메뉴 건너뛰기




Volumn 86, Issue 8, 2012, Pages 4182-4193

Budding of retroviruses utilizing divergent L domains requires nucleocapsid

Author keywords

[No Author keywords available]

Indexed keywords

ESCRT PROTEIN; GAG PROTEIN;

EID: 84861393911     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.07105-11     Document Type: Article
Times cited : (18)

References (80)
  • 1
    • 0025266663 scopus 로고
    • Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus
    • Aldovini A, Young RA. 1990. Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus. J. Virol. 64:1920-1926.
    • (1990) J. Virol. , vol.64 , pp. 1920-1926
    • Aldovini, A.1    Young, R.A.2
  • 2
    • 0034636984 scopus 로고    scopus 로고
    • NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA packaging signal. Implications for genome recognition
    • Amarasinghe GK, et al. 2000. NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA packaging signal. Implications for genome recognition. J. Mol. Biol. 301:491-511.
    • (2000) J. Mol. Biol. , vol.301 , pp. 491-511
    • Amarasinghe, G.K.1
  • 3
    • 33646377434 scopus 로고    scopus 로고
    • Structural features in EIAV NCp11: a lentivirus nucleocapsid protein with a short linker
    • Amodeo P, Castiglione Morelli MA, Ostuni A, Battistuzzi G, Bavoso A. 2006. Structural features in EIAV NCp11: a lentivirus nucleocapsid protein with a short linker. Biochemistry 45:5517-5526.
    • (2006) Biochemistry , vol.45 , pp. 5517-5526
    • Amodeo, P.1    Castiglione Morelli, M.A.2    Ostuni, A.3    Battistuzzi, G.4    Bavoso, A.5
  • 4
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T, Emr SD. 2002. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev. Cell 3:271-282.
    • (2002) Dev. Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 5
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst M, Sato TK, Banta LM, Emr SD. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 16:1820-1831.
    • (1997) EMBO J , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 6
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst M, Wendland B, Estepa EJ, Emr SD. 1998. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17:2982-2993.
    • (1998) EMBO J , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 7
    • 80055114108 scopus 로고    scopus 로고
    • Distal leucines are key functional determinants of Alix-binding SIVsmE543 and SIVmac239 type 3 L domains
    • Bello NF, et al. 2011. Distal leucines are key functional determinants of Alix-binding SIVsmE543 and SIVmac239 type 3 L domains. J. Virol. 85: 11532-11537.
    • (2011) J. Virol. , vol.85 , pp. 11532-11537
    • Bello, N.F.1
  • 8
    • 0027496344 scopus 로고
    • Specific binding of human immunodeficiency virus type 1 gag polyprotein and nucleocapsid protein to viral RNAs detected by RNA mobility shift assays
    • Berkowitz RD, Luban J, Goff SP. 1993. Specific binding of human immunodeficiency virus type 1 gag polyprotein and nucleocapsid protein to viral RNAs detected by RNA mobility shift assays. J. Virol. 67:7190-7200.
    • (1993) J. Virol. , vol.67 , pp. 7190-7200
    • Berkowitz, R.D.1    Luban, J.2    Goff, S.P.3
  • 9
    • 11244326067 scopus 로고    scopus 로고
    • Complete genome analysis of one of the earliest SIVcpzPtt strains from Gabon (SIVcpzGAB2)
    • Bibollet-Ruche F, et al. 2004. Complete genome analysis of one of the earliest SIVcpzPtt strains from Gabon (SIVcpzGAB2). AIDS Res. Hum. Retroviruses 20:1377-1381.
    • (2004) AIDS Res. Hum. Retroviruses , vol.20 , pp. 1377-1381
    • Bibollet-Ruche, F.1
  • 10
    • 67649407509 scopus 로고    scopus 로고
    • The cell biology of HIV-1 virion genesis
    • Bieniasz PD. 2009. The cell biology of HIV-1 virion genesis. Cell Host Microbe 5:550-558.
    • (2009) Cell Host Microbe , vol.5 , pp. 550-558
    • Bieniasz, P.D.1
  • 11
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M, Ratner L. 1990. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl. Acad. Sci. U. S. A. 87:523-527.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 12
    • 0032874018 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein
    • Burniston MT, Cimarelli A, Colgan J, Curtis SP, Luban J. 1999. Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein. J. Virol. 73:8527-8540.
