyay, S.3    Fisher, B.R.4    Hernandez, R.5    Brown, D.T.6    Baker, T.S.7    Rossmann, M.G.8    Kuhn, R.J.9
  • 197
    • 79955438650 scopus 로고    scopus 로고
    • Structure of a packaging-defective mutant of minute virus of mice indicates that the genome is packaged via a pore at a 5-fold axis
    • PLEVKA, P., HAFENSTEIN, S., LI, L., D'ABRGAMO JR, A., COTMORE, S. F., ROSSMANN, M.G. & TATTERSALL, P. (2011a). Structure of a packaging-defective mutant of minute virus of mice indicates that the genome is packaged via a pore at a 5-fold axis. Journal of Virology 85, 4822-4827.
    • (2011) Journal of Virology , vol.85 , pp. 4822-4827
    • Plevka, P.1    Hafenstein, S.2    Li, L.3    D'Abrgamo Jr., A.4    Cotmore, S.F.5    Rossmann, M.G.6    Tattersall, P.7
  • 201
    • 67749119776 scopus 로고    scopus 로고
    • Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2
    • PLEVKA, P., TARS, K. & LILJAS, L. (2009). Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2. Protein Science 18, 1653-61.
    • (2009) Protein Science , vol.18 , pp. 1653-1661
    • Plevka, P.1    Tars, K.2    Liljas, L.3
  • 203
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • RAO, V. B. & FEISS, M. (2008). The bacteriophage DNA packaging motor. Annual Review of Genetics 42, 647-681.
    • (2008) Annual Review of Genetics , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 204
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and implications for virus assembly
    • DOI 10.1038/378743a0
    • RAO, Z., BELYAEV, A. S., FRY, E., ROY, P., JONES, I.M. & STUART, D. I. (1995). Crystal structure of SIV matrix antigen and implications for virus assembly. Nature 378, 743-747. (Pubitemid 26001950)
    • (1995) Nature , vol.378 , Issue.6558 , pp. 743-747
    • Rao, Z.1    Belyaev, A.S.2    Fry, E.3    Roy, P.4    Jonest, I.M.5    Stuart, D.I.6
  • 206
    • 77956128250 scopus 로고    scopus 로고
    • Crystal structure of human adenovirus at 3-5 Å resolution
    • Polyoma virus capsid structure at 22-5 Å resolution. Nature 295, 110-115 (issue cover). REDDY, V. S., NATCHIAR, S. K., STEWART, P.L. & NEMEROW, G. R. (2010). Crystal structure of human adenovirus at 3-5 Å resolution. Science 329, 1071-1075.
    • (2010) Science , vol.329 , pp. 1071-1075
    • Reddy, V.S.1    Natchiar, S.K.2    Stewart, P.L.3    Nemerow, G.R.4
  • 207
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A ̊ resolution
    • REY, F. A., HEINZ, F. X., MANDL, C., KUNZ, C. & HARRISON, S. C. (1995). The envelope glycoprotein from tick-borne encephalitis virus at 2 A ̊ resolution. Nature 375, 291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 208
    • 0023059423 scopus 로고
    • Three-dimensional structure of the adenovirus major coat protein hexon
    • ROBERTS, M. M., WHITE, J. L., GRüTTER, M.G. & BURNETT, R. M. (1986). Three-dimensional structure of the adenovirus major coat protein hexon. Science 232, 1148-1151.
    • (1986) Science , vol.232 , pp. 1148-1151
    • Roberts, M.M.1    White, J.L.2    Grütter, M.G.3    Burnett, R.M.4
  • 210
    • 0000731339 scopus 로고
    • Processing oscillation diffraction data for very large unit cells with an automatic convolution technique and profile fitting
    • ROSSMANN, M. G. (1979). Processing oscillation diffraction data for very large unit cells with an automatic convolution technique and profile fitting. Journal of Applied Crystallography 12, 225-238.
    • (1979) Journal of Applied Crystallography , vol.12 , pp. 225-238
    • Rossmann, M.G.1
  • 211
    • 84881036086 scopus 로고
    • Synchrotron radiation studies of large proteins and supramolecular structures
    • (ED. G.P.G. Diakun, C. D.), Daresbury: Science and Engineering Research Council
    • ROSSMANN, M. G. (1984). Synchrotron radiation studies of large proteins and supramolecular structures. In Biological Systems: Structure and Analysis (ED. G.P.G. Diakun, C. D.), pp. 28-40. Daresbury: Science and Engineering Research Council.
