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Volumn 79, Issue 9, 2005, Pages 5557-5567

ATPγS disrupts human immunodeficiency virus type 1 virion core integrity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; COMPLEMENTARY DNA; GAG PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; NUCLEOTIDE DERIVATIVE; POLYPEPTIDE; VIRUS DNA; ADENOSINE 5'-O-(3-THIOTRIPHOSPHATE); ADENOSINE TRIPHOSPHATE; DRUG DERIVATIVE; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR;

EID: 17444384197     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.9.5557-5567.2005     Document Type: Article
Times cited : (27)

References (82)
  • 1
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
    • Accola, M. A., B. Strack, and H. G. Gottlinger. 2000. Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain. J. Virol. 74:5395-5402.
    • (2000) J. Virol. , vol.74 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 2
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi, A., H. E. Gendelman, S. Koenig, T. Folks, R. Willey, A. Rabson, and M. A. Martin. 1986. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 59:284-291.
    • (1986) J. Virol. , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 3
    • 0034666051 scopus 로고    scopus 로고
    • Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex
    • Agostini, I., S. Popov, J. Li, L. Dubrovsky, T. Hao, and M. Bukrinsky. 2000. Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex. Exp. Cell Res. 259:398-403.
    • (2000) Exp. Cell Res. , vol.259 , pp. 398-403
    • Agostini, I.1    Popov, S.2    Li, J.3    Dubrovsky, L.4    Hao, T.5    Bukrinsky, M.6
  • 4
    • 4544232464 scopus 로고    scopus 로고
    • APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein
    • Alce, T. M., and W. Popik. 2004. APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein. J. Biol. Chem. 279:34083-34086.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34083-34086
    • Alce, T.M.1    Popik, W.2
  • 5
    • 0142157237 scopus 로고    scopus 로고
    • Production of ribosome components in effector CD4+ T cells is accelerated by TCR stimulation and coordinated by ERK-MAPK
    • Asmal, M., J. Colgan, F. Naef, B. Yu, Y. Lee, M. Magnasco, and J. Luban. 2003. Production of ribosome components in effector CD4+ T cells is accelerated by TCR stimulation and coordinated by ERK-MAPK. Immunity 19:535-548.
    • (2003) Immunity , vol.19 , pp. 535-548
    • Asmal, M.1    Colgan, J.2    Naef, F.3    Yu, B.4    Lee, Y.5    Magnasco, M.6    Luban, J.7
  • 7
    • 0026022720 scopus 로고
    • Equine infectious anemia virus and human immunodeficiency virus DNA synthesis in vitro: Characterization of the endogenous reverse transcriptase reaction
    • Borroto-Esoda, K., and L. R. Boone. 1991. Equine infectious anemia virus and human immunodeficiency virus DNA synthesis in vitro: characterization of the endogenous reverse transcriptase reaction. J. Virol. 65:1952-1959.
    • (1991) J. Virol. , vol.65 , pp. 1952-1959
    • Borroto-Esoda, K.1    Boone, L.R.2
  • 8
    • 0035031936 scopus 로고    scopus 로고
    • Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase
    • Boyer, P. L., S. G. Saraflanos, E. Arnold, and S. H. Hughes. 2001. Selective excision of AZTMP by drug-resistant human immunodeficiency virus reverse transcriptase. J. Virol. 75:4832-4842.
    • (2001) J. Virol. , vol.75 , pp. 4832-4842
    • Boyer, P.L.1    Saraflanos, S.G.2    Arnold, E.3    Hughes, S.H.4
  • 9
    • 0029949799 scopus 로고    scopus 로고
    • Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription
    • Braaten, D., E. K. Franke, and J. Luban. 1996. Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type 1 before the initiation of reverse transcription. J. Virol. 70:3551-3560.
    • (1996) J. Virol. , vol.70 , pp. 3551-3560
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 10
    • 0029887104 scopus 로고    scopus 로고
    • Cyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus SIV(CPZ)GAB but not group O HIV-1 or other primate immunodeficiency viruses
    • Braaten, D., E. K. Franke, and J. Luban. 1996. Cyclophilin A is required for the replication of group M human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus SIV(CPZ)GAB but not group O HIV-1 or other primate immunodeficiency viruses. J. Virol. 70:4220-4227.
