메뉴 건너뛰기




Volumn 2, Issue 3, 2015, Pages 343-369

Morphology and ultrastructure of retrovirus particles

Author keywords

Capsid protein shell; Cryo electron microscopy; Cryo electron tomography; Envelop protein complex; Gag lattice; Retrovirus structure; Sub tomogram averaging

Indexed keywords


EID: 85018198563     PISSN: None     EISSN: 23779098     Source Type: Journal    
DOI: 10.3934/biophy.2015.3.343     Document Type: Review
Times cited : (46)

References (157)
  • 3
    • 84920772149 scopus 로고    scopus 로고
    • The Evolution of HIV-1 Interactions with Coreceptors and Mannose C-Type Lectin Receptors
    • Borggren M, Jansson M (2015) The Evolution of HIV-1 Interactions with Coreceptors and Mannose C-Type Lectin Receptors. Prog Mol Biol Transl Sci 129C: 109-140.
    • (2015) Prog Mol Biol Transl Sci , vol.129C , pp. 109-140
    • Borggren, M.1    Jansson, M.2
  • 4
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K, Kim Y, Latinovic O, et al. (2009) HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 137: 433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3
  • 5
    • 0034634728 scopus 로고    scopus 로고
    • Maturation of HIV envelope glycoprotein precursors by cellular endoproteases
    • Moulard M, Decroly E (2000) Maturation of HIV envelope glycoprotein precursors by cellular endoproteases. Biochim Biophys Acta 1469: 121-132.
    • (2000) Biochim Biophys Acta , vol.1469 , pp. 121-132
    • Moulard, M.1    Decroly, E.2
  • 6
    • 84903943879 scopus 로고    scopus 로고
    • Structure and dynamics of the HIV-1 frameshift element RNA
    • Low JT, Garcia-Miranda P, Mouzakis KD, et al. (2014) Structure and dynamics of the HIV-1 frameshift element RNA. Biochemistry 53: 4282-4291.
    • (2014) Biochemistry , vol.53 , pp. 4282-4291
    • Low, J.T.1    Garcia-Miranda, P.2    Mouzakis, K.D.3
  • 7
    • 84878881937 scopus 로고    scopus 로고
    • Three-dimensional RNA structure of the major HIV-1 packaging signal region
    • Stephenson JD, Li H, Kenyon JC, et al. (2013) Three-dimensional RNA structure of the major HIV-1 packaging signal region. Structure 21: 951-962.
    • (2013) Structure , vol.21 , pp. 951-962
    • Stephenson, J.D.1    Li, H.2    Kenyon, J.C.3
  • 8
    • 68449092202 scopus 로고    scopus 로고
    • Architecture and secondary structure of an entire HIV-1 RNA genome
    • Watts JM, Dang KK, Gorelick RJ, et al. (2009) Architecture and secondary structure of an entire HIV-1 RNA genome. Nature 460: 711-716.
    • (2009) Nature , vol.460 , pp. 711-716
    • Watts, J.M.1    Dang, K.K.2    Gorelick, R.J.3
  • 9
    • 0004220419 scopus 로고    scopus 로고
    • Synthesis, Assembly, and Processing of Viral Proteins
    • Coffin JM HS, Varmus HE, editor New York: Cold Spring Harbor Laboratory Press
    • Swanstrom R, Wills JW (1997) Synthesis, Assembly, and Processing of Viral Proteins. In: Coffin JM HS, Varmus HE, editor. Retroviruses. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
    • (1997) Retroviruses Cold Spring Harbor
    • Swanstrom, R.1    Wills, J.W.2
  • 10
    • 80051737642 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation
    • Checkley MA, Luttge BG, Freed EO (2011) HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation. J Mol Biol 410: 582-608.
    • (2011) J Mol Biol , vol.410 , pp. 582-608
    • Checkley, M.A.1    Luttge, B.G.2    Freed, E.O.3
  • 11
    • 84871950126 scopus 로고    scopus 로고
    • The tale of the long tail: the cytoplasmic domain of HIV-1 gp41
    • Postler TS, Desrosiers RC (2013) The tale of the long tail: the cytoplasmic domain of HIV-1 gp41. J Virol 87: 2-15.
    • (2013) J Virol , vol.87 , pp. 2-15
    • Postler, T.S.1    Desrosiers, R.C.2
  • 12
    • 84863982480 scopus 로고    scopus 로고
    • Structure of the immature retroviral capsid at 8 A resolution by cryo-electron microscopy
    • Bharat TA, Davey NE, Ulbrich P, et al. (2012) Structure of the immature retroviral capsid at 8 A resolution by cryo-electron microscopy. Nature 487: 385-389.
    • (2012) Nature , vol.487 , pp. 385-389
    • Bharat, T.A.1    Davey, N.E.2    Ulbrich, P.3
  • 13
    • 84904887065 scopus 로고    scopus 로고
    • New insights into retroviral Gag-Gag and Gag-membrane interactions
    • Maldonado JO, Martin JL, Mueller JD, et al. (2014) New insights into retroviral Gag-Gag and Gag-membrane interactions. Front Microbiol 5: 302.
    • (2014) Front Microbiol , vol.5 , pp. 302
    • Maldonado, J.O.1    Martin, J.L.2    Mueller, J.D.3
  • 14
    • 84872973963 scopus 로고    scopus 로고
    • Membrane domains and the 'lipid raft' concept
    • Sonnino S, Prinetti A (2013) Membrane domains and the 'lipid raft' concept. Curr Med Chem 20: 4-21.
    • (2013) Curr Med Chem , vol.20 , pp. 4-21
    • Sonnino, S.1    Prinetti, A.2
  • 15
    • 78751668182 scopus 로고    scopus 로고
    • Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcription
    • Levin JG, Mitra M, Mascarenhas A, et al. (2010) Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcription. RNA Biol 7: 754-774.
    • (2010) RNA Biol , vol.7 , pp. 754-774
    • Levin, J.G.1    Mitra, M.2    Mascarenhas, A.3
  • 16
    • 35348908350 scopus 로고    scopus 로고
    • Maturation-dependent human immunodeficiency virus type 1 particle fusion requires a carboxyl-terminal region of the gp41 cytoplasmic tail
    • Jiang J, Aiken C (2007) Maturation-dependent human immunodeficiency virus type 1 particle fusion requires a carboxyl-terminal region of the gp41 cytoplasmic tail. J Virol 81: 9999-10008.
    • (2007) J Virol , vol.81 , pp. 9999-10008
    • Jiang, J.1    Aiken, C.2
  • 17
    • 1842457792 scopus 로고    scopus 로고
    • Coupling of human immunodeficiency virus type 1 fusion to virion maturation: a novel role of the gp41 cytoplasmic tail
    • Wyma DJ, Jiang J, Shi J, et al. (2004) Coupling of human immunodeficiency virus type 1 fusion to virion maturation: a novel role of the gp41 cytoplasmic tail. J Virol 78: 3429-3435.
    • (2004) J Virol , vol.78 , pp. 3429-3435
    • Wyma, D.J.1    Jiang, J.2    Shi, J.3
  • 19
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey BM, von Schwedler U, Sundquist WI, et al. (2002) Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J Virol 76: 5667-5677.
