메뉴 건너뛰기




Volumn 74, Issue 1, 1998, Pages 576-588

Refinement of herpesvirus B-capsid structure on parallel supercomputers

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER; CONFERENCE PAPER; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; HERPES SIMPLEX VIRUS 1; NONHUMAN; PROTEIN STRUCTURE; THREE DIMENSIONAL IMAGING; VIRUS CAPSID;

EID: 0031982794     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77816-6     Document Type: Conference Paper
Times cited : (57)

References (53)
  • 1
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker, T. S., and R. H. Cheng. 1996. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116:120-130.
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 2
    • 0023704386 scopus 로고
    • Reconstruction of the three-dimensional structure of simian virus 40 and visualization of chromatin core
    • Baker, T. S., J. Drak, and M. Bina. 1988. Reconstruction of the three-dimensional structure of simian virus 40 and visualization of chromatin core. Proc. Natl. Acad. Sci. USA. 85:422-426.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 422-426
    • Baker, T.S.1    Drak, J.2    Bina, M.3
  • 3
    • 0000677137 scopus 로고    scopus 로고
    • Principles of virus structure determination
    • Oxford University Press, New York
    • Baker, T. S., and J. E. Johnson. 1997. Principles of virus structure determination. In Structural Biology of Viruses. Oxford University Press, New York. 38-79.
    • (1997) Structural Biology of Viruses , pp. 38-79
    • Baker, T.S.1    Johnson, J.E.2
  • 4
    • 0030584685 scopus 로고    scopus 로고
    • Difference imaging reveals ordered regions of RNA in turnip yellow mosaic virus
    • Böttcher, B., and R. A. Crowther. 1996. Difference imaging reveals ordered regions of RNA in turnip yellow mosaic virus. Structure. 4:387-394.
    • (1996) Structure , vol.4 , pp. 387-394
    • Böttcher, B.1    Crowther, R.A.2
  • 5
    • 1842409555 scopus 로고    scopus 로고
    • Detemination of the fold of hepatitis B virus core protein by electron cryo-microscopy
    • Böttcher, B., S. A. Wynne, and R. A. Crowther. 1997. Detemination of the fold of hepatitis B virus core protein by electron cryo-microscopy. Nature. 386:88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 7
    • 0025970346 scopus 로고
    • Contrast analysis of cryo-imagcs of n-paraffin recorded at 400 kV out to 2.1 Å resolution
    • Brink, J., and W. Chiu. 1991. Contrast analysis of cryo-imagcs of n-paraffin recorded at 400 kV out to 2.1 Å resolution. J. Microsc. 161: 279-295.
    • (1991) J. Microsc. , vol.161 , pp. 279-295
    • Brink, J.1    Chiu, W.2
  • 8
    • 0002917513 scopus 로고    scopus 로고
    • Principles of virion structure, function and assembly
    • Oxford University Press, New York
    • Casjens, S. 1997. Principles of virion structure, function and assembly. In Structural Biology of Viruses. Oxford University Press, New York. 3-37.
    • (1997) Structural Biology of Viruses , pp. 3-37
    • Casjens, S.1
  • 9
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar, D. L. D., and A. Klug. 1962. Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27:1-32.
    • (1962) Cold Spring Harb. Symp. Quant. Biol. , vol.27 , pp. 1-32
    • Caspar, D.L.D.1    Klug, A.2
  • 10
    • 0026540521 scopus 로고
    • Cauliflower mosaic virus: A 420 subunit (T = 7), multilayer structure
    • Cheng, R. H., N. H. Olson, and T. S. Baker. 1992. Cauliflower mosaic virus: a 420 subunit (T = 7), multilayer structure. Virology. 186: 655-668.