    • (1996) J. Virol. , vol.70 , pp. 4220-4227
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 12
    • 0033027711 scopus 로고    scopus 로고
    • In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain
    • Campbell, S., and A. Rein. 1999. In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain. J. Virol. 73:2270-2279.
    • (1999) J. Virol. , vol.73 , pp. 2270-2279
    • Campbell, S.1    Rein, A.2
  • 13
    • 0030947591 scopus 로고    scopus 로고
    • In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: Identification of the p10 domain as a morphological determinant in the formation of spherical particles
    • Campbell, S., and V. M. Vogt. 1997. In vitro assembly of virus-like particles with Rous sarcoma virus Gag deletion mutants: identification of the p10 domain as a morphological determinant in the formation of spherical particles. J. Virol. 71:4425-4435.
    • (1997) J. Virol. , vol.71 , pp. 4425-4435
    • Campbell, S.1    Vogt, V.M.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., and V. M. Vogt. 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
  • 16
    • 0042317020 scopus 로고    scopus 로고
    • Active cAMP-dependent protein kinase incorporated within highly purified HIV-1 particles is required for viral infectivity and interacts with viral capsid protein
    • Cartier, C., B. Hemonnot, B. Gay, M. Bardy, C. Sanchiz, C. Devaux, and L. Briant. 2003. Active cAMP-dependent protein kinase incorporated within highly purified HIV-1 particles is required for viral infectivity and interacts with viral capsid protein. J. Biol. Chem. 278:35211-35219.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35211-35219
    • Cartier, C.1    Hemonnot, B.2    Gay, B.3    Bardy, M.4    Sanchiz, C.5    Devaux, C.6    Briant, L.7
  • 17
    • 0019971350 scopus 로고
    • Resistance to phosphatase of thiophosphorylated epidermal growth factor receptor in A431 membranes
    • Cassel, D., and L. Glaser. 1982. Resistance to phosphatase of thiophosphorylated epidermal growth factor receptor in A431 membranes. Proc. Natl. Acad. Sci. USA 79:2231-2235.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2231-2235
    • Cassel, D.1    Glaser, L.2
  • 18
    • 0018594325 scopus 로고
    • Irreversible thiophosphorylation and activation of tension in functionally skinned rabbit ileum strips by [35S]ATP gamma S
    • Cassidy, P., P. E. Hoar, and W. G. Kerrick. 1979. Irreversible thiophosphorylation and activation of tension in functionally skinned rabbit ileum strips by [35S]ATP gamma S. J. Biol. Chem. 254:11148-11153.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11148-11153
    • Cassidy, P.1    Hoar, P.E.2    Kerrick, W.G.3
  • 19
    • 0036844376 scopus 로고    scopus 로고
    • A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes
    • Cavrois, M., C. De Noronha, and W. C. Greene. 2002. A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes. Nat. Biotechnol. 20:1151-1154.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1151-1154
    • Cavrois, M.1    De Noronha, C.2    Greene, W.C.3
  • 22
    • 0032989103 scopus 로고    scopus 로고
    • Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 Gag polyprotein
    • Cimarelli, A., and J. Luban. 1999. Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 Gag polyprotein. J. Virol. 73:5388-5401.
    • (1999) J. Virol. , vol.73 , pp. 5388-5401
    • Cimarelli, A.1    Luban, J.2
  • 23
    • 0034003379 scopus 로고    scopus 로고
    • Rescue of multiple viral functions by a second-site suppressor of a human immunodeficiency virus type 1 nucleocapsid mutation
    • Cimarelli, A., S. Sandin, S. Hoglund, and J. Luban. 2000. Rescue of multiple viral functions by a second-site suppressor of a human immunodeficiency virus type 1 nucleocapsid mutation. J. Virol. 74:4273-4283.