    • (1984) Biological Systems: Structure and Analysis , pp. 28-40
    • Rossmann, M.G.1
  • 212
    • 0024431279 scopus 로고
    • The canyon hypothesis. Hiding the host cell receptor attachment site on a viral surface from immune surveillance
    • ROSSMANN, M. G. (1989a). The canyon hypothesis. Hiding the host cell receptor attachment site on a viral surface from immune surveillance. Journal of Biological Chemistry 264, 14587-14590. (Pubitemid 19237265)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.25 , pp. 14587-14590
    • Rossmann, M.G.1
  • 213
    • 84881036541 scopus 로고
    • Determination of virus structures by the use of molecular replacement density averaging
    • (EDS. S. Bailey, E. Dodson & S. Phillips), Daresbury: Science and Engineering Research Council
    • ROSSMANN, M. G. (1989b). Determination of virus structures by the use of molecular replacement density averaging. In Improving Protein Phases. Proceedings of the Study Weekend held at Daresbury, 1988 (EDS. S. Bailey, E. Dodson & S. Phillips), pp. 49-56. Daresbury: Science and Engineering Research Council.
    • (1989) Improving Protein Phases. Proceedings of the Study Weekend Held at Daresbury , vol.1988 , pp. 49-56
    • Rossmann, M.G.1
  • 214
    • 0028032395 scopus 로고
    • Viral cell recognition and entry
    • ROSSMANN, M. G. (1994). Viral cell recognition and entry. Protein Science 3, 1712-1725. (Pubitemid 24356594)
    • (1994) Protein Science , vol.3 , Issue.10 , pp. 1712-1725
    • Rossmann, M.G.1
  • 215
    • 0033469145 scopus 로고    scopus 로고
    • Synchrotron radiation as a tool for investigating virus structures
    • ROSSMANN, M. G. (1999). Synchrotron radiation as a tool for investigating virus structures. Journal of Synchrotron Radiation 6, 816-821. (Pubitemid 129494691)
    • (1999) Journal of Synchrotron Radiation , vol.6 , Issue.4 , pp. 816-821
    • Rossmann, M.G.1
  • 216
  • 217
    • 0022401514 scopus 로고
    • Structure of a human common cold virus and functional relationship to other picornaviruses
    • DOI 10.1038/317145a0
    • ROSSMANN, M. G., ARNOLD, E., ERICKSON, J. W., FRANKENBERGER, E. A., GRIFFITH, J. P., HECHT, H. J., JOHNSON, J. E., KAMER, G., LUO, M., MOSSER, A. G., RUECKERT, R. R., SHERRY, B. & VRIEND, G. (1985). Structure of a human common cold virus and functional relationship to other picornaviruses. Nature 317, 145-153. (Pubitemid 16243130)
    • (1985) Nature , vol.317 , Issue.6033 , pp. 145-153
    • Rossmann, M.G.1    Arnold, E.2    Erickson, J.W.3
  • 219
    • 0034630455 scopus 로고    scopus 로고
    • Cell recognition and entry by rhino- and enteroviruses
    • DOI 10.1006/viro.2000.0258
    • ROSSMANN, M. G., BELLA, J., KOLATKAR, P. R., HE, Y., WIMMER, E., KUHN, R.J. & BAKER, T. S. (2000). Minireview: cell recognition and entry by rhino- and enteroviruses. Virology 269, 239-247. (Pubitemid 30210896)
    • (2000) Virology , vol.269 , Issue.2 , pp. 239-247
    • Rossmann, M.G.1    Bella, J.2    Kolatkar, P.R.3    He, Y.4    Wimmer, E.5    Kuhn, R.J.6    Baker, T.S.7
  • 220
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • ROSSMANN, M. G.& BLOW, D. M. (1962). The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallographica 15, 24-31.