    • (1992) Virology , vol.186 , pp. 655-668
    • Cheng, R.H.1    Olson, N.H.2    Baker, T.S.3
  • 11
    • 0028773272 scopus 로고
    • Functional implications of quasi-equivalence in a T = 3 icosahedral animal virus established by cryo-electron microscopy and x-ray crystallography
    • Cheng, R. H., V. S. Reddy, N. H. Olson, A. J. Fisher, T. S. Baker, and J. E. Johnson. 1994. Functional implications of quasi-equivalence in a T = 3 icosahedral animal virus established by cryo-electron microscopy and x-ray crystallography. Structure. 2:271-282.
    • (1994) Structure , vol.2 , pp. 271-282
    • Cheng, R.H.1    Reddy, V.S.2    Olson, N.H.3    Fisher, A.J.4    Baker, T.S.5    Johnson, J.E.6
  • 12
    • 0022924042 scopus 로고
    • Potential for high-resolution electron crystallography at intermediate high voltage
    • Chiu, W., T.-W. Jengs L. L. Degn, and B. V. Prasad. 1986. Potential for high-resolution electron crystallography at intermediate high voltage. Ann. N. Y. Acad. Sci. 483:149-156.
    • (1986) Ann. N. Y. Acad. Sci. , vol.483 , pp. 149-156
    • Chiu, W.1    Jengs, T.-W.2    Degn, L.L.3    Prasad, B.V.4
  • 13
    • 0028221575 scopus 로고
    • Structural studies of virus-antibody complexes by electron cryomicroscopy and x-ray crystallography
    • Chiu, W., and T. J. Smith. 1994. Structural studies of virus-antibody complexes by electron cryomicroscopy and x-ray crystallography. Curr. Opin. Struct. Biol. 4:219-224.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 219-224
    • Chiu, W.1    Smith, T.J.2
  • 14
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of the 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway, J. F., N. Cheng, A. Zlotnick, P. T. Wingfield, S. J. Stahl, and A. C. Steven. 1997. Visualization of the 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature. 386:91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 15
    • 0028847173 scopus 로고
    • Proteolytic and conformational control of virus capsid maturation: The bacteriophage HK97 system
    • Conway, J. F., R. L. Duda, R. W. Hendrix, and A. C. Steven. 1995. Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system. J. Mol. Biol. 253:86-99.
    • (1995) J. Mol. Biol. , vol.253 , pp. 86-99
    • Conway, J.F.1    Duda, R.L.2    Hendrix, R.W.3    Steven, A.C.4
  • 16
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther, R. A. 1971. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Philos. Trans. R. Soc. Lond. B. 261:221-230.
    • (1971) Philos. Trans. R. Soc. Lond. B , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 17
    • 0014894609 scopus 로고
    • The reconstruction of a three-dimensional structure from projections and its application to electron microscopy
    • Crowther, R. A., D. J. DeRosier, and A. Klug. 1970. The reconstruction of a three-dimensional structure from projections and its application to electron microscopy. Proc. R. Soc. Lond. 317:319-340.
    • (1970) Proc. R. Soc. Lond. , vol.317 , pp. 319-340
    • Crowther, R.A.1    DeRosier, D.J.2    Klug, A.3
  • 18
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional structures from electron micrographs
    • DeRosier, D. J., and A. Klug. 1968. Reconstruction of three-dimensional structures from electron micrographs. Nature. 217:130-134.
    • (1968) Nature , vol.217 , pp. 130-134
    • Derosier, D.J.1    Klug, A.2
  • 19
    • 0026031904 scopus 로고
    • Spot-scan imaging in transmission electron microscopy
    • Downing, K. H. 1991. Spot-scan imaging in transmission electron microscopy. Science. 251:53-59.
    • (1991) Science , vol.251 , pp. 53-59
    • Downing, K.H.1
  • 20
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformations
    • Dryden, K. A., G. J. Wang, M. Yeager, M. L. Nibert, K. M. Coombs, D. B. Furlong, B. N. Fields, and T. S. Baker. 1993. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformations. J. Cell Biol. 122:1023-1041.