    • (2002) J Virol , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3
  • 22
    • 84878527131 scopus 로고    scopus 로고
    • Structural biology in situ-the potential of subtomogram averaging
    • Briggs JA (2013) Structural biology in situ-the potential of subtomogram averaging. Curr Opin Struct Biol 23: 261-267.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 261-267
    • Briggs, J.A.1
  • 23
    • 84878618663 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein structure
    • Merk A, Subramaniam S (2013) HIV-1 envelope glycoprotein structure. Curr Opin Struct Biol 23: 268-276.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 268-276
    • Merk, A.1    Subramaniam, S.2
  • 24
  • 25
    • 39049108146 scopus 로고    scopus 로고
    • RSV capsid polymorphism correlates with polymerization efficiency and envelope glycoprotein content: implications that nucleation controls morphogenesis
    • Butan C, Winkler DC, Heymann JB, et al. (2008) RSV capsid polymorphism correlates with polymerization efficiency and envelope glycoprotein content: implications that nucleation controls morphogenesis. J Mol Biol 376: 1168-1181.
    • (2008) J Mol Biol , vol.376 , pp. 1168-1181
    • Butan, C.1    Winkler, D.C.2    Heymann, J.B.3
  • 26
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle
    • Fuller SD, Wilk T, Gowen BE, et al. (1997) Cryo-electron microscopy reveals ordered domains in the immature HIV-1 particle. Curr Biol 7: 729-738.
    • (1997) Curr Biol , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3
  • 27
    • 0035782860 scopus 로고    scopus 로고
    • The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy
    • Kingston RL, Olson NH, Vogt VM (2001) The organization of mature Rous sarcoma virus as studied by cryoelectron microscopy. J Struct Biol 136: 67-80.
    • (2001) J Struct Biol , vol.136 , pp. 67-80
    • Kingston, R.L.1    Olson, N.H.2    Vogt, V.M.3
  • 28
    • 0032560502 scopus 로고    scopus 로고
    • Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms
    • Yeager M, Wilson-Kubalek EM, Weiner SG, et al. (1998) Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms. Proc Natl Acad Sci U S A 95: 7299-7304.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7299-7304
    • Yeager, M.1    Wilson-Kubalek, E.M.2    Weiner, S.G.3
  • 29
    • 84881193881 scopus 로고    scopus 로고
    • Three-dimensional analysis of budding sites and released virus suggests a revised model for HIV-1 morphogenesis
    • Carlson LA, Briggs JA, Glass B, et al. (2008) Three-dimensional analysis of budding sites and released virus suggests a revised model for HIV-1 morphogenesis. Cell Host Microbe 4: 592-599.
    • (2008) Cell Host Microbe , vol.4 , pp. 592-599
    • Carlson, L.A.1    Briggs, J.A.2    Glass, B.3
  • 30
    • 84881194271 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals conserved and divergent features of gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus
    • Briggs JA, Johnson MC, Simon MN, et al. (2006) Cryo-electron microscopy reveals conserved and divergent features of gag packing in immature particles of Rous sarcoma virus and human immunodeficiency virus. J Mol Biol 355: 157-168.
    • (2006) J Mol Biol , vol.355 , pp. 157-168
    • Briggs, J.A.1    Johnson, M.C.2    Simon, M.N.3
  • 32
    • 84888036006 scopus 로고    scopus 로고
    • A two-pronged structural analysis of retroviral maturation indicates that core formation proceeds by a disassembly-reassembly pathway rather than a displacive transition
    • Keller PW, Huang RK, England MR, et al. (2013) A two-pronged structural analysis of retroviral maturation indicates that core formation proceeds by a disassembly-reassembly pathway rather than a displacive transition. J Virol 87: 13655-13664.
    • (2013) J Virol , vol.87 , pp. 13655-13664
    • Keller, P.W.1    Huang, R.K.2    England, M.R.3
  • 33
    • 34247185183 scopus 로고    scopus 로고
    • Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells
    • Wright ER, Schooler JB, Ding HJ, et al. (2007) Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells. EMBO J 26: 2218-2226.
    • (2007) EMBO J , vol.26 , pp. 2218-2226
    • Wright, E.R.1    Schooler, J.B.2    Ding, H.J.3
  • 34
    • 78049516342 scopus 로고    scopus 로고
    • Conserved and variable features of Gag structure and arrangement in immature retrovirus particles
    • de Marco A, Davey NE, Ulbrich P, et al. (2010) Conserved and variable features of Gag structure and arrangement in immature retrovirus particles. J Virol 84: 11729-11736.
    • (2010) J Virol , vol.84 , pp. 11729-11736
    • de Marco, A.1    Davey, N.E.2    Ulbrich, P.3
  • 35
    • 79955399123 scopus 로고    scopus 로고
    • On the role of the SP1 domain in HIV-1 particle assembly: a molecular switch
    • Datta SA, Temeselew LG, Crist RM, et al. (2011) On the role of the SP1 domain in HIV-1 particle assembly: a molecular switch. J Virol 85: 4111-4121.
    • (2011) J Virol , vol.85 , pp. 4111-4121
    • Datta, S.A.1    Temeselew, L.G.2    Crist, R.M.3
  • 36
    • 0036828096 scopus 로고    scopus 로고
    • Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag
    • Liang C, Hu J, Russell RS, et al. (2002) Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag. J Virol 76: 11729-11737.
    • (2002) J Virol , vol.76 , pp. 11729-11737
    • Liang, C.1    Hu, J.2    Russell, R.S.3
  • 37
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • Briggs JA, Wilk T, Welker R, et al. (2003) Structural organization of authentic, mature HIV-1 virions and cores. EMBO J 22: 1707-1715.
    • (2003) EMBO J , vol.22 , pp. 1707-1715
    • Briggs, J.A.1    Wilk, T.2    Welker, R.3
  • 38
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • Ganser BK, Li S, Klishko VY, et al. (1999) Assembly and analysis of conical models for the HIV-1 core. Science 283: 80-83.
    • (1999) Science , vol.283 , pp. 80-83
    • Ganser, B.K.1    Li, S.2    Klishko, V.Y.3
  • 39
    • 48549098071 scopus 로고    scopus 로고
    • Irregular and Semi-Regular Polyhedral Models for Rous Sarcoma Virus Cores
    • Heymann JB, Butan C, Winkler DC, et al. (2008) Irregular and Semi-Regular Polyhedral Models for Rous Sarcoma Virus Cores. Comput Math Methods Med 9: 197-210.
    • (2008) Comput Math Methods Med , vol.9 , pp. 197-210
    • Heymann, J.B.1    Butan, C.2    Winkler, D.C.3
  • 40
    • 84921632829 scopus 로고    scopus 로고
    • Analysis of human T-cell leukemia virus type 1 particles using cryo-electron tomography
    • Cao S, Maldonado JO, Grigsby IF, et al. (2015) Analysis of human T-cell leukemia virus type 1 particles using cryo-electron tomography. J Virol 89: 2430-2435.
    • (2015) J Virol , vol.89 , pp. 2430-2435
    • Cao, S.1    Maldonado, J.O.2    Grigsby, I.F.3
  • 41
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S, Hill CP, Sundquist WI, et al. (2000) Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature 407: 409-413.