    • (1962) Acta Crystallographica , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 221
    • 0001704894 scopus 로고
    • Oscillation photography of radiation-sensitive crystals using a synchrotron source
    • ROSSMANN, M.G. & ERICKSON, J. W. (1983). Oscillation photography of radiation-sensitive crystals using a synchrotron source. Journal of Applied Crystallography 16, 629-636.
    • (1983) Journal of Applied Crystallography , vol.16 , pp. 629-636
    • Rossmann, M.G.1    Erickson, J.W.2
  • 223
    • 0036645722 scopus 로고    scopus 로고
    • Picornavirus-receptor interactions
    • DOI 10.1016/S0966-842X(02)02383-1, PII S0966842X02023831
    • ROSSMANN, M. G., HE, Y. & KUHN, R. J. (2002). Picornavirus-receptor interactions. Trends in Microbiology 10, 324-331. (Pubitemid 34756532)
    • (2002) Trends in Microbiology , vol.10 , Issue.7 , pp. 324-331
    • Rossmann, M.G.1    He, Y.2    Kuhn, R.J.3
  • 227
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide- binding protein
    • ROSSMANN, M. G., MORAS, D. & OLSEN, K.W. (1974). Chemical and biological evolution of a nucleotide- binding protein. Nature 250, 194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 228
    • 0023894622 scopus 로고
    • Conservation of the putative receptor attachment site in picornaviruses
    • ROSSMANN, M.G. & PALMENBERG, A. C. (1988). Conservation of the putative receptor attachment site in picornaviruses. Virology 164, 373-382.
    • (1988) Virology , vol.164 , pp. 373-382
    • Rossmann, M.G.1    Palmenberg, A.C.2
  • 229
    • 33644799064 scopus 로고    scopus 로고
    • Structure and interactions at the viral surface of the envelope protein E1 of semliki forest virus
    • DOI 10.1016/j.str.2005.09.014, PII S0969212605003941
    • ROUSSEL, A., LESCAR, J., VANEY, M. C., WENGLER, G. & REY, F. A. (2006). Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus. Structure 14, 75-86. (Pubitemid 43350075)
    • (2006) Structure , vol.14 , Issue.1 , pp. 75-86
    • Roussel, A.1    Lescar, J.2    Vaney, M.-C.3    Wengler, G.4    Wengler, G.5    Rey, F.A.6
  • 230
    • 84864834137 scopus 로고    scopus 로고
    • Small terminase couples viral DNA binding to genome-packaging ATPase activity
    • ROY, A., BHARDWAJ, A., DATTA, P., LANDER, G.C. & CINGOLANI, G. (2012). Small terminase couples viral DNA binding to genome-packaging ATPase activity. Structure 20, 1403-1413.
    • (2012) Structure , vol.20 , pp. 1403-1413
    • Roy, A.1    Bhardwaj, A.2    Datta, P.3    Lander, G.C.4    Cingolani, G.5
  • 231
    • 0015449722 scopus 로고
    • Isolation of paramyxovirus glycoproteins. Association of both hemagglutinating and neuraminidase activities with the larger SV5 glycoprotein
    • SCHEID, A., CALIGUIRI, L. A., COMPANS, R.W. & CHOPPIN, P. W. (1972). Isolation of paramyxovirus glycoproteins. Association of both hemagglutinating and neuraminidase activities with the larger SV5 glycoprotein. Virology 50, 640-652.