    • (2000) J. Virol. , vol.74 , pp. 4273-4283
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 24
    • 0024278041 scopus 로고
    • Sequence and spacing requirements of a retrovirus integration site
    • Colicelli, J., and S. P. Goff. 1988. Sequence and spacing requirements of a retrovirus integration site. J. Mol. Biol. 199:47-59.
    • (1988) J. Mol. Biol. , vol.199 , pp. 47-59
    • Colicelli, J.1    Goff, S.P.2
  • 25
    • 0028849795 scopus 로고
    • In vivo and in vitro association of hsc70 with polyomavirus capsid proteins
    • Cripe, T. P., S. E. Delos, P. A. Estes, and R. L. Garcea. 1995. In vivo and in vitro association of hsc70 with polyomavirus capsid proteins. J. Virol. 69: 7807-7813.
    • (1995) J. Virol. , vol.69 , pp. 7807-7813
    • Cripe, T.P.1    Delos, S.E.2    Estes, P.A.3    Garcea, R.L.4
  • 26
    • 0842326036 scopus 로고    scopus 로고
    • Conservation of a stepwise, energy-sensitive pathway involving HP68 for assembly of primate lentivirus capsids in cells
    • Dooher, J. E., and J. R. Lingappa. 2004. Conservation of a stepwise, energy-sensitive pathway involving HP68 for assembly of primate lentivirus capsids in cells. J. Virol. 78:1645-1656.
    • (2004) J. Virol. , vol.78 , pp. 1645-1656
    • Dooher, J.E.1    Lingappa, J.R.2
  • 27
    • 0021891882 scopus 로고
    • Nucleoside phosphorothioates
    • Eckstein, F. 1985. Nucleoside phosphorothioates. Annu. Rev. Biochem. 54: 367-402.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 367-402
    • Eckstein, F.1
  • 28
    • 11144229594 scopus 로고    scopus 로고
    • Structural requirements for recognition of the human immunodeficiency virus type 1 core during host restriction in owl monkey cells
    • Forshey, B. M., J. Shi, and C. Aiken. 2005. Structural requirements for recognition of the human immunodeficiency virus type 1 core during host restriction in owl monkey cells. J. Virol. 79:869-875.
    • (2005) J. Virol. , vol.79 , pp. 869-875
    • Forshey, B.M.1    Shi, J.2    Aiken, C.3
  • 29
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey, B. M., U. von Schwedler, W. I. Sundquist, and C. Aiken. 2002. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J. Virol. 76:5667-5677.
    • (2002) J. Virol. , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    Von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 30
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • Franke, E. K., H. E. Yuan, and J. Luban. 1994. Specific incorporation of cyclophilin A into HIV-1 virions. Nature 372:359-362.
    • (1994) Nature , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.2    Luban, J.3
  • 31
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 gag proteins: Diverse functions in the virus life cycle
    • Freed, E. O. 1998. HIV-1 gag proteins: diverse functions in the virus life cycle. Virology 251:1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 32
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble, T. R., F. F. Vajdos, S. Yoo, D. K. Worthylake, M. Houseweart, W. I. Sundquist, and C. P. Hill. 1996. Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87:1285-1294.
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Vajdos, F.F.2    Yoo, S.3    Worthylake, D.K.4    Houseweart, M.5    Sundquist, W.I.6    Hill, C.P.7
  • 33
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • Ganser, B. K., S. Li, V. Y. Klishko, J. T. Finch, and W. I. Sundquist. 1999. Assembly and analysis of conical models for the HIV-1 core. Science 283: 80-83.
    • (1999) Science , vol.283 , pp. 80-83
    • Ganser, B.K.1    Li, S.2    Klishko, V.Y.3    Finch, J.T.4    Sundquist, W.I.5
  • 34
    • 0029080761 scopus 로고
    • Interaction of nucleotide-free Hsc70 with ciathrin and peptide and effect of ATP analogues
    • Gao, B., E. Eisenberg, and L. Greene. 1995. Interaction of nucleotide-free Hsc70 with ciathrin and peptide and effect of ATP analogues. Biochemistry 34:11882-11888.