    • (1993) J. Cell Biol. , vol.122 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.J.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 21
    • 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
  • 22
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles - The uncommon line
    • Fuller, S. D., S. J. Butcher, R. H. Cheng, and T. S. Baker. 1996. Three-dimensional reconstruction of icosahedral particles - the uncommon line. J. Struct. Biol. 116:48-55.
    • (1996) J. Struct. Biol. , vol.116 , pp. 48-55
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 23
    • 0001926296 scopus 로고    scopus 로고
    • Virus structure
    • Lippincott-Raven, Philadelphia
    • Harrison, S., D. C. Wiley, and J. J. Skehel. 1996. Virus structure. In Virology. Lippincott-Raven, Philadelphia. 59-100.
    • (1996) Virology , pp. 59-100
    • Harrison, S.1    Wiley, D.C.2    Skehel, J.J.3
  • 25
    • 0028732612 scopus 로고
    • Orientation determination in the 3D reconstruction of icosahedral viruses using a parallel computer
    • IEEE Computer Society Press, Los Alamitos, CA
    • Johnson, C. A., N. I. Weisenfeld, J. F. C. B. L. Trus, R. L. Martino, and A. C. Steven. 1994. Orientation determination in the 3D reconstruction of icosahedral viruses using a parallel computer. In Supercomputing '94. IEEE Computer Society Press, Los Alamitos, CA. 550-559.
    • (1994) Supercomputing '94 , pp. 550-559
    • Johnson, C.A.1    Weisenfeld, N.I.2    Trus, J.F.C.B.L.3    Martino, R.L.4    Steven, A.C.5
  • 26
    • 0030026807 scopus 로고    scopus 로고
    • Functional implications of protein-protein interactions in icosahedral viruses
    • Johnson, J. E. 1996. Functional implications of protein-protein interactions in icosahedral viruses. Proc. Natl. Acad. Sci. USA. 93:27-33.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 27-33
    • Johnson, J.E.1
  • 27
    • 0001841724 scopus 로고
    • TreadMarks: Distributed shared memory on standard workstations and operating systems
    • Keleher, P., S. Dwarkadas, A. L. Cox, and W. Zwaenepoel. 1994. TreadMarks: distributed shared memory on standard workstations and operating systems. In Winter 94 usenix conference. 115-131.
    • (1994) Winter 94 Usenix Conference , pp. 115-131
    • Keleher, P.1    Dwarkadas, S.2    Cox, A.L.3    Zwaenepoel, W.4
  • 31
  • 33
    • 0027291013 scopus 로고
    • Structure of the herpes simplex virus capsid: Molecular composition of the pentons and the triplexes
    • Newcomb, W. W., B. L. Trus, F. P. Booy, A. C. Steven, J. S. Wall, and J. C. Brown. 1993. Structure of the herpes simplex virus capsid: molecular composition of the pentons and the triplexes. J. Mol. Biol. 232: 499-511.
    • (1993) J. Mol. Biol. , vol.232 , pp. 499-511
    • Newcomb, W.W.1    Trus, B.L.2    Booy, F.P.3    Steven, A.C.4    Wall, J.S.5    Brown, J.C.6
  • 34
    • 0024475524 scopus 로고
    • Magnification calibration and the determination of spherical virus diameters using cryo-microscopy
    • Olson, N. H., and T. S. Baker, 1989. Magnification calibration and the determination of spherical virus diameters using cryo-microscopy. Ultramicroscopy. 30:281-97.
    • (1989) Ultramicroscopy , vol.30 , pp. 281-297
    • Olson, N.H.1    Baker, T.S.2
  • 36
    • 37349067504 scopus 로고    scopus 로고
    • Virtal memory versus file interfaces for large, memory-intensive scientific applications
    • IEEE Computer Society Press, Los Alamitos, CA
    • Park, Y., R. Scott, and S. Sechrest. 1996. Virtal memory versus file interfaces for large, memory-intensive scientific applications. In Supercomputing '96. IEEE Computer Society Press, Los Alamitos, CA.