    • (1999) J. Virol. , vol.73 , pp. 8527-8540
    • Burniston, M.T.1    Cimarelli, A.2    Colgan, J.3    Curtis, S.P.4    Luban, J.5
  • 13
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell S, Rein A. 1999. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J. Virol. 73:2270-2279.14.
    • (1999) J. Virol. , vol.73 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 14
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell S, Vogt VM. 1995. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J. Virol. 69:6487-6497.
    • (1995) J. Virol. , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 15
    • 0036568729 scopus 로고    scopus 로고
    • Tsg101: HIV-1's ticket to ride
    • Carter CA. 2002. Tsg101: HIV-1's ticket to ride. Trends Microbiol. 10: 203-205.
    • (2002) Trends Microbiol , vol.10 , pp. 203-205
    • Carter, C.A.1
  • 16
    • 44949099395 scopus 로고    scopus 로고
    • The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus
    • Chatel-Chaix L, Boulay K, Mouland AJ, Desgroseillers L. 2008. The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus. Retrovirology 5:41.
    • (2008) Retrovirology , vol.5 , pp. 41
    • Chatel-Chaix, L.1    Boulay, K.2    Mouland, A.J.3    Desgroseillers, L.4
  • 17
    • 0034011267 scopus 로고    scopus 로고
    • Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA
    • Cimarelli A, Sandin S, Hoglund S, Luban J. 2000. Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA. J. Virol. 74:3046-3057.
    • (2000) J. Virol. , vol.74 , pp. 3046-3057
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 18
    • 0031907566 scopus 로고    scopus 로고
    • Development and characterization of an in vivo pathogenic molecular clone of equine infectious anemia virus
    • Cook RF, et al. 1998. Development and characterization of an in vivo pathogenic molecular clone of equine infectious anemia virus. J. Virol. 72:1383-1393.
    • (1998) J. Virol. , vol.72 , pp. 1383-1393
    • Cook, R.F.1
  • 19
    • 80051712397 scopus 로고    scopus 로고
    • Flexible nature and specific functions of the HIV-1 nucleocapsid protein
    • Darlix JL, et al. 2011. Flexible nature and specific functions of the HIV-1 nucleocapsid protein. J. Mol. Biol. 410:565-581.
    • (2011) J. Mol. Biol. , vol.410 , pp. 565-581
    • Darlix, J.L.1
  • 20
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • De Guzman RN, et al. 1998. Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science 279:384-388.
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1
  • 22
    • 0037154214 scopus 로고    scopus 로고
    • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function
    • Demirov DG, Ono A, Orenstein JM, Freed EO. 2002. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc. Natl. Acad. Sci. U. S. A. 99:955-960.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 955-960
    • Demirov, D.G.1    Ono, A.2    Orenstein, J.M.3    Freed, E.O.4
  • 23
    • 0026628854 scopus 로고
    • Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingers
    • De Rocquigny H, et al. 1992. Viral RNA annealing activities of human immunodeficiency virus type 1 nucleocapsid protein require only peptide domains outside the zinc fingers. Proc. Natl. Acad. Sci. U. S. A. 89:6472-6476.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6472-6476
    • De Rocquigny, H.1
  • 24
    • 77953312134 scopus 로고    scopus 로고
    • An LYPSL late domain in the gag protein contributes to the efficient release and replication of Rous sarcoma virus
    • Dilley KA, Gregory D, Johnson MC, Vogt VM. 2010. An LYPSL late domain in the gag protein contributes to the efficient release and replication of Rous sarcoma virus. J. Virol. 84:6276-6287.
    • (2010) J. Virol. , vol.84 , pp. 6276-6287
    • Dilley, K.A.1    Gregory, D.2    Johnson, M.C.3    Vogt, V.M.4
  • 25
    • 34247516888 scopus 로고    scopus 로고
    • Host ABCE1 is at plasma membrane HIV assembly sites and its dissociation from Gag is linked to subsequent events of virus production
    • Dooher JE, Schneider BL, Reed JC, Lingappa JR. 2007. Host ABCE1 is at plasma membrane HIV assembly sites and its dissociation from Gag is linked to subsequent events of virus production. Traffic 8:195-211.