    • (1995) Biochemistry , vol.34 , pp. 11882-11888
    • Gao, B.1    Eisenberg, E.2    Greene, L.3
  • 36
    • 0034466779 scopus 로고    scopus 로고
    • A human nuclear shuttling protein that interacts with human immunodeficiency virus type 1 matrix is packaged into virions
    • Gupta, K., D. Ott, T. J. Hope, R. F. Siliciano, and J. D. Boeke. 2000. A human nuclear shuttling protein that interacts with human immunodeficiency virus type 1 matrix is packaged into virions. J. Virol. 74:11811-11824.
    • (2000) J. Virol. , vol.74 , pp. 11811-11824
    • Gupta, K.1    Ott, D.2    Hope, T.J.3    Siliciano, R.F.4    Boeke, J.D.5
  • 37
    • 0036227658 scopus 로고    scopus 로고
    • Specific incorporation of heat shock protein 70 family members into primate lentiviral virions
    • Gurer, C., A. Cimarelli, and J. Luban. 2002. Specific incorporation of heat shock protein 70 family members into primate lentiviral virions. J. Virol. 76:4666-4670.
    • (2002) J. Virol. , vol.76 , pp. 4666-4670
    • Gurer, C.1    Cimarelli, A.2    Luban, J.3
  • 38
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 39
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., and M. Hayer-Hartl. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 41
    • 0034990535 scopus 로고    scopus 로고
    • Replication of phenotypically mixed human immunodeficiency virus type 1 virions containing catalytically active and catalytically inactive reverse transcriptase
    • Julias, J. G., A. L. Ferris, P. L. Boyer, and S. H. Hughes. 2001. Replication of phenotypically mixed human immunodeficiency virus type 1 virions containing catalytically active and catalytically inactive reverse transcriptase. J. Virol. 75:6537-6546.
    • (2001) J. Virol. , vol.75 , pp. 6537-6546
    • Julias, J.G.1    Ferris, A.L.2    Boyer, P.L.3    Hughes, S.H.4
  • 43
    • 0031932598 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 matrix protein interacts with cellular protein HO3
    • Lama, J., and D. Trono. 1998. Human immunodeficiency virus type 1 matrix protein interacts with cellular protein HO3. J. Virol. 72:1671-1676.
    • (1998) J. Virol. , vol.72 , pp. 1671-1676
    • Lama, J.1    Trono, D.2
  • 44
    • 0024406717 scopus 로고
    • Dextran sulfate and heparin interact with CD4 molecules to inhibit the binding of coat protein (gp120) of HIV
    • Lederman, S., R. Gulick, and L. Chess. 1989. Dextran sulfate and heparin interact with CD4 molecules to inhibit the binding of coat protein (gp120) of HIV. J. Immunol. 143:1149-1154.
    • (1989) J. Immunol. , vol.143 , pp. 1149-1154
    • Lederman, S.1    Gulick, R.2    Chess, L.3
  • 45
    • 0031044374 scopus 로고    scopus 로고
    • A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system
    • Lingappa, J. R., R. L. Hill, M. L. Wong, and R. S. Hegde. 1997. A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system. J. Cell Biol. 136:567-581.
    • (1997) J. Cell Biol. , vol.136 , pp. 567-581
    • Lingappa, J.R.1    Hill, R.L.2    Wong, M.L.3    Hegde, R.S.4
  • 46
    • 0026024732 scopus 로고
    • Association of HSP70 with the adenovirus type 5 fiber protein in infected HEp-2 cells
    • Macejak, D. G., and R. B. Luftig. 1991. Association of HSP70 with the adenovirus type 5 fiber protein in infected HEp-2 cells. Virology 180:120-125.
    • (1991) Virology , vol.180 , pp. 120-125
    • Macejak, D.G.1    Luftig, R.B.2
  • 47
    • 0026525537 scopus 로고
    • Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells
    • Macejak, D. G., and P. Sarnow. 1992. Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells. J. Virol. 66: 1520-1527.