    • (1972) Virology , vol.50 , pp. 640-652
    • Scheid, A.1    Caliguiri, L.A.2    Compans, R.W.3    Choppin, P.W.4
  • 232
    • 0022644644 scopus 로고
    • Use of monoclonal antibodies to identify four neutralization immunogens on a common cold picornavirus, human rhinovirus 14
    • SHERRY, B., MOSSER, A. G., COLONNO, R.J. & RUECKERT, R. R. (1986). Use of monoclonal antibodies to identify four neutralization immunogens on a common cold picornavirus, human rhinovirus 14. Journal of Virology 57, 246-257. (Pubitemid 16147940)
    • (1986) Journal of Virology , vol.57 , Issue.1 , pp. 246-257
    • Sherry, B.1    Mosser, A.G.2    Colonno, R.J.3    Rueckert, R.R.4
  • 233
    • 0021971892 scopus 로고
    • Evidence for at least two dominant neutralization antigens on human rhinovirus 14
    • SHERRY, B. & RUECKERT, R. (1985). Evidence for at least two dominant neutralization antigens on human rhinovirus 14. Journal of Virology 53, 137-143. (Pubitemid 15194946)
    • (1985) Journal of Virology , vol.53 , Issue.1 , pp. 137-143
    • Sherry, B.1    Rueckert, R.2
  • 234
    • 36348992573 scopus 로고    scopus 로고
    • Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain
    • DOI 10.1083/jcb.200705062
    • SHNYROVA, A. V., AYLLON, J., MIKHALYOV, I. I., VILLAR, E., ZIMMERBERG, J. & FROLOV, V. A. (2007). Vesicle formation by self-assembly of membrane-bound matrix proteins into a fluidlike budding domain. Journal of Cell Biology 179, 627-633. (Pubitemid 350146250)
    • (2007) Journal of Cell Biology , vol.179 , Issue.4 , pp. 627-633
    • Shnyrova, A.V.1    Ayllon, J.2    Mikhalyov, I.I.3    Villar, E.4    Zimmerberg, J.5    Frolov, V.A.6
  • 236
    • 0032533456 scopus 로고    scopus 로고
    • The structure of an insect parvovirus (Galleria mellonella densovirus) at 3.7 Å resolution
    • SIMPSON, A. A., CHIPMAN, P. R., BAKER, T. S., TIJSSEN, P.& ROSSMANN, M. G. (1998). The structure of an insect parvovirus (Galleria mellonella densovirus) at 3-7 Å resolution. Structure 6, 1355-1367. (Pubitemid 28541880)
    • (1998) Structure , vol.6 , Issue.11 , pp. 1355-1367
    • Simpson, A.A.1    Chipman, P.R.2    Baker, T.S.3    Tijssen, P.4    Rossmann, M.G.5
  • 240
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage φ29 portal motor can package DNA against a large internal force
    • DOI 10.1038/35099581
    • SMITH, D. E., TANS, S. J., SMITH, S. B., GRIMES, S., ANDERSON, D. L. & BUSTAMANTE, C. (2001). The bacteriophage Q29 portal motor can package DNA against a large internal force. Nature 413, 748-752. (Pubitemid 33009954)
    • (2001) Nature , vol.413 , Issue.6857 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 241
    • 0029743275 scopus 로고    scopus 로고
    • Neutralizing antibody to human rhinovirus 14 penetrates the receptor- binding canyon
    • DOI 10.1038/383350a0
    • SMITH, T. J., CHASE, E. S., SCHMIDT, T. J., OLSON, N.H. & BAKER, T. S. (1996). Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon. Nature 383, 350-354. (Pubitemid 26321767)
    • (1996) Nature , vol.383 , Issue.6598 , pp. 350-354
    • Smith, T.J.1    Chase, E.S.2    Schmidt, T.J.3    Olson, N.H.4    Baker, T.S.5
  • 242
    • 0022489613 scopus 로고
    • The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating
    • SMITH, T. J., KREMER, M. J., LUO, M., VRIEND, G., ARNOLD, E., KAMER, G., ROSSMANN, M. G., MCKINLAY, M. A., DIANA, G.D. & OTTO, M. J. (1986). The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. Science 233, 1286-1293. (Pubitemid 16002229)
    • (1986) Science , vol.233 , Issue.4770 , pp. 1286-1293
    • Smith, T.J.1    Kremer, M.J.2    Luo, M.3
  • 244
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • STADLER, K., ALLISON, S. L., SCHALICH, J. & HEINZ, F.X. (1997). Proteolytic activation of tick-borne encephalitis virus by furin. Journal of Virology 71, 8475-8481. (Pubitemid 27446428)