    • (2007) Traffic , vol.8 , pp. 195-211
    • Dooher, J.E.1    Schneider, B.L.2    Reed, J.C.3    Lingappa, J.R.4
  • 26
    • 63449121941 scopus 로고    scopus 로고
    • nL late domains to recruit the cellular machinery necessary for viral budding
    • nL late domains to recruit the cellular machinery necessary for viral budding. PLoS Pathog. 5:e1000339.
    • (2009) PLoS Pathog , vol.5
    • Dussupt, V.1
  • 27
    • 79551702980 scopus 로고    scopus 로고
    • Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding
    • Dussupt V, et al. 2011. Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding. J. Virol. 85:2304-2315.
    • (2011) J. Virol. , vol.85 , pp. 2304-2315
    • Dussupt, V.1
  • 28
    • 0026762403 scopus 로고
    • Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro
    • Ehrlich LS, Agresta BE, Carter CA. 1992. Assembly of recombinant human immunodeficiency virus type 1 capsid protein in vitro. J. Virol. 66:4874-4883.
    • (1992) J. Virol. , vol.66 , pp. 4874-4883
    • Ehrlich, L.S.1    Agresta, B.E.2    Carter, C.A.3
  • 29
    • 84855862412 scopus 로고    scopus 로고
    • The cellular protein Lyric interacts with HIV-1 Gag
    • Engeland CE, et al. 2011. The cellular protein Lyric interacts with HIV-1 Gag. J. Virol. 85:13322-13332.
    • (2011) J. Virol. , vol.85 , pp. 13322-13332
    • Engeland, C.E.1
  • 30
    • 33847355934 scopus 로고    scopus 로고
    • Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding
    • Fisher RD, et al. 2007. Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell 128:841-852.
    • (2007) Cell , vol.128 , pp. 841-852
    • Fisher, R.D.1
  • 31
    • 0030693391 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
    • Gamble TR, 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
  • 32
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • Garrus JE, et al. 2001. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell 107:55-65.
    • (2001) Cell , vol.107 , pp. 55-65
    • Garrus, J.E.1
  • 34
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Göttlinger HG, Sodroski JG, Haseltine WA. 1989. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. U. S. A. 86:5781-5785.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5781-5785
    • Göttlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 35
    • 0031954466 scopus 로고    scopus 로고
    • N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
    • Gross I, Hohenberg H, Huckhagel C, Kräusslich HG. 1998. N-terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J. Virol. 72:4798-4810.
    • (1998) J. Virol. , vol.72 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckhagel, C.3    Kräusslich, H.G.4
  • 36
    • 0031033036 scopus 로고    scopus 로고
    • A molecularly cloned, pathogenic, neutralizationresistant simian immunodeficiency virus, SIVsmE543-3
    • Hirsch V, et al. 1997. A molecularly cloned, pathogenic, neutralizationresistant simian immunodeficiency virus, SIVsmE543-3. J. Virol. 71: 1608-1620.
    • (1997) J. Virol. , vol.71 , pp. 1608-1620
    • Hirsch, V.1
  • 37
    • 67650439272 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding
    • Hogue IB, Hoppe A, Ono A. 2009. Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding. J. Virol. 83:7322-7336.
    • (2009) J. Virol. , vol.83 , pp. 7322-7336
    • Hogue, I.B.1    Hoppe, A.2    Ono, A.3
  • 38
    • 42449129244 scopus 로고    scopus 로고
    • Nucleocapsid mutations turn HIV-1 into a DNAcontaining virus
    • Houzet L, et al. 2008. Nucleocapsid mutations turn HIV-1 into a DNAcontaining virus. Nucleic Acids Res. 36:2311-2319.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2311-2319
    • Houzet, L.1
  • 39
    • 0028971135 scopus 로고
    • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Huang M, Orenstein JM, Martin MA, Freed EO. 1995. p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69:6810-6818.