    • (1992) J. Virol. , vol.66 , pp. 1520-1527
    • Macejak, D.G.1    Sarnow, P.2
  • 48
    • 0344736902 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions
    • Mansharamani, M., D. R. Graham, D. Monie, K. K. Lee, J. E. Hildreth, R. F. Siliciano, and K. L. Wilson. 2003. Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions. J. Virol. 77:13084-13092.
    • (2003) J. Virol. , vol.77 , pp. 13084-13092
    • Mansharamani, M.1    Graham, D.R.2    Monie, D.3    Lee, K.K.4    Hildreth, J.E.5    Siliciano, R.F.6    Wilson, K.L.7
  • 49
    • 0002929135 scopus 로고
    • Stress-70 proteins and their interaction with nucleotides
    • R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.) . Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • McKay, D. B., S. M. Wilbanks, K. M. Flaherty, J.-H. Ha, M. C. O'Brien, and L. L. Shirvanee. 1994. Stress-70 proteins and their interaction with nucleotides. p. 153-178. In R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 153-178
    • McKay, D.B.1    Wilbanks, S.M.2    Flaherty, K.M.3    Ha, J.-H.4    O'Brien, M.C.5    Shirvanee, L.L.6
  • 50
    • 2442700372 scopus 로고    scopus 로고
    • Reconstitution of retroviral fusion and uncoating in a cell-free system
    • Narayan, S., and J. A. Young. 2004. Reconstitution of retroviral fusion and uncoating in a cell-free system. Proc. Natl. Acad. Sci. USA 101:7721-7726.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7721-7726
    • Narayan, S.1    Young, J.A.2
  • 51
    • 0035809183 scopus 로고    scopus 로고
    • Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo
    • Newmyer, S. L., and S. L. Schmid. 2001. Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo. J. Cell Biol. 152:607-620.
    • (2001) J. Cell Biol. , vol.152 , pp. 607-620
    • Newmyer, S.L.1    Schmid, S.L.2
  • 52
    • 4444241947 scopus 로고    scopus 로고
    • A Trim5-cyclophilin A fusion protein found in owl monkey kidney cells can restrict HIV-1
    • Nisole, S., C. Lynch, J. P. Stoye, and M. W. Yap. 2004. A Trim5-cyclophilin A fusion protein found in owl monkey kidney cells can restrict HIV-1. Proc. Natl. Acad. Sci. USA 101:13324-13328.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13324-13328
    • Nisole, S.1    Lynch, C.2    Stoye, J.P.3    Yap, M.W.4
  • 53
    • 0030018744 scopus 로고    scopus 로고
    • Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis
    • O'Brien, M. C., K. M. Flaherty, and D. B. McKay. 1996. Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis. J. Biol. Chem. 271:15874-15878.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15874-15878
    • O'Brien, M.C.1    Flaherty, K.M.2    McKay, D.B.3
  • 54
    • 0347634393 scopus 로고    scopus 로고
    • Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body
    • Ono, A., and E. O., Freed. 2004. Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body. J. Virol. 78:1552-1563.
    • (2004) J. Virol. , vol.78 , pp. 1552-1563
    • Ono, A.1    Freed, E.O.2
  • 55
    • 0031900144 scopus 로고    scopus 로고
    • Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus
    • Ott, D. E., L. V. Coren, T. D. Copeland, B. P. Kane, D. G. Johnson, R. C. Sowder, 2nd, Y. Yoshinaka, S. Oroszlan, L. O. Arthur, and L. E. Henderson. 1998. Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus. J. Virol. 72:2962-2968.