    • (1997) Journal of Virology , vol.71 , Issue.11 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 245
    • 0024521781 scopus 로고
    • A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses
    • DOI 10.1016/0092-8674(89)90689-2
    • STAUNTON, D. E., MERLUZZI, V. J., ROTHLEIN, R., BARTON, R., MARLIN, S.D. & SPRINGER, T. A. (1989). A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses. Cell 56, 849-853. (Pubitemid 19082520)
    • (1989) Cell , vol.56 , Issue.5 , pp. 849-853
    • Staunton, D.E.1    Merluzzi, V.J.2    Rothlein, R.3    Barton, R.4    Marlin, S.D.5    Springer, T.A.6
  • 246
    • 0030584124 scopus 로고    scopus 로고
    • The structure of simian virus 40 refined at 3.1 Å resolution
    • STEHLE, T., GAMBLIN, S. J., YAN, Y. & HARRISON, S.C. (1996). The structure of simian virus 40 refined at 3-1 Å resolution. Structure 4, 165-182. (Pubitemid 126658980)
    • (1996) Structure , vol.4 , Issue.2 , pp. 165-182
    • Stehle, T.1    Gamblin, S.J.2    Yan, Y.3    Harrison, S.C.4
  • 247
    • 0029795282 scopus 로고    scopus 로고
    • Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus
    • STIASNY, K., ALLISON, S. L.,MARCHLER-BAUER, A., KUNZ, C. & HEINZ, F. X. (1996). Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. Journal of Virology 70, 8142-8147. (Pubitemid 26339127)
    • (1996) Journal of Virology , vol.70 , Issue.11 , pp. 8142-8147
    • Stiasny, K.1    Allison, S.L.2    Marchler-Bauer, A.3    Kunz, C.4    Heinz, F.X.5
  • 248
    • 33749042583 scopus 로고    scopus 로고
    • Flavivirus membrane fusion
    • DOI 10.1099/vir.0.82210-0
    • STIASNY, K. & HEINZ, F. X. (2006). Flavivirus membrane fusion. Journal of General Virology 87, 2755-2766. (Pubitemid 44463884)
    • (2006) Journal of General Virology , vol.87 , Issue.10 , pp. 2755-2766
    • Stiasny, K.1    Heinz, F.X.2
  • 251
    • 0017740556 scopus 로고
    • Structure of RNA and RNA binding site in tobacco mosaic virus from 4 Å map calculated from X ray fibre diagrams
    • STUBBS, G., WARREN, S. &HOLMES, K. (1977). Structure of RNA and RNA binding site in tobacco mosaic virus from 4 A ̊ map calculated from X-ray fibre diagrams. Nature 267, 216-221. (Pubitemid 8095583)
    • (1977) Nature , vol.267 , Issue.5608 , pp. 216-221
    • Stubbs, G.1    Warren, S.2    Holmes, K.3
  • 254
    • 33947281384 scopus 로고    scopus 로고
    • The Structure of the ATPase that Powers DNA Packaging into Bacteriophage T4 Procapsids
    • DOI 10.1016/j.molcel.2007.02.013, PII S109727650700113X
    • SUN, S., KONDABAGIL, K., GENTZ, P. M., ROSSMANN, M.G. & RAO, V. B. (2007). The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids. Molecular Cell 25, 943-949. (Pubitemid 46436529)
    • (2007) Molecular Cell , vol.25 , Issue.6 , pp. 943-949
    • Sun, S.1    Kondabagil, K.2    Gentz, P.M.3    Rossmann, M.G.4    Rao, V.B.5
  • 256
    • 84879051627 scopus 로고    scopus 로고
    • Structural analyses at pseudo atomic resolution of Chikungunya virus and antibodies show mechanisms of neutralization
    • in press. doi: 10.7554/eLife.00435
    • SUN, S., XIANG, Y., WATARU, A., HOLDAWAY, H., PAL, P., ZHANG, X., DIAMOND, M. S., NABEL, G. J. & ROSSMANN, M. G. (2013). Structural analyses at pseudo atomic resolution of Chikungunya virus and antibodies show mechanisms of neutralization. eLIFE, in press. doi: 10.7554/eLife.00435.
    • (2013) ELIFE
    • Sun, S.1    Xiang, Y.2    Wataru, A.3    Holdaway, H.4    Pal, P.5    Zhang, X.6    Diamond, M.S.7    Nabel, G.J.8    Rossmann, M.G.9
  • 257
    • 82555176572 scopus 로고    scopus 로고
    • Molecular links between the E2 envelope glycoprotein and nucleocapsid core in Sindbis virus
    • TANG, J., JOSE, J., CHIPMAN, P., ZHANG, W., KUHN, R. J. & BAKER, T. S. (2011). Molecular links between the E2 envelope glycoprotein and nucleocapsid core in Sindbis virus. Journal of Molecular Biology 414, 442-459.