    • (1995) J. Virol. , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 40
    • 79953296191 scopus 로고    scopus 로고
    • Dynamics of ESCRT protein recruitment during retroviral assembly
    • Jouvenet N, Zhadina M, Bieniasz PD, Simon SM. 2011. Dynamics of ESCRT protein recruitment during retroviral assembly. Nat. Cell Biol. 13:394-401.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 394-401
    • Jouvenet, N.1    Zhadina, M.2    Bieniasz, P.D.3    Simon, S.M.4
  • 41
    • 0141643096 scopus 로고    scopus 로고
    • The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting
    • Katoh K, et al. 2003. The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. J. Biol. Chem. 278:39104-39113.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39104-39113
    • Katoh, K.1
  • 42
    • 0035949489 scopus 로고    scopus 로고
    • Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells
    • Kikonyogo A, et al. 2001. Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells. Proc. Natl. Acad. Sci. U. S. A. 98:11199-11204.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11199-11204
    • Kikonyogo, A.1
  • 43
    • 19944375126 scopus 로고    scopus 로고
    • Structural basis for endosomal targeting by the Bro1 domain
    • Kim J, et al. 2005. Structural basis for endosomal targeting by the Bro1 domain. Dev. Cell 8:937-947.
    • (2005) Dev. Cell , vol.8 , pp. 937-947
    • Kim, J.1
  • 44
    • 78751668182 scopus 로고    scopus 로고
    • Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcription
    • Levin JG, Mitra M, Mascarenhas A, Musier-Forsyth K. 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    Musier-Forsyth, K.4
  • 45
    • 0036148338 scopus 로고    scopus 로고
    • Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication
    • Li F, Chen C, Puffer BA, Montelaro RC. 2002. Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication. J. Virol. 76:1569-1577.
    • (2002) J. Virol. , vol.76 , pp. 1569-1577
    • Li, F.1    Chen, C.2    Puffer, B.A.3    Montelaro, R.C.4
  • 46
    • 36349029236 scopus 로고    scopus 로고
    • Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells
    • Li H, Dou J, Ding L, Spearman P. 2007. Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells. J. Virol. 81:12899-12910.
    • (2007) J. Virol. , vol.81 , pp. 12899-12910
    • Li, H.1    Dou, J.2    Ding, L.3    Spearman, P.4
  • 47
    • 78449233400 scopus 로고    scopus 로고
    • Nucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cells
    • Llewellyn GN, Hogue IB, Grover JR, Ono A. 2010. Nucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cells. PLoS Pathog. 6:e1001167.
    • (2010) PLoS Pathog , vol.6
    • Llewellyn, G.N.1    Hogue, I.B.2    Grover, J.R.3    Ono, A.4
  • 48
    • 0242331710 scopus 로고    scopus 로고
    • A bipartite late-budding domain in human immunodeficiency virus type 1
    • Martin-Serrano J, Bieniasz PD. 2003. A bipartite late-budding domain in human immunodeficiency virus type 1. J. Virol. 77:12373-12377.
    • (2003) J. Virol. , vol.77 , pp. 12373-12377
    • Martin-Serrano, J.1    Bieniasz, P.D.2
  • 49
    • 12144258074 scopus 로고    scopus 로고
    • HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway
    • Martin-Serrano J, Eastman SW, Chung W, Bieniasz PD. 2005. HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway. J. Cell Biol. 168:89-101.
    • (2005) J. Cell Biol. , vol.168 , pp. 89-101
    • Martin-Serrano, J.1    Eastman, S.W.2    Chung, W.3    Bieniasz, P.D.4
  • 50
    • 2442670346 scopus 로고    scopus 로고
    • Context-dependent effects of L domains and ubiquitination on viral budding
    • Martin-Serrano J, Perez-Caballero D, Bieniasz PD. 2004. Context-dependent effects of L domains and ubiquitination on viral budding. J. Virol. 78:5554-5563.
    • (2004) J. Virol. , vol.78 , pp. 5554-5563
    • Martin-Serrano, J.1    Perez-Caballero, D.2    Bieniasz, P.D.3
  • 51
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano J, Yarovoy A, Perez-Caballero D, Bieniasz PD. 2003. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl. Acad. Sci. U. S. A. 100:12414-12419.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 52
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano J, Zang T, Bieniasz PD. 2001. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7:1313-1319.
    • (2001) Nat. Med. , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 54
    • 78751663443 scopus 로고    scopus 로고
    • Features, processing states, and heterologous protein interactions in the modulation of the retroviral nucleocapsid protein function
    • Mirambeau G, Lyonnais S, Gorelick RJ. 2010. Features, processing states, and heterologous protein interactions in the modulation of the retroviral nucleocapsid protein function. RNA Biol. 7:724-734.