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3
  • 42
    • 0028136474 scopus 로고
    • Mass analysis of biological macromolecular complexes by STEM
    • Thomas D, Schultz P, Steven AC, et al. (1994) Mass analysis of biological macromolecular complexes by STEM. Biol Cell 80: 181-192.
    • (1994) Biol Cell , vol.80 , pp. 181-192
    • Thomas, D.1    Schultz, P.2    Steven, A.C.3
  • 43
    • 79959660777 scopus 로고    scopus 로고
    • New insights into HTLV-1 particle structure, assembly, and Gag-Gag interactions in living cells
    • Fogarty KH, Zhang W, Grigsby IF, et al. (2011) New insights into HTLV-1 particle structure, assembly, and Gag-Gag interactions in living cells. Viruses 3: 770-793.
    • (2011) Viruses , vol.3 , pp. 770-793
    • Fogarty, K.H.1    Zhang, W.2    Grigsby, I.F.3
  • 44
    • 78349257099 scopus 로고    scopus 로고
    • Characterization of brightness and stoichiometry of bright particles by flow-fluorescence fluctuation spectroscopy
    • Johnson J, Chen Y, Mueller JD (2010) Characterization of brightness and stoichiometry of bright particles by flow-fluorescence fluctuation spectroscopy. Biophys J 99: 3084-3092.
    • (2010) Biophys J , vol.99 , pp. 3084-3092
    • Johnson, J.1    Chen, Y.2    Mueller, J.D.3
  • 45
    • 0034849767 scopus 로고    scopus 로고
    • Analysis of Mason-Pfizer monkey virus Gag particles by scanning transmission electron microscopy
    • Parker SD, Wall JS, Hunter E (2001) Analysis of Mason-Pfizer monkey virus Gag particles by scanning transmission electron microscopy. J Virol 75: 9543-9548.
    • (2001) J Virol , vol.75 , pp. 9543-9548
    • Parker, S.D.1    Wall, J.S.2    Hunter, E.3
  • 46
    • 0032795497 scopus 로고    scopus 로고
    • Mass determination of rous sarcoma virus virions by scanning transmission electron microscopy
    • Vogt VM, Simon MN (1999) Mass determination of rous sarcoma virus virions by scanning transmission electron microscopy. J Virol 73: 7050-7055.
    • (1999) J Virol , vol.73 , pp. 7050-7055
    • Vogt, V.M.1    Simon, M.N.2
  • 47
    • 0035123571 scopus 로고    scopus 로고
    • Characterization of Rous sarcoma virus Gag particles assembled in vitro
    • Yu F, Joshi SM, Ma YM, et al. (2001) Characterization of Rous sarcoma virus Gag particles assembled in vitro. J Virol 75: 2753-2764.
    • (2001) J Virol , vol.75 , pp. 2753-2764
    • Yu, F.1    Joshi, S.M.2    Ma, Y.M.3
  • 48
    • 65549100184 scopus 로고    scopus 로고
    • Fluorescence fluctuation spectroscopy on viral-like particles reveals variable gag stoichiometry
    • Chen Y, Wu B, Musier-Forsyth K, et al. (2009) Fluorescence fluctuation spectroscopy on viral-like particles reveals variable gag stoichiometry. Biophys J 96: 1961-1969.
    • (2009) Biophys J , vol.96 , pp. 1961-1969
    • Chen, Y.1    Wu, B.2    Musier-Forsyth, K.3
  • 49
    • 77956631502 scopus 로고    scopus 로고
    • Biophysical analysis of HTLV-1 particles reveals novel insights into particle morphology and Gag stochiometry
    • Grigsby IF, Zhang W, Johnson JL, et al. (2010) Biophysical analysis of HTLV-1 particles reveals novel insights into particle morphology and Gag stochiometry. Retrovirology 7: 75.
    • (2010) Retrovirology , vol.7 , pp. 75
    • Grigsby, I.F.1    Zhang, W.2    Johnson, J.L.3
  • 50
    • 3042648569 scopus 로고    scopus 로고
    • Key interactions in HIV-1 maturation identified by hydrogen-deuterium exchange
    • Lanman J, Lam TT, Emmett MR, et al. (2004) Key interactions in HIV-1 maturation identified by hydrogen-deuterium exchange. Nat Struct Mol Biol 11: 676-677.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 676-677
    • Lanman, J.1    Lam, T.T.2    Emmett, M.R.3
  • 51
    • 1242274447 scopus 로고    scopus 로고
    • Cryoelectron microscopy of mouse mammary tumor virus
    • Briggs JA, Watson BE, Gowen BE, et al. (2004) Cryoelectron microscopy of mouse mammary tumor virus. J Virol 78: 2606-2608.
    • (2004) J Virol , vol.78 , pp. 2606-2608
    • Briggs, J.A.1    Watson, B.E.2    Gowen, B.E.3
  • 52
    • 16344390563 scopus 로고    scopus 로고
    • Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography
    • Forster F, Medalia O, Zauberman N, et al. (2005) Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography. Proc Natl Acad Sci U S A 102: 4729-4734.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4729-4734
    • Forster, F.1    Medalia, O.2    Zauberman, N.3
  • 53
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions
    • Briggs JA, Grunewald K, Glass B, et al. (2006) The mechanism of HIV-1 core assembly: insights from three-dimensional reconstructions of authentic virions. Structure 14: 15-20.
    • (2006) Structure , vol.14 , pp. 15-20
    • Briggs, J.A.1    Grunewald, K.2    Glass, B.3
  • 54
    • 84934906249 scopus 로고    scopus 로고
    • The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation
    • Hamann MV, Mullers E, Reh J, et al. (2014) The cooperative function of arginine residues in the Prototype Foamy Virus Gag C-terminus mediates viral and cellular RNA encapsidation. Retrovirology 11: 87.
    • (2014) Retrovirology , vol.11 , pp. 87
    • Hamann, M.V.1    Mullers, E.2    Reh, J.3
  • 55
    • 34147104516 scopus 로고    scopus 로고
    • AIDS virus envelope spike structure
    • Roux KH, Taylor KA (2007) AIDS virus envelope spike structure. Curr Opin Struct Biol 17: 244-252.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 244-252
    • Roux, K.H.1    Taylor, K.A.2
  • 56
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • Liu J, Bartesaghi A, Borgnia MJ, et al. (2008) Molecular architecture of native HIV-1 gp120 trimers. Nature 455: 109-113.
    • (2008) Nature , vol.455 , pp. 109-113
    • Liu, J.1    Bartesaghi, A.2    Borgnia, M.J.3
  • 57
    • 33748038359 scopus 로고    scopus 로고
    • Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ
    • Zanetti G, Briggs JA, Grunewald K, et al. (2006) Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ. PLoS Pathog 2: e83.
    • (2006) PLoS Pathog , vol.2
    • Zanetti, G.1    Briggs, J.A.2    Grunewald, K.3
  • 58
    • 79960974710 scopus 로고    scopus 로고
    • Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures
    • Harris A, Borgnia MJ, Shi D, et al. (2011) Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures. Proc Natl Acad Sci U S A 108: 11440-11445.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 11440-11445
    • Harris, A.1    Borgnia, M.J.2    Shi, D.3
  • 59
    • 84872189908 scopus 로고    scopus 로고
    • Molecular structures of trimeric HIV-1 Env in complex with small antibody derivatives
    • Meyerson JR, Tran EE, Kuybeda O, et al. (2013) Molecular structures of trimeric HIV-1 Env in complex with small antibody derivatives. Proc Natl Acad Sci U S A 110: 513-518.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 513-518
    • Meyerson, J.R.1    Tran, E.E.2    Kuybeda, O.3
  • 60
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • Tran EE, Borgnia MJ, Kuybeda O, et al. (2012) Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog 8: e1002797.