    • (2011) Journal of Molecular Biology , vol.414 , pp. 442-459
    • Tang, J.1    Jose, J.2    Chipman, P.3    Zhang, W.4    Kuhn, R.J.5    Baker, T.S.6
  • 258
    • 0032582665 scopus 로고    scopus 로고
    • Assembly of a tailed bacterial virus and its genome release studied in three dimensions
    • DOI 10.1016/S0092-8674(00)81773-0
    • TAO, Y., OLSON, N. H., XU, W., ANDERSON, D. L., ROSSMANN, M.G. & BAKER, T. S. (1998). Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell 95, 431-437. (Pubitemid 28507330)
    • (1998) Cell , vol.95 , Issue.3 , pp. 431-437
    • Tao, Y.1    Olson, N.H.2    Xu, W.3    Anderson, D.L.4    Rossmann, M.G.5    Baker, T.S.6
  • 259
    • 0042463705 scopus 로고    scopus 로고
    • The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold
    • DOI 10.1016/S0022-2836(03)00755-1
    • THOMASSEN, E., GIELEN, G., SCHUTZ, M., SCHOEHN, G., ABRAHAMS, J. P., MILLER, S. & VAN RAAIJ, M. J. (2003). The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold. Journal of Molecular Biology 331, 361-373. (Pubitemid 36904021)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.2 , pp. 361-373
    • Thomassen, E.1    Gielen, G.2    Schutz, M.3    Schoehn, G.4    Abrahams, J.P.5    Miller, S.6    Van Raaij, M.J.7
  • 264
    • 0025344593 scopus 로고
    • The three-dimensional structure of the bacterial virus MS2
    • VALEGÅRD, K., LILJAS, L., FRIDBORG, K.&UNGE, T. (1990). The three-dimensional structure of the bacterial virus MS2. Nature 345, 36-41.
    • (1990) Nature , vol.345 , pp. 36-41
    • Valegård, K.1    Liljas, L.2    Fridborg, K.3    Unge, T.4
  • 265
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • DOI 10.1038/371623a0
    • VALEGÅRD, K., MURRAY, J. B., STOCKLEY, P. G., STONEHOUSE, N. J. & LILJAS, L. (1994). Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 371, 623-626. (Pubitemid 24315746)
    • (1994) Nature , vol.371 , Issue.6498 , pp. 623-626
    • Valegard, K.1    Murray, J.B.2    Stockley, P.G.3    Stonehouset, N.J.4    Liljas, L.5
  • 266
    • 0035861998 scopus 로고    scopus 로고
    • Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre
    • DOI 10.1006/jmbi.2000.5204
    • VAN RAAIJ, M. J., SCHOEHN, G., BURDA, M. R. &MILLER, S. (2001). Crystal structure of a heat and protease-stable part of the bacteriophage T4 short tail fibre. Journal of Molecular Biology 314, 1137-1146. (Pubitemid 34073076)
    • (2001) Journal of Molecular Biology , vol.314 , Issue.5 , pp. 1137-1146
    • Van Raaij, M.J.1    Schoehn, G.2    Burda, M.R.3    Miller, S.4
  • 267
    • 0016821407 scopus 로고
    • Sindbis virus glycoproteins form a regular icosahedral surface lattice
    • VON BONSDORFF, C.H. & HARRISON, S. C. (1975). Sindbis virus glycoproteins form a regular icosahedral surface lattice. Journal of Virology 16, 141-145.
    • (1975) Journal of Virology , vol.16 , pp. 141-145
    • Von Bonsdorff, C.H.1    Harrison, S.C.2
  • 268
    • 0018141590 scopus 로고
    • Hexagonal glycoprotein arrays from Sindbis virus membranes
    • VON BONSDORFF, C.H. & HARRISON, S. C. (1978). Hexagonal glycoprotein arrays from Sindbis virus membranes. Journal of Virology 28, 578-583. (Pubitemid 9041713)
    • (1978) Journal of Virology , vol.28 , Issue.2 , pp. 578-583
    • Von Bonsdorff, C.H.1    Harrison, S.C.2
  • 272
    • 33749048664 scopus 로고
    • Genetical implications of the structure of deoxyribonucleic acid
    • WATSON, J.D. & CRICK, F. H. C. (1953a). Genetical implications of the structure of deoxyribonucleic acid. Nature 171, 964-967.