    • (2010) RNA Biol , vol.7 , pp. 724-734
    • Mirambeau, G.1    Lyonnais, S.2    Gorelick, R.J.3
  • 55
    • 0021236382 scopus 로고
    • Antigenic variation during persistent infection by equine infectious anemia virus, a retrovirus
    • Montelaro RC, Parekh B, Orrego A, Issel CJ. 1984. Antigenic variation during persistent infection by equine infectious anemia virus, a retrovirus. J. Biol. Chem. 259:10539-10544.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10539-10544
    • Montelaro, R.C.1    Parekh, B.2    Orrego, A.3    Issel, C.J.4
  • 56
    • 79952640255 scopus 로고    scopus 로고
    • ESCRT-III protein requirements for HIV-1 budding
    • Morita E, et al. 2011. ESCRT-III protein requirements for HIV-1 budding. Cell Host Microbe 9:235-242.
    • (2011) Cell Host Microbe , vol.9 , pp. 235-242
    • Morita, E.1
  • 58
    • 78751670345 scopus 로고    scopus 로고
    • Properties and functions of the nucleocapsid protein in virus assembly
    • Muriaux D, Darlix JL. 2010. Properties and functions of the nucleocapsid protein in virus assembly. RNA Biol. 7:744-753.
    • (2010) RNA Biol , vol.7 , pp. 744-753
    • Muriaux, D.1    Darlix, J.L.2
  • 60
    • 0038710633 scopus 로고    scopus 로고
    • Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant
    • Ott DE, et al. 2003. Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant. J. Virol. 77:5547-5556.
    • (2003) J. Virol. , vol.77 , pp. 5547-5556
    • Ott, D.E.1
  • 61
    • 66749147856 scopus 로고    scopus 로고
    • A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments
    • Pires R, et al. 2009. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure 17:843-856.
    • (2009) Structure , vol.17 , pp. 843-856
    • Pires, R.1
  • 62
    • 38349174466 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid
    • Popov S, Popova E, Inoue M, Göttlinger HG. 2008. Human immunodeficiency virus type 1 Gag engages the Bro1 domain of ALIX/AIP1 through the nucleocapsid. J. Virol. 82:1389-1398.
    • (2008) J. Virol. , vol.82 , pp. 1389-1398
    • Popov, S.1    Popova, E.2    Inoue, M.3    Göttlinger, H.G.4
  • 63
    • 77953319640 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid-p1 confers ESCRT pathway dependence
    • Popova E, Popov S, Göttlinger HG. 2010. Human immunodeficiency virus type 1 nucleocapsid-p1 confers ESCRT pathway dependence. J. Virol. 84:6590-6597.
    • (2010) J. Virol. , vol.84 , pp. 6590-6597
    • Popova, E.1    Popov, S.2    Göttlinger, H.G.3
  • 64
    • 67549109069 scopus 로고    scopus 로고
    • X-ray structures of the hexameric building block of the HIV capsid
    • Pornillos O, 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
  • 65
    • 0030858622 scopus 로고    scopus 로고
    • Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein
    • Puffer BA, Parent LJ, Wills JW, Montelaro RC. 1997. Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein. J. Virol. 71:6541-6546.
    • (1997) J. Virol. , vol.71 , pp. 6541-6546
    • Puffer, B.A.1    Parent, L.J.2    Wills, J.W.3    Montelaro, R.C.4
  • 67
    • 80054078255 scopus 로고    scopus 로고
    • The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release
    • Sette P, et al. 2011. The Phe105 loop of Alix Bro1 domain plays a key role in HIV-1 release. Structure 19:1485-1495.
    • (2011) Structure , vol.19 , pp. 1485-1495
    • Sette, P.1
  • 68
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B, Calistri A, Craig S, Popova E, Göttlinger HG. 2003. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114:689-699.
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Göttlinger, H.G.5
  • 69
    • 0036094492 scopus 로고    scopus 로고
    • Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis
    • Strack B, Calistri A, Göttlinger HG. 2002. Late assembly domain function can exhibit context dependence and involves ubiquitin residues implicated in endocytosis. J. Virol. 76:5472-5479.