    • (2012) PLoS Pathog , vol.8
    • Tran, E.E.1    Borgnia, M.J.2    Kuybeda, O.3
  • 61
    • 81255213876 scopus 로고    scopus 로고
    • Three-dimensional structures of soluble CD4-bound states of trimeric simian immunodeficiency virus envelope glycoproteins determined by using cryo-electron tomography
    • White TA, Bartesaghi A, Borgnia MJ, et al. (2011) Three-dimensional structures of soluble CD4-bound states of trimeric simian immunodeficiency virus envelope glycoproteins determined by using cryo-electron tomography. J Virol 85: 12114-12123.
    • (2011) J Virol , vol.85 , pp. 12114-12123
    • White, T.A.1    Bartesaghi, A.2    Borgnia, M.J.3
  • 62
    • 78651241895 scopus 로고    scopus 로고
    • Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: strain-dependent variation in quaternary structure
    • White TA, Bartesaghi A, Borgnia MJ, et al. (2010) Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: strain-dependent variation in quaternary structure. PLoS Pathog 6: e1001249.
    • (2010) PLoS Pathog , vol.6
    • White, T.A.1    Bartesaghi, A.2    Borgnia, M.J.3
  • 63
    • 84861218412 scopus 로고    scopus 로고
    • Maturation cleavage of the murine leukemia virus Env precursor separates the transmembrane subunits to prime it for receptor triggering
    • Loving R, Wu SR, Sjoberg M, et al. (2012) Maturation cleavage of the murine leukemia virus Env precursor separates the transmembrane subunits to prime it for receptor triggering. Proc Natl Acad Sci U S A 109: 7735-7740.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 7735-7740
    • Loving, R.1    Wu, S.R.2    Sjoberg, M.3
  • 64
    • 84899112185 scopus 로고    scopus 로고
    • Furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure
    • Sjoberg M, Wu SR, Loving R, et al. (2014) Furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure. Proc Natl Acad Sci U S A 111: 6034-6039.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 6034-6039
    • Sjoberg, M.1    Wu, S.R.2    Loving, R.3
  • 65
    • 54349087513 scopus 로고    scopus 로고
    • Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion
    • Wu SR, Sjoberg M, Wallin M, et al. (2008) Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion. EMBO J 27: 2799-2808.
    • (2008) EMBO J , vol.27 , pp. 2799-2808
    • Wu, S.R.1    Sjoberg, M.2    Wallin, M.3
  • 66
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P, Liu J, Bess J, Jr., et al. (2006) Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441: 847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1    Liu, J.2    Bess, J.3
  • 67
    • 84924189026 scopus 로고    scopus 로고
    • Structure of the immature HIV-1 capsid in intact virus particles at 8.8 A resolution
    • Schur FK, Hagen WJ, Rumlova M, et al. (2015) Structure of the immature HIV-1 capsid in intact virus particles at 8.8 A resolution. Nature 517: 505-508.
    • (2015) Nature , vol.517 , pp. 505-508
    • Schur, F.K.1    Hagen, W.J.2    Rumlova, M.3
  • 68
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen EF, Goddard TD, Huang CC, et al. (2004) UCSF Chimera-a visualization system for exploratory research and analysis. J Comput Chem 25: 1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3
  • 69
    • 84878381053 scopus 로고    scopus 로고
    • Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics
    • Zhao G, Perilla JR, Yufenyuy EL, et al. (2013) Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Nature 497: 643-646.
    • (2013) Nature , vol.497 , pp. 643-646
    • Zhao, G.1    Perilla, J.R.2    Yufenyuy, E.L.3
  • 70
    • 59649084913 scopus 로고    scopus 로고
    • Visualization of a missing link in retrovirus capsid assembly
    • Cardone G, Purdy JG, Cheng N, et al. (2009) Visualization of a missing link in retrovirus capsid assembly. Nature 457: 694-698.
    • (2009) Nature , vol.457 , pp. 694-698
    • Cardone, G.1    Purdy, J.G.2    Cheng, N.3
  • 71
    • 77952032915 scopus 로고    scopus 로고
    • Proton-driven assembly of the Rous Sarcoma virus capsid protein results in the formation of icosahedral particles
    • Hyun JK, Radjainia M, Kingston RL, et al. (2010) Proton-driven assembly of the Rous Sarcoma virus capsid protein results in the formation of icosahedral particles. J Biol Chem 285: 15056-15064.
    • (2010) J Biol Chem , vol.285 , pp. 15056-15064
    • Hyun, J.K.1    Radjainia, M.2    Kingston, R.L.3
  • 72
    • 34848866243 scopus 로고    scopus 로고
    • Structure of full-length HIV-1 CA: a model for the mature capsid lattice
    • Ganser-Pornillos BK, Cheng A, Yeager M (2007) Structure of full-length HIV-1 CA: a model for the mature capsid lattice. Cell 131: 70-79.
    • (2007) Cell , vol.131 , pp. 70-79
    • Ganser-Pornillos, B.K.1    Cheng, A.2    Yeager, M.3
  • 73
    • 84890196626 scopus 로고    scopus 로고
    • Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy
    • Bartesaghi A, Merk A, Borgnia MJ, et al. (2013) Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy. Nat Struct Mol Biol 20: 1352-1357.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 1352-1357
    • Bartesaghi, A.1    Merk, A.2    Borgnia, M.J.3
  • 74
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D, Julien JP, de Val N, et al. (2013) Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 342: 1484-1490.
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1    Julien, J.P.2    de Val, N.3
  • 75
    • 84870505107 scopus 로고    scopus 로고
    • Protein secondary structure determination by constrained single-particle cryo-electron tomography
    • Bartesaghi A, Lecumberry F, Sapiro G, et al. (2012) Protein secondary structure determination by constrained single-particle cryo-electron tomography. Structure 20: 2003-2013.
    • (2012) Structure , vol.20 , pp. 2003-2013
    • Bartesaghi, A.1    Lecumberry, F.2    Sapiro, G.3
  • 76
    • 84888074636 scopus 로고    scopus 로고
    • Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging
    • Schur FK, Hagen WJ, de Marco A, et al. (2013) Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging. J Struct Biol 184: 394-400.
    • (2013) J Struct Biol , vol.184 , pp. 394-400
    • Schur, F.K.1    Hagen, W.J.2    de Marco, A.3
  • 77
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang C, Ndassa Y, Summers MF (2002) Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat Struct Biol 9: 537-543.
    • (2002) Nat Struct Biol , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 78
    • 67549109069 scopus 로고    scopus 로고
    • X-ray structures of the hexameric building block of the HIV capsid
    • Pornillos O, Ganser-Pornillos BK, Kelly BN, et al. (2009) X-ray structures of the hexameric building block of the HIV capsid. Cell 137: 1282-1292.