    • (1953) Nature , vol.171 , pp. 964-967
    • Watson, J.D.1    Crick, F.H.C.2
  • 273
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids: A structure for deoxyribose nucleic acid
    • WATSON, J.D. & CRICK, F. H. C. (1953b). Molecular structure of nucleic acids: a structure for deoxyribose nucleic acid. Nature 171, 737-738.
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 274
  • 275
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • DOI 10.1038/289373a0
    • WILEY, D. C., WILSON, I.A. & SKEHEL, J. J. (1981). Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 289, 373-378. (Pubitemid 11135143)
    • (1981) Nature , vol.289 , Issue.5796 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2
  • 276
    • 4243385935 scopus 로고
    • The polyhedral form of the Tipula iridescent virus
    • WILLIAMS, R.C. & SMITH, K. M. (1958). The polyhedral form of the Tipula iridescent virus. Biochimica et Biophysica Acta 28, 464-469.
    • (1958) Biochimica et Biophysica Acta , vol.28 , pp. 464-469
    • Williams, R.C.1    Smith, K.M.2
  • 278
    • 0014546234 scopus 로고
    • An electron microscope study of the structure of Sericesthis iridescent virus
    • WRIGLEY, N. G. (1969). An electron microscope study of the structure of Sericesthis iridescent virus. Journal of General Virology 5, 123-134.
    • (1969) Journal of General Virology , vol.5 , pp. 123-134
    • Wrigley, N.G.1
  • 279
    • 0027431751 scopus 로고
    • The canine parvovirus empty capsid structure
    • DOI 10.1006/jmbi.1993.1502
    • WU, H. & ROSSMANN, M. G. (1993). The canine parvovirus empty capsid structure. Journal of Molecular Biology 233, 231-244. (Pubitemid 23297593)
    • (1993) Journal of Molecular Biology , vol.233 , Issue.2 , pp. 231-244
    • Wu, H.1    Rossmann, M.G.2
  • 285
    • 84881072729 scopus 로고    scopus 로고
    • Design of capsid-binding antiviral agents against human rhinoviruses
    • (EDS M Agbandje-McKenna & R McKenna), London, England: Royal Society of Chemistry
    • XIAO, C., MCKINLAY, M.A. & ROSSMANN, M. G. (2011). Design of capsid-binding antiviral agents against human rhinoviruses. In RSC Biomolecular Sciences Series, No. 21, Structural Virology (EDS. M. Agbandje-McKenna & R. McKenna), pp. 321-339. London, England: Royal Society of Chemistry.
    • (2011) RSC Biomolecular Sciences Series, No 21 Structural Virology , pp. 321-339
    • Xiao, C.1    McKinlay, M.A.2    Rossmann, M.G.3
  • 286
    • 84855700639 scopus 로고    scopus 로고
    • Structures of giant icosahedral eukaryotic dsDNA viruses
    • XIAO, C. & ROSSMANN, M. G. (2011). Structures of giant icosahedral eukaryotic dsDNA viruses. Current Opinion in Virology 1, 101-109.