    • (1998) J. Virol. , vol.72 , pp. 2962-2968
    • Ott, D.E.1    Coren, L.V.2    Copeland, T.D.3    Kane, B.P.4    Johnson, D.G.5    Sowder II, R.C.6    Yoshinaka, Y.7    Oroszlan, S.8    Arthur, L.O.9    Henderson, L.E.10
  • 56
    • 0029151733 scopus 로고
    • Analysis and localization of cyclophilin A found in the virions of human immunodeficiency virus type 1 MN strain
    • Ott, D. E., L. V. Coren, D. G. Johnson, R. C. Sowder, 2nd, L. O. Arthur, and L. E. Henderson. 1995. Analysis and localization of cyclophilin A found in the virions of human immunodeficiency virus type 1 MN strain. AIDS Res. Hum. Retroviruses 11:1003-1006.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 1003-1006
    • Ott, D.E.1    Coren, L.V.2    Johnson, D.G.3    Sowder II, R.C.4    Arthur, L.O.5    Henderson, L.E.6
  • 58
    • 0025187440 scopus 로고
    • Topoisomerase I activity associated with human immunodeficiency virus (HIV) particles and equine infectious anemia virus core
    • Priel, E., S. D. Showalter, M. Roberts, S. Oroszlan, S. Segal, M. Aboud, and D. G. Blair. 1990. Topoisomerase I activity associated with human immunodeficiency virus (HIV) particles and equine infectious anemia virus core. EMBO J. 9:4167-4172.
    • (1990) EMBO J. , vol.9 , pp. 4167-4172
    • Priel, E.1    Showalter, S.D.2    Roberts, M.3    Oroszlan, S.4    Segal, S.5    Aboud, M.6    Blair, D.G.7
  • 60
    • 0029961364 scopus 로고    scopus 로고
    • The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle
    • Reicin, A. S., A. Ohagen, L. Yin, S. Hoglund, and S. P. Goff. 1996. The role of Gag in human immunodeficiency virus type 1 virion morphogenesis and early steps of the viral life cycle. J. Virol. 70:8645-8652.
    • (1996) J. Virol. , vol.70 , pp. 8645-8652
    • Reicin, A.S.1    Ohagen, A.2    Yin, L.3    Hoglund, S.4    Goff, S.P.5
  • 61
    • 0026675014 scopus 로고
    • Identification of heat shock protein 70 in the rabies virion
    • Sagara, J., and A. Kawai. 1992. Identification of heat shock protein 70 in the rabies virion. Virology 190:845-848.
    • (1992) Virology , vol.190 , pp. 845-848
    • Sagara, J.1    Kawai, A.2
  • 62
    • 0039174260 scopus 로고    scopus 로고
    • Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70
    • Saphire, A. C., T. Guan, E. C. Schirmer, G. R. Nemerow, and L. Gerace. 2000. Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70. J. Biol. Chem. 275:4298-4304.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4298-4304
    • Saphire, A.C.1    Guan, T.2    Schirmer, E.C.3    Nemerow, G.R.4    Gerace, L.5
  • 63
    • 3242876747 scopus 로고    scopus 로고
    • Cyclophilin A retrotransposition into TRIMS explains owl monkey resistance to HIV-1
    • Sayah, D. M., E. Sokolskaja, L. Berthoux, and J. Luban. 2004. Cyclophilin A retrotransposition into TRIMS explains owl monkey resistance to HIV-1. Nature 430:569-573.
    • (2004) Nature , vol.430 , pp. 569-573
    • Sayah, D.M.1    Sokolskaja, E.2    Berthoux, L.3    Luban, J.4
  • 65
    • 0037015028 scopus 로고    scopus 로고
    • An intracellular block to primate lentivirus replication
    • Stoye, J. P. 2002. An intracellular block to primate lentivirus replication. Proc. Natl. Acad. Sci. USA 99:11549-11551.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11549-11551
    • Stoye, J.P.1
  • 66
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack, B., A. Calistri, S. Craig, E. Popova, and H. G. Gottlinger. 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    Gottlinger, H.G.5
  • 67
    • 0034855639 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells
    • Tang, S., T. Murakami, B. E. Agresta, S. Campbell, E. O. Freed, and J. G. Levin. 2001. Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells. J. Virol. 75:9357-9366.