    • (2009) Cell , vol.137 , pp. 1282-1292
    • Pornillos, O.1    Ganser-Pornillos, B.K.2    Kelly, B.N.3
  • 79
    • 68949177099 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of capsid protein from the mason-pfizer monkey virus
    • Macek P, Chmelik J, Krizova I, et al. (2009) NMR structure of the N-terminal domain of capsid protein from the mason-pfizer monkey virus. J Mol Biol 392: 100-114.
    • (2009) J Mol Biol , vol.392 , pp. 100-114
    • Macek, P.1    Chmelik, J.2    Krizova, I.3
  • 80
    • 84901846907 scopus 로고    scopus 로고
    • Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly
    • Bharat TA, Castillo Menendez LR, Hagen WJ, et al. (2014) Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly. Proc Natl Acad Sci U S A 111: 8233-8238.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 8233-8238
    • Bharat, T.A.1    Castillo Menendez, L.R.2    Hagen, W.J.3
  • 81
    • 84866061123 scopus 로고    scopus 로고
    • Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer
    • Mao Y, Wang L, Gu C, et al. (2012) Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer. Nat Struct Mol Biol 19: 893-899.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 893-899
    • Mao, Y.1    Wang, L.2    Gu, C.3
  • 82
    • 84880678141 scopus 로고    scopus 로고
    • Molecular architecture of the uncleaved HIV-1 envelope glycoprotein trimer
    • Mao Y, Wang L, Gu C, et al. (2013) Molecular architecture of the uncleaved HIV-1 envelope glycoprotein trimer. Proc Natl Acad Sci U S A 110: 12438-12443.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 12438-12443
    • Mao, Y.1    Wang, L.2    Gu, C.3
  • 83
    • 84881041750 scopus 로고    scopus 로고
    • Structural biology. Is high-tech view of HIV too good to be true?
    • Cohen J Structural biology. Is high-tech view of HIV too good to be true? Science 341: 443-444.
    • Science , vol.341 , pp. 443-444
    • Cohen, J.1
  • 84
    • 84887271303 scopus 로고    scopus 로고
    • Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise
    • Henderson R Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise. Proc Natl Acad Sci U S A 110: 18037-18041.
    • Proc Natl Acad Sci U S A , vol.110 , pp. 18037-18041
    • Henderson, R.1
  • 85
    • 84887299506 scopus 로고    scopus 로고
    • Reply to Subramaniam, van Heel, and Henderson: Validity of the cryo-electron microscopy structures of the HIV-1 envelope glycoprotein complex
    • Mao Y, Castillo-Menendez LR, Sodroski JG Reply to Subramaniam, van Heel, and Henderson: Validity of the cryo-electron microscopy structures of the HIV-1 envelope glycoprotein complex. Proc Natl Acad Sci U S A 110: E4178-4182.
    • Proc Natl Acad Sci U S A , vol.110 , pp. E4178-E4182
    • Mao, Y.1    Castillo-Menendez, L.R.2    Sodroski, J.G.3
  • 86
    • 84937255386 scopus 로고    scopus 로고
    • Maturation of the HIV-1 core by a non-diffusional phase transition
    • Frank GA, Narayan K, Bess JW, Jr., et al. (2015) Maturation of the HIV-1 core by a non-diffusional phase transition. Nat Commun 6: 5854.
    • (2015) Nat Commun , vol.6 , pp. 5854
    • Frank, G.A.1    Narayan, K.2    Bess, J.W.3
  • 87
    • 84887282198 scopus 로고    scopus 로고
    • Finding trimeric HIV-1 envelope glycoproteins in random noise
    • van Heel M Finding trimeric HIV-1 envelope glycoproteins in random noise. Proc Natl Acad Sci U S A 110: E4175-4177.
    • Proc Natl Acad Sci U S A , vol.110 , pp. E4175-E4177
    • van Heel, M.1
  • 88
    • 0028342554 scopus 로고
    • Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis
    • Mammano F, Ohagen A, Hoglund S, et al. (1994) Role of the major homology region of human immunodeficiency virus type 1 in virion morphogenesis. J Virol 68: 4927-4936.
    • (1994) J Virol , vol.68 , pp. 4927-4936
    • Mammano, F.1    Ohagen, A.2    Hoglund, S.3
  • 89
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler UK, Stray KM, Garrus JE, et al. (2003) Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J Virol 77: 5439-5450.
    • (2003) J Virol , vol.77 , pp. 5439-5450
    • von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3
  • 90
    • 33749356701 scopus 로고    scopus 로고
    • Mutations in the alpha-helix directly C-terminal to the major homology region of human immunodeficiency virus type 1 capsid protein disrupt Gag multimerization and markedly impair virus particle production
    • Chu HH, Chang YF, Wang CT (2006) Mutations in the alpha-helix directly C-terminal to the major homology region of human immunodeficiency virus type 1 capsid protein disrupt Gag multimerization and markedly impair virus particle production. J Biomed Sci 13: 645-656.
    • (2006) J Biomed Sci , vol.13 , pp. 645-656
    • Chu, H.H.1    Chang, Y.F.2    Wang, C.T.3
  • 91
    • 0030693391 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
    • Gamble TR, Yoo S, Vajdos FF, et al. (1997) Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science 278: 849-853.
    • (1997) Science , vol.278 , pp. 849-853
    • Gamble, T.R.1    Yoo, S.2    Vajdos, F.F.3
  • 92
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4, 5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
    • Ono A, Ablan SD, Lockett SJ, et al. (2004) Phosphatidylinositol (4, 5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane. Proc Natl Acad Sci U S A 101: 14889-14894.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 14889-14894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3
  • 93
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • Saad JS, Miller J, Tai J, et al. (2006) Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc Natl Acad Sci U S A 103: 11364-11369.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Tai, J.3
  • 94
    • 79953896583 scopus 로고    scopus 로고
    • Characterization of cytoplasmic Gag-gag interactions by dual-color z-scan fluorescence fluctuation spectroscopy
    • Fogarty KH, Chen Y, Grigsby IF, et al. (2011) Characterization of cytoplasmic Gag-gag interactions by dual-color z-scan fluorescence fluctuation spectroscopy. Biophys J 100: 1587-1595.
    • (2011) Biophys J , vol.100 , pp. 1587-1595
    • Fogarty, K.H.1    Chen, Y.2    Grigsby, I.F.3
  • 95
    • 2442662800 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag contains a dileucine-like motif that regulates association with multivesicular bodies
    • Lindwasser OW, Resh MD (2004) Human immunodeficiency virus type 1 Gag contains a dileucine-like motif that regulates association with multivesicular bodies. J Virol 78: 6013-6023.
    • (2004) J Virol , vol.78 , pp. 6013-6023
    • Lindwasser, O.W.1    Resh, M.D.2
  • 96
    • 0035942236 scopus 로고    scopus 로고
    • RNA is a structural element in retrovirus particles
    • Muriaux D, Mirro J, Harvin D, et al. (2001) RNA is a structural element in retrovirus particles. Proc Natl Acad Sci U S A 98: 5246-5251.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5246-5251
    • Muriaux, D.1    Mirro, J.2    Harvin, D.3
  • 97
    • 23844460841 scopus 로고    scopus 로고
    • HIV-1 Gag-RNA interaction occurs at a perinuclear/centrosomal site; analysis by confocal microscopy and FRET
    • Poole E, Strappe P, Mok HP, et al. (2005) HIV-1 Gag-RNA interaction occurs at a perinuclear/centrosomal site; analysis by confocal microscopy and FRET. Traffic 6: 741-755.