    • (2011) Current Opinion in Virology , vol.1 , pp. 101-109
    • Xiao, C.1    Rossmann, M.G.2
  • 288
    • 0030573015 scopus 로고    scopus 로고
    • Canine parvovirus capsid structure, analyzed at 2.9 Å resolution
    • DOI 10.1006/jmbi.1996.0657
    • XIE, Q. & CHAPMAN, M. S. (1996). Canine parvovirus capsid structure, analyzed at 2-9 Å resolution. Journal of Molecular Biology 264, 497-520. (Pubitemid 27010741)
    • (1996) Journal of Molecular Biology , vol.264 , Issue.3 , pp. 497-520
    • Xie, Q.1    Chapman, M.S.2
  • 289
    • 0037334514 scopus 로고    scopus 로고
    • The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions
    • DOI 10.1016/S0969-2126(03)00023-6, PII S0969212603000236
    • XU, L., BENSON, S. D., BUTCHER, S. J., BAMFORD, D.H. & BURNETT, R. M. (2003). The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions. Structure 11, 309-322. (Pubitemid 36292170)
    • (2003) Structure , vol.11 , Issue.3 , pp. 309-322
    • Xu, L.1    Benson, S.D.2    Butcher, S.J.3    Bamford, D.H.4    Burnett, R.M.5
  • 290
    • 21644489830 scopus 로고    scopus 로고
    • The marine algal virus PpV01 has an icosahedral capsid with T=219 quasisymmetry
    • DOI 10.1128/JVI.79.14.9236-9243.2005
    • YAN, X., CHIPMAN, P. R., CASTBERG, T., BRATBAK, G. & BAKER, T. S. (2005). The marine algal virus PpV01 has an icosahedral capsid with T=219 quasi-symmetry. Journal of Virology 79, 9236-9243. (Pubitemid 40934835)
    • (2005) Journal of Virology , vol.79 , Issue.14 , pp. 9236-9243
    • Yan, X.1    Chipman, P.R.2    Castberg, T.3    Bratbak, G.4    Baker, T.S.5
  • 294
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • DOI 10.1038/nature04322
    • YIN, H. S., WEN, X., PATERSON, R. G., LAMB, R.A. & JARDETZKY, T. S. (2006). Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439, 38-44. (Pubitemid 43053622)
    • (2006) Nature , vol.439 , Issue.7072 , pp. 38-44
    • Yin, H.-S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 295
    • 70450208515 scopus 로고    scopus 로고
    • Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion
    • YU, I.-M., HOLDAWAY, H. A., CHIPMAN, P. R., KUHN, R. J., ROSSMANN, M.G. & CHEN, J. (2009). Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. Journal of Virology 83, 12101-12107.
    • (2009) Journal of Virology , vol.83 , pp. 12101-12107
    • Yu, I.M.1    Holdaway, H.A.2    Chipman, P.R.3    Kuhn, R.J.4    Rossmann, M.G.5    Chen, J.6
  • 296
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • DOI 10.1126/science.1153264
    • YU, I.-M., ZHANG, W., HOLDAWAY, H. A., LI, L., KOSTYUCHENKO, V. A., CHIPMAN, P. R., KUHN, R. J., ROSSMANN, M.G. & CHEN, J. (2008). Structure of the immature dengue virus at low pH primes proteolytic maturation. Science 319, 1834-1837. (Pubitemid 351451592)
    • (2008) Science , vol.319 , Issue.5871 , pp. 1834-1837
    • Yu, I.-M.1    Zhang, W.2    Holdaway, H.A.3    Li, L.4    Kostyuchenko, V.A.5    Chipman, P.R.6    Kuhn, R.J.7    Rossmann, M.G.8    Chen, J.9
  • 305
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase λ3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å
    • DOI 10.1038/nsb1009
    • ZHANG, X., WALKER, S. B., CHIPMAN, P. R., NIBERT, M. L. & BAKER, T. S. (2003b). Reovirus polymerase l3 localized by cryo-electron microscopy of virions at a resolution of 7-6 Å . Nature Structural Biology 10, 1011-1018. (Pubitemid 37500493)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5
  • 308
  • 309
    • 4444338894 scopus 로고    scopus 로고
    • Conformational changes of the flavivirus E glycoprotein
    • DOI 10.1016/j.str.2004.06.019, PII S0969212604002722
    • ZHANG, Y., ZHANG, W., OGATA, S., CLEMENTS, D., STRAUSS, J. H., BAKER, T. S., KUHN, R. J. & ROSSMANN, M.G. (2004). Conformational changes of the flavivirus E glycoprotein. Structure 12, 1607-1618. (Pubitemid 39200514)
    • (2004) Structure , vol.12 , Issue.9 , pp. 1607-1618
    • Zhang, Y.1    Zhang, W.2    Ogata, S.3    Clements, D.4    Strauss, J.H.5    Baker, T.S.6    Kuhn, R.J.7    Rossmann, M.G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.