    • (2002) J. Virol. , vol.76 , pp. 5472-5479
    • Strack, B.1    Calistri, A.2    Göttlinger, H.G.3
  • 70
    • 35148900389 scopus 로고    scopus 로고
    • ESCRT-III recognition by VPS4 ATPases
    • Stuchell-Brereton MD, et al. 2007. ESCRT-III recognition by VPS4 ATPases. Nature 449:740-744.
    • (2007) Nature , vol.449 , pp. 740-744
    • Stuchell-Brereton, M.D.1
  • 71
    • 52649129852 scopus 로고    scopus 로고
    • Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription
    • Thomas JA, Bosche WJ, Shatzer TL, Johnson DG, Gorelick RJ. 2008. Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription. J. Virol. 82:9318-9328.
    • (2008) J. Virol. , vol.82 , pp. 9318-9328
    • Thomas, J.A.1    Bosche, W.J.2    Shatzer, T.L.3    Johnson, D.G.4    Gorelick, R.J.5
  • 72
    • 34249943479 scopus 로고    scopus 로고
    • Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site
    • Usami Y, Popov S, Göttlinger HG. 2007. Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site. J. Virol. 81:6614-6622.
    • (2007) J. Virol. , vol.81 , pp. 6614-6622
    • Usami, Y.1    Popov, S.2    Göttlinger, H.G.3
  • 73
    • 0034940214 scopus 로고    scopus 로고
    • Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)
    • VerPlank L, et al. 2001. Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag). Proc. Natl. Acad. Sci. U. S. A. 98:7724-7729.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7724-7729
    • VerPlank, L.1
  • 74
    • 10744233294 scopus 로고    scopus 로고
    • The protein network of HIV budding
    • von Schwedler UK, et al. 2003. The protein network of HIV budding. Cell 114:701-713.
    • (2003) Cell , vol.114 , pp. 701-713
    • von Schwedler, U.K.1
  • 75
    • 0036889123 scopus 로고    scopus 로고
    • RNA incorporation is critical for retroviral particle integrity after cell membrane assembly of Gag complexes
    • Wang SW, Aldovini A. 2002. RNA incorporation is critical for retroviral particle integrity after cell membrane assembly of Gag complexes. J. Virol. 76:11853-11865.
    • (2002) J. Virol. , vol.76 , pp. 11853-11865
    • Wang, S.W.1    Aldovini, A.2
  • 76
    • 0033854158 scopus 로고    scopus 로고
    • Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses
    • Yuan B, Campbell S, Bacharach E, Rein A, Goff SP. 2000. Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses. J. Virol. 74:7250-7260.
    • (2000) J. Virol. , vol.74 , pp. 7250-7260
    • Yuan, B.1    Campbell, S.2    Bacharach, E.3    Rein, A.4    Goff, S.P.5
  • 77
    • 37849024338 scopus 로고    scopus 로고
    • Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV
    • Zhai Q, et al. 2008. Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV. Nat. Struct. Mol. Biol. 15:43-49.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 43-49
    • Zhai, Q.1
  • 78
    • 78650056790 scopus 로고    scopus 로고
    • Identification and structural characterization of the ALIX-binding late domains of simian immunodeficiency virus SIVmac239 and SIVagmTan-1
    • Zhai Q, Landesman MB, Robinson H, Sundquist WI, Hill CP. 2011. Identification and structural characterization of the ALIX-binding late domains of simian immunodeficiency virus SIVmac239 and SIVagmTan-1. J. Virol. 85:632-637.
    • (2011) J. Virol. , vol.85 , pp. 632-637
    • Zhai, Q.1    Landesman, M.B.2    Robinson, H.3    Sundquist, W.I.4    Hill, C.P.5
  • 79
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
    • Zhou W, Parent LJ, Wills JW, Resh MD. 1994. Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68:2556-2569.
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4
  • 80
    • 0037011924 scopus 로고    scopus 로고
    • Identification of a host protein essential for assembly of immature HIV-1 capsids
    • Zimmerman C, et al. 2002. Identification of a host protein essential for assembly of immature HIV-1 capsids. Nature 415:88-92.
    • (2002) Nature , vol.415 , pp. 88-92
    • Zimmerman, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.