    • (2005) Traffic , vol.6 , pp. 741-755
    • Poole, E.1    Strappe, P.2    Mok, H.P.3
  • 98
    • 84857658242 scopus 로고    scopus 로고
    • A structural model for the generation of continuous curvature on the surface of a retroviral capsid
    • Bailey GD, Hyun JK, Mitra AK, et al. (2012) A structural model for the generation of continuous curvature on the surface of a retroviral capsid. J Mol Biol 417: 212-223.
    • (2012) J Mol Biol , vol.417 , pp. 212-223
    • Bailey, G.D.1    Hyun, J.K.2    Mitra, A.K.3
  • 99
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza GB, Haire LF, Stevens A, et al. (2004) High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431: 481-485.
    • (2004) Nature , vol.431 , pp. 481-485
    • Mortuza, G.B.1    Haire, L.F.2    Stevens, A.3
  • 100
    • 70350771279 scopus 로고    scopus 로고
    • Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function
    • Byeon IJ, Meng X, Jung J, et al. (2009) Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139: 780-790.
    • (2009) Cell , vol.139 , pp. 780-790
    • Byeon, I.J.1    Meng, X.2    Jung, J.3
  • 101
    • 84868548565 scopus 로고    scopus 로고
    • Structural insight into HIV-1 capsid recognition by rhesus TRIM5alpha
    • Yang H, Ji X, Zhao G, et al. (2012) Structural insight into HIV-1 capsid recognition by rhesus TRIM5alpha. Proc Natl Acad Sci U S A 109: 18372-18377.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 18372-18377
    • Yang, H.1    Ji, X.2    Zhao, G.3
  • 102
    • 79953278280 scopus 로고    scopus 로고
    • Rhesus TRIM5alpha disrupts the HIV-1 capsid at the inter-hexamer interfaces
    • Zhao G, Ke D, Vu T, et al. (2011) Rhesus TRIM5alpha disrupts the HIV-1 capsid at the inter-hexamer interfaces. PLoS Pathog 7: e1002009.
    • (2011) PLoS Pathog , vol.7
    • Zhao, G.1    Ke, D.2    Vu, T.3
  • 103
    • 85018642388 scopus 로고    scopus 로고
    • X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability
    • Gres AT, Kirby KA, KewalRamani VN, et al. (2015) X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability. Science.
    • (2015) Science
    • Gres, A.T.1    Kirby, K.A.2    KewalRamani, V.N.3
  • 104
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • Dalgleish AG, Beverley PC, Clapham PR, et al. (1984) The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 312: 763-767.
    • (1984) Nature , vol.312 , pp. 763-767
    • Dalgleish, A.G.1    Beverley, P.C.2    Clapham, P.R.3
  • 105
    • 16144365317 scopus 로고    scopus 로고
    • CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5
    • Trkola A, Dragic T, Arthos J, et al. (1996) CD4-dependent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5. Nature 384: 184-187.
    • (1996) Nature , vol.384 , pp. 184-187
    • Trkola, A.1    Dragic, T.2    Arthos, J.3
  • 106
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens
    • Wyatt R, Sodroski J (1998) The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280: 1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 107
    • 77954059555 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions
    • Buzon V, Natrajan G, Schibli D, et al. (2010) Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog 6: e1000880.
    • (2010) PLoS Pathog , vol.6
    • Buzon, V.1    Natrajan, G.2    Schibli, D.3
  • 108
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, et al. (1997) Core structure of gp41 from the HIV envelope glycoprotein. Cell 89: 263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3
  • 109
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K, Liu J, Wang J, et al. (1997) Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc Natl Acad Sci U S A 94: 12303-12308.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3
  • 110
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • Weissenhorn W, Dessen A, Harrison SC, et al. (1997) Atomic structure of the ectodomain from HIV-1 gp41. Nature 387: 426-430.
    • (1997) Nature , vol.387 , pp. 426-430
    • Weissenhorn, W.1    Dessen, A.2    Harrison, S.C.3
  • 111
    • 70450182950 scopus 로고    scopus 로고
    • Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    • Chen L, Kwon YD, Zhou T, et al. (2009) Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 326: 1123-1127.
    • (2009) Science , vol.326 , pp. 1123-1127
    • Chen, L.1    Kwon, Y.D.2    Zhou, T.3
  • 112
    • 34848868199 scopus 로고    scopus 로고
    • Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4
    • Huang CC, Lam SN, Acharya P, et al. (2007) Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4. Science 317: 1930-1934.
    • (2007) Science , vol.317 , pp. 1930-1934
    • Huang, C.C.1    Lam, S.N.2    Acharya, P.3
  • 113
    • 27744597054 scopus 로고    scopus 로고
    • Structure of a V3-containing HIV-1 gp120 core
    • Huang CC, Tang M, Zhang MY, et al. (2005) Structure of a V3-containing HIV-1 gp120 core. Science 310: 1025-1028.
    • (2005) Science , vol.310 , pp. 1025-1028
    • Huang, C.C.1    Tang, M.2    Zhang, M.Y.3
  • 114
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang J, Ofek G, Laub L, et al. (2012) Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 491: 406-412.
    • (2012) Nature , vol.491 , pp. 406-412
    • Huang, J.1    Ofek, G.2    Laub, L.3
  • 115
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R, Robinson J, et al. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393: 648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3
  • 116
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, Pancera M, Carrico C, et al. (2011) Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 480: 336-343.
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1    Pancera, M.2    Carrico, C.3
  • 117
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal R, Doores KJ, Walker LM, et al. (2011) A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 334: 1097-1103.
    • (2011) Science , vol.334 , pp. 1097-1103
    • Pejchal, R.1    Doores, K.J.2    Walker, L.M.3
  • 118
    • 84921606536 scopus 로고    scopus 로고
    • Insights into the trimeric HIV-1 envelope glycoprotein structure
    • Ward AB, Wilson IA (2015) Insights into the trimeric HIV-1 envelope glycoprotein structure. Trends Biochem Sci 40: 101-107.
    • (2015) Trends Biochem Sci , vol.40 , pp. 101-107
    • Ward, A.B.1    Wilson, I.A.2
  • 119
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T, Georgiev I, Wu X, et al. (2010) Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329: 811-817.
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1    Georgiev, I.2    Wu, X.3
  • 120
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou T, Xu L, Dey B, et al. (2007) Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 445: 732-737.
    • (2007) Nature , vol.445 , pp. 732-737
    • Zhou, T.1    Xu, L.2    Dey, B.3
  • 121
    • 84907963599 scopus 로고    scopus 로고
    • Visualization of retroviral envelope spikes in complex with the V3 loop antibody 447-52D on intact viruses by cryo-electron tomography
    • Dutta M, Liu J, Roux KH, et al. (2014) Visualization of retroviral envelope spikes in complex with the V3 loop antibody 447-52D on intact viruses by cryo-electron tomography. J Virol 88: 12265-12275.
    • (2014) J Virol , vol.88 , pp. 12265-12275
    • Dutta, M.1    Liu, J.2    Roux, K.H.3
  • 122
    • 84878608643 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1
    • Harris AK, Bartesaghi A, Milne JL, et al. (2013) HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1. J Virol 87: 7191-7196.