    • (1996) Supercomputing '96
    • Park, Y.1    Scott, R.2    Sechrest, S.3
  • 37
    • 0027278758 scopus 로고
    • Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus
    • Prasad, B. V. V., P. E. Prevelige, E. Marietta, R. O. Chen, D. Thomas, J. King, and W. Chiu. 1993. Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus. J. Mol. Biol. 231:65-74.
    • (1993) J. Mol. Biol. , vol.231 , pp. 65-74
    • Prasad, B.V.V.1    Prevelige, P.E.2    Marietta, E.3    Chen, R.O.4    Thomas, D.5    King, J.6    Chiu, W.7
  • 38
    • 0029839752 scopus 로고    scopus 로고
    • Visualization of ordered genomic RNA and localization of the transcription enzymes in rotavirus
    • Prasad, B. V. V., R. Rothnagel, C. Q.-Y. Zeng, J. Jakana, J. A. Lawton, W. Chiu, and M. K. Estes. 1996. Visualization of ordered genomic RNA and localization of the transcription enzymes in rotavirus. Nature. 382: 471-473.
    • (1996) Nature , vol.382 , pp. 471-473
    • Prasad, B.V.V.1    Rothnagel, R.2    Zeng, C.Q.-Y.3    Jakana, J.4    Lawton, J.A.5    Chiu, W.6    Estes, M.K.7
  • 40
    • 0028831519 scopus 로고
    • Structural studies on the mechanisms of antibody-mediated neutralization of human rhninovirus
    • Smith, T. J., A. G. Mosser, and T. S. Baker. 1995. Structural studies on the mechanisms of antibody-mediated neutralization of human rhninovirus. Semin. Virol. 6:233-242.
    • (1995) Semin. Virol. , vol.6 , pp. 233-242
    • Smith, T.J.1    Mosser, A.G.2    Baker, T.S.3
  • 41
    • 0001860050 scopus 로고    scopus 로고
    • Herpesvirus capsid assembly and enelopment
    • Oxford University Press, New York
    • Steven, A. C., and P. G. Spear. 1997. Herpesvirus capsid assembly and enelopment. In Structural Biology of Viruses. Oxford University Press, New York. 312-351.
    • (1997) Structural Biology of Viruses , pp. 312-351
    • Steven, A.C.1    Spear, P.G.2
  • 42
    • 0027184774 scopus 로고
    • Difference imaging of adenovirus: Bridging the resolution gap between X-ray crystallography and electron microscopy
    • Stewart, P. L., S. D. Fuller, and R. M. Burnett. 1993. Difference imaging of adenovirus: bridging the resolution gap between X-ray crystallography and electron microscopy. EMBO J. 12:2589-2599.
    • (1993) EMBO J. , vol.12 , pp. 2589-2599
    • Stewart, P.L.1    Fuller, S.D.2    Burnett, R.M.3
  • 43
    • 0031982564 scopus 로고    scopus 로고
    • Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures
    • Thuman-Commike, B. G. P. A., J. A. Malinski, J. King, and W. Chiu. 1997. Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures. Biophys. J. 73:559-568.
    • (1997) Biophys. J. , vol.73 , pp. 559-568
    • Thuman-Commike, B.G.P.A.1    Malinski, J.A.2    King, J.3    Chiu, W.4
  • 44
    • 0029991984 scopus 로고    scopus 로고
    • PTOOL: A software package for the selection of particles from electron cryomicroscopy spot-scan images
    • Thuman-Commike, P. A., and W. Chiu. 1996. PTOOL: a software package for the selection of particles from electron cryomicroscopy spot-scan images. J. Struct. Biol. 116:41-47.
