메뉴 건너뛰기




Volumn 346, Issue 2, 2005, Pages 577-588

Three-dimensional structure of HIV-1 virus-like particles by electron cryotomography

Author keywords

capsid; electron cryomicroscopy; HIV; tomography; virus structure

Indexed keywords

FULLERENE DERIVATIVE; VIRUS PROTEIN;

EID: 12544255655     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.11.064     Document Type: Article
Times cited : (155)

References (42)
  • 1
    • 12444347873 scopus 로고
    • Fine-structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins
    • H.R. Gelderblom, E.H.S. Hausmann, M. Ozel, G. Pauli, and M.A. Koch Fine-structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins Micron Microsc. Acta 18 1987 335 336
    • (1987) Micron Microsc. Acta , vol.18 , pp. 335-336
    • Gelderblom, H.R.1    Hausmann, E.H.S.2    Ozel, M.3    Pauli, G.4    Koch, M.A.5
  • 2
    • 0032052406 scopus 로고    scopus 로고
    • The life-cycle of human immunodeficiency virus type 1
    • T. Goto, M. Nakai, and K. Ikuta The life-cycle of human immunodeficiency virus type 1 Micron 29 1998 123 318
    • (1998) Micron , vol.29 , pp. 123-318
    • Goto, T.1    Nakai, M.2    Ikuta, K.3
  • 3
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • J.A.G. Briggs, T. Wilk, R. Welker, H.G. Krausslich, and S.D. Fuller Structural organization of authentic, mature HIV-1 virions and cores EMBO J. 22 2003 1707 1715
    • (2003) EMBO J. , vol.22 , pp. 1707-1715
    • Briggs, J.A.G.1    Wilk, T.2    Welker, R.3    Krausslich, H.G.4    Fuller, S.D.5
  • 6
    • 0347364638 scopus 로고    scopus 로고
    • Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions
    • P. Zhu, E. Chertova, J. Bess, J.D. Lifson, L.O. Arthur, and J. Liu Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions Proc. Natl Acad. Sci. USA 100 2003 15812 15817
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15812-15817
    • Zhu, P.1    Chertova, E.2    Bess, J.3    Lifson, J.D.4    Arthur, L.O.5    Liu, J.6
  • 8
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and implications for virus assembly
    • Z. Rao, A.S. Belyaev, E. Fry, P. Roy, I.M. Jones, and D.I. Stuart Crystal structure of SIV matrix antigen and implications for virus assembly Nature 378 1995 743 747
    • (1995) Nature , vol.378 , pp. 743-747
    • Rao, Z.1    Belyaev, A.S.2    Fry, E.3    Roy, P.4    Jones, I.M.5    Stuart, D.I.6
  • 9
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly
    • C.P. Hill, D. Worthylake, D.P. Bancroft, A.M. Christensen, and W.I. Sundquist Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly Proc. Natl Acad. Sci. USA 93 1996 3099 3104
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 11
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1CA protein
    • S. Li, C.P. Hill, W.I. Sundquist, and J.T. Finch Image reconstructions of helical assemblies of the HIV-1CA protein Nature 407 2000 409 413
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 13
    • 4243782069 scopus 로고
    • Observation of fullerene cones
    • M. Ge, and K. Sattler Observation of fullerene cones Chem. Phys. Letters 220 1994 192 196
    • (1994) Chem. Phys. Letters , vol.220 , pp. 192-196
    • Ge, M.1    Sattler, K.2
  • 14
    • 0001029056 scopus 로고    scopus 로고
    • Cones and tubes: Geometry in the chemistry of carbon
    • T. Ebbesen Cones and tubes: geometry in the chemistry of carbon Accts Chem. Res. 31 1998 558 566
    • (1998) Accts Chem. Res. , vol.31 , pp. 558-566
    • Ebbesen, T.1
  • 16
    • 0033548068 scopus 로고    scopus 로고
    • Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26
    • Z.M. Jin, L. Jin, D.L. Peterson, and C.L. Lawson Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26 J. Mol. Biol. 286 1999 83 93
    • (1999) J. Mol. Biol. , vol.286 , pp. 83-93
    • Jin, Z.M.1    Jin, L.2    Peterson, D.L.3    Lawson, C.L.4
  • 20
    • 0037435031 scopus 로고    scopus 로고
    • From words to literature in structural proteomics
    • A. Sali, R. Glaeser, T. Earnest, and W. Baumeister From words to literature in structural proteomics Nature 422 2003 216 225
    • (2003) Nature , vol.422 , pp. 216-225
    • Sali, A.1    Glaeser, R.2    Earnest, T.3    Baumeister, W.4
  • 21
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • J.R. Kremer, D.N. Mastronarde, and J.R. McIntosh Computer visualization of three-dimensional image data using IMOD J. Struct. Biol. 116 1996 71 76
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 22
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • A.S. Frangakis, and R. Hegerl Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion J. Struct. Biol. 135 2001 239 250
    • (2001) J. Struct. Biol. , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 24
    • 0032007554 scopus 로고    scopus 로고
    • Inhibiting virus-capsid assembly by altering the polymerisation pathway
    • P.E. Prevelige Jr Inhibiting virus-capsid assembly by altering the polymerisation pathway Trends Biotechnol. 16 1998 61 65
    • (1998) Trends Biotechnol. , vol.16 , pp. 61-65
    • Prevelige, P.E.1    Jr2
  • 25
    • 0345686713 scopus 로고    scopus 로고
    • PA-457: A potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing
    • F. Li, R. Goila-Gaur, K. Salzwedel, N.R. Kilgore, M. Reddick, and C. Matallana PA-457: a potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing Proc. Natl Acad. Sci. USA 100 2003 13555 13560
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13555-13560
    • Li, F.1    Goila-Gaur, R.2    Salzwedel, K.3    Kilgore, N.R.4    Reddick, M.5    Matallana, C.6
  • 29
    • 0033958427 scopus 로고    scopus 로고
    • Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1
    • R. Welker, H. Hohenberg, U. Tessmer, C. Huckhagel, and H.G. Krausslich Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1 J. Virol. 74 2000 1168 1177
    • (2000) J. Virol. , vol.74 , pp. 1168-1177
    • Welker, R.1    Hohenberg, H.2    Tessmer, U.3    Huckhagel, C.4    Krausslich, H.G.5
  • 30
    • 0032863144 scopus 로고    scopus 로고
    • Association of Nef with the human immunodeficiency virus type 1 core
    • A. Kotov, J. Zhou, P. Flicker, and C. Aiken Association of Nef with the human immunodeficiency virus type 1 core J. Virol. 73 1999 8824 88230
    • (1999) J. Virol. , vol.73 , pp. 8824-88230
    • Kotov, A.1    Zhou, J.2    Flicker, P.3    Aiken, C.4
  • 31
    • 0034125738 scopus 로고    scopus 로고
    • Isolation of human immunodeficiency virus type 1 cores: Retention of Vpr in the absence of p6(gag)
    • M.A. Accola, A. Ohagen, and H.G. Gottlinger Isolation of human immunodeficiency virus type 1 cores: retention of Vpr in the absence of p6(gag) J. Virol. 74 2000 6198 6202
    • (2000) J. Virol. , vol.74 , pp. 6198-6202
    • Accola, M.A.1    Ohagen, A.2    Gottlinger, H.G.3
  • 32
    • 0034751087 scopus 로고    scopus 로고
    • Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants
    • T.M. Cairns, and R.C. Craven Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants J. Virol. 75 2001 242 250
    • (2001) J. Virol. , vol.75 , pp. 242-250
    • Cairns, T.M.1    Craven, R.C.2
  • 33
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • B.M. Forshey, U. von Schwedler, W.I. Sundquist, and C. Aiken Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication J. Virol. 76 2002 5667 5677
    • (2002) J. Virol. , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    Von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 35
    • 0042167432 scopus 로고    scopus 로고
    • Focus gradient correction applied to tilt series image data used in electron tomography
    • H. Winkler, and K.A. Taylor Focus gradient correction applied to tilt series image data used in electron tomography J. Struct. Biol. 143 2003 24 32
    • (2003) J. Struct. Biol. , vol.143 , pp. 24-32
    • Winkler, H.1    Taylor, K.A.2
  • 36
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: An approach with alignment methods that preserve resolution
    • D.N. Mastronarde Dual-axis tomography: an approach with alignment methods that preserve resolution J. Struct. Biol. 120 1997 343 352
    • (1997) J. Struct. Biol. , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 38
    • 0030947406 scopus 로고    scopus 로고
    • The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix
    • S. Swingler, P. Gallay, D. Camaur, J. Song, A. Abo, and D. Trono The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix J. Virol. 71 1997 4372 4377
    • (1997) J. Virol. , vol.71 , pp. 4372-4377
    • Swingler, S.1    Gallay, P.2    Camaur, D.3    Song, J.4    Abo, A.5    Trono, D.6
  • 39
    • 0026500566 scopus 로고
    • Cassette mutagenesis of the reverse-transcriptase of human- immunodeficiency-virus type-1
    • P.L. Boyer, A.L. Ferris, and S.H. Hughes Cassette mutagenesis of the reverse-transcriptase of human-immunodeficiency-virus type-1 J. Virol. 66 1992 1031 1039
    • (1992) J. Virol. , vol.66 , pp. 1031-1039
    • Boyer, P.L.1    Ferris, A.L.2    Hughes, S.H.3
  • 40
    • 0029786278 scopus 로고    scopus 로고
    • Biochemical analysis of catalytically crucial aspartate mutants of human immunodeficiency virus type 1 reverse transcriptase
    • N. Kaushik, N. Rege, P.N.S. Yadav, S.G. Sarafianos, M.J. Modak, and V.N. Pandey Biochemical analysis of catalytically crucial aspartate mutants of human immunodeficiency virus type 1 reverse transcriptase Biochemistry 35 1996 11536 11546
    • (1996) Biochemistry , vol.35 , pp. 11536-11546
    • Kaushik, N.1    Rege, N.2    Yadav, P.N.S.3    Sarafianos, S.G.4    Modak, M.J.5    Pandey, V.N.6
  • 41
    • 0026056935 scopus 로고
    • Mutations within the RNase-H domain of human-immunodeficiency-virus type-1 reverse-transcriptase abolish virus infectivity
    • M. Tisdale, T. Schulze, B.A. Larder, and K. Moelling Mutations within the RNase-H domain of human-immunodeficiency-virus type-1 reverse-transcriptase abolish virus infectivity J. Gen. Virol. 72 1991 59 66
    • (1991) J. Gen. Virol. , vol.72 , pp. 59-66
    • Tisdale, M.1    Schulze, T.2    Larder, B.A.3    Moelling, K.4
  • 42
    • 2942608087 scopus 로고    scopus 로고
    • An improved strategy for automated electron microscopic tomography
    • Q.S. Zheng, M.B. Braunfeld, J.W. Sedat, and D.A. Agard An improved strategy for automated electron microscopic tomography J. Struct. Biol. 147 2004 91 101
    • (2004) J. Struct. Biol. , vol.147 , pp. 91-101
    • Zheng, Q.S.1    Braunfeld, M.B.2    Sedat, J.W.3    Agard, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.