    • (2013) J Virol , vol.87 , pp. 7191-7196
    • Harris, A.K.1    Bartesaghi, A.2    Milne, J.L.3
  • 123
    • 79952368717 scopus 로고    scopus 로고
    • Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop
    • Hu G, Liu J, Taylor KA, et al. (2011) Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop. J Virol 85: 2741-2750.
    • (2011) J Virol , vol.85 , pp. 2741-2750
    • Hu, G.1    Liu, J.2    Taylor, K.A.3
  • 124
    • 57149107577 scopus 로고    scopus 로고
    • Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs
    • Zhu P, Winkler H, Chertova E, et al. (2008) Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathog 4: e1000203.
    • (2008) PLoS Pathog , vol.4
    • Zhu, P.1    Winkler, H.2    Chertova, E.3
  • 125
    • 0036333661 scopus 로고    scopus 로고
    • Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • Sanders RW, Vesanen M, Schuelke N, et al. (2002) Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J Virol 76: 8875-8889.
    • (2002) J Virol , vol.76 , pp. 8875-8889
    • Sanders, R.W.1    Vesanen, M.2    Schuelke, N.3
  • 126
    • 84881028558 scopus 로고    scopus 로고
    • Catching HIV 'in the act' with 3D electron microscopy
    • Earl LA, Lifson JD, Subramaniam S (2013) Catching HIV 'in the act' with 3D electron microscopy. Trends Microbiol 21: 397-404.
    • (2013) Trends Microbiol , vol.21 , pp. 397-404
    • Earl, L.A.1    Lifson, J.D.2    Subramaniam, S.3
  • 127
    • 84884239080 scopus 로고    scopus 로고
    • Cryo-electron tomography: the challenge of doing structural biology in situ
    • Lucic V, Rigort A, Baumeister W (2013) Cryo-electron tomography: the challenge of doing structural biology in situ. J Cell Biol 202: 407-419.
    • (2013) J Cell Biol , vol.202 , pp. 407-419
    • Lucic, V.1    Rigort, A.2    Baumeister, W.3
  • 128
    • 80855156720 scopus 로고    scopus 로고
    • Direct visualization of HIV-1 with correlative live-cell microscopy and cryo-electron tomography
    • Jun S, Ke D, Debiec K, et al. (2011) Direct visualization of HIV-1 with correlative live-cell microscopy and cryo-electron tomography. Structure 19: 1573-1581.
    • (2011) Structure , vol.19 , pp. 1573-1581
    • Jun, S.1    Ke, D.2    Debiec, K.3
  • 129
    • 84885865666 scopus 로고    scopus 로고
    • Correlative microscopy for 3D structural analysis of dynamic interactions
    • Jun S, Zhao G, Ning J, et al. (2013) Correlative microscopy for 3D structural analysis of dynamic interactions. J Vis Exp.
    • (2013) J Vis Exp
    • Jun, S.1    Zhao, G.2    Ning, J.3
  • 130
    • 48249105841 scopus 로고    scopus 로고
    • Human T-lymphotropic virus-1 visualized at the virological synapse by electron tomography
    • Majorovits E, Nejmeddine M, Tanaka Y, et al. (2008) Human T-lymphotropic virus-1 visualized at the virological synapse by electron tomography. PLoS One 3: e2251.
    • (2008) PLoS One , vol.3
    • Majorovits, E.1    Nejmeddine, M.2    Tanaka, Y.3
  • 131
    • 77949412821 scopus 로고    scopus 로고
    • Virological synapse-mediated spread of human immunodeficiency virus type 1 between T cells is sensitive to entry inhibition
    • Martin N, Welsch S, Jolly C, et al. (2010) Virological synapse-mediated spread of human immunodeficiency virus type 1 between T cells is sensitive to entry inhibition. J Virol 84: 3516-3527.
    • (2010) J Virol , vol.84 , pp. 3516-3527
    • Martin, N.1    Welsch, S.2    Jolly, C.3
  • 132
    • 84906336180 scopus 로고    scopus 로고
    • Three-dimensional imaging of HIV-1 virological synapses reveals membrane architectures involved in virus transmission
    • Do T, Murphy G, Earl LA, et al. (2014) Three-dimensional imaging of HIV-1 virological synapses reveals membrane architectures involved in virus transmission. J Virol 88: 10327-10339.
    • (2014) J Virol , vol.88 , pp. 10327-10339
    • Do, T.1    Murphy, G.2    Earl, L.A.3
  • 133
    • 84870540260 scopus 로고    scopus 로고
    • 3D imaging of cells and tissues by focused ion beam/scanning electron microscopy (FIB/SEM)
    • Drobne D (2013) 3D imaging of cells and tissues by focused ion beam/scanning electron microscopy (FIB/SEM). Methods Mol Biol 950: 275-292.
    • (2013) Methods Mol Biol , vol.950 , pp. 275-292
    • Drobne, D.1
  • 135
    • 78651270028 scopus 로고    scopus 로고
    • Correlated fluorescence and 3D electron microscopy with high sensitivity and spatial precision
    • Kukulski W, Schorb M, Welsch S, et al. (2011) Correlated fluorescence and 3D electron microscopy with high sensitivity and spatial precision. J Cell Biol 192: 111-119.
    • (2011) J Cell Biol , vol.192 , pp. 111-119
    • Kukulski, W.1    Schorb, M.2    Welsch, S.3
  • 136
    • 35148839574 scopus 로고    scopus 로고
    • Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography
    • Sartori A, Gatz R, Beck F, et al. (2007) Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography. J Struct Biol 160: 135-145.
    • (2007) J Struct Biol , vol.160 , pp. 135-145
    • Sartori, A.1    Gatz, R.2    Beck, F.3
  • 137
    • 84885871508 scopus 로고    scopus 로고
    • Correlative cryo-electron tomography and optical microscopy of cells
    • Zhang P (2013) Correlative cryo-electron tomography and optical microscopy of cells. Curr Opin Struct Biol 23: 763-770.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 763-770
    • Zhang, P.1
  • 138
    • 84928530069 scopus 로고    scopus 로고
    • Electron cryo-tomography studies of maturing HIV-1 particles reveal the assembly pathway of the viral core
    • Woodward CL, Cheng SN, Jensen GJ (2014) Electron cryo-tomography studies of maturing HIV-1 particles reveal the assembly pathway of the viral core. J Virol.
    • (2014) J Virol
    • Woodward, C.L.1    Cheng, S.N.2    Jensen, G.J.3
  • 139
    • 79251517063 scopus 로고    scopus 로고
    • Cryo electron tomography of native HIV-1 budding sites
    • Carlson LA, de Marco A, Oberwinkler H, et al. (2010) Cryo electron tomography of native HIV-1 budding sites. PLoS Pathog 6: e1001173.
    • (2010) PLoS Pathog , vol.6
    • Carlson, L.A.1    de Marco, A.2    Oberwinkler, H.3
  • 140
    • 84880883715 scopus 로고    scopus 로고
    • Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission
    • Dobro MJ, Samson RY, Yu Z, et al. (2013) Electron cryotomography of ESCRT assemblies and dividing Sulfolobus cells suggests that spiraling filaments are involved in membrane scission. Mol Biol Cell 24: 2319-2327.