    • (1996) J. Struct. Biol. , vol.116 , pp. 41-47
    • Thuman-Commike, P.A.1    Chiu, W.2
  • 45
    • 0031214838 scopus 로고    scopus 로고
    • Improved common-line based icosahedral virus particle image orientation estimation algorithms
    • Thuman-Commike, P. A., and W. Chiu. 1997. Improved common-line based icosahedral virus particle image orientation estimation algorithms. Ultramicroscopy. 68:231-256.
    • (1997) Ultramicroscopy , vol.68 , pp. 231-256
    • Thuman-Commike, P.A.1    Chiu, W.2
  • 46
    • 0028783737 scopus 로고
    • Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: Structural authenticity and localization of vp26
    • Trus, B. L., F. L. Homa, F. P. Booy, W. W. Newcomb, D. R. Thomsen, N. Cheng, J. C. Brown, and A. C. Steven. 1995. Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of vp26. J. Virol. 69:7362-7366.
    • (1995) J. Virol. , vol.69 , pp. 7362-7366
    • Trus, B.L.1    Homa, F.L.2    Booy, F.P.3    Newcomb, W.W.4    Thomsen, D.R.5    Cheng, N.6    Brown, J.C.7    Steven, A.C.8
  • 47
    • 0030931283 scopus 로고    scopus 로고
    • Novel structural features of bovine papillomavirus capsid revealed by a three dimensional reconstruction to 9 Å resolution
    • Trus, B. L., R. B. Roden, H. L. Greenstone, M. Vrhel, J. Schiller, and F. P. Booy. 1997. Novel structural features of bovine papillomavirus capsid revealed by a three dimensional reconstruction to 9 Å resolution. Nature Struct. Biol. 4:411-418.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 411-418
    • Trus, B.L.1    Roden, R.B.2    Greenstone, H.L.3    Vrhel, M.4    Schiller, J.5    Booy, F.P.6
  • 50
    • 0027543395 scopus 로고
    • Prospects for using an IVEM with a FEG for imaging macromolecules towards atomic resolution
    • Zhou, Z. H., and W. Chiu. 1993. Prospects for using an IVEM with a FEG for imaging macromolecules towards atomic resolution. Ultramicroscopy. 49:407-416.
    • (1993) Ultramicroscopy , vol.49 , pp. 407-416
    • Zhou, Z.H.1    Chiu, W.2
  • 51
    • 0029928874 scopus 로고    scopus 로고
    • CTF determination of images of ice-embedded single particles using a graphics interface
    • Zhou, Z. H., S. Hardt, B. Wang, M. B. Sherman, J. Jakana, and W. Chiu. 1996. CTF determination of images of ice-embedded single particles using a graphics interface. J. Struct. Biol. 116:216-222.
    • (1996) J. Struct. Biol. , vol.116 , pp. 216-222
    • Zhou, Z.H.1    Hardt, S.2    Wang, B.3    Sherman, M.B.4    Jakana, J.5    Chiu, W.6
  • 52
    • 0028804828 scopus 로고
    • Assembly of VP26 in HSV-1 inferred from structures of wild-type and recombinant capsids
    • Zhou, Z. H., J. He, J. Jakana, J. Tatman, F. Rixon, and W. Chiu. 1995. Assembly of VP26 in HSV-1 inferred from structures of wild-type and recombinant capsids. Nature Struct. Biol. 2:1026-1030.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1026-1030
    • Zhou, Z.H.1    He, J.2    Jakana, J.3    Tatman, J.4    Rixon, F.5    Chiu, W.6
  • 53
    • 0028151168 scopus 로고
    • Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy
    • Zhou, Z. H., B. V. V. Prasad, J. Jakana, F. Rixon, and W. Chiu. 1994. Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy. J. Mol. Biol. 242:458-469.
    • (1994) J. Mol. Biol. , vol.242 , pp. 458-469
    • Zhou, Z.H.1    Prasad, B.V.V.2    Jakana, J.3    Rixon, F.4    Chiu, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.