메뉴 건너뛰기




Volumn 12, Issue 5, 2012, Pages 389-409

Retroviral protein transfer: Falling apart to make an impact

Author keywords

Human Immunodeficiency Virus; Mouse Leukemia Virus; Retroviral imaging; Retroviral protein transfer; Retroviral vector; Virus like particle

Indexed keywords

LENTIVIRUS VECTOR; MESSENGER RNA; RECOMBINANT PROTEIN; RETROVIRUS VECTOR; VIRUS PROTEIN;

EID: 84867004626     PISSN: 15665232     EISSN: 18755631     Source Type: Journal    
DOI: 10.2174/156652312802762581     Document Type: Review
Times cited : (12)

References (205)
  • 1
    • 84863115198 scopus 로고    scopus 로고
    • Intrinsic antiviral immunity
    • Yan N, Chen ZJ. Intrinsic antiviral immunity. Nat Immunol 2012; 13: 214-22.
    • (2012) Nat Immunol , vol.13 , pp. 214-222
    • Yan, N.1    Chen, Z.J.2
  • 2
    • 77958182786 scopus 로고    scopus 로고
    • Immune evasion and counteraction of restriction factors by HIV-1 and other primate lentiviruses
    • Kirchhoff F. Immune evasion and counteraction of restriction factors by HIV-1 and other primate lentiviruses. Cell Host Microbe 2010; 8: 55-67.
    • (2010) Cell Host Microbe , vol.8 , pp. 55-67
    • Kirchhoff, F.1
  • 3
    • 0036713498 scopus 로고    scopus 로고
    • Critical role of human T-lymphotropic virus type 1 accessory proteins in viral replication and pathogenesis
    • Albrecht B, Lairmore MD. Critical role of human T-lymphotropic virus type 1 accessory proteins in viral replication and pathogenesis. Microbiol Mol Biol R 2002; 66: 396-406.
    • (2002) Microbiol Mol Biol R , vol.66 , pp. 396-406
    • Albrecht, B.1    Lairmore, M.D.2
  • 4
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins-ensuring viral survival in a hostile environment
    • Malim MH, Emerman M. HIV-1 accessory proteins-ensuring viral survival in a hostile environment. Cell Host Microbe 2008; 3: 388-98.
    • (2008) Cell Host Microbe , vol.3 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 6
    • 0032037421 scopus 로고    scopus 로고
    • TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus
    • Grüter P, Tabernero C, von Kobbe C, et al. TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus. Mol Cell 1998; 1: 649-59.
    • (1998) Mol Cell , vol.1 , pp. 649-659
    • Grüter, P.1    Tabernero, C.2    von Kobbe, C.3
  • 7
    • 0031710231 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus Rev and human T-cell leukemia virus Rex function, but not Mason-Pfizer monkey virus constitutive transport element activity, by a mutant human nucleoporin targeted to Crm1
    • Bogerd HP, Echarri A, Ross TM, Cullen BR. Inhibition of human immunodeficiency virus Rev and human T-cell leukemia virus Rex function, but not Mason-Pfizer monkey virus constitutive transport element activity, by a mutant human nucleoporin targeted to Crm1. J Virol 1998; 72: 8627-35.
    • (1998) J Virol , vol.72 , pp. 8627-8635
    • Bogerd, H.P.1    Echarri, A.2    Ross, T.M.3    Cullen, B.R.4
  • 8
    • 0024518918 scopus 로고
    • The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA
    • Malim MH, Hauber J, Le SY, et al. The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature 1989; 338: 254-7.
    • (1989) Nature , vol.338 , pp. 254-257
    • Malim, M.H.1    Hauber, J.2    Le, S.Y.3
  • 9
    • 34248559432 scopus 로고    scopus 로고
    • Tap and Dbp5, but not Gag, are involved in DR-mediated nuclear export of unspliced Rous sarcoma virus RNA
    • LeBlanc JJ, Uddowla S, Abraham B, Clatterbuck S, Beemon KL. Tap and Dbp5, but not Gag, are involved in DR-mediated nuclear export of unspliced Rous sarcoma virus RNA. Virology 2007; 363: 376-86.
    • (2007) Virology , vol.363 , pp. 376-386
    • Leblanc, J.J.1    Uddowla, S.2    Abraham, B.3    Clatterbuck, S.4    Beemon, K.L.5
  • 10
    • 75649143667 scopus 로고    scopus 로고
    • Limited complementarity between U1 snRNA and a retroviral 5' splice site permits its attenuation via RNA secondary structure
    • Zychlinski D, Erkelenz S, Melhorn V, et al. Limited complementarity between U1 snRNA and a retroviral 5' splice site permits its attenuation via RNA secondary structure. Nucleic Acids Res 2009; 37: 7429-40.
    • (2009) Nucleic Acids Res , vol.37 , pp. 7429-7440
    • Zychlinski, D.1    Erkelenz, S.2    Melhorn, V.3
  • 11
    • 33846003846 scopus 로고    scopus 로고
    • Murine Leukemia Virus Regulates Alternative Splicing through Sequences Upstream of the 5' Splice Site
    • Kraunus J, Zychlinski D, Heise T, et al. Murine Leukemia Virus Regulates Alternative Splicing through Sequences Upstream of the 5' Splice Site. J Biol Chem 2006; 281: 37381-90.
    • (2006) J Biol Chem , vol.281 , pp. 37381-37390
    • Kraunus, J.1    Zychlinski, D.2    Heise, T.3
  • 12
    • 0035138477 scopus 로고    scopus 로고
    • Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity
    • Shehu-Xhilaga M, Crowe SM, Mak J. Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity. J Virol 2001; 75: 1834-41.
    • (2001) J Virol , vol.75 , pp. 1834-1841
    • Shehu-Xhilaga, M.1    Crowe, S.M.2    Mak, J.3
  • 13
    • 0026018243 scopus 로고
    • Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production
    • Park J, Morrow CD. Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production. J Virol 1991; 65: 5111-7.
    • (1991) J Virol , vol.65 , pp. 5111-5117
    • Park, J.1    Morrow, C.D.2
  • 14
    • 0040870513 scopus 로고
    • Murine leukemia virus protease is encoded by the gag-pol gene and is synthesized through suppression of an amber termination codon
    • Yoshinaka Y, Katoh I, Copeland T, Oroszlan S. Murine leukemia virus protease is encoded by the gag-pol gene and is synthesized through suppression of an amber termination codon. Proc Natl Acad Sci USA 1985; 82: 1618-22.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1618-1622
    • Yoshinaka, Y.1    Katoh, I.2    Copeland, T.3    Oroszlan, S.4
  • 15
    • 0023870815 scopus 로고
    • Characterization of ribosomal frameshifting in HIV-1 gag-pol expression
    • Jacks T, Power M, Masiarz F, et al. Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature 1988; 331: 280-3.
    • (1988) Nature , vol.331 , pp. 280-283
    • Jacks, T.1    Power, M.2    Masiarz, F.3
  • 16
    • 0023891579 scopus 로고
    • Expression of the gag-pol fusion protein of Moloney murine leukemia virus without gag protein does not induce virion formation or proteolytic processing
    • Felsenstein KM, Goff SP. Expression of the gag-pol fusion protein of Moloney murine leukemia virus without gag protein does not induce virion formation or proteolytic processing. J Virol 1988; 62: 2179-82.
    • (1988) J Virol , vol.62 , pp. 2179-2182
    • Felsenstein, K.M.1    Goff, S.P.2
  • 17
    • 0030835321 scopus 로고    scopus 로고
    • Pseudotyping human immunodeficiency virus type 1 (HIV-1) by the glycoprotein of vesicular stomatitis virus targets HIV-1 entry to an endocytic pathway and suppresses both the requirement for Nef and the sensitivity to cyclosporin A
    • Aiken C. Pseudotyping human immunodeficiency virus type 1 (HIV-1) by the glycoprotein of vesicular stomatitis virus targets HIV-1 entry to an endocytic pathway and suppresses both the requirement for Nef and the sensitivity to cyclosporin A. J Virol 1997; 71: 5871-7.
    • (1997) J Virol , vol.71 , pp. 5871-5877
    • Aiken, C.1
  • 19
    • 22944458202 scopus 로고    scopus 로고
    • Altering the tropism of lentiviral vectors through pseudotyping
    • Cronin J, Zhang XY, Reiser J. Altering the tropism of lentiviral vectors through pseudotyping. Curr Gene Ther 2005; 5: 387-98.
    • (2005) Curr Gene Ther , vol.5 , pp. 387-398
    • Cronin, J.1    Zhang, X.Y.2    Reiser, J.3
  • 20
    • 78049345098 scopus 로고    scopus 로고
    • Specific gene transfer to neurons, endothelial cells and hematopoietic progenitors with lentiviral vectors
    • Anliker B, Abel T, Kneissl S, et al. Specific gene transfer to neurons, endothelial cells and hematopoietic progenitors with lentiviral vectors. Nat Methods 2010; 7: 929-35.
    • (2010) Nat Methods , vol.7 , pp. 929-935
    • Anliker, B.1    Abel, T.2    Kneissl, S.3
  • 21
    • 33847139800 scopus 로고    scopus 로고
    • The road to chromatin-nuclear entry of retroviruses
    • Suzuki Y, Craigie R. The road to chromatin-nuclear entry of retroviruses. Nat Rev Microbiol 2007; 5: 187-96.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 187-196
    • Suzuki, Y.1    Craigie, R.2
  • 22
    • 0024515364 scopus 로고
    • Unmyristylated Moloney murine leukemia virus Pr65gag is excluded from virus assembly and maturation events
    • Schultz AM, Rein A. Unmyristylated Moloney murine leukemia virus Pr65gag is excluded from virus assembly and maturation events. J Virol 1989; 63: 2370-3.
    • (1989) J Virol , vol.63 , pp. 2370-2373
    • Schultz, A.M.1    Rein, A.2
  • 23
    • 0022794486 scopus 로고
    • Myristylation site in Pr65gag is essential for virus particle formation by Moloney murine leukemia virus
    • Rein A, McClure MR, Rice NR, Luftig RB, Schultz AM. Myristylation site in Pr65gag is essential for virus particle formation by Moloney murine leukemia virus. Proc Natl Acad Sci USA 1986; 83: 7246-50.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7246-7250
    • Rein, A.1    McClure, M.R.2    Rice, N.R.3    Luftig, R.B.4    Schultz, A.M.5
  • 24
    • 0142060842 scopus 로고    scopus 로고
    • Murine leukemia virus particle assembly quantitated by fluorescence microscopy: Role of Gag-Gag interactions and membrane association
    • Andrawiss M, Takeuchi Y, Hewlett L, Collins M. Murine leukemia virus particle assembly quantitated by fluorescence microscopy: role of Gag-Gag interactions and membrane association. J Virol 2003; 77: 11651-60.
    • (2003) J Virol , vol.77 , pp. 11651-11660
    • Andrawiss, M.1    Takeuchi, Y.2    Hewlett, L.3    Collins, M.4
  • 25
    • 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. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 1989; 86: 5781-5.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5781-5785
    • Göttlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 26
    • 84861323711 scopus 로고    scopus 로고
    • TNPO3 is Required for HIV-1 Replication After Nuclear Import but Prior to Integration and Binds the HIV-1 Core
    • Valle-Casuso JC, Di Nunzio F, Yang Y, et al. TNPO3 is Required for HIV-1 Replication After Nuclear Import but Prior to Integration and Binds the HIV-1 Core. J Virol 2012; 86: 5931-6.
    • (2012) J Virol , vol.86 , pp. 5931-5936
    • Valle-Casuso, J.C.1    Di Nunzio, F.2    Yang, Y.3
  • 27
    • 84855278211 scopus 로고    scopus 로고
    • HIV-1 Capsid-Cyclophilin Interactions Determine Nuclear Import Pathway, Integration Targeting and Replication Efficiency
    • Schaller T, Ocwieja KE, Rasaiyaah J, et al. HIV-1 Capsid-Cyclophilin Interactions Determine Nuclear Import Pathway, Integration Targeting and Replication Efficiency. PLoS Pathog 2011; 7: e1002439.
    • (2011) PLoS Pathog , vol.7
    • Schaller, T.1    Ocwieja, K.E.2    Rasaiyaah, J.3
  • 28
    • 79960415929 scopus 로고    scopus 로고
    • The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid
    • Matreyek KA, Engelman A. The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid. J Virol 2011; 85: 7818-27.
    • (2011) J Virol , vol.85 , pp. 7818-7827
    • Matreyek, K.A.1    Engelman, A.2
  • 29
    • 33644768125 scopus 로고    scopus 로고
    • A small loop in the capsid protein of Moloney murine leukemia virus controls assembly of spherical cores
    • Auerbach MR, Brown KR, Kaplan A, de Las Nueces D, Singh IR. A small loop in the capsid protein of Moloney murine leukemia virus controls assembly of spherical cores. J Virol 2006; 80: 2884-93.
    • (2006) J Virol , vol.80 , pp. 2884-2893
    • Auerbach, M.R.1    Brown, K.R.2    Kaplan, A.3    de Las Nueces, D.4    Singh, I.R.5
  • 30
    • 0030586691 scopus 로고    scopus 로고
    • Amino acid substitutions in the CA protein of Moloney murine leukemia virus that block early events in infection
    • Alin K, Goff SP. Amino acid substitutions in the CA protein of Moloney murine leukemia virus that block early events in infection. Virology 1996; 222: 339-51.
    • (1996) Virology , vol.222 , pp. 339-351
    • Alin, K.1    Goff, S.P.2
  • 31
    • 39349097864 scopus 로고    scopus 로고
    • Identification of host proteins required for HIV infection through a functional genomic screen
    • Brass AL, Dykxhoorn DM, Benita Y, et al. Identification of host proteins required for HIV infection through a functional genomic screen. Science 2008; 319: 921-6.
    • (2008) Science , vol.319 , pp. 921-926
    • Brass, A.L.1    Dykxhoorn, D.M.2    Benita, Y.3
  • 32
    • 52949130695 scopus 로고    scopus 로고
    • Global analysis of hostpathogen interactions that regulate early-stage HIV-1 replication
    • König R, Zhou Y, Elleder D, et al. Global analysis of hostpathogen interactions that regulate early-stage HIV-1 replication. Cell 2008; 135: 49-60.
    • (2008) Cell , vol.135 , pp. 49-60
    • König, R.1    Zhou, Y.2    Elleder, D.3
  • 33
    • 6344243521 scopus 로고    scopus 로고
    • Retroviral pseudotransduction for targeted cell manipulation
    • Galla M, Will E, Kraunus J, Chen L, Baum C. Retroviral pseudotransduction for targeted cell manipulation. Mol Cell 2004; 16: 309-15.
    • (2004) Mol Cell , vol.16 , pp. 309-315
    • Galla, M.1    Will, E.2    Kraunus, J.3    Chen, L.4    Baum, C.5
  • 34
    • 77952368672 scopus 로고    scopus 로고
    • Protein transduction from retroviral Gag precursors
    • Voelkel C, Galla M, Maetzig T, et al. Protein transduction from retroviral Gag precursors. Proc Natl Acad Sci USA 2010; 107: 7805-10.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7805-7810
    • Voelkel, C.1    Galla, M.2    Maetzig, T.3
  • 35
    • 5444268171 scopus 로고    scopus 로고
    • Recombinant HIV-1 Pr55gag virus-like particles: Potent stimulators of innate and acquired immune responses
    • Deml L, Speth C, Dierich MP, Wolf H, Wagner R. Recombinant HIV-1 Pr55gag virus-like particles: potent stimulators of innate and acquired immune responses. Mol Immunol 2005; 42: 259-77.
    • (2005) Mol Immunol , vol.42 , pp. 259-277
    • Deml, L.1    Speth, C.2    Dierich, M.P.3    Wolf, H.4    Wagner, R.5
  • 37
    • 37549006787 scopus 로고    scopus 로고
    • Virus-like particles-universal molecular toolboxes
    • Ludwig C, Wagner R. Virus-like particles-universal molecular toolboxes. Curr Opin Biotechnol 2007; 18: 537-45.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 537-545
    • Ludwig, C.1    Wagner, R.2
  • 38
    • 0025398116 scopus 로고
    • Retrovirus packaging cells
    • Miller AD. Retrovirus packaging cells. Hum Gene Ther 1990; 1: 5-14.
    • (1990) Hum Gene Ther , vol.1 , pp. 5-14
    • Miller, A.D.1
  • 39
    • 33750023988 scopus 로고    scopus 로고
    • Overcoming promoter competition in packaging cells improves production of selfinactivating retroviral vectors
    • Schambach A, Mueller D, Galla M, et al. Overcoming promoter competition in packaging cells improves production of selfinactivating retroviral vectors. Gene Ther 2006; 13: 1524-33.
    • (2006) Gene Ther , vol.13 , pp. 1524-1533
    • Schambach, A.1    Mueller, D.2    Galla, M.3
  • 40
    • 0029993858 scopus 로고    scopus 로고
    • Efficient transfer, integration, and sustained long-term expression of the transgene in adult rat brains injected with a lentiviral vector
    • Naldini L, Blömer U, Gage FH, Trono D, Verma IM. Efficient transfer, integration, and sustained long-term expression of the transgene in adult rat brains injected with a lentiviral vector. Proc Natl Acad Sci USA 1996; 93: 11382-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11382-11388
    • Naldini, L.1    Blömer, U.2    Gage, F.H.3    Trono, D.4    Verma, I.M.5
  • 41
    • 0027236954 scopus 로고
    • Production of hightiter helper-free retroviruses by transient transfection
    • Pear WS, Nolan GP, Scott ML, Baltimore D. Production of hightiter helper-free retroviruses by transient transfection. Proc Natl Acad Sci USA 1993; 90: 8392-6.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 42
    • 77953311295 scopus 로고    scopus 로고
    • Selfinactivating alpharetroviral vectors with a split-packaging design
    • Suerth JD, Maetzig T, Galla M, Baum C, Schambach A. Selfinactivating alpharetroviral vectors with a split-packaging design. J Virol 2010; 84: 6626-35.
    • (2010) J Virol , vol.84 , pp. 6626-6635
    • Suerth, J.D.1    Maetzig, T.2    Galla, M.3    Baum, C.4    Schambach, A.5
  • 43
    • 0036199768 scopus 로고    scopus 로고
    • Improved primate foamy virus vectors and packaging constructs
    • Heinkelein M, Dressler M, Jármy G, et al. Improved primate foamy virus vectors and packaging constructs. J Virol 2002; 76: 3774-83.
    • (2002) J Virol , vol.76 , pp. 3774-3783
    • Heinkelein, M.1    Dressler, M.2    Jármy, G.3
  • 44
    • 0346132122 scopus 로고
    • Self-inactivating retroviral vectors designed for transfer of whole genes into mammalian cells
    • Yu SF, Von Rüden T, Kantoff PW, et al. Self-inactivating retroviral vectors designed for transfer of whole genes into mammalian cells. Proc Natl Acad Sci USA 1986; 83: 3194-8.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3194-3198
    • Yu, S.F.1    von Rüden, T.2    Kantoff, P.W.3
  • 45
    • 0031743608 scopus 로고    scopus 로고
    • Self-inactivating lentivirus vector for safe and efficient in vivo gene delivery
    • Zufferey R, Dull T, Mandel RJ, et al. Self-inactivating lentivirus vector for safe and efficient in vivo gene delivery. J Virol 1998; 72: 9873-80.
    • (1998) J Virol , vol.72 , pp. 9873-9880
    • Zufferey, R.1    Dull, T.2    Mandel, R.J.3
  • 46
    • 41149133413 scopus 로고    scopus 로고
    • Physiological promoters reduce the genotoxic risk of integrating gene vectors
    • Zychlinski D, Schambach A, Modlich U, et al. Physiological promoters reduce the genotoxic risk of integrating gene vectors. Mol Ther 2008; 16: 718-25.
    • (2008) Mol Ther , vol.16 , pp. 718-725
    • Zychlinski, D.1    Schambach, A.2    Modlich, U.3
  • 47
    • 70449127230 scopus 로고    scopus 로고
    • Insertional transformation of hematopoietic cells by self-inactivating lentiviral and gammaretroviral vectors
    • Modlich U, Navarro S, Zychlinski D, et al. Insertional transformation of hematopoietic cells by self-inactivating lentiviral and gammaretroviral vectors. Mol Ther 2009; 17: 1919-28.
    • (2009) Mol Ther , vol.17 , pp. 1919-1928
    • Modlich, U.1    Navarro, S.2    Zychlinski, D.3
  • 48
    • 0034694017 scopus 로고    scopus 로고
    • Rev-independent expression of synthetic gag-pol genes of human immunodeficiency virus type 1 and simian immunodeficiency virus: Implications for the safety of lentiviral vectors
    • Wagner R, Graf M, Bieler K, et al. Rev-independent expression of synthetic gag-pol genes of human immunodeficiency virus type 1 and simian immunodeficiency virus: implications for the safety of lentiviral vectors. Hum Gene Ther 2000; 11: 2403-13.
    • (2000) Hum Gene Ther , vol.11 , pp. 2403-2413
    • Wagner, R.1    Graf, M.2    Bieler, K.3
  • 49
    • 29744458522 scopus 로고    scopus 로고
    • A phase I/II clinical trial of betaglobin gene therapy for beta-thalassemia
    • Bank A, Dorazio R, Leboulch P. A phase I/II clinical trial of betaglobin gene therapy for beta-thalassemia. Ann NY Acad Sci 2005; 1054: 308-16.
    • (2005) Ann NY Acad Sci , vol.1054 , pp. 308-316
    • Bank, A.1    Dorazio, R.2    Leboulch, P.3
  • 50
    • 79954994720 scopus 로고    scopus 로고
    • Genetic therapy for beta-thalassemia: From the bench to the bedside
    • Arumugam P, Malik P. Genetic therapy for beta-thalassemia: from the bench to the bedside. ASH Education Program Book 2010; 2010: 445-50.
    • (2010) ASH Education Program Book , vol.2010 , pp. 445-450
    • Arumugam, P.1    Malik, P.2
  • 51
    • 0031710033 scopus 로고    scopus 로고
    • A third-generation lentivirus vector with a conditional packaging system
    • Dull T, Zufferey R, Kelly M, et al. A third-generation lentivirus vector with a conditional packaging system. J Virol 1998; 72: 8463-71.
    • (1998) J Virol , vol.72 , pp. 8463-8471
    • Dull, T.1    Zufferey, R.2    Kelly, M.3
  • 52
    • 0035120461 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef functions at the level of virus entry by enhancing cytoplasmic delivery of virions
    • Schaeffer E, Geleziunas R, Greene WC. Human immunodeficiency virus type 1 Nef functions at the level of virus entry by enhancing cytoplasmic delivery of virions. J Virol 2001; 75: 2993-3000.
    • (2001) J Virol , vol.75 , pp. 2993-3000
    • Schaeffer, E.1    Geleziunas, R.2    Greene, W.C.3
  • 53
    • 56649109712 scopus 로고    scopus 로고
    • Live cell imaging of the HIV-1 life cycle
    • Campbell EM, Hope TJ. Live cell imaging of the HIV-1 life cycle. Trends Microbiol 2008; 16: 580-7.
    • (2008) Trends Microbiol , vol.16 , pp. 580-587
    • Campbell, E.M.1    Hope, T.J.2
  • 55
    • 0027429412 scopus 로고
    • Incorporation of Vpr into human immunodeficiency virus type 1 virions: Requirement for the p6 region of gag and mutational analysis
    • Paxton W, Connor R, Landau N. Incorporation of Vpr into human immunodeficiency virus type 1 virions: requirement for the p6 region of gag and mutational analysis. J Virol 1993; 67: 7229-37.
    • (1993) J Virol , vol.67 , pp. 7229-7237
    • Paxton, W.1    Connor, R.2    Landau, N.3
  • 56
    • 0029655927 scopus 로고    scopus 로고
    • A conserved LXXLF sequence is the major determinant in p6gag required for the incorporation of human immunodeficiency virus type 1 Vpr
    • Kondo E, Gottlinger HG. A conserved LXXLF sequence is the major determinant in p6gag required for the incorporation of human immunodeficiency virus type 1 Vpr. J Virol 1996; 70: 159-64.
    • (1996) J Virol , vol.70 , pp. 159-164
    • Kondo, E.1    Gottlinger, H.G.2
  • 57
    • 80051792497 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 modified to package simian immunodeficiency virus vpx efficiently infects macrophages and dendritic cells
    • Sunseri N, O'Brien M, Bhardwaj N, Landau NR. Human immunodeficiency virus type 1 modified to package simian immunodeficiency virus vpx efficiently infects macrophages and dendritic cells. J Virol 2011; 85: 6263-74.
    • (2011) J Virol , vol.85 , pp. 6263-6274
    • Sunseri, N.1    O'Brien, M.2    Bhardwaj, N.3    Landau, N.R.4
  • 58
    • 0036844376 scopus 로고    scopus 로고
    • A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes
    • Cavrois M, De Noronha C, Greene WC. A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes. Nat Biotechnol 2002; 20: 1151-4.
    • (2002) Nat Biotechnol , vol.20 , pp. 1151-1154
    • Cavrois, M.1    de Noronha, C.2    Greene, W.C.3
  • 59
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K, Kim Y, Latinovic O, Morozov V, Melikyan GB. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 2009; 137: 433-44.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 60
    • 33847267353 scopus 로고    scopus 로고
    • Double-labelled HIV-1 particles for study of virus-cell interaction
    • Lampe M, Briggs JAG, Endress T, et al. Double-labelled HIV-1 particles for study of virus-cell interaction. Virology 2007; 360: 92-104.
    • (2007) Virology , vol.360 , pp. 92-104
    • Lampe, M.1    Briggs, J.A.G.2    Endress, T.3
  • 61
    • 67649410579 scopus 로고    scopus 로고
    • Inhibition of HIV-1 Infection and Replication by Enhancing Viral Incorporation of Innate Anti-HIV-1 Protein A3G
    • Green LA, Liu Y, He JJ. Inhibition of HIV-1 Infection and Replication by Enhancing Viral Incorporation of Innate Anti-HIV-1 Protein A3G. J Biol Chem 2009; 284: 13363-72.
    • (2009) J Biol Chem , vol.284 , pp. 13363-13372
    • Green, L.A.1    Liu, Y.2    He, J.J.3
  • 62
    • 79951831625 scopus 로고    scopus 로고
    • Labeling of multiple HIV-1 proteins with the biarsenical-tetracysteine system
    • Pereira CF, Ellenberg PC, Jones KL, et al. Labeling of multiple HIV-1 proteins with the biarsenical-tetracysteine system. PloS One 2011; 6: e17016.
    • (2011) PloS One , vol.6
    • Pereira, C.F.1    Ellenberg, P.C.2    Jones, K.L.3
  • 63
    • 79960666968 scopus 로고    scopus 로고
    • A SNAP-Tagged Derivative of HIV-1-A Versatile Tool to Study Virus-Cell Interactions
    • Eckhardt M, Anders M, Muranyi W, et al. A SNAP-Tagged Derivative of HIV-1-A Versatile Tool to Study Virus-Cell Interactions. PloS One 2011; 6: e22007.
    • (2011) PloS One , vol.6
    • Eckhardt, M.1    Anders, M.2    Muranyi, W.3
  • 64
    • 0037064608 scopus 로고    scopus 로고
    • Visualization of the intracellular behavior of HIV in living cells
    • McDonald D, Vodicka MA, Lucero G, et al. Visualization of the intracellular behavior of HIV in living cells. J Cell Biol 2002; 159: 441-52.
    • (2002) J Cell Biol , vol.159 , pp. 441-452
    • McDonald, D.1    Vodicka, M.A.2    Lucero, G.3
  • 65
    • 4544232723 scopus 로고    scopus 로고
    • Construction and characterization of a fluorescently labeled infectious human immunodeficiency virus type 1 derivative
    • Müller B, Daecke J, Fackler OT, et al. Construction and characterization of a fluorescently labeled infectious human immunodeficiency virus type 1 derivative. J Virol 2004; 78: 10803-13.
    • (2004) J Virol , vol.78 , pp. 10803-10813
    • Müller, B.1    Daecke, J.2    Fackler, O.T.3
  • 66
    • 0035078745 scopus 로고    scopus 로고
    • Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1
    • Fassati A, Goff SP. Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1. J Virol 2001; 75: 3626-35.
    • (2001) J Virol , vol.75 , pp. 3626-3635
    • Fassati, A.1    Goff, S.P.2
  • 67
    • 70449481802 scopus 로고    scopus 로고
    • Visualizing fusion of pseudotyped HIV-1 particles in real time by live cell microscopy
    • Koch P, Lampe M, Godinez WJ, et al. Visualizing fusion of pseudotyped HIV-1 particles in real time by live cell microscopy. Retrovirology 2009; 6: 84.
    • (2009) Retrovirology , vol.6 , pp. 84
    • Koch, P.1    Lampe, M.2    Godinez, W.J.3
  • 68
    • 28644442495 scopus 로고    scopus 로고
    • Time-resolved imaging of HIV-1 Env-mediated lipid and content mixing between a single virion and cell membrane
    • Markosyan RM, Cohen FS, Melikyan GB. Time-resolved imaging of HIV-1 Env-mediated lipid and content mixing between a single virion and cell membrane. Mol Biol Cell 2005; 16: 5502-13.
    • (2005) Mol Biol Cell , vol.16 , pp. 5502-5513
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 69
    • 10744224318 scopus 로고    scopus 로고
    • Visualization of retroviral replication in living cells reveals budding into multivesicular bodies
    • Sherer NM, Lehmann MJ, Jimenez-Soto LF, et al. Visualization of retroviral replication in living cells reveals budding into multivesicular bodies. Traffic 2003; 4: 785-801.
    • (2003) Traffic , vol.4 , pp. 785-801
    • Sherer, N.M.1    Lehmann, M.J.2    Jimenez-Soto, L.F.3
  • 70
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • Martin BR, Giepmans BNG, Adams SR, Tsien RY. Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat Biotechnol 2005; 23: 1308-14.
    • (2005) Nat Biotechnol , vol.23 , pp. 1308-1314
    • Martin, B.R.1    Giepmans, B.N.G.2    Adams, S.R.3    Tsien, R.Y.4
  • 71
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin BA, Adams SR, Tsien RY. Specific covalent labeling of recombinant protein molecules inside live cells. Science 1998; 281: 269-72.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 72
    • 0034802605 scopus 로고    scopus 로고
    • The protein-labeling reagent FLASH-EDT 2 binds not only to CCXXCC motifs but also nonspecifically to endogenous cysteine-rich proteins
    • Stroffekova K, Proenza C, Beam KG. The protein-labeling reagent FLASH-EDT 2 binds not only to CCXXCC motifs but also nonspecifically to endogenous cysteine-rich proteins. Pflug Arch Eur J Phy 2001; 442: 859-66.
    • (2001) Pflug Arch Eur J Phy , vol.442 , pp. 859-866
    • Stroffekova, K.1    Proenza, C.2    Beam, K.G.3
  • 73
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams SR, Campbell RE, Gross LA, et al. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J Am Chem Soc 2002; 124: 6063-76.
    • (2002) J Am Chem Soc , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3
  • 74
    • 42949175719 scopus 로고    scopus 로고
    • Real-time visualization of HIV-1 GAG trafficking in infected macrophages
    • Gousset K, Ablan SD, Coren LV, et al. Real-time visualization of HIV-1 GAG trafficking in infected macrophages. PLoS Pathog 2008; 4: e1000015.
    • (2008) PLoS Pathog , vol.4
    • Gousset, K.1    Ablan, S.D.2    Coren, L.V.3
  • 75
  • 76
    • 33749005371 scopus 로고    scopus 로고
    • Quantitative fourdimensional tracking of cytoplasmic and nuclear HIV-1 complexes
    • Arhel N, Genovesio A, Kim KA, et al. Quantitative fourdimensional tracking of cytoplasmic and nuclear HIV-1 complexes. Nat Methods 2006; 3: 817-24.
    • (2006) Nat Methods , vol.3 , pp. 817-824
    • Arhel, N.1    Genovesio, A.2    Kim, K.A.3
  • 79
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler A, Gendreizig S, Gronemeyer T, et al. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat Biotechnol 2002; 21: 86-9.
    • (2002) Nat Biotechnol , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3
  • 80
    • 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, Aiken C. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J Virol 2002; 76: 5667-77.
    • (2002) J Virol , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 81
    • 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. Direct Visualization of HIV-1 with Correlative Live-Cell Microscopy and Cryo-Electron Tomography. Structure 2011; 19: 1573-81.
    • (2011) Structure , vol.19 , pp. 1573-1581
    • Jun, S.1    Ke, D.2    Debiec, K.3
  • 82
    • 79959988674 scopus 로고    scopus 로고
    • Complementary assays reveal a relationship between HIV-1 uncoating and reverse transcription
    • Hulme AE, Perez O, Hope TJ. Complementary assays reveal a relationship between HIV-1 uncoating and reverse transcription. Proc Natl Acad Sci USA 2011; 108: 9975-80.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 9975-9980
    • Hulme, A.E.1    Perez, O.2    Hope, T.J.3
  • 83
    • 34250824708 scopus 로고    scopus 로고
    • HIV-1 DNA Flap formation promotes uncoating of the pre-integration complex at the nuclear pore
    • Arhel NJ, Souquere-Besse S, Munier S, et al. HIV-1 DNA Flap formation promotes uncoating of the pre-integration complex at the nuclear pore. Embo J 2007; 26: 3025-37.
    • (2007) Embo J , vol.26 , pp. 3025-3037
    • Arhel, N.J.1    Souquere-Besse, S.2    Munier, S.3
  • 84
    • 79959629606 scopus 로고    scopus 로고
    • Avoiding cytotoxicity of transposases by dose-controlled mRNA delivery
    • Galla M, Schambach A, Falk CS, et al. Avoiding cytotoxicity of transposases by dose-controlled mRNA delivery. Nucleic Acids Res 2011; 39: 7147-60.
    • (2011) Nucleic Acids Res , vol.39 , pp. 7147-7160
    • Galla, M.1    Schambach, A.2    Falk, C.S.3
  • 86
    • 78650552567 scopus 로고    scopus 로고
    • Replication of biotinylated human immunodeficiency viruses
    • Belshan M, Matthews JM, Madson CJ. Replication of biotinylated human immunodeficiency viruses. J Virol Methods 2010; 171: 299-302.
    • (2010) J Virol Methods , vol.171 , pp. 299-302
    • Belshan, M.1    Matthews, J.M.2    Madson, C.J.3
  • 87
    • 0033856584 scopus 로고    scopus 로고
    • Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging
    • Hermida-Matsumoto L, Resh MD. Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J Virol 2000; 74: 8670-9.
    • (2000) J Virol , vol.74 , pp. 8670-8679
    • Hermida-Matsumoto, L.1    Resh, M.D.2
  • 88
    • 0031949314 scopus 로고    scopus 로고
    • The I domain is required for efficient plasma membrane binding of human immunodeficiency virus type 1 Pr55Gag
    • Sandefur S, Varthakavi V, Spearman P. The I domain is required for efficient plasma membrane binding of human immunodeficiency virus type 1 Pr55Gag. J Virol 1998; 72: 2723-32.
    • (1998) J Virol , vol.72 , pp. 2723-2732
    • Sandefur, S.1    Varthakavi, V.2    Spearman, P.3
  • 89
    • 0037309056 scopus 로고    scopus 로고
    • The proline-rich region of the ecotropic Moloney murine leukaemia virus envelope protein tolerates the insertion of the green fluorescent protein and allows the generation of replication-competent virus
    • Erlwein O, Buchholz CJ, Schnierle BS. The proline-rich region of the ecotropic Moloney murine leukaemia virus envelope protein tolerates the insertion of the green fluorescent protein and allows the generation of replication-competent virus. J Gen Virol 2003; 84: 369-73.
    • (2003) J Gen Virol , vol.84 , pp. 369-373
    • Erlwein, O.1    Buchholz, C.J.2    Schnierle, B.S.3
  • 90
    • 0033590168 scopus 로고    scopus 로고
    • Rapid and efficient cell-to-cell transmission of human immunodeficiency virus infection from monocyte-derived macrophages to peripheral blood lymphocytes
    • Carr J, Hocking H, Li P, Burrell CJ. Rapid and efficient cell-to-cell transmission of human immunodeficiency virus infection from monocyte-derived macrophages to peripheral blood lymphocytes. Virology 1999; 265: 319-29.
    • (1999) Virology , vol.265 , pp. 319-329
    • Carr, J.1    Hocking, H.2    Li, P.3    Burrell, C.J.4
  • 91
    • 33846036832 scopus 로고    scopus 로고
    • Inefficient human immunodeficiency virus replication in mobile lymphocytes
    • Sourisseau M, Sol-Foulon N, Porrot F, Blanchet F, Schwartz O. Inefficient human immunodeficiency virus replication in mobile lymphocytes. J Virol 2007; 81: 1000-12.
    • (2007) J Virol , vol.81 , pp. 1000-1012
    • Sourisseau, M.1    Sol-Foulon, N.2    Porrot, F.3    Blanchet, F.4    Schwartz, O.5
  • 92
    • 79960422189 scopus 로고    scopus 로고
    • Viral determinants of polarized assembly for the murine leukemia virus
    • Jin J, Li F, Mothes W. Viral determinants of polarized assembly for the murine leukemia virus. J Virol 2011; 85: 7672-82.
    • (2011) J Virol , vol.85 , pp. 7672-7682
    • Jin, J.1    Li, F.2    Mothes, W.3
  • 93
    • 68049136145 scopus 로고    scopus 로고
    • Assembly of the murine leukemia virus is directed towards sites of cell-cell contact
    • Jin J, Sherer NM, Heidecker G, Derse D, Mothes W. Assembly of the murine leukemia virus is directed towards sites of cell-cell contact. PLoS Biol 2009; 7: e1000163.
    • (2009) PLoS Biol , vol.7
    • Jin, J.1    Sherer, N.M.2    Heidecker, G.3    Derse, D.4    Mothes, W.5
  • 94
    • 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. Retroviruses can establish filopodial bridges for efficient cell-to-cell transmission. Nat Cell Biol 2007; 9: 310-5.
    • (2007) Nat Cell Biol , vol.9 , pp. 310-315
    • Sherer, N.M.1    Lehmann, M.J.2    Jimenez-Soto, L.F.3
  • 95
    • 0032875453 scopus 로고    scopus 로고
    • Analysis of receptor usage by ecotropic murine retroviruses, using green fluorescent protein-tagged cationic amino acid transporters
    • Masuda M, Kakushima N, Wilt SG, et al. Analysis of receptor usage by ecotropic murine retroviruses, using green fluorescent protein-tagged cationic amino acid transporters. J Virol 1999; 73: 8623-9.
    • (1999) J Virol , vol.73 , pp. 8623-8629
    • Masuda, M.1    Kakushima, N.2    Wilt, S.G.3
  • 96
    • 22944446447 scopus 로고    scopus 로고
    • Actin-and myosin-driven movement of viruses along filopodia precedes their entry into cells
    • Lehmann MJ, Sherer NM, Marks CB, Pypaert M, Mothes W. Actin-and myosin-driven movement of viruses along filopodia precedes their entry into cells. J Cell Biol 2005; 170: 317-25.
    • (2005) J Cell Biol , vol.170 , pp. 317-325
    • Lehmann, M.J.1    Sherer, N.M.2    Marks, C.B.3    Pypaert, M.4    Mothes, W.5
  • 97
    • 84858052754 scopus 로고    scopus 로고
    • Pseudotype-independent non-specific uptake of gammaretroviral and lentiviral particles in human cells
    • Voelkel C, Galla M, Dannhauser P, et al. Pseudotype-independent non-specific uptake of gammaretroviral and lentiviral particles in human cells. Hum Gene Ther 2011; 23: 274-86.
    • (2011) Hum Gene Ther , vol.23 , pp. 274-286
    • Voelkel, C.1    Galla, M.2    Dannhauser, P.3
  • 98
    • 0033755986 scopus 로고    scopus 로고
    • Separable mechanisms of attachment and cell uptake during retrovirus infection
    • Sharma S, Miyanohara A, Friedmann T. Separable mechanisms of attachment and cell uptake during retrovirus infection. J Virol 2000; 74: 10790-5.
    • (2000) J Virol , vol.74 , pp. 10790-10795
    • Sharma, S.1    Miyanohara, A.2    Friedmann, T.3
  • 99
    • 0030922804 scopus 로고    scopus 로고
    • Noninfectious virus-like particles produced by Moloney murine leukemia virusbased retrovirus packaging cells deficient in viral envelope become infectious in the presence of lipofection reagents
    • Sharma S, Murai F, Miyanohara A, Friedmann T. Noninfectious virus-like particles produced by Moloney murine leukemia virusbased retrovirus packaging cells deficient in viral envelope become infectious in the presence of lipofection reagents. Proc Natl Acad Sci USA 1997; 94: 10803-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10803-10808
    • Sharma, S.1    Murai, F.2    Miyanohara, A.3    Friedmann, T.4
  • 100
    • 0034796426 scopus 로고    scopus 로고
    • Evidence for nonspecific adsorption of targeted retrovirus vector particles to cells
    • Pizzato M, Blair E, Fling M, et al. Evidence for nonspecific adsorption of targeted retrovirus vector particles to cells. Gene Ther 2001; 8: 1088-96.
    • (2001) Gene Ther , vol.8 , pp. 1088-1096
    • Pizzato, M.1    Blair, E.2    Fling, M.3
  • 101
    • 0036112584 scopus 로고    scopus 로고
    • Cell surface heparan sulfate is a receptor for attachment of envelope proteinfree retrovirus-like particles and VSV-G pseudotyped MLVderived retrovirus vectors to target cells
    • Guibinga GH, Miyanohara A, Esko JD, Friedmann T. Cell surface heparan sulfate is a receptor for attachment of envelope proteinfree retrovirus-like particles and VSV-G pseudotyped MLVderived retrovirus vectors to target cells. Mol Ther 2002; 5: 538-46.
    • (2002) Mol Ther , vol.5 , pp. 538-546
    • Guibinga, G.H.1    Miyanohara, A.2    Esko, J.D.3    Friedmann, T.4
  • 102
    • 0032823293 scopus 로고    scopus 로고
    • Initial binding of murine leukemia virus particles to cells does not require specific Env-receptor interaction
    • Pizzato M, Marlow SA, Blair ED, Takeuchi Y. Initial binding of murine leukemia virus particles to cells does not require specific Env-receptor interaction. J Virol 1999; 73: 8599-611.
    • (1999) J Virol , vol.73 , pp. 8599-8611
    • Pizzato, M.1    Marlow, S.A.2    Blair, E.D.3    Takeuchi, Y.4
  • 103
    • 23244461734 scopus 로고    scopus 로고
    • Caveola-dependent endocytic entry of amphotropic murine leukemia virus
    • Beer C, Andersen DS, Rojek A, Pedersen L. Caveola-dependent endocytic entry of amphotropic murine leukemia virus. J Virol 2005; 79: 10776-87.
    • (2005) J Virol , vol.79 , pp. 10776-10787
    • Beer, C.1    Andersen, D.S.2    Rojek, A.3    Pedersen, L.4
  • 104
    • 0035039738 scopus 로고    scopus 로고
    • Infectious entry by amphotropic as well as ecotropic murine leukemia viruses occurs through an endocytic pathway
    • Katen LJ, Januszeski MM, Anderson WF, Hasenkrug KJ, Evans LH. Infectious entry by amphotropic as well as ecotropic murine leukemia viruses occurs through an endocytic pathway. J Virol 2001; 75: 5018-26.
    • (2001) J Virol , vol.75 , pp. 5018-5026
    • Katen, L.J.1    Januszeski, M.M.2    Anderson, W.F.3    Hasenkrug, K.J.4    Evans, L.H.5
  • 105
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat transactivator protein
    • Green M, Loewenstein PM. Autonomous functional domains of chemically synthesized human immunodeficiency virus tat transactivator protein. Cell 1988; 55: 1179-88.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 106
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel AD, Pabo CO. Cellular uptake of the tat protein from human immunodeficiency virus. Cell 1988; 55: 1189-93.
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 109
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi D, Joliot AH, Chassaing G, Prochiantz A. The third helix of the Antennapedia homeodomain translocates through biological membranes. J Biol Chem 1994; 269: 10444-50.
    • (1994) J Biol Chem , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 110
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • Vivès E, Brodin P, Lebleu B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem 1997; 272: 16010-7.
    • (1997) J Biol Chem , vol.272 , pp. 16010-16017
    • Vivès, E.1    Brodin, P.2    Lebleu, B.3
  • 111
    • 77951144106 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Nanocarrier for macromolecule delivery in living cells
    • Chugh A, Eudes F, Shim YS. Cell-penetrating peptides: Nanocarrier for macromolecule delivery in living cells. IUBMB Life 2010; 62: 183-93.
    • (2010) IUBMB Life , vol.62 , pp. 183-193
    • Chugh, A.1    Eudes, F.2    Shim, Y.S.3
  • 112
    • 10344221003 scopus 로고    scopus 로고
    • Cellular uptake of argininerich peptides: Roles for macropinocytosis and actin rearrangement
    • Nakase I, Niwa M, Takeuchi T, et al. Cellular uptake of argininerich peptides: roles for macropinocytosis and actin rearrangement. Mol Ther 2004; 10: 1011-22.
    • (2004) Mol Ther , vol.10 , pp. 1011-1022
    • Nakase, I.1    Niwa, M.2    Takeuchi, T.3
  • 113
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia JS, Stan RV, Dowdy SF. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 2004; 10: 310-5.
    • (2004) Nat Med , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 114
    • 82755194760 scopus 로고    scopus 로고
    • Protein transduction domain delivery of therapeutic macromolecules
    • van den Berg A, Dowdy SF. Protein transduction domain delivery of therapeutic macromolecules. Curr Opin Biotech 2011.
    • (2011) Curr Opin Biotech
    • van den Berg, A.1    Dowdy, S.F.2
  • 115
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of macromolecules using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment
    • El-Sayed A, Futaki S, Harashima H. Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment. Aaps J 2009; 11: 13-22.
    • (2009) Aaps J , vol.11 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 116
    • 67149093390 scopus 로고    scopus 로고
    • Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein
    • Eguchi A, Meade BR, Chang YC, et al. Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein. Nat Biotechnol 2009; 27: 567-71.
    • (2009) Nat Biotechnol , vol.27 , pp. 567-571
    • Eguchi, A.1    Meade, B.R.2    Chang, Y.C.3
  • 118
    • 80051564046 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) immunopathogenesis and vaccine development: A review
    • Girard MP, Osmanov S, Assossou OM, Kieny MP. Human immunodeficiency virus (HIV) immunopathogenesis and vaccine development: A review. Vaccine 2011; 29: 6191-218.
    • (2011) Vaccine , vol.29 , pp. 6191-6218
    • Girard, M.P.1    Osmanov, S.2    Assossou, O.M.3    Kieny, M.P.4
  • 119
    • 0035913225 scopus 로고    scopus 로고
    • Evolution and transmission of stable CTL escape mutations in HIV infection
    • Goulder PJR, Brander C, Tang Y, et al. Evolution and transmission of stable CTL escape mutations in HIV infection. Nature 2001; 412: 334-8.
    • (2001) Nature , vol.412 , pp. 334-338
    • Goulder, P.J.R.1    Brander, C.2    Tang, Y.3
  • 120
    • 1842741699 scopus 로고    scopus 로고
    • HIV evolution: CTL escape mutation and reversion after transmission
    • Leslie A, Pfafferott K, Chetty P, et al. HIV evolution: CTL escape mutation and reversion after transmission. Nat Med 2004; 10: 282-9.
    • (2004) Nat Med , vol.10 , pp. 282-289
    • Leslie, A.1    Pfafferott, K.2    Chetty, P.3
  • 121
    • 29444442970 scopus 로고    scopus 로고
    • Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection
    • Frost SDW, Wrin T, Smith DM, et al. Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection. Proc Natl Acad Sci USA 2005; 102: 18514-9.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18514-18519
    • Frost, S.D.W.1    Wrin, T.2    Smith, D.M.3
  • 123
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman DD, Wrin T, Little SJ, Petropoulos CJ. Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc Natl Acad Sci USA 2003; 100: 4144-9.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4144-4149
    • Richman, D.D.1    Wrin, T.2    Little, S.J.3    Petropoulos, C.J.4
  • 124
    • 0027043276 scopus 로고
    • Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene
    • Daniel MD, Kirchhoff F, Czajak SC, Sehgal PK, Desrosiers RC. Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene. Science 1992; 258: 1938-41.
    • (1992) Science , vol.258 , pp. 1938-1941
    • Daniel, M.D.1    Kirchhoff, F.2    Czajak, S.C.3    Sehgal, P.K.4    Desrosiers, R.C.5
  • 125
  • 126
    • 0031929672 scopus 로고    scopus 로고
    • Identification of highly attenuated mutants of simian immunodeficiency virus
    • Desrosiers RC, Lifson JD, Gibbs JS, et al. Identification of highly attenuated mutants of simian immunodeficiency virus. J Virol 1998; 72: 1431-7.
    • (1998) J Virol , vol.72 , pp. 1431-1437
    • Desrosiers, R.C.1    Lifson, J.D.2    Gibbs, J.S.3
  • 127
    • 0032932711 scopus 로고    scopus 로고
    • Genetic instability of live, attenuated human immunodeficiency virus type 1 vaccine strains
    • Berkhout B, Verhoef K, van Wamel JLB, Back NKT. Genetic instability of live, attenuated human immunodeficiency virus type 1 vaccine strains. J Virol 1999; 73: 1138-45.
    • (1999) J Virol , vol.73 , pp. 1138-1145
    • Berkhout, B.1    Verhoef, K.2    van Wamel, J.L.B.3    Back, N.K.T.4
  • 128
    • 0342505323 scopus 로고    scopus 로고
    • Pathogenic conversion of live attenuated simian immunodeficiency virus vaccines is associated with expression of truncated Nef
    • Sawai ET, Hamza MS, Ye M, Shaw KES, Luciw PA. Pathogenic conversion of live attenuated simian immunodeficiency virus vaccines is associated with expression of truncated Nef. J Virol 2000; 74: 2038-45.
    • (2000) J Virol , vol.74 , pp. 2038-2045
    • Sawai, E.T.1    Hamza, M.S.2    Ye, M.3    Shaw, K.E.S.4    Luciw, P.A.5
  • 129
    • 0034124730 scopus 로고    scopus 로고
    • Evidence for recombination of live, attenuated immunodeficiency virus vaccine with challenge virus to a more virulent strain
    • Gundlach BR, Lewis MG, Sopper S, et al. Evidence for recombination of live, attenuated immunodeficiency virus vaccine with challenge virus to a more virulent strain. J Virol 2000; 74: 3537-42.
    • (2000) J Virol , vol.74 , pp. 3537-3542
    • Gundlach, B.R.1    Lewis, M.G.2    Sopper, S.3
  • 130
    • 0035932984 scopus 로고    scopus 로고
    • In vitro evolution of a highly replicating, doxycycline-dependent HIV for applications in vaccine studies
    • Marzio G, Verhoef K, Vink M, Berkhout B. In vitro evolution of a highly replicating, doxycycline-dependent HIV for applications in vaccine studies. Proc Natl Acad Sci USA 2001; 98: 6342-7.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6342-6347
    • Marzio, G.1    Verhoef, K.2    Vink, M.3    Berkhout, B.4
  • 131
    • 33751247662 scopus 로고    scopus 로고
    • Modification of the Tet-On regulatory system prevents the conditional-live HIV-1 variant from losing doxycycline-control
    • Zhou X, Vink M, Berkhout B, Das A. Modification of the Tet-On regulatory system prevents the conditional-live HIV-1 variant from losing doxycycline-control. Retrovirology 2006; 3: 82.
    • (2006) Retrovirology , vol.3 , pp. 82
    • Zhou, X.1    Vink, M.2    Berkhout, B.3    Das, A.4
  • 132
    • 14744272158 scopus 로고    scopus 로고
    • Improving the safety of a conditional-live human immunodeficiency virus type 1 vaccine by controlling both gene expression and cell entry
    • Das AT, Baldwin CE, Vink M, Berkhout B. Improving the safety of a conditional-live human immunodeficiency virus type 1 vaccine by controlling both gene expression and cell entry. J Virol 2005; 79: 3855-8.
    • (2005) J Virol , vol.79 , pp. 3855-3858
    • Das, A.T.1    Baldwin, C.E.2    Vink, M.3    Berkhout, B.4
  • 133
    • 37549026844 scopus 로고    scopus 로고
    • Replicating and non-replicating viral vectors for vaccine development
    • Robert-Guroff M. Replicating and non-replicating viral vectors for vaccine development. Curr Opin Biotechnol 2007; 18: 546-56.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 546-556
    • Robert-Guroff, M.1
  • 134
    • 77951882041 scopus 로고    scopus 로고
    • Toward an antibody-based HIV-1 vaccine
    • Hoxie JA. Toward an antibody-based HIV-1 vaccine. Annu Rev Med 2010; 61: 135-52.
    • (2010) Annu Rev Med , vol.61 , pp. 135-152
    • Hoxie, J.A.1
  • 135
    • 77952311370 scopus 로고    scopus 로고
    • The role of antibodies in HIV vaccines
    • Mascola JR, Montefiori DC. The role of antibodies in HIV vaccines. Ann Rev Immunol 2009; 28: 413-44.
    • (2009) Ann Rev Immunol , vol.28 , pp. 413-444
    • Mascola, J.R.1    Montefiori, D.C.2
  • 137
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P, Liu J, Bess J, et al. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 2006; 441: 847-52.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1    Liu, J.2    Bess, J.3
  • 138
    • 33144486096 scopus 로고    scopus 로고
    • Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
    • Moore PL, Crooks ET, Porter L, et al. Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J Virol 2006; 80: 2515-28.
    • (2006) J Virol , vol.80 , pp. 2515-2528
    • Moore, P.L.1    Crooks, E.T.2    Porter, L.3
  • 139
    • 34548577658 scopus 로고    scopus 로고
    • A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and soluble monomeric gp120
    • Crooks ET, Moore PL, Franti M, et al. A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and soluble monomeric gp120. Virology 2007; 366: 245-62.
    • (2007) Virology , vol.366 , pp. 245-262
    • Crooks, E.T.1    Moore, P.L.2    Franti, M.3
  • 140
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • Crooks ET, Tong T, Osawa K, Binley JM. Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. J Virol 2011; 85: 5825-39.
    • (2011) J Virol , vol.85 , pp. 5825-5839
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3    Binley, J.M.4
  • 141
    • 79952579918 scopus 로고    scopus 로고
    • Mechanisms for Env glycoprotein acquisition by retroviruses
    • Johnson MC. Mechanisms for Env glycoprotein acquisition by retroviruses. AIDS Res Hum Retrov 2011; 27: 239-47.
    • (2011) AIDS Res Hum Retrov , vol.27 , pp. 239-247
    • Johnson, M.C.1
  • 142
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells
    • Gheysen D, Jacobs E, de Foresta F, et al. Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells. Cell 1989; 59: 103-12.
    • (1989) Cell , vol.59 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    de Foresta, F.3
  • 143
    • 0024555367 scopus 로고
    • The protease and gag gene products of the human immunodeficiency virus: Authentic cleavage and post-translational modification in an insect cell expression system
    • Overton HA, Fujii Y, Price IR, Jones IM. The protease and gag gene products of the human immunodeficiency virus: Authentic cleavage and post-translational modification in an insect cell expression system. Virology 1989; 170: 107-16.
    • (1989) Virology , vol.170 , pp. 107-116
    • Overton, H.A.1    Fujii, Y.2    Price, I.R.3    Jones, I.M.4
  • 144
    • 0026572387 scopus 로고
    • Expression and extracellular release of human immunodeficiency virus type 1 Gag precursors by recombinant baculovirus-infected cells
    • Royer M, Hong S, Gay B, Cerutti M, Boulanger P. Expression and extracellular release of human immunodeficiency virus type 1 Gag precursors by recombinant baculovirus-infected cells. J Virol 1992; 66: 3230-5.
    • (1992) J Virol , vol.66 , pp. 3230-3235
    • Royer, M.1    Hong, S.2    Gay, B.3    Cerutti, M.4    Boulanger, P.5
  • 145
    • 0025200595 scopus 로고
    • Expression of gag precursor protein and secretion of virus-like gag particles of HIV-2 from recombinant baculovirus-infected insect cells
    • Luo L, Li Y, Kang CY. Expression of gag precursor protein and secretion of virus-like gag particles of HIV-2 from recombinant baculovirus-infected insect cells. Virology 1990; 179: 874-80.
    • (1990) Virology , vol.179 , pp. 874-880
    • Luo, L.1    Li, Y.2    Kang, C.Y.3
  • 146
    • 0027205329 scopus 로고
    • Analysis of protein expression and virus-like particle formation in mammalian cell lines stably expressing HIV-1 gag and env gene products with or without active HIV proteinase
    • Kräusslich HG, Ochsenbauer C, Traenckner AM, et al. Analysis of protein expression and virus-like particle formation in mammalian cell lines stably expressing HIV-1 gag and env gene products with or without active HIV proteinase. Virology 1993; 192: 605-17.
    • (1993) Virology , vol.192 , pp. 605-617
    • Kräusslich, H.G.1    Ochsenbauer, C.2    Traenckner, A.M.3
  • 147
    • 33846420615 scopus 로고    scopus 로고
    • Membrane embedded HIV-1 envelope on the surface of a virus-like particle elicits broader immune responses than soluble envelopes
    • McBurney SP, Young KR, Ross TM. Membrane embedded HIV-1 envelope on the surface of a virus-like particle elicits broader immune responses than soluble envelopes. Virology 2007; 358: 334-46.
    • (2007) Virology , vol.358 , pp. 334-346
    • McBurney, S.P.1    Young, K.R.2    Ross, T.M.3
  • 148
    • 0027764291 scopus 로고
    • The influence of antigen organization on B cell responsiveness
    • Bachmann MF, Rohrer UH, Kundig TM, et al. The influence of antigen organization on B cell responsiveness. Science 1993; 262: 1448-51.
    • (1993) Science , vol.262 , pp. 1448-1451
    • Bachmann, M.F.1    Rohrer, U.H.2    Kundig, T.M.3
  • 149
    • 0036230153 scopus 로고    scopus 로고
    • Induction of neutralizing antibodies and cytotoxic T lymphocytes in Balb/c mice immunized with virus-like particles presenting a gp120 molecule from a HIV-1 isolate of clade A
    • Buonaguro L, Racioppi L, Tornesello M, et al. Induction of neutralizing antibodies and cytotoxic T lymphocytes in Balb/c mice immunized with virus-like particles presenting a gp120 molecule from a HIV-1 isolate of clade A. Antivir Res 2002; 54: 189-201.
    • (2002) Antivir Res , vol.54 , pp. 189-201
    • Buonaguro, L.1    Racioppi, L.2    Tornesello, M.3
  • 150
    • 0034628629 scopus 로고    scopus 로고
    • Priming of strong, broad, and long-lived HIV type 1 p55gag-specific CD8+ cytotoxic T cells after administration of a virus-like particle vaccine in rhesus macaques
    • Paliard X, Liu Y, Wagner R, et al. Priming of strong, broad, and long-lived HIV type 1 p55gag-specific CD8+ cytotoxic T cells after administration of a virus-like particle vaccine in rhesus macaques. AIDS Res Hum Retrov 2000; 16: 273-82.
    • (2000) AIDS Res Hum Retrov , vol.16 , pp. 273-282
    • Paliard, X.1    Liu, Y.2    Wagner, R.3
  • 151
    • 33745863446 scopus 로고    scopus 로고
    • Immunogenicity and efficacy of immunodeficiency virus-like particles pseudotyped with the G protein of vesicular stomatitis virus
    • Kuate S, Stahl-Hennig C, Stoiber H, et al. Immunogenicity and efficacy of immunodeficiency virus-like particles pseudotyped with the G protein of vesicular stomatitis virus. Virology 2006; 351: 133-44.
    • (2006) Virology , vol.351 , pp. 133-144
    • Kuate, S.1    Stahl-Hennig, C.2    Stoiber, H.3
  • 152
    • 0035106473 scopus 로고    scopus 로고
    • MHC-I-restricted presentation of HIV-1 virion antigens without viral replication
    • Buseyne F, Le Gall S, Boccaccio C, et al. MHC-I-restricted presentation of HIV-1 virion antigens without viral replication. Nat Med 2001; 7: 344-9.
    • (2001) Nat Med , vol.7 , pp. 344-349
    • Buseyne, F.1    Le Gall, S.2    Boccaccio, C.3
  • 153
    • 0036310322 scopus 로고    scopus 로고
    • Enhanced presentation of major histocompatibility complex class I-restricted human immunodeficiency virus type 1 (HIV-1) Gag-specific epitopes after DNA immunization with vectors coding for vesicular stomatitis virus glycoprotein-pseudotyped HIV-1 Gag particles
    • Marsac D, Loirat D, Petit C, Schwartz O, Michel ML. Enhanced presentation of major histocompatibility complex class I-restricted human immunodeficiency virus type 1 (HIV-1) Gag-specific epitopes after DNA immunization with vectors coding for vesicular stomatitis virus glycoprotein-pseudotyped HIV-1 Gag particles. J Virol 2002; 76: 7544-53.
    • (2002) J Virol , vol.76 , pp. 7544-7553
    • Marsac, D.1    Loirat, D.2    Petit, C.3    Schwartz, O.4    Michel, M.L.5
  • 155
    • 0032711215 scopus 로고    scopus 로고
    • In vivo priming by DNA injection occurs predominantly by antigen transfer
    • Corr M, von Damm A, Lee DJ, Tighe H. In vivo priming by DNA injection occurs predominantly by antigen transfer. J Immunol 1999; 163: 4721-7.
    • (1999) J Immunol , vol.163 , pp. 4721-4727
    • Corr, M.1    von Damm, A.2    Lee, D.J.3    Tighe, H.4
  • 156
    • 33748794562 scopus 로고    scopus 로고
    • Virus-like particles: Passport to immune recognition
    • Grgacic EVL, Anderson DA. Virus-like particles: passport to immune recognition. Methods 2006; 40: 60-5.
    • (2006) Methods , vol.40 , pp. 60-65
    • Grgacic, E.V.L.1    Anderson, D.A.2
  • 157
    • 79551699386 scopus 로고    scopus 로고
    • Viral nanoparticles and virus-like particles: Platforms for contemporary vaccine design
    • Plummer EM, Manchester M. Viral nanoparticles and virus-like particles: platforms for contemporary vaccine design. Rev Nanomed Nanobiotechnol 2011; 3: 174-96.
    • (2011) Rev Nanomed Nanobiotechnol , vol.3 , pp. 174-196
    • Plummer, E.M.1    Manchester, M.2
  • 158
    • 79953848334 scopus 로고    scopus 로고
    • HIV-1 Accessory Protein Vpr: Relevance in the pathogenesis of HIV and potential for therapeutic intervention
    • Kogan M, Rappaport J. HIV-1 Accessory Protein Vpr: Relevance in the pathogenesis of HIV and potential for therapeutic intervention. Retrovirology 2011; 8: 25.
    • (2011) Retrovirology , vol.8 , pp. 25
    • Kogan, M.1    Rappaport, J.2
  • 159
    • 79959858243 scopus 로고    scopus 로고
    • Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein
    • Hrecka K, Hao C, Gierszewska M, et al. Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein. Nature 2011; 474: 658-61.
    • (2011) Nature , vol.474 , pp. 658-661
    • Hrecka, K.1    Hao, C.2    Gierszewska, M.3
  • 160
    • 79959843617 scopus 로고    scopus 로고
    • SAMHD1 is the dendritic-and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx
    • Laguette N, Sobhian B, Casartelli N, et al. SAMHD1 is the dendritic-and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx. Nature 2011; 474: 654-7.
    • (2011) Nature , vol.474 , pp. 654-657
    • Laguette, N.1    Sobhian, B.2    Casartelli, N.3
  • 161
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Göttlinger HG, Dorfman T, Sodroski JG, Haseltine WA. Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc Natl Acad Sci USA 1991; 88: 3195-9.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3195-3199
    • Göttlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 162
    • 0025295307 scopus 로고
    • Human immunodeficiency virus vpr product is a virion-associated regulatory protein
    • Cohen EA, Dehni G, Sodroski JG, Haseltine WA. Human immunodeficiency virus vpr product is a virion-associated regulatory protein. J Virol 1990; 64: 3097-9.
    • (1990) J Virol , vol.64 , pp. 3097-3099
    • Cohen, E.A.1    Dehni, G.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 163
    • 0034629234 scopus 로고    scopus 로고
    • Extent of incorporation of HIV-1 Vpr into the virus particles is flexible and can be modulated by expression level in cells
    • Lai D, Singh SP, Cartas M, et al. Extent of incorporation of HIV-1 Vpr into the virus particles is flexible and can be modulated by expression level in cells. FEBS Lett 2000; 469: 191-5.
    • (2000) FEBS Lett , vol.469 , pp. 191-195
    • Lai, D.1    Singh, S.P.2    Cartas, M.3
  • 164
    • 0033809608 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr protein is incorporated into the virion in significantly smaller amounts than gag and is phosphorylated in infected cells
    • Muller B, Tessmer U, Schubert U, Krausslich HG. Human immunodeficiency virus type 1 Vpr protein is incorporated into the virion in significantly smaller amounts than gag and is phosphorylated in infected cells. J Virol 2000; 74: 9727.
    • (2000) J Virol , vol.74 , pp. 9727
    • Muller, B.1    Tessmer, U.2    Schubert, U.3    Krausslich, H.G.4
  • 165
    • 0035946308 scopus 로고    scopus 로고
    • Virion-associated HIV-1 Vpr: Variable amount in virus particles derived from cells upon virus infection or proviral DNA transfection
    • Singh S, Tungaturthi P, Cartas M, et al. Virion-associated HIV-1 Vpr: variable amount in virus particles derived from cells upon virus infection or proviral DNA transfection. Virology 2001; 283: 78-83.
    • (2001) Virology , vol.283 , pp. 78-83
    • Singh, S.1    Tungaturthi, P.2    Cartas, M.3
  • 166
    • 0029821868 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 Vif particle incorporation
    • Camaur D, Trono D. Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J Virol 1996; 70: 6106-11.
    • (1996) J Virol , vol.70 , pp. 6106-6111
    • Camaur, D.1    Trono, D.2
  • 167
    • 0029961360 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins
    • Fouchier R, Simon J, Jaffe AB, Malim MH. Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins. J Virol 1996; 70: 8263-9.
    • (1996) J Virol , vol.70 , pp. 8263-8269
    • Fouchier, R.1    Simon, J.2    Jaffe, A.B.3    Malim, M.H.4
  • 168
    • 0029975546 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Nef protein is incorporated into virus particles and specifically cleaved by the viral proteinase
    • Welker R, Kottler H, Kalbitzer H, Kräusslich H. Human immunodeficiency virus type 1 Nef protein is incorporated into virus particles and specifically cleaved by the viral proteinase. Virology 1996; 219: 228-36.
    • (1996) Virology , vol.219 , pp. 228-236
    • Welker, R.1    Kottler, H.2    Kalbitzer, H.3    Kräusslich, H.4
  • 169
    • 0028987472 scopus 로고
    • The p6gag domain of human immunodeficiency virus type 1 is sufficient for the incorporation of Vpr into heterologous viral particles
    • Kondo E, Mammano F, Cohen EA, Göttlinger H. The p6gag domain of human immunodeficiency virus type 1 is sufficient for the incorporation of Vpr into heterologous viral particles. J Virol 1995; 69: 2759-64.
    • (1995) J Virol , vol.69 , pp. 2759-2764
    • Kondo, E.1    Mammano, F.2    Cohen, E.A.3    Göttlinger, H.4
  • 170
    • 0029039296 scopus 로고
    • Targeting foreign proteins to human immunodeficiency virus particles via fusion with Vpr and Vpx
    • Wu X, Liu H, Xiao H, et al. Targeting foreign proteins to human immunodeficiency virus particles via fusion with Vpr and Vpx. J Virol 1995; 69: 3389-98.
    • (1995) J Virol , vol.69 , pp. 3389-3398
    • Wu, X.1    Liu, H.2    Xiao, H.3
  • 171
    • 0029895892 scopus 로고    scopus 로고
    • Proteolytic activity of human immunodeficiency virus Vpr-and Vpx-protease fusion proteins
    • Wu X, Liu H, Xiao H, Kappes J. Proteolytic activity of human immunodeficiency virus Vpr-and Vpx-protease fusion proteins. Virology 1996; 219: 307-13.
    • (1996) Virology , vol.219 , pp. 307-313
    • Wu, X.1    Liu, H.2    Xiao, H.3    Kappes, J.4
  • 172
    • 0031799928 scopus 로고    scopus 로고
    • Virion-targeted viral inactivation of human immunodeficiency virus type 1 by using Vpr fusion proteins
    • Kobinger GP, Borsetti A, Nie Z, et al. Virion-targeted viral inactivation of human immunodeficiency virus type 1 by using Vpr fusion proteins. J Virol 1998; 72: 5441-8.
    • (1998) J Virol , vol.72 , pp. 5441-5448
    • Kobinger, G.P.1    Borsetti, A.2    Nie, Z.3
  • 173
    • 44849100325 scopus 로고    scopus 로고
    • Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection
    • Ao Z, Yu Z, Wang L, Zheng Y, Yao X. Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection. PLoS One 2008; 3: e1995.
    • (2008) PLoS One , vol.3
    • Ao, Z.1    Yu, Z.2    Wang, L.3    Zheng, Y.4    Yao, X.5
  • 175
    • 0034095092 scopus 로고    scopus 로고
    • Packageable antiviral therapeutics against human immunodeficiency virus type 1: Viriontargeted virus inactivation by incorporation of a single-chain antibody against viral integrase into progeny virions
    • Okui N, Sakuma R, Kobayashi N, et al. Packageable antiviral therapeutics against human immunodeficiency virus type 1: viriontargeted virus inactivation by incorporation of a single-chain antibody against viral integrase into progeny virions. Hum Gene Ther 2000; 11: 537-46.
    • (2000) Hum Gene Ther , vol.11 , pp. 537-546
    • Okui, N.1    Sakuma, R.2    Kobayashi, N.3
  • 176
    • 0033925327 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication and infectivity by expression of a fusion protein, VPR-anti-integrase single-chain variable fragment (SFv): Intravirion molecular therapies
    • BouHamdan M, Kulkosky J, Duan L, Pomerantz R. Inhibition of HIV-1 replication and infectivity by expression of a fusion protein, VPR-anti-integrase single-chain variable fragment (SFv): intravirion molecular therapies. J Hum Virol 2000; 3: 6-15.
    • (2000) J Hum Virol , vol.3 , pp. 6-15
    • Bouhamdan, M.1    Kulkosky, J.2    Duan, L.3    Pomerantz, R.4
  • 177
    • 0030792182 scopus 로고    scopus 로고
    • Complementation of integrase function in HIV-1 virions
    • Fletcher TM, Soares MA, McPhearson S, et al. Complementation of integrase function in HIV-1 virions. Embo J 1997; 16: 5123-38.
    • (1997) Embo J , vol.16 , pp. 5123-5138
    • Fletcher, T.M.1    Soares, M.A.2    McPhearson, S.3
  • 178
    • 0030851908 scopus 로고    scopus 로고
    • Functional RT and IN incorporated into HIV-1 particles independently of the Gag/Pol precursor protein
    • Wu X, Liu H, Xiao H, et al. Functional RT and IN incorporated into HIV-1 particles independently of the Gag/Pol precursor protein. Embo J 1997; 16: 5113-22.
    • (1997) Embo J , vol.16 , pp. 5113-5122
    • Wu, X.1    Liu, H.2    Xiao, H.3
  • 179
    • 0030768798 scopus 로고    scopus 로고
    • Incorporation of functional human immunodeficiency virus type 1 integrase into virions independent of the Gag-Pol precursor protein
    • Liu H, Wu X, Xiao H, Conway JA, Kappes JC. Incorporation of functional human immunodeficiency virus type 1 integrase into virions independent of the Gag-Pol precursor protein. J Virol 1997; 71: 7704-10.
    • (1997) J Virol , vol.71 , pp. 7704-7710
    • Liu, H.1    Wu, X.2    Xiao, H.3    Conway, J.A.4    Kappes, J.C.5
  • 180
    • 0034218268 scopus 로고    scopus 로고
    • Development of a novel translentiviral vector that affords predictable safety
    • Wu X, Wakefield JK, Liu H, et al. Development of a novel translentiviral vector that affords predictable safety. Mol Ther 2000; 2: 47-55.
    • (2000) Mol Ther , vol.2 , pp. 47-55
    • Wu, X.1    Wakefield, J.K.2    Liu, H.3
  • 181
    • 40349106153 scopus 로고    scopus 로고
    • Design of a trans protease lentiviral packaging system that produces high titer virus
    • Westerman K, Ao Z, Cohen É, Leboulch P. Design of a trans protease lentiviral packaging system that produces high titer virus. Retrovirology 2007; 4: 96.
    • (2007) Retrovirology , vol.4 , pp. 96
    • Westerman, K.1    Ao, Z.2    Cohen, É.3    Leboulch, P.4
  • 182
    • 19344375031 scopus 로고    scopus 로고
    • Retroviral DNA integration: ASLV, HIV, and MLV show distinct target site preferences
    • Mitchell RS, Beitzel BF, Schroder ARW, et al. Retroviral DNA integration: ASLV, HIV, and MLV show distinct target site preferences. PLoS Biol 2004; 2: e234.
    • (2004) PLoS Biol , vol.2
    • Mitchell, R.S.1    Beitzel, B.F.2    Schroder, A.R.W.3
  • 183
    • 33745684269 scopus 로고    scopus 로고
    • Retroviral DNA integration: Viral and cellular determinants of target-site selection
    • Lewinski MK, Yamashita M, Emerman M, et al. Retroviral DNA integration: viral and cellular determinants of target-site selection. PLoS Pathog 2006; 2: e60.
    • (2006) PLoS Pathog , vol.2
    • Lewinski, M.K.1    Yamashita, M.2    Emerman, M.3
  • 184
    • 35948946526 scopus 로고    scopus 로고
    • Gene editing in human stem cells using zinc finger nucleases and integrasedefective lentiviral vector delivery
    • Lombardo A, Genovese P, Beausejour CM, et al. Gene editing in human stem cells using zinc finger nucleases and integrasedefective lentiviral vector delivery. Nat Biotechnol 2007; 25: 1298-306.
    • (2007) Nat Biotechnol , vol.25 , pp. 1298-1306
    • Lombardo, A.1    Genovese, P.2    Beausejour, C.M.3
  • 185
    • 80053350622 scopus 로고    scopus 로고
    • Site-specific integration and tailoring of cassette design for sustainable gene transfer
    • Lombardo A, Cesana D, Genovese P, et al. Site-specific integration and tailoring of cassette design for sustainable gene transfer. Nat Methods 2011; 8: 861-9.
    • (2011) Nat Methods , vol.8 , pp. 861-869
    • Lombardo, A.1    Cesana, D.2    Genovese, P.3
  • 186
    • 79960424171 scopus 로고    scopus 로고
    • In vivo genome editing restores haemostasis in a mouse model of haemophilia
    • Li H, Haurigot V, Doyon Y, et al. In vivo genome editing restores haemostasis in a mouse model of haemophilia. Nature 2011; 475: 217-21.
    • (2011) Nature , vol.475 , pp. 217-221
    • Li, H.1    Haurigot, V.2    Doyon, Y.3
  • 187
    • 80053195536 scopus 로고    scopus 로고
    • Efficient gene targeting mediated by a lentiviral vector-associated meganuclease
    • Izmiryan A, Basmaciogullari S, Henry A, Paques F, Danos O. Efficient gene targeting mediated by a lentiviral vector-associated meganuclease. Nucleic Acids Res 2011; 39: 7610-9.
    • (2011) Nucleic Acids Res , vol.39 , pp. 7610-7619
    • Izmiryan, A.1    Basmaciogullari, S.2    Henry, A.3    Paques, F.4    Danos, O.5
  • 188
    • 77957608958 scopus 로고    scopus 로고
    • Site-specific gene insertion mediated by a Cre-loxP-carrying lentiviral vector
    • Michel G, Yu Y, Chang T, Yee JK. Site-specific gene insertion mediated by a Cre-loxP-carrying lentiviral vector. Mol Ther 2010; 18: 1814-21.
    • (2010) Mol Ther , vol.18 , pp. 1814-1821
    • Michel, G.1    Yu, Y.2    Chang, T.3    Yee, J.K.4
  • 189
    • 0343415768 scopus 로고    scopus 로고
    • Mammalian genomes contain active recombinase recognition sites
    • Thyagarajan B, Guimaraes M, Groth A, Calos M. Mammalian genomes contain active recombinase recognition sites. Gene 2000; 244: 47-54.
    • (2000) Gene , vol.244 , pp. 47-54
    • Thyagarajan, B.1    Guimaraes, M.2    Groth, A.3    Calos, M.4
  • 190
    • 0034754491 scopus 로고    scopus 로고
    • Alteration of Cre recombinase site specificity by substrate-linked protein evolution
    • Buchholz F, Stewart AF. Alteration of Cre recombinase site specificity by substrate-linked protein evolution. Nat Biotechnol 2001; 19: 1047-52.
    • (2001) Nat Biotechnol , vol.19 , pp. 1047-1052
    • Buchholz, F.1    Stewart, A.F.2
  • 191
    • 34347398120 scopus 로고    scopus 로고
    • HIV-1 proviral DNA excision using an evolved recombinase
    • Sarkar I, Hauber I, Hauber J, Buchholz F. HIV-1 proviral DNA excision using an evolved recombinase. Science 2007; 316: 1912-5.
    • (2007) Science , vol.316 , pp. 1912-1915
    • Sarkar, I.1    Hauber, I.2    Hauber, J.3    Buchholz, F.4
  • 192
    • 33744832621 scopus 로고    scopus 로고
    • With a little help from a friend: Increasing HIV transduction of monocytederived dendritic cells with virion-like particles of SIVMAC
    • Goujon C, Jarrosson-Wuilleme L, Bernaud J, et al. With a little help from a friend: increasing HIV transduction of monocytederived dendritic cells with virion-like particles of SIVMAC. Gene Ther 2006; 13: 991-4.
    • (2006) Gene Ther , vol.13 , pp. 991-994
    • Goujon, C.1    Jarrosson-Wuilleme, L.2    Bernaud, J.3
  • 193
    • 58149459998 scopus 로고    scopus 로고
    • SIVMAC Vpx improves the transduction of dendritic cells with nonintegrative HIV-1-derived vectors
    • Berger G, Goujon C, Darlix J, Cimarelli A. SIVMAC Vpx improves the transduction of dendritic cells with nonintegrative HIV-1-derived vectors. Gene Ther 2008; 16: 159-63.
    • (2008) Gene Ther , vol.16 , pp. 159-163
    • Berger, G.1    Goujon, C.2    Darlix, J.3    Cimarelli, A.4
  • 194
    • 27144505682 scopus 로고    scopus 로고
    • Nef is physically recruited into the immunological synapse and potentiates T cell activation early after TCR engagement
    • Fenard D, Yonemoto W, de Noronha C, et al. Nef is physically recruited into the immunological synapse and potentiates T cell activation early after TCR engagement. J Immunol 2005; 175: 6050-7.
    • (2005) J Immunol , vol.175 , pp. 6050-6057
    • Fenard, D.1    Yonemoto, W.2    de Noronha, C.3
  • 195
    • 0030684068 scopus 로고    scopus 로고
    • Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nefinduced CD4 down-regulation
    • Greenberg ME, Bronson S, Lock M, et al. Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nefinduced CD4 down-regulation. Embo J 1997; 16: 6964-76.
    • (1997) Embo J , vol.16 , pp. 6964-6976
    • Greenberg, M.E.1    Bronson, S.2    Lock, M.3
  • 196
    • 0036889125 scopus 로고    scopus 로고
    • Direct binding of human immunodeficiency virus type 1 Nef to the major histocompatibility complex class I (MHC-I) cytoplasmic tail disrupts MHC-I trafficking
    • Williams M, Roeth JF, Kasper MR, et al. Direct binding of human immunodeficiency virus type 1 Nef to the major histocompatibility complex class I (MHC-I) cytoplasmic tail disrupts MHC-I trafficking. J Virol 2002; 76: 12173-84.
    • (2002) J Virol , vol.76 , pp. 12173-12184
    • Williams, M.1    Roeth, J.F.2    Kasper, M.R.3
  • 197
    • 0031958099 scopus 로고    scopus 로고
    • gag, vif, and nef genes contribute to the homologous viral interference induced by a nonproducer human immunodeficiency virus type 1 (HIV-1) variant: Identification of novel HIV-1-inhibiting viral protein mutants
    • D'Aloja P, Olivetta E, Bona R, et al. gag, vif, and nef genes contribute to the homologous viral interference induced by a nonproducer human immunodeficiency virus type 1 (HIV-1) variant: identification of novel HIV-1-inhibiting viral protein mutants. J Virol 1998; 72: 4308-19.
    • (1998) J Virol , vol.72 , pp. 4308-4319
    • D'Aloja, P.1    Olivetta, E.2    Bona, R.3
  • 198
    • 28444447368 scopus 로고    scopus 로고
    • Cell death induced by the herpes simplex virus-1 thymidine kinase delivered by human immunodeficiency virus-1-based virus-like particles
    • Peretti S, Schiavoni I, Pugliese K, Federico M. Cell death induced by the herpes simplex virus-1 thymidine kinase delivered by human immunodeficiency virus-1-based virus-like particles. Mol Ther 2005; 12: 1185-96.
    • (2005) Mol Ther , vol.12 , pp. 1185-1196
    • Peretti, S.1    Schiavoni, I.2    Pugliese, K.3    Federico, M.4
  • 199
    • 30844469306 scopus 로고    scopus 로고
    • Selective elimination of HIV-1-infected cells by Env-directed, HIV-1-based viruslike particles
    • Peretti S, Schiavoni I, Pugliese K, Federico M. Selective elimination of HIV-1-infected cells by Env-directed, HIV-1-based viruslike particles. Virology 2006; 345: 115-26.
    • (2006) Virology , vol.345 , pp. 115-126
    • Peretti, S.1    Schiavoni, I.2    Pugliese, K.3    Federico, M.4
  • 200
    • 33748352970 scopus 로고    scopus 로고
    • Direct stimulation of T lymphocytes by immunosomes: Virus-like particles decorated with T cell receptor/CD3 ligands plus costimulatory molecules
    • Derdak SV, Kueng HJ, Leb VM, et al. Direct stimulation of T lymphocytes by immunosomes: virus-like particles decorated with T cell receptor/CD3 ligands plus costimulatory molecules. Proc Natl Acad Sci USA 2006; 103: 13144-9.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13144-13149
    • Derdak, S.V.1    Kueng, H.J.2    Leb, V.M.3
  • 201
    • 34547770261 scopus 로고    scopus 로고
    • General strategy for decoration of enveloped viruses with functionally active lipid-modified cytokines
    • Kueng HJ, Leb VM, Haiderer D, et al. General strategy for decoration of enveloped viruses with functionally active lipid-modified cytokines. J Virol 2007; 81: 8666-76.
    • (2007) J Virol , vol.81 , pp. 8666-8676
    • Kueng, H.J.1    Leb, V.M.2    Haiderer, D.3
  • 202
    • 77952319044 scopus 로고    scopus 로고
    • Fluorosomes: A convenient new reagent to detect and block multivalent and complex receptorligand interactions
    • Kueng HJ, Manta C, Haiderer D, et al. Fluorosomes: a convenient new reagent to detect and block multivalent and complex receptorligand interactions. Faseb J 2010; 24: 1572-82.
    • (2010) Faseb J , vol.24 , pp. 1572-1582
    • Kueng, H.J.1    Manta, C.2    Haiderer, D.3
  • 203
    • 33947647023 scopus 로고    scopus 로고
    • High-efficiency FLP and C31 sitespecific recombination in mammalian cells
    • Raymond CS, Soriano P. High-efficiency FLP and C31 sitespecific recombination in mammalian cells. PLoS One 2007; 2: e162.
    • (2007) PLoS One , vol.2
    • Raymond, C.S.1    Soriano, P.2
  • 204
    • 80052564938 scopus 로고    scopus 로고
    • Protein transduction by pseudotyped lentivirus-like nanoparticles
    • Aoki T, Miyauchi K, Urano E, Ichikawa R, Komano J. Protein transduction by pseudotyped lentivirus-like nanoparticles. Gene Ther 2011; 18: 936-41.
    • (2011) Gene Ther , vol.18 , pp. 936-941
    • Aoki, T.1    Miyauchi, K.2    Urano, E.3    Ichikawa, R.4    Komano, J.5
  • 205
    • 68249112926 scopus 로고    scopus 로고
    • Integration-deficient lentiviral vectors: A slow coming of age
    • Wanisch K, Yáñez-Muñoz RJ. Integration-deficient lentiviral vectors: a slow coming of age. Mol Ther 2009; 17: 1316-32.
    • (2009) Mol Ther , vol.17 , pp. 1316-1332
    • Wanisch, K.1    Yáñez-Muñoz, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.