    • (2013) Mol Biol Cell , vol.24 , pp. 2319-2327
    • Dobro, M.J.1    Samson, R.Y.2    Yu, Z.3
  • 141
    • 84872617312 scopus 로고    scopus 로고
    • ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding
    • Effantin G, Dordor A, Sandrin V, et al. (2013) ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. Cell Microbiol 15: 213-226.
    • (2013) Cell Microbiol , vol.15 , pp. 213-226
    • Effantin, G.1    Dordor, A.2    Sandrin, V.3
  • 142
    • 84907081816 scopus 로고    scopus 로고
    • Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly
    • Shen QT, Schuh AL, Zheng Y, et al. (2014) Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly. J Cell Biol 206: 763-777.
    • (2014) J Cell Biol , vol.206 , pp. 763-777
    • Shen, Q.T.1    Schuh, A.L.2    Zheng, Y.3
  • 143
    • 84893719820 scopus 로고    scopus 로고
    • Distribution of ESCRT machinery at HIV assembly sites reveals virus scaffolding of ESCRT subunits
    • Van Engelenburg SB, Shtengel G, Sengupta P, et al. (2014) Distribution of ESCRT machinery at HIV assembly sites reveals virus scaffolding of ESCRT subunits. Science 343: 653-656.
    • (2014) Science , vol.343 , pp. 653-656
    • Van Engelenburg, S.B.1    Shtengel, G.2    Sengupta, P.3
  • 144
    • 79251521481 scopus 로고    scopus 로고
    • Structural analysis of HIV-1 maturation using cryo-electron tomography
    • de Marco A, Muller B, Glass B, et al. (2010) Structural analysis of HIV-1 maturation using cryo-electron tomography. PLoS Pathog 6: e1001215.
    • (2010) PLoS Pathog , vol.6
    • de Marco, A.1    Muller, B.2    Glass, B.3
  • 145
    • 84870664162 scopus 로고    scopus 로고
    • Role of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivity
    • de Marco A, Heuser AM, Glass B, et al. (2012) Role of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivity. J Virol 86: 13708-13716.
    • (2012) J Virol , vol.86 , pp. 13708-13716
    • de Marco, A.1    Heuser, A.M.2    Glass, B.3
  • 146
    • 84879534949 scopus 로고    scopus 로고
    • Gag-Pol processing during HIV-1 virion maturation: a systems biology approach
    • Konnyu B, Sadiq SK, Turanyi T, et al. (2013) Gag-Pol processing during HIV-1 virion maturation: a systems biology approach. PLoS Comput Biol 9: e1003103.
    • (2013) PLoS Comput Biol , vol.9
    • Konnyu, B.1    Sadiq, S.K.2    Turanyi, T.3
  • 147
    • 78951488338 scopus 로고    scopus 로고
    • HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice
    • Keller PW, Adamson CS, Heymann JB, et al. (2011) HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice. J Virol 85: 1420-1428.
    • (2011) J Virol , vol.85 , pp. 1420-1428
    • Keller, P.W.1    Adamson, C.S.2    Heymann, J.B.3
  • 148
    • 12544255655 scopus 로고    scopus 로고
    • Three-dimensional structure of HIV-1 virus-like particles by electron cryotomography
    • Benjamin J, Ganser-Pornillos BK, Tivol WF, et al. (2005) Three-dimensional structure of HIV-1 virus-like particles by electron cryotomography. J Mol Biol 346: 577-588.
    • (2005) J Mol Biol , vol.346 , pp. 577-588
    • Benjamin, J.1    Ganser-Pornillos, B.K.2    Tivol, W.F.3
  • 149
    • 65649146785 scopus 로고    scopus 로고
    • Nonequilibirum assembly, retroviruses, and conical structures
    • Levandovsky A, Zandi R (2009) Nonequilibirum assembly, retroviruses, and conical structures. Phys Rev Lett 102: 198102.
    • (2009) Phys Rev Lett , vol.102
    • Levandovsky, A.1    Zandi, R.2
  • 150
    • 84871810150 scopus 로고    scopus 로고
    • Unclosed HIV-1 capsids suggest a curled sheet model of assembly
    • Yu Z, Dobro MJ, Woodward CL, et al. (2013) Unclosed HIV-1 capsids suggest a curled sheet model of assembly. J Mol Biol 425: 112-123.
    • (2013) J Mol Biol , vol.425 , pp. 112-123
    • Yu, Z.1    Dobro, M.J.2    Woodward, C.L.3
  • 151
    • 34249672782 scopus 로고    scopus 로고
    • Electron tomography of the contact between T cells and SIV/HIV-1: implications for viral entry
    • Sougrat R, Bartesaghi A, Lifson JD, et al. (2007) Electron tomography of the contact between T cells and SIV/HIV-1: implications for viral entry. PLoS Pathog 3: e63.
    • (2007) PLoS Pathog , vol.3
    • Sougrat, R.1    Bartesaghi, A.2    Lifson, J.D.3
  • 152
    • 84869120630 scopus 로고    scopus 로고
    • Visualization of the two-step fusion process of the retrovirus avian sarcoma/leukosis virus by cryo-electron tomography
    • Cardone G, Brecher M, Fontana J, et al. (2012) Visualization of the two-step fusion process of the retrovirus avian sarcoma/leukosis virus by cryo-electron tomography. J Virol 86: 12129-12137.
    • (2012) J Virol , vol.86 , pp. 12129-12137
    • Cardone, G.1    Brecher, M.2    Fontana, J.3
  • 153
    • 77955781209 scopus 로고    scopus 로고
    • 3D visualization of HIV transfer at the virological synapse between dendritic cells and T cells
    • Felts RL, Narayan K, Estes JD, et al. (2010) 3D visualization of HIV transfer at the virological synapse between dendritic cells and T cells. Proc Natl Acad Sci U S A 107: 13336-13341.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 13336-13341
    • Felts, R.L.1    Narayan, K.2    Estes, J.D.3
  • 154
    • 33847366661 scopus 로고    scopus 로고
    • Retroviruses can establish filopodial bridges for efficient cell-to-cell transmission
    • Sherer NM, Lehmann MJ, Jimenez-Soto LF, et al. (2007) Retroviruses can establish filopodial bridges for efficient cell-to-cell transmission. Nat Cell Biol 9: 310-315.
    • (2007) Nat Cell Biol , vol.9 , pp. 310-315
    • Sherer, N.M.1    Lehmann, M.J.2    Jimenez-Soto, L.F.3
  • 155
    • 84875782383 scopus 로고    scopus 로고
    • Pathways of cell-cell transmission of HTLV-1
    • Pique C, Jones KS (2012) Pathways of cell-cell transmission of HTLV-1. Front Microbiol 3: 378.
    • (2012) Front Microbiol , vol.3 , pp. 378
    • Pique, C.1    Jones, K.S.2
  • 156
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly
    • Hill CP, Worthylake D, Bancroft DP, et al. (1996) Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc Natl Acad Sci U S A 93: 3099-3104.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3
  • 157
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and implications for virus assembly
    • Rao Z, Belyaev AS, Fry E, et al. (1995) Crystal structure of SIV matrix antigen and implications for virus assembly. Nature 378: 743-747.
    • (1995) Nature , vol.378 , pp. 743-747
    • Rao, Z.1    Belyaev, A.S.2    Fry, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.