    • (2001) J. Virol. , vol.75 , pp. 9357-9366
    • Tang, S.1    Murakami, T.2    Agresta, B.E.3    Campbell, S.4    Freed, E.O.5    Levin, J.G.6
  • 68
    • 0242409380 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 N-terminal capsid mutants containing cores with abnormally high levels of capsid protein and virtually no reverse transcriptase
    • Tang, S., T. Murakami, N. Cheng, A. C. Steven, E. O. Freed, and J. G. Levin. 2003. Human immunodeficiency virus type 1 N-terminal capsid mutants containing cores with abnormally high levels of capsid protein and virtually no reverse transcriptase. J. Virol. 77:12592-12602.
    • (2003) J. Virol. , vol.77 , pp. 12592-12602
    • Tang, S.1    Murakami, T.2    Cheng, N.3    Steven, A.C.4    Freed, E.O.5    Levin, J.G.6
  • 70
  • 71
    • 0035012785 scopus 로고    scopus 로고
    • The late stage of human immunodeficiency virus type 1 assembly is an energy-dependent process
    • Tritel, M., and M. D. Resh. 2001. The late stage of human immunodeficiency virus type 1 assembly is an energy-dependent process. J. Virol. 75:5473-5481.
    • (2001) J. Virol. , vol.75 , pp. 5473-5481
    • Tritel, M.1    Resh, M.D.2
  • 73
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • von Schwedler, U. K., K. M. Stray, J. E. Garrus, and W. I. Sundquist. 2003. Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77:5439-5450.
    • (2003) J. Virol. , vol.77 , pp. 5439-5450
    • Von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 74
    • 2642608675 scopus 로고    scopus 로고
    • Type D retrovirus capsid assembly and release are active events requiring ATP
    • Weldon, R. A., Jr., W. B. Parker, M. Sakalian, and E. Hunter. 1998. Type D retrovirus capsid assembly and release are active events requiring ATP. J. Virol. 72:3098-3106.
    • (1998) J. Virol. , vol.72 , pp. 3098-3106
    • Weldon Jr., R.A.1    Parker, W.B.2    Sakalian, M.3    Hunter, E.4
  • 75
    • 0033958427 scopus 로고    scopus 로고
    • Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1
    • Welker, R., H. Hohenberg, U. Tessmer, C. Huckhagel, and H. G. Krausslich. 2000. Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1. J. Virol. 74:1168-1177.
    • (2000) J. Virol. , vol.74 , pp. 1168-1177
    • Welker, R.1    Hohenberg, H.2    Tessmer, U.3    Huckhagel, C.4    Krausslich, H.G.5
  • 76
    • 0028287525 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants
    • Wilbanks, S. M., C. DeLuca-Flaherty, and D. B. McKay. 1994. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants. J. Biol. Chem. 269:12893-12898.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12893-12898
    • Wilbanks, S.M.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 78
    • 0029985975 scopus 로고    scopus 로고
    • Endogenous reverse transcription of human immunodeficiency virus type 1 in physiological microenviroments: An important stage for viral infection of nondividing cells
    • Zhang, H., G. Dornadula, and R. J. Pomerantz. 1996. Endogenous reverse transcription of human immunodeficiency virus type 1 in physiological microenviroments: an important stage for viral infection of nondividing cells. J. Virol. 70:2809-2824.
    • (1996) J. Virol. , vol.70 , pp. 2809-2824
    • Zhang, H.1    Dornadula, G.2    Pomerantz, R.J.3
  • 79
    • 0027880142 scopus 로고
    • Reverse transcription takes place within extracellular HIV-1 virions: Potential biological significance
    • Zhang, H., Y. Zhang, T. P. Spicer, L. Z. Abbott, M. Abbott, and B. J. Poiesz. 1993. Reverse transcription takes place within extracellular HIV-1 virions: potential biological significance. AIDS Res. Hum. Retroviruses 9:1287-1296.
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 1287-1296
    • Zhang, H.1    Zhang, Y.2    Spicer, T.P.3    Abbott, L.Z.4    Abbott, M.5    Poiesz, B.J.6
  • 82
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey, R., D. Nagy, R. J. Mandel, L. Naldini, and D. Trono. 1997. Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat. Biotechnol. 15:871-875